CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Target MGE spacer number	Prophage number
NZ_CP051677	Spirosoma sp. CJU-R4 chromosome, complete genome	7 crisprs	DinG,WYL,csa3,PD-DExK,DEDDh,Cas9_archaeal,cas3	1	1
NZ_CP051678	Spirosoma sp. CJU-R4 plasmid unnamed1, complete sequence	1 crisprs	PD-DExK	1	0
NZ_CP051679	Spirosoma sp. CJU-R4 plasmid unnamed2, complete sequence	0 crisprs	NA	0	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP051677_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP051677_1

632706-632807

Orphan

Consensus_repeat	Method
CCCCTTCAGGGGGCTGGGGGTAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP051677_1

>merge|NZ_CP051677|1|632706-632807|CRISPRCasFinder
CCCCTTCAGGGGGCTGGGGGTAAACGGGCCGAAGGAAATTTGCTAGCTATCTAAGCTAATACAAGAACTTAACAGCCCTGCCCTTCAGGGGGCTGGGGGTAA

>NZ_CP051677|1|1|632706-632807|CRISPRCasFinder
CCCCTTCAGGGGGCTGGGGGTAA	ACGGGCCGAAGGAAATTTGCTAGCTATCTAAGCTAATACAAGAACTTAACAGCCCT
GCCCTTCAGGGGGCTGGGGGTAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051677.1\|WP_169549344.1\|631660_632524_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP051677.1\|WP_169549335.1\|623384_624185_+\|DUF3473-domain-containing-protein	unknown	unknown	gnl\|CDD\|200566
NZ_CP051677.1\|WP_169549352.1\|644853_646161_-\|anthranilate-synthase-component-I-family-protein	unknown	unknown	gnl\|CDD\|223225
NZ_CP051677.1\|WP_169549336.1\|624253_624583_-\|DUF721-domain-containing-protein	unknown	unknown	gnl\|CDD\|377496
NZ_CP051677.1\|WP_169549341.1\|628514_629711_-\|amine-oxidase	unknown	unknown	gnl\|CDD\|274539
NZ_CP051677.1\|WP_169549350.1\|637934_639152_-\|aminotransferase-class-V-fold-PLP-dependent-enzyme	unknown	unknown	gnl\|CDD\|223594
NZ_CP051677.1\|WP_169549339.1\|626781_627237_+\|response-regulator	unknown	unknown	gnl\|CDD\|381108
NZ_CP051677.1\|WP_169553244.1\|639331_640771_+\|PLP-dependent-aminotransferase-family-protein	unknown	unknown	gnl\|CDD\|224089
NZ_CP051677.1\|WP_169549338.1\|626284_626755_+\|response-regulator	unknown	unknown	gnl\|CDD\|381108
NZ_CP051677.1\|WP_169549346.1\|633909_634629_+\|DUF4136-domain-containing-protein	unknown	unknown	gnl\|CDD\|379281
NZ_CP051677.1\|WP_169549343.1\|630757_631633_-\|UbiA-like-protein-EboC	unknown	unknown	gnl\|CDD\|260127
NZ_CP051677.1\|WP_169553243.1\|636109_637012_-\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|274042
NZ_CP051677.1\|WP_169549337.1\|625067_626144_+\|homoserine-O-acetyltransferase	unknown	unknown	gnl\|CDD\|273596
NZ_CP051677.1\|WP_169549345.1\|632816_633749_-\|hydrolase-TatD	unknown	unknown	gnl\|CDD\|224024
NZ_CP051677.1\|WP_169549347.1\|634638_635304_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169549342.1\|629807_630632_-\|5'-methylthioadenosine/adenosylhomocysteine-nucleosidase	unknown	unknown	gnl\|CDD\|350159
NZ_CP051677.1\|WP_169549351.1\|640773_641529_-\|GLPGLI-family-protein	unknown	unknown	gnl\|CDD\|273495
NZ_CP051677.1\|WP_169549340.1\|627399_628488_-\|lipase-family-protein	unknown	unknown	gnl\|CDD\|238287
NZ_CP051677.1\|WP_169549348.1\|635405_636080_-\|EboA-domain-containing-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169549349.1\|637110_637848_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP051677.1\|WP_169549344.1\|631660_632524_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	6.70812e-14
NZ_CP051677.1\|WP_169549335.1\|623384_624185_+\|DUF3473-domain-containing-protein	gnl\|CDD\|200566	cd10941, CE4_PuuE_HpPgdA_like_2, Putative catalytic domain of uncharacterized prokaryotic polysaccharide deacetylases similar to bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). This family contains many uncharacterized prokaryotic polysaccharide deacetylases (DCAs) that show high sequence similarity to the catalytic domain of bacterial PuuE allantoinases and Helicobacter pylori peptidoglycan deacetylase (HpPgdA). PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as homotetramers. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of DCA-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, PuuE allantoinase and HpPgdA do not exhibit a solvent-accessible polysaccharide binding groove and might only bind a small molecule at the active site.	4.18977e-52
NZ_CP051677.1\|WP_169549352.1\|644853_646161_-\|anthranilate-synthase-component-I-family-protein	gnl\|CDD\|223225	COG0147, TrpE, Anthranilate/para-aminobenzoate synthases component I [Amino acid transport and metabolism / Coenzyme metabolism].	2.38908e-125
NZ_CP051677.1\|WP_169549336.1\|624253_624583_-\|DUF721-domain-containing-protein	gnl\|CDD\|377496	pfam05258, DUF721, Protein of unknown function (DUF721). This family contains several actinomycete proteins of unknown function.	7.6834e-17
NZ_CP051677.1\|WP_169549341.1\|628514_629711_-\|amine-oxidase	gnl\|CDD\|274539	TIGR03356, BGL, beta-galactosidase.	0.00391611
NZ_CP051677.1\|WP_169549350.1\|637934_639152_-\|aminotransferase-class-V-fold-PLP-dependent-enzyme	gnl\|CDD\|223594	COG0520, csdA, Selenocysteine lyase/Cysteine desulfurase [Posttranslational modification, protein turnover, chaperones].	3.08333e-63
NZ_CP051677.1\|WP_169549339.1\|626781_627237_+\|response-regulator	gnl\|CDD\|381108	cd17557, REC_Rcp-like, phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains. This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	4.27029e-23
NZ_CP051677.1\|WP_169549338.1\|626284_626755_+\|response-regulator	gnl\|CDD\|381108	cd17557, REC_Rcp-like, phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains. This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	2.23032e-37
NZ_CP051677.1\|WP_169549346.1\|633909_634629_+\|DUF4136-domain-containing-protein	gnl\|CDD\|379281	pfam13590, DUF4136, Domain of unknown function (DUF4136). This domain is found in bacterial lipoproteins. The function is not known.	1.16077e-16
NZ_CP051677.1\|WP_169549343.1\|630757_631633_-\|UbiA-like-protein-EboC	gnl\|CDD\|260127	cd13964, PT_UbiA_1, UbiA family of prenyltransferases (PTases), Unknown subgroup. Many characterized members of the UbiA prenyltransferase family are aromatic prenyltransferases and play an important role in the biosynthesis of heme, chlorophyll, vitamin E, and vitamin K. They contain two copies of a motif similar to the active site DxxD motif of trans-prenyltransferases and are potentially related. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. The function of this subgroup is unknown.	3.37019e-90
NZ_CP051677.1\|WP_169553243.1\|636109_637012_-\|tyrosine-type-recombinase/integrase	gnl\|CDD\|274042	TIGR02224, Tyrosine_recombinase_XerC, tyrosine recombinase XerC. The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This model represents XerC, one of two closely related chromosomal proteins along with XerD (TIGR02225). XerC and XerD are site-specific recombinases which help resolve chromosome dimers to monomers for cell division after DNA replication. In species with a large chromosome and homologs of XerC on other replicons, the chomosomal copy was preferred for building this model. This model does not detect all XerC, as some apparent XerC examples score in the gray zone between trusted (450) and noise (410) cutoffs, along with some XerD examples. XerC and XerD interact with cell division protein FtsK. [DNA metabolism, DNA replication, recombination, and repair].	2.08975e-106
NZ_CP051677.1\|WP_169549337.1\|625067_626144_+\|homoserine-O-acetyltransferase	gnl\|CDD\|273596	TIGR01392, Homoserine_O-acetyltransferase, homoserine O-acetyltransferase. This family describes homoserine-O-acetyltransferase, an enzyme of methionine biosynthesis. This model has been rebuilt to identify sequences more broadly, including a number of sequences suggested to be homoserine O-acetyltransferase based on proximity to other Met biosynthesis genes. [Amino acid biosynthesis, Aspartate family].	1.07238e-127
NZ_CP051677.1\|WP_169549345.1\|632816_633749_-\|hydrolase-TatD	gnl\|CDD\|224024	COG1099, COG1099, Predicted metal-dependent hydrolases with the TIM-barrel fold [General function prediction only].	3.47718e-106
NZ_CP051677.1\|WP_169549342.1\|629807_630632_-\|5'-methylthioadenosine/adenosylhomocysteine-nucleosidase	gnl\|CDD\|350159	cd09008, MTAN, 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases. This subfamily includes both bacterial and plant 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidases (MTANs): bacterial MTANs show comparable efficiency in hydrolyzing MTA and SAH, while plant enzymes are highly specific for MTA and are unable to metabolize SAH or show significantly reduced activity towards SAH. MTAN is involved in methionine and S-adenosyl-methionine recycling, polyamine biosynthesis, and bacterial quorum sensing. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.	7.01009e-88
NZ_CP051677.1\|WP_169549340.1\|627399_628488_-\|lipase-family-protein	gnl\|CDD\|238287	cd00519, Lipase_3, Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site. .	1.93777e-17
NZ_CP051677.1\|WP_169553244.1\|639331_640771_+\|PLP-dependent-aminotransferase-family-protein	gnl\|CDD\|224089	COG1167, ARO8, Transcriptional regulators containing a DNA-binding HTH domain and an aminotransferase domain (MocR family) and their eukaryotic orthologs [Transcription / Amino acid transport and metabolism].	6.70371e-121
NZ_CP051677.1\|WP_169549351.1\|640773_641529_-\|GLPGLI-family-protein	gnl\|CDD\|273495	TIGR01200, conserved_hypothetical_protein, GLPGLI family protein. This protein family was first noted as a paralogous set in Porphyromonas gingivalis, but it is more widely distributed among the Bacteroidetes. The protein family is now renamed GLPGLI after its best-conserved motif.	1.40506e-38

>NZ_CP051677.1|WP_169549344.1|631660_632524_-|tetratricopeptide-repeat-protein
MLELTALTAFVGYIIYLRYYADQRTAAQKEADRLRDGINLYDGGQTADALAYFNAALAEQPKSSVAYLYRARIYHDLGDPAAALTDLNRGKSYDDTVSELHLETGKIHYEQGDYEQAFTDFDKAVFHNSTDLPEPYRWRGMAGQKLRRTDLSRSDLERADTLANAATVPIGGEPAPTAFFDRRFVLHMGLVVLTSTLLLLIIKRSNVIHWPYLAAAIVGVLIGFLETRKGWALAIEQALLLWLGYTFVLGPAVGGHRQDLENFSLYGSIGLTFIGSLLGSVIKRAQG
>NZ_CP051677.1|WP_169549343.1|630757_631633_-|UbiA-like-protein-EboC
MLKALLSLTRPANLVTAIADVLAGMAIAGYFATNSPAPAPIGWLALATVGLYGGGVVFNDVFDAELDAVERPERPIPSGVVSKGAAAGLGAGLYALGVITAFLVNNTAGLLALAIVVVSLVYDRFGKHHSLAGPLNMGLCRGLNLLLGVSILPDQLMPWLWVGIIPIIYIAAITMISRGEVHGGSPVVLRVAGLLYALVIGCVAALAQDRQQLGTAFPFLALFGYYIFPPLWQAVREPIGPNIGRAVKAGVLSLIVMNAAWVAAFASFPLAMLVFCLLPLSRLLAKVFAVT
>NZ_CP051677.1|WP_169549342.1|629807_630632_-|5'-methylthioadenosine/adenosylhomocysteine-nucleosidase
MLKYLLLAFAFLIQPAYAQRYKTRPVTGLLGAFGAEVALVKQSLKKPKEVVVDGIVFTTGQLGKQRVVVAETGIGKVNAAMTTALLLDHFRPRRVLFTGIAGGTNPDLQPGDIVIASRTAHHDYSSVTDKNTPVRQTRDAITRQFNPLYFPADSTLLGLAQRVSGAVTLEGIPLADGGVSNRPVRVMTGTVVTGDVFVASAAKGVSLRTDFGADATEMEGAAVAQVCYQLQVPHLIIRSLSDRADAEAHIAYDKFYPTAARNSAKLVLAIVQGL
>NZ_CP051677.1|WP_169549341.1|628514_629711_-|amine-oxidase
MPSTLSVSTTGNPFRSFWWAGYECTDQLNAFGNRVDFLPLTGHLQLIQQDYEDLKQFDLRTVREGIRWSQVEKTAYQYDWRTVESMLAEGHRQGIQQVWDLCHFGYPDDLTPLHPMFARRFAALGRAFVRFYRDLYPDEPLIVTPINEVSFMSWLGGDARGTSPYCTKQGWEVKRGLMRGYIECVAAMREIDPSIRILTTEPLVHIVPPLPATKAERDRAAEGHNNQFQSVDMLAGRISPELGGSPEFLDILGFNYYYNNQWISGTHTFLGWADAVPDPRWVPLRKLLIEAHDRYKRPIALTETSHPGIDRPQWIRMIGQECAAALLAGVPLWGVCLYPIVDRPDWDHLTPWHKSGLWDADLSTTPPGRVLYQPYADALLQAQAEVAPLLPVAEQLLI
>NZ_CP051677.1|WP_169549340.1|627399_628488_-|lipase-family-protein
MKNGLLVLLACLSLTHIAQAQKLKPGFDKAEYVELLSVFAKQVDTLPANTPIPKPQRFARLYRSPIVGLDNRWELWSSPDSVGVISIRGTTLNPVGWLENFYAAMVPAKGNIVMTNDYKFDYQLANDPRAAVHIGWLIGTAFLAQDIMPRLDSCVRKGITNFYVMGHSQGGAIAYLMTAHLKQLQRSGKIPASVQFKTYCSAAPKPGNLQFAYEYEAMAVGGWSFNVVNAADWVPEMPITIQTLDDFNPVNPFANAPALIKKQKFPKNLALRYVFNRLSKPAQKASKVYRKYLGEYASRYVKTNLKEYVPPTFHQSSDYVRTGTIISLVPDEAYYKKYPQEREKIFTNHLLPPYFDLVRLLP
>NZ_CP051677.1|WP_169549339.1|626781_627237_+|response-regulator
MYNKKDHYLPEEELYPVCYVVADDDPDELLLMRAALSQQQRPLPVREFVDGQYVVDYLLDNRESRNDEDVHWLLILDMHMPRLNGLETVKAIRQNHNWDTIPILLFTEEDNDSLIQEALASGANGCITKPERLDDYRQLFDKFFSPYLRNW
>NZ_CP051677.1|WP_169549338.1|626284_626755_+|response-regulator
MNSHCELSYVVVDDDEDDRLLMRLALEQSQRTLPVLEFSDGQELIDYLSQDTSARPDEDMHWLVIMDVNMPRMNGLDALQTLRQDPHWAKLPVLMLSTADDDVTRQLSLEKGANGYLVKPTSMQDYGPLFDRHFAPWLAVDSSQWPDYSSQADQSL
>NZ_CP051677.1|WP_169549337.1|625067_626144_+|homoserine-O-acetyltransferase
MSAPSTIHYFDYKYSFPLESGATLPGFRLAYTTQGTLRQENGQSNVVWICHALTGNANVSDWWGGMVGAGKFFDPEKHFIVCANVLGSCYGSSGPLSENPATGEPFYHDFPVVTVRDIVNSLDLLRQELGIDRIHTCIGGSLGGEQALEWAIDQPDLIQRLILIASGAVASPWCIAFNEAQRMAIEADPTWTERRADAGAMGMKAARAMAMISYRNYDTYGFTQALDNNEQLDDYKAATYQRYQGDKIVDRYNAFTYRLLSKVMDSHNVGRNRGSIPQALGRVKSRTLVVGIRSDLLFPPSEQQFLARHIPNASYQEIDSLYGHDGFLIEFRPLTALIRTWTASLDVAQPGTVRTNPA
>NZ_CP051677.1|WP_169549336.1|624253_624583_-|DUF721-domain-containing-protein
MSQQTYRYNRDNATRAAGVTSLKDAIGQLLKAYQLQGRFNETYLEAFWGRMMGPAIATRTKRLYVRDGKLYIELSSAPLRNELVNAKQKLIQLVNRDMGSEVITDVVFI
>NZ_CP051677.1|WP_169549335.1|623384_624185_+|DUF3473-domain-containing-protein
MGTAGRSRPQILFTVDVEEFDTAVEFGHDIPLTEQIAVSTRGLRLLAERFDAVGARTTLFTTANYALHETELIRSLSHKHEIASHGYYHTTFEPADLLKSRLELEKLLGQPITGFRRARMGFVDPTDVQQAGYQYNSSLHPTWLPGRYNHWGEPRHPFREQGVWQIPASVTPTLRLPLFWLSLKNFPWAYYKQLCRQTLKADGFLNLYVHPWEFTDLSAYEKIPAYVKRHSRDELLDRVESLLRYLKPQGEFSTMGEFARGLTFHV
>NZ_CP051677.1|WP_169549345.1|632816_633749_-|hydrolase-TatD
MDFMDSIRGMSFFDMHVHMTSRTTDDYQAMADAGVVAMIEPAFWLGQPRTGVDSFRDYFASLVGWERFRASQFGIRHYCTIGLNSKEANQEELAEQVMEILPLFIYKEGVVGIGEIGFDDQTVSEEKYYRAQLDLAKEAGLPVQIHTPHRDKKQGTSRSMDIAIEHGIDPGMVIVDHNNEETVRETLDRGFWAGFTIYPFTKMGNERMVEIVKQYGPERIMINSAADWGISDPLAVPKTAALMKQHGISDEAIRLVTFTNAVTAFAQSGQLSLDELSQPLGIDQSQRFNGSSVLRGGQAPRVDKESTIIR
>NZ_CP051677.1|WP_169549346.1|633909_634629_+|DUF4136-domain-containing-protein
MVRSQSARSARWLLGIAATLAIGTGLTACNKDAINDLTPDQSQVYITNYDRSVNFSQYKTFSLPDSVVVESNTGYTTSLGSVESRFVSNVAAALTARGFTRVAAGQKADLGVAVIKVNNRYTGVGVDPYGSYYSNYWGGGFGYGGFGGYYPYYPTYYTYQVTDRYWEIQAVDLKNAPAGAGTGTGTGTGTGTGTGTGTTQPQLNVVYDATVRGDDITDTQSVDAATTAIFNQSSYLRPN
>NZ_CP051677.1|WP_169549347.1|634638_635304_+|hypothetical-protein
MNRYMLPALLAITLALPALAQTTPERPYVYESVSEYDRYVTFNLSARYGVALPMGGLKTYTSGTSATNLALDGEWLFPQRFSIGLKSGYQYTSERLPRQTIYYGDQTISAVQTRTFSVIPVMASLSYYFAQNSGAIRPYVQIAGGGAFVDYINYFGALADQSKGFKGAIAPAIGLKFYGRPEQKFGAEIQAQYQNVFFNYGQLPNNAPSLMLSAGLIYRWY
>NZ_CP051677.1|WP_169549348.1|635405_636080_-|EboA-domain-containing-protein
MTILAMSQTLLYLLEQQPDSAAGVQYLREQTDQLQIEPKPALFYRVFTAMPRYVGRQVIEVPQDMAFAIERIRPDFTVAGWTRDRLARVWWLLQLPADDEERYVSTITQLFKAAELNELVALYSALPVLSYPERWRFQATEGIRNNIADVQSAIMLHNPYPAEQFDEAAWNQLILKAFFTDKDITQITGLHERKNARLAQTLTDYAAERRAAGRSLPPHIGELM
>NZ_CP051677.1|WP_169553243.1|636109_637012_-|tyrosine-type-recombinase/integrase
MNQTDDFLKHIRFEKRLSQHTLTAYTGDMAQFSQFLTTECNVDQPERADFRHIRSWIVSMVEGGMDKTSVNRKIATLRAFFGYLLRRKVIAVDPMTKIQALKMSRKLPVYVEEKPMETLLDEVEFPDTFEGLRDKLVIELLYGTGIRLSELIGLKTVDVNLYNRTITVLGKRNKHRLIPLTQTLYDLIQQYTTLKETEFNGQADATVLIVSDKGVGAYPVLIQRIVKKHLSVVTTLEKKSPHVLRHTFATHLLNRGGDLNAIKDLLGHSSLAATQIYTHTSLEQLKKTYDQAHPKAKKDG
>NZ_CP051677.1|WP_169549349.1|637110_637848_+|hypothetical-protein
MRLLPIVVLLLSSLMACQSPQDPAQSLIDQAIAAHGGDAINNTRISFDFRKAHLVLEQQGGRFRYERTQPDSTGQLVRDVLTNDGFTRHIDGKPQVLDTAQVGKYSRSVNSIAYFVLLPWKLHDPAVVPTLLGSEQIDGQTYDKVQVKFRADGGGKDHGDTFVYWFNQRTYTLDCLAYSEGGPRFRRAIHPQTVAGIRFQDYINYKSDADTLDVATYARRYQARQMVELSRIEQKNIQVTPLPKP
>NZ_CP051677.1|WP_169549350.1|637934_639152_-|aminotransferase-class-V-fold-PLP-dependent-enzyme
MQTDQVIPIDKNTVRADTPGLATATLFMNSAGASLMPRPVITAMQDYLHLETQVGGYETERVRADHMAQLYGEIAKLINARPDNIAFSYSAMAAYTQALSAIPFQPGDVILTTTNDYISNQLAFLSMQQRLGIRLIRINDLDNGDLDLMHLEQLIQQHHPVLVAITHIPTNSGIVQPAELIGAICSRYDCWYLLDAAQSAGQLPLDVERIQADFLVATGRKFLRGPRNTGFLYVSDKVLATGLTPLFVDRQGADWTSPDTFAVRANAKRFEPQEKSLSVVGLVEAVRYANQLGIEAIAQVNQVLMQRLRTGLSQIDGIDLTDLGSVQSNILTFHSTRQPLATLDTALRQGGVLFTVQHKQGAIIDFTRKGIDWIIRLAPHYFNTEAEIDAVVELVDQAVTLPPAP
>NZ_CP051677.1|WP_169553244.1|639331_640771_+|PLP-dependent-aminotransferase-family-protein
MTSRTPKYQTIARQLGDKLRLGQLDDDVKLPSVRTLSRELRVSINTVQQAYYCLESEGLVEARPQSGYYARSRSRRQDALPHHSQPTPGTHQSDQPAKDSLLLRLIGLQNQPDWLPFSMNVPAPGLIPIQKLNKALQQALRTMPNAGIGYDAIPGNLALRQQIARHTMFWGGNLTADELITTEGCTAALTLCLKAVTKPGDTVAVESPAYFGILQTVLSLELQVLELPTDPLTGIDLPTLDGHLKAGRVQACLFVTNFSNPLGSCMTDTGKQQLVRLLETYQVPLIEDDLYGDLHYASHRPVPCKAYDRQGLVLWCGSFSKTLAPGYRVGWVAPGRYYDALLQLKRFQAGVSPGITQQAIAHFLANDRYELHLHRLRKTLKSNCVRYQQTIRASFPAGTRISEPQGSFSLWLELDPAIDTVSLCEDLLLQKISIMPGSMFSLQPQYANCLRLSYGMTYDQRVEAGLQQIGQFVSQYYAG
>NZ_CP051677.1|WP_169549351.1|640773_641529_-|GLPGLI-family-protein
MYRLLIGLLLLSLPSLVMAQKTEGVVEYRRITHWNKIYSRMTYLSQEQKDRIMLRSKNWEDDNKGEKMKLLFTPTQSLYTYSGDASESQDEGYSWRQSELIMTRNFEKERQMDIMEMLGRVYIVEDSLRTPTWKIGNQIKDVAGYICMKAETTDPIKNQTITAWFAQDIPVSAGPERMSGLPGLILELDLNDGDVEIIAQSVTFRPVTADDLKLPKTKGKKITDADYNAMVKKKITESITAHENPYWSIRY
>NZ_CP051677.1|WP_169549352.1|644853_646161_-|anthranilate-synthase-component-I-family-protein
MDTNLEHKTSNVELVFWQRALAWALAQPQNDGVVALLNNSNIEYPNDPFPNRLFVGAKRVVGVSDASDGPDAFELLRLAQAERPSHWVGYLGYDLKNQLERLNSRHPNRIGFADAFFAEPRWIIDYHDGAPTLAGEGDTDALLTDLLAFPMPAFLPVDPQQVQCRVTSDAYMTTVRQIQQFIRAGEVYELNYCVEFFAEQARLDPMATYWALNERSPMPFSAFLKLDDHYMMGASPERFLKKTGATLTSQPIKGTIRRGKTADEDAQLRVRLLNSEKERAENLMIVDLVRNDLARSAQTGTVRVDELFGIYSFRQVFQMISTVSATLHPDSSWTDAIRNAFPMGSMTGAPKIRSMELIDELESSRRGLYSGAFGYVTSDNNFDFNVVIRSLLYDARQQYASFSVGSAITYDADPAQEWDECLLKARAIRDLLEGC

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Crispr_ID: NZ_CP051677_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP051677_2

3169605-3169709

Orphan

Consensus_repeat	Method
CCCTTCAGGGGGCTGGGGGGTAAAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP051677_2

>merge|NZ_CP051677|2|3169605-3169709|CRISPRCasFinder
CCCTTCAGGGGGCTGGGGGGTAAACAGATCTAAGGAAATTTGGCAATAGATAACACCAAGTCAAGAACTTAACAGCCCTGCCCTTCAGGGGGCTGGGGGGTAGAC

>NZ_CP051677|2|2|3169605-3169709|CRISPRCasFinder
CCCTTCAGGGGGCTGGGGGGTAAAC	AGATCTAAGGAAATTTGGCAATAGATAACACCAAGTCAAGAACTTAACAGCCCTG
CCCTTCAGGGGGCTGGGGGGTAGAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051677.1\|WP_169553379.1\|3159758_3160394_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169551215.1\|3174634_3176188_+\|glycosyl-hydrolase-43-family-protein	unknown	unknown	gnl\|CDD\|350115
NZ_CP051677.1\|WP_169551207.1\|3155759_3156818_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340952
NZ_CP051677.1\|WP_169551205.1\|3154386_3155211_+\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|226145
NZ_CP051677.1\|WP_169551216.1\|3181754_3182645_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223730
NZ_CP051677.1\|WP_169551206.1\|3155427_3155841_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|340952
NZ_CP051677.1\|WP_169551213.1\|3169772_3171452_+\|glycoside-hydrolase-family-43-protein	unknown	unknown	gnl\|CDD\|350129
NZ_CP051677.1\|WP_169551220.1\|3186656_3187736_+\|esterase	unknown	unknown	gnl\|CDD\|225256
NZ_CP051677.1\|WP_169551211.1\|3160457_3160943_-\|(2Fe-2S)-binding-protein	unknown	unknown	gnl\|CDD\|224991
NZ_CP051677.1\|WP_169551214.1\|3174097_3174607_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|366361
NZ_CP051677.1\|WP_169551221.1\|3187940_3189059_+\|esterase	unknown	unknown	gnl\|CDD\|199888
NZ_CP051677.1\|WP_169551210.1\|3157597_3159751_-\|xanthine-dehydrogenase-family-protein-molybdopterin-binding-subunit	unknown	unknown	gnl\|CDD\|224446
NZ_CP051677.1\|WP_169551217.1\|3182704_3184267_+\|carboxylesterase-family-protein	unknown	unknown	gnl\|CDD\|365897
NZ_CP051677.1\|WP_169551218.1\|3184314_3185454_+\|esterase	unknown	unknown	gnl\|CDD\|199894
NZ_CP051677.1\|WP_169553380.1\|3161996_3165101_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP051677.1\|WP_169551219.1\|3185475_3186645_+\|esterase	unknown	unknown	gnl\|CDD\|199894
NZ_CP051677.1\|WP_169551208.1\|3156819_3157146_+\|L-rhamnose-mutarotase	unknown	unknown	gnl\|CDD\|377501
NZ_CP051677.1\|WP_169553381.1\|3180925_3181729_+\|sialate-O-acetylesterase	unknown	unknown	gnl\|CDD\|377084
NZ_CP051677.1\|WP_169551212.1\|3165114_3166929_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_CP051677.1\|WP_169551209.1\|3157242_3157404_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP051677.1\|WP_169551215.1\|3174634_3176188_+\|glycosyl-hydrolase-43-family-protein	gnl\|CDD\|350115	cd09001, GH43_FsAxh1-like, Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase. This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	3.65921e-136
NZ_CP051677.1\|WP_169551207.1\|3155759_3156818_+\|MFS-transporter	gnl\|CDD\|340952	cd17394, MFS_FucP_like, Fucose permease and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of L-fucose permease (also called L-fucose-proton symporter) and similar proteins such as glucose/galactose transporter and N-acetyl glucosamine transporter NagP. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. Glucose/galactose transporter functions in the uptake of of glucose and galactose. The FucP-like subfamily belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.57851e-81
NZ_CP051677.1\|WP_169551205.1\|3154386_3155211_+\|amidohydrolase-family-protein	gnl\|CDD\|226145	COG3618, COG3618, Predicted metal-dependent hydrolase of the TIM-barrel fold [General function prediction only].	4.82338e-61
NZ_CP051677.1\|WP_169551216.1\|3181754_3182645_+\|alpha/beta-hydrolase	gnl\|CDD\|223730	COG0657, Aes, Esterase/lipase [Lipid metabolism].	2.34444e-28
NZ_CP051677.1\|WP_169551206.1\|3155427_3155841_+\|hypothetical-protein	gnl\|CDD\|340952	cd17394, MFS_FucP_like, Fucose permease and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of L-fucose permease (also called L-fucose-proton symporter) and similar proteins such as glucose/galactose transporter and N-acetyl glucosamine transporter NagP. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. Glucose/galactose transporter functions in the uptake of of glucose and galactose. The FucP-like subfamily belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	2.88384e-29
NZ_CP051677.1\|WP_169551213.1\|3169772_3171452_+\|glycoside-hydrolase-family-43-protein	gnl\|CDD\|350129	cd18617, GH43_XynB-like, Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	3.94416e-156
NZ_CP051677.1\|WP_169551220.1\|3186656_3187736_+\|esterase	gnl\|CDD\|225256	COG2382, Fes, Enterochelin esterase and related enzymes [Inorganic ion transport and metabolism].	1.73875e-33
NZ_CP051677.1\|WP_169551211.1\|3160457_3160943_-\|(2Fe-2S)-binding-protein	gnl\|CDD\|224991	COG2080, CoxS, Aerobic-type carbon monoxide dehydrogenase, small subunit CoxS/CutS homologs [Energy production and conversion].	4.1011e-74
NZ_CP051677.1\|WP_169551214.1\|3174097_3174607_+\|VOC-family-protein	gnl\|CDD\|366361	pfam00903, Glyoxalase, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.	3.02491e-08
NZ_CP051677.1\|WP_169551221.1\|3187940_3189059_+\|esterase	gnl\|CDD\|199888	cd02858, E_set_Esterase_N, N-terminal Early set domain associated with the catalytic domain of esterase. E or "early" set domains are associated with the catalytic domain of esterase at the N-terminal end. Esterases catalyze the hydrolysis of organic esters to release an alcohol or thiol and acid. The term esterase can be applied to enzymes that hydrolyze carboxylate, phosphate and sulphate esters, but is more often restricted to the first class of substrate. The N-terminal domain of esterase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.	1.70839e-34
NZ_CP051677.1\|WP_169551210.1\|3157597_3159751_-\|xanthine-dehydrogenase-family-protein-molybdopterin-binding-subunit	gnl\|CDD\|224446	COG1529, CoxL, Aerobic-type carbon monoxide dehydrogenase, large subunit CoxL/CutL homologs [Energy production and conversion].	2.26326e-85
NZ_CP051677.1\|WP_169551217.1\|3182704_3184267_+\|carboxylesterase-family-protein	gnl\|CDD\|365897	pfam00135, COesterase, Carboxylesterase family.	4.6179e-131
NZ_CP051677.1\|WP_169551218.1\|3184314_3185454_+\|esterase	gnl\|CDD\|199894	cd11294, E_set_Esterase_like_N, N-terminal Early set domain associated with the catalytic domain of putative esterases. E or "early" set domains are associated with the catalytic domain of esterase at the N-terminal end. Esterases catalyze the hydrolysis of organic esters to release an alcohol or thiol and acid. The term esterase can be applied to enzymes that hydrolyze carboxylate, phosphate and sulphate esters, but is more often restricted to the first class of substrate. The N-terminal domain of esterase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.	8.59996e-35
NZ_CP051677.1\|WP_169553380.1\|3161996_3165101_+\|TonB-dependent-receptor	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_CP051677.1\|WP_169551219.1\|3185475_3186645_+\|esterase	gnl\|CDD\|199894	cd11294, E_set_Esterase_like_N, N-terminal Early set domain associated with the catalytic domain of putative esterases. E or "early" set domains are associated with the catalytic domain of esterase at the N-terminal end. Esterases catalyze the hydrolysis of organic esters to release an alcohol or thiol and acid. The term esterase can be applied to enzymes that hydrolyze carboxylate, phosphate and sulphate esters, but is more often restricted to the first class of substrate. The N-terminal domain of esterase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others.	1.21917e-32
NZ_CP051677.1\|WP_169551208.1\|3156819_3157146_+\|L-rhamnose-mutarotase	gnl\|CDD\|377501	pfam05336, rhaM, L-rhamnose mutarotase. This family contains L-rhamnose mutarotase which is a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer. In Escherichia coli this enzyme is the product of the rhaM gene (also known as yiiL). The tertiary structure has been solved, in complex with L-rhamnose, and the catalytic mechanism determined. His22 is the proton donor. The enzyme naturally exists as a dimer.	2.49452e-39
NZ_CP051677.1\|WP_169553381.1\|3180925_3181729_+\|sialate-O-acetylesterase	gnl\|CDD\|377084	pfam03629, SASA, Carbohydrate esterase, sialic acid-specific acetylesterase. The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.	4.00407e-38
NZ_CP051677.1\|WP_169551212.1\|3165114_3166929_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	1.79368e-32

>NZ_CP051677.1|WP_169551212.1|3165114_3166929_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKAIKFCAVLGLTAVLSTGCEKILEENPQSQIVPSYFNSASGVLGGIAGVYNDIRGQWGTEGFTIEMQAGTDEFLRGASAGSSTAYDYNGLNGSNFGSAWGTAFQDINTLNGVLQYGQTVDLADATRKQYLAQAKFLRGFWYFYLVQTWGDVPLHTQFITVPSQAASRQPVAQVYEQIIKDLTEAAADLPNTPTSPFLGKAATKPVAQLLLAKAYLTRGWLNNTASDFTQAASICADIIANKSSYGLDLWQDYGDAFNPSNDYGKETMFVSDHVLDPKYGYYTVGGAAGGGAAQNLSPWFTNWNYPNTSGVNSFKNASGGLVNNGTSGMIRDSYYGRPYVRMRPNSDKQKSGDNVGKSYFLDQAFTNRTVDSRFANSFYTVYISNTSITNAANAANNQRGIGFTTVVGQDTAVWLPDYEVTGAPQFVGTRPFKGIVVPPSLWNNGIFPALKKFMDPSRGANFNDPSTRPAVLYRFADVYMTGAEAYFKAGDNTKAAALINVVRQRAAYRRTNTAAQNAAAVTAMTIQPSDVTLDFILDERSREFFGEWQRWHDLVRTRSLVRRVKAWNPEAAPYIQDFNMLRPIPQSQIDRVVDGPAFKQNTGY
>NZ_CP051677.1|WP_169553380.1|3161996_3165101_+|TonB-dependent-receptor
MHTSRIAGLDVQDVQVSGRVVDEKGEGLPGVNIQIKSTTRGTTTDASGNYKLTVPNGAVLVFSLVGYAAKEITVGSQSVINVNLSPDDKTLDEVVVVGYGVQRKRDITGSVASVNESTLKEVPAPNLVSQLKGRAAGVSIVSNGTTPGSQGQIRIRGNRTLTTSQGGSDGLDGPLVVVDGIPYGGLNDINPDDIVNLEILKDASATAIYGSRGSGGVILVTTKRGKVGKPVFTYDGYHGVTNIMGKYNVFNGSEYAQFKSDAAKYNRSSPGTTAYPLTPKEQEALAAGVSTDWQDLIYRSGFMTNHQLGMTGGVENTQYSLGLGYFNETGVIPGQDFTRVNIRATIDQRLGSRIKFGLNTLNTLTYQNTPGGGGIPGGLVSLTPLASPYNADGSVNLFPAEGSIDAARISPLTILTKTDSYLNRTRSLRTFNSLYAEVNLLPGLRYRFNAGLNYSQSAFNGYNGPLTYFNQATVQSSSNAEISNTEYWDVNMQHLLYYDKTVGKHKIGVTGLYEYTKNHSLGSRFTITGVPADYIKTANFSLASGTPVAASDFGNSFAETGLLSYMGRVNYSYNDRYLLTLTLRRDGSSTLSPGNRYFNYPAIGAGWNIIEEPFMKSVPVISNLKLRGSWGLAGNRNVGAYATLGALSAGYYNFGLGTAGQQLAYTVTSLPATNLGWQSTAQLDLGIDFGFLNNRITGSVDYYHQKTKDILLSVPLPASNGAGSTLKNLGATEGRGLETSLTVDIFRNPKGFNWGVDAIYYFNREKITQLTTPTEQANIGAGWFVGQPLSVIYDYKKIGIWQTSDKENGTLAKQTSPAQQPGQIRVEDVNGDGKIDPSDRQILGNFQPKFEAGLTNRFSYKNFDLSIVTFARMGMKVVVPYLTGNSGGGGGFAFFNQARSNQVKVDYWTETNPTNAFPAPDANNAVQYFASTLGYYDGSFIKIRSINLGYTIPTQFLRKVRVSSARLYLNVTNPLILYSPLVRDHLAVDPEGNGYASSTVAAQGADTGTQARQIAINLNNPPVRQFTFGVNLKF
>NZ_CP051677.1|WP_169551211.1|3160457_3160943_-|(2Fe-2S)-binding-protein
MAIIKCTINGKEYSFEADPQMPLLWAIRDVVGLKGTKFGCGVAQCGACTVHLNGDAVRSCVTRVSRANGQKIVTIEGLSKNNDHPVQLAWQEIDVPQCGYCHSGQIMSAAVLLRDNPNPTDADIDAAMAGNICRCGTYLRVRKAIHMAAAGVDRKVSSSNE
>NZ_CP051677.1|WP_169553379.1|3159758_3160394_-|hypothetical-protein
MVRPDWLNQKLMALLSAGLFATAVGTSAFTEPAKPVMRPVPLAVAPIQKDSVTSVKAFASVYKVLMSPRCMNCHPAGDIPLQGDDSHLHAMAPRRGTDGKGIYAMKCTNCHQPTNLPGVHTPPGNPNWHLPPATARMVFQGRTPNQLAKQLIDPKQNGGKNREQLLEHAHDGLVVAGWNPGEGRTLPPLSHAEFTKAWTTWIKTGAFAPKP
>NZ_CP051677.1|WP_169551210.1|3157597_3159751_-|xanthine-dehydrogenase-family-protein-molybdopterin-binding-subunit
MDTQPVSRRNFLKVSGLTGVMLSLGLYLPARAEEAEIINTAGTANLGTDMNAWIRIDALGKVTITDHRAEMGQGSYQAVPQIIAEELEVALDEVAVVFAQGNKKYGSQITGGSSTVRGSYKNLLKLSATAREMLIQAAANQWSVPAADCYAEAGHVIHKPSGKKANYGTLVADAAKLEPPKDVVLKKRADYKQIGKPLHRPDTPLKTNGTAGFGLDKTLPGMLYAAVERNPRMRGKVKSFDDTAARKVPGVKHVLKVKMLVYSTYREGVAIVADSTWAALQGKKALKVVWDDSGFEHLNTDEIYKRQQEALQTKEGLSLKKQGDVTDALAKGATKLDVVYETPYQSHSCMEPLNCTAHYQANKVEIWGPIQAPDWVQDSISKEMNVPREKVIVNMTFLGGGFGRKAFMDYPHEAVFISKAVGAPIQVVWTREDDTTQGPFRPGVSYRCEGALADGKISAFKLRMAGQNLGHWMGAPKDKPNDSTDEGFLKPYTDSIKNLSIADVPFETPMPVLWWRSVYASTNGFAYESFVDELAHEARKDPMTFRREHLPDERVQKQLDKLAEVSGWNSRKPGEGYGMAITECFSSTVGQVVKVSKNPDGGVKIDHVWAVMDCGWYVNPDTVKAQVEGSIVMALGAATQHEVTFKDGMAVDKNFYSYQMPRITDIPPIDVFIMDNDADAGGVGEPGLPAFAPALTNAIFDLTGQRIRKLPFSLATV
>NZ_CP051677.1|WP_169551209.1|3157242_3157404_+|hypothetical-protein
MEKDKPTKKDIPSLLLEGVKLGHRRLVEQAKREDDTLVIMRDGKIEHVRAREL
>NZ_CP051677.1|WP_169551208.1|3156819_3157146_+|L-rhamnose-mutarotase
MRYCLALDLKDDPALIAEYERQHVQIRPEIDASIRTSGINDMQIFRVGNRLFMIIETDENFSFDTKAAMDAANPAVQEWETFVSTFQQPLPFARPGEKWVLMKQIFAL
>NZ_CP051677.1|WP_169551207.1|3155759_3156818_+|MFS-transporter
MYGFFLVALFTMACGIACLETAANLYVTVLGDPEKSEWRINFSQSFNGISIIMGPIIGALFIFSKTEYTPEMLTAMAPAEAETIRVQEALSVQGPYLVIGTIIALVTLLFAFTKMPEVGEEEETNSNVSIGRLFRHRHLVLGIVAQFANVGAQAVLWGYFVDLKLDFSRDVHWGPALGFMHLINGLTGNEGGQLSATQIAGFHASFALVLLMLGRFVGTFLMTKMRPNLVLAIFSAVAVALVAIAITVGGLTAVIALSFVYFCQSIMFPTIFALATKNLGAESKLASSLVIMSIVGGAVMPLVAGGLFASGAVYALIVPLVCFAYIVFFAASGYKITSTDLRTPNTPPELVP
>NZ_CP051677.1|WP_169551206.1|3155427_3155841_+|hypothetical-protein
MALPTPTTPVKIKPGSGGSYGLAFALVTSLFFLWGLANSLNGSLIKQFQIALDLNRFQAGIVDFAFYLGYFFMALPAGYVMRRFGYKRGILLGLILYGGGRFCSTRRPKRGCTASFWSRCLRWPAALPVWKRPLTST
>NZ_CP051677.1|WP_169551205.1|3154386_3155211_+|amidohydrolase-family-protein
MTIDAHQHFWHYDPVRDSWITDDMAVIQRDFLPEDLEPVLVQNGIDGCVAVQADQSLAETQFLVQMAQTYDIVKGVVGWVDLTAPDLRDQLSELAQYPELKGFRHVAQAEPNDFLARPAIVAGIRQLAEFGFTYDILIYPNQLKAALHLVREVPEVSFVVDHIAKPYVKTGEITRWSNFMTQLAAQPNVQCKLSGLVTEADWQNWSKRDFFPYLNVLFDRFGPDRLMFGSDWPVCLVAANYTQVKTLIEEYVDPWGSDVRDKIFGANAVSFYRL
>NZ_CP051677.1|WP_169551213.1|3169772_3171452_+|glycoside-hydrolase-family-43-protein
MKKRIITALCAALLAGMGQVTLAQTTTLVNPIMTGFYPDPSIVKVGSDYYLINSTFSYFPGIPVLHSKDLKNWKQIGNVIERPEQMDFMGERMTRGLFAPAISYHKGTYYVTCTDIDHDGNFVVTATNPAGPWSNPVKLPEVKGIDPSLYFDESTDKAYILYNSDAPDRKPLYPGHRTIRMYEFDAKNLKVLGEEKQLVNGGVDLSKKPVWIEGPHIMKRNNWYYLYAAEGGTSVNHSEVVLRSKDVWGPYVPFEGNPILTQRGLPADRKDPITSAGHAQFVEGPDGKWYSIFLAVRPYEGNYYNTGRETFIAPLTWTNDWPMIEHGEKPIAYSYVGNFKEVKQKDARPQNGNFAYTINFDKTLDPALLFLRTRDDKSFSLGKANGLTMNLKPETISEMGNPSFIGKRQQHLYCTAETALDFTAKSADEKAGLVIFQDEKHFYFLAKSTEQGKPVVQLFKSTNDKNLELLAHTPVSADAKKIMLRIDAKGDAYDFYVADKPNDWKLLKDKVDGKFLSTQVAGGFIGCVFGLYATSSGSNSDNHASFNYLRYSGNDPMYK
>NZ_CP051677.1|WP_169551214.1|3174097_3174607_+|VOC-family-protein
MKTFSLFILTLLLTHFGVAQSNFTSKVIGVGVVVADVDKSVDFYVNGIGMVKTGNFTITEDFGKRSGLSNGVAAAVTILKLENSPEATDWKLMSFGKKASHPKPKYIQDDTGMQYITIQVKALQPIIDRLTKMKVPFLGSTPTLLNDKAHFVFVQDPDGNFIELIGPLN
>NZ_CP051677.1|WP_169551215.1|3174634_3176188_+|glycosyl-hydrolase-43-family-protein
MKYLLICLTGLLVLSGQPSALAQKATNPIIFADVPDLAMIRVGKTYYMSSTTMHLSPGLPIMKSTDLVNWKLVGYAYDTLATVDALNLTNGQSTYGRGSWASSLRLHNGTYYATTFAQTTGRTHVYSTKNIEKGPWKAVSFKPSFHDHSLFFDDDGRVYMVYGAGKLRIVELNADVSGVKPGTERVLIENASEPSGTGRGLPAEGSQLFKVNGKYYLFNITWPQGGMRTVVIHRADQLAGPWEGRIGLQDLGVAQGGLIDTPDGRWFAYLFRDFGGVGRIPYLVPVTWKDGWPVLGVDGKVTQTLDLPASNGLIPGIVASDEFTRKRGEPALPLAWQWNHNPDNSLWSVSERNGFLRLKTGRTDTSFVMARNTLTQRTIGPQCTGSTRLDVSKLTDGDFAGLSLLQKQYGLVGVKQTDGTRAIVMVSAASGKAVEMQRVPLSASVVYLKAECDFRDRKDTGRFFYSLDGKTWEAIGEPIKMPYTIPHFMGYRFGLFNYATRQPGGYADFDYFRVNSQ
>NZ_CP051677.1|WP_169553381.1|3180925_3181729_+|sialate-O-acetylesterase
MAAQAQDPNFHVYLCLGQSNMEGNAKIEAQDTVGVNPRFQVLEAVDCPDLSRTKGNWYTAIPPLCRCRTGLTPADYFGRTLLTYLPPTTRVGVIDVAVGGCRIELFDKDQYQTYVATVPGWMKNFISEYGGNPYARLVEMGKRAQQDGVIKGILLHQGESNPNDSLWTKKVKKVYDNLLADLNLPPNSVPLLAGETVNADQDGICAGMNRIIATLPQAVPTAHVISSAGCTDSSDNLHFNAAGYRKLGKRYAYQMLTLLGYTVKAED
>NZ_CP051677.1|WP_169551216.1|3181754_3182645_+|alpha/beta-hydrolase
MKKNPLFLVWLLASGLSAQAQEIIPLYAGTVPNVKPSSVQETYTSGMFRNVTKPTLEVYLPDKAIATGTAVVVIPGGGYSVVVYQGEGIGTAKALVQKGVAAFVLKYRLPSDSSMTDKTIGPLQDAQQAIKLVREGAAKWGIDPGKIGIMGFSAGGHLASTEATHFEKALIDNPENTRLRPDFQVLVYPVISMGDSLAHRGSRDNLLGKNPSRQTIDLYSNEKQIRANTPPTYLTHAADDKVVDVDNSIVYFETLRRQKIPVEMHIYPKGDHGFIFRQPGWIDPLFDWMKRNNWIK
>NZ_CP051677.1|WP_169551217.1|3182704_3184267_+|carboxylesterase-family-protein
MKKVNPFVAFALSLVSAVAFAQQPAPVRVKGGQVRGTVEEGLTVYRGIPFAAPPVGELRWKAPQPVQTWTGVRDANRFAPAAMQGGNTPSGKSEDCLYLNVWSPARTTTDRIPVLVWIYGGGFSFGATSDPNYSGEKLAQKGVVVVSIAYRVGPLGFLAHPQLSAENPQRVSGNYGLLDMIAGLKWVQQNIAAFGGDPTKVTIFGESAGGIAVSMLCASPQAKGLFRGAISQSGGSFGPTRATTYPGENMKRLDEAEKAGEAYAQKAGASSLADLRKIEADKLPGGWGVGSSWPIVDGYVIPDDQHKLYEAGNYNQTPILVGYNSDEGASFSPPKTPGEYIESTKKRYGPFADDLLKAYPVGANSVPKTARDLMRDAAFGWQTWSWANLQATTSKQKVFYYYFDQHPDYPADSPKAGAGSGHGQEVSYVFGHIDPANPQTTKTDLAISDAMGTYWTNFTKYGDPNGTGVPQWPVFSKTNPAVMYFNQTPHVGPVPSADALNVLNTYFNWRRIPEGEAWAK
>NZ_CP051677.1|WP_169551218.1|3184314_3185454_+|esterase
MDVRYHPPYASRLLFVWYLFCLYTIALAQPPGGPVVVSPQVNADNTVTFRYLAPAAKDVKLNAQFEKAPVPMTKDAQGIWSVTTSPVKPDMYPYSFSVDGISVADPKNSAIFPNEGFQSSVVEITGPTPLVHTLQNVPHGTLSYRFYTSPELGQRPVVIYTPPGYETDTKATYPVLYLLHGTTDLEETWTKVGRANIILDNLIAQGKARPMVIVMPYGRAYPTISKSSGSLRNWDNLQEFKKDFMGNLFPFVEKNYRVKKDKDSRAIAGFSGGGGETLYLGLNNPELFGWVCGFAPGMLKDEFERNNATAFANPAQTNQRLKLFWIGVGKEDGLYPVVNDYLKVLDEKKIRHETLFSEGGHTWMNCKLYLSTIAQKLFM
>NZ_CP051677.1|WP_169551219.1|3185475_3186645_+|esterase
MKQYTQNRVRAMLMVALLCAVGIVRAQPPRGPLVVSPQVNADKSVTFRYLAPSASDVKLGAQFEKAPVPMTKDAQGIWSVTVGPVKPDIYPYSFSVDGITVMDPANVAFFPNERFKASLVDIPGDTPLIHSLKDVPHGSVSYEYYPSVEGTTGSLVVYTPPGYDKNPKAKYPVYYLISGTTDTEETFFKVGHTNLILDNLIAEGKAKPMVIVMPNGNIAARLAEQKGGSKPADPIGRDNPEAVKRANDFGADLTGNIIPYIEKNYRTLANRENRAIGGFSRGGGQTLRTAFSNMDKFAWVCAYSAYLSPTEMERSYSPIVTNVANTNKQLKLLWVSVGSDDFLYKGTVEFMDYLKAKNVNYKSLITDGGHTWMNVKTYVAATTPLLFQP
>NZ_CP051677.1|WP_169551220.1|3186656_3187736_+|esterase
MKRIVYLLQAVLFSGVTAVAQQRPPAISSPDVHPDHSITFRYFSRNAKKVTVNGEFLKAPVALMKDTSGVWSVTVPPVTPDIYPYSFRVDSVELADPSNTYIFANERFKRSIVDVPGDKPLVHSLQNVPHGKVSYRYYKSGTLGTTRQLLVYTPPGFDPNGKTKYPVLYLIHGGSDTEETWTKVGRANLIADNLIAQGKAKPMLIVMPYGNVRPAPMADFTKDMVSDIVPFVEANYPVVKESKGRAVAGFSVGGGQTLNIGLTNPETFAYVCSYAPYTATDEFKKNFTNWSPNADALNKQLKLFTISVGTDDFLYEPVKQNIAMFNEKKVAVKPLIVPGGHTWMNCKLYLANTLPQLFR
>NZ_CP051677.1|WP_169551221.1|3187940_3189059_+|esterase
MNRKNTAAVLVAALLSANSFAQTTSSAPAEDFKPSALNQPGQEYPQVNSQGYARFRINAPKADSVKVSLGLGGRGGTRLTKGADGFWTGTTEGPMDEGFHYYNVTIDGGKFNDPGAQNYYGSVRWESGIEIPAHDQAFYELKAVPHGNVQQILFPSKSTNTSRRAFVYTPPGYEKDKSKKYPVLYLQHGWGEDETAWSNQGHANLIMDNLIAENKTKPFIIVMTYGMTNEVKFGKIREFKIDPFQTVLTDELIPYVDANFRTLANRDNRAMAGLSMGGMETKMITLNKPELFGYYGLLSGGLYNPEDLNGKAKPKLVFVSCGSRERPDGVKKAATDLTAAGYKAVSYVSENTGHEFQTWRRSLHELAPMLFN

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Crispr_ID: NZ_CP051677_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP051677_3

3226591-3226698

Orphan

Consensus_repeat	Method
AATCATAGTCCATCAGCGTAATCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP051677_3

>merge|NZ_CP051677|3|3226591-3226698|CRISPRCasFinder
AATCATAGTCCATCAGCGTAATCACAGTTCAAGATTATCTGAACTATGATTCCTTTGATTAGTTGATTGCCCTGATTCAGAAAAAATCACAGTCCATCAGCGTAATCA

>NZ_CP051677|3|3|3226591-3226698|CRISPRCasFinder
AATCATAGTCCATCAGCGTAATCA	CAGTTCAAGATTATCTGAACTATGATTCCTTTGATTAGTTGATTGCCCTGATTCAGAAAA
AATCACAGTCCATCAGCGTAATCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051677.1\|WP_169551228.1\|3200236_3201289_-\|glycoside-hydrolase-family-43-protein	unknown	unknown	gnl\|CDD\|350131
NZ_CP051677.1\|WP_169551244.1\|3235398_3235890_+\|acyltransferase	unknown	unknown	gnl\|CDD\|100053
NZ_CP051677.1\|WP_169551230.1\|3202155_3204261_-\|alpha-glucuronidase	unknown	unknown	gnl\|CDD\|226187
NZ_CP051677.1\|WP_169551243.1\|3233364_3234321_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169551227.1\|3198979_3200038_-\|endo-1,4-beta-xylanase	unknown	unknown	gnl\|CDD\|366032
NZ_CP051677.1\|WP_169551245.1\|3235873_3237052_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340856
NZ_CP051677.1\|WP_169551242.1\|3232639_3233287_+\|4'-phosphopantetheinyl-transferase-superfamily-protein	unknown	unknown	gnl\|CDD\|225002
NZ_CP051677.1\|WP_169551238.1\|3227447_3228890_-\|MOP-flippase-family-protein	unknown	unknown	gnl\|CDD\|240532
NZ_CP051677.1\|WP_169551233.1\|3208916_3210848_+\|CocE/NonD-family-hydrolase	unknown	unknown	gnl\|CDD\|225487
NZ_CP051677.1\|WP_169551235.1\|3212595_3213405_+\|TolC-family-protein	unknown	unknown	gnl\|CDD\|367035
NZ_CP051677.1\|WP_169551231.1\|3204460_3207343_-\|glycosyl-hydrolase	unknown	unknown	gnl\|CDD\|379757
NZ_CP051677.1\|WP_169551232.1\|3207798_3208824_+\|LacI-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224525
NZ_CP051677.1\|WP_169551236.1\|3215660_3222482_+\|amino-acid-adenylation-domain-containing-protein	unknown	unknown	gnl\|CDD\|225858
NZ_CP051677.1\|WP_169551229.1\|3201351_3202155_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP051677.1\|WP_169551241.1\|3231420_3232368_-\|T9SS-type-B-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|372639
NZ_CP051677.1\|WP_169551240.1\|3229274_3231359_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|367090
NZ_CP051677.1\|WP_169551234.1\|3211167_3212376_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|372656
NZ_CP051677.1\|WP_169551246.1\|3237055_3238546_-\|O-antigen-ligase-domain-containing-protein	unknown	unknown	gnl\|CDD\|377422
NZ_CP051677.1\|WP_169551237.1\|3226727_3227294_-\|pentapeptide-repeat-containing-protein	unknown	unknown	gnl\|CDD\|224276
NZ_CP051677.1\|WP_169551239.1\|3228999_3229203_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP051677.1\|WP_169551228.1\|3200236_3201289_-\|glycoside-hydrolase-family-43-protein	gnl\|CDD\|350131	cd18619, GH43_CoXyl43_like, Glycosyl hydrolase family 43 protein such as metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Included in this subfamily is the metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43, which shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	0
NZ_CP051677.1\|WP_169551230.1\|3202155_3204261_-\|alpha-glucuronidase	gnl\|CDD\|226187	COG3661, AguA, Alpha-glucuronidase [Carbohydrate transport and metabolism].	0
NZ_CP051677.1\|WP_169551244.1\|3235398_3235890_+\|acyltransferase	gnl\|CDD\|100053	cd04647, LbH_MAT_like, Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.	8.18476e-35
NZ_CP051677.1\|WP_169551227.1\|3198979_3200038_-\|endo-1,4-beta-xylanase	gnl\|CDD\|366032	pfam00331, Glyco_hydro_10, Glycosyl hydrolase family 10.	6.21313e-137
NZ_CP051677.1\|WP_169551245.1\|3235873_3237052_-\|glycosyltransferase	gnl\|CDD\|340856	cd04950, GT4_TuaH-like, teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	2.76384e-46
NZ_CP051677.1\|WP_169551238.1\|3227447_3228890_-\|MOP-flippase-family-protein	gnl\|CDD\|240532	cd13127, MATE_tuaB_like, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. This family might function as a translocase for lipopolysaccharides and participate in the biosynthesis of cell wall components such as teichuronic acid. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.	1.08534e-106
NZ_CP051677.1\|WP_169551233.1\|3208916_3210848_+\|CocE/NonD-family-hydrolase	gnl\|CDD\|225487	COG2936, COG2936, Predicted acyl esterases [General function prediction only].	2.67439e-82
NZ_CP051677.1\|WP_169551235.1\|3212595_3213405_+\|TolC-family-protein	gnl\|CDD\|367035	pfam02321, OEP, Outer membrane efflux protein. The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.	8.02929e-08
NZ_CP051677.1\|WP_169551231.1\|3204460_3207343_-\|glycosyl-hydrolase	gnl\|CDD\|379757	pfam15979, Glyco_hydro_115, Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-.	0
NZ_CP051677.1\|WP_169551232.1\|3207798_3208824_+\|LacI-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	3.47879e-105
NZ_CP051677.1\|WP_169551236.1\|3215660_3222482_+\|amino-acid-adenylation-domain-containing-protein	gnl\|CDD\|225858	COG3321, COG3321, Polyketide synthase modules and related proteins [Secondary metabolites biosynthesis, transport, and catabolism].	0
NZ_CP051677.1\|WP_169551229.1\|3201351_3202155_-\|SDR-family-oxidoreductase	gnl\|CDD\|212491	cd05233, SDR_c, classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	9.95626e-78
NZ_CP051677.1\|WP_169551241.1\|3231420_3232368_-\|T9SS-type-B-sorting-domain-containing-protein	gnl\|CDD\|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	8.98504e-18
NZ_CP051677.1\|WP_169551240.1\|3229274_3231359_-\|hypothetical-protein	gnl\|CDD\|367090	pfam02449, Glyco_hydro_42, Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.	0.00373262
NZ_CP051677.1\|WP_169551234.1\|3211167_3212376_+\|glycosyltransferase	gnl\|CDD\|372656	pfam13641, Glyco_tranf_2_3, Glycosyltransferase like family 2. Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.	5.47772e-25
NZ_CP051677.1\|WP_169551246.1\|3237055_3238546_-\|O-antigen-ligase-domain-containing-protein	gnl\|CDD\|377422	pfam04932, Wzy_C, O-Antigen ligase. This group of bacterial proteins is involved in the synthesis of O-antigen, a lipopolysaccharide found in the outer membrane in gram-negative bacteria. This family includes O-antigen ligases such as E. coli RfaL.	8.29087e-06
NZ_CP051677.1\|WP_169551237.1\|3226727_3227294_-\|pentapeptide-repeat-containing-protein	gnl\|CDD\|224276	COG1357, COG1357, Pentapeptide repeats containing protein [Function unknown].	4.04321e-07
NZ_CP051677.1\|WP_169551242.1\|3232639_3233287_+\|4'-phosphopantetheinyl-transferase-superfamily-protein	gnl\|CDD\|225002	COG2091, Sfp, Phosphopantetheinyl transferase [Coenzyme metabolism].	1.20999e-31

>NZ_CP051677.1|WP_169551236.1|3215660_3222482_+|amino-acid-adenylation-domain-containing-protein
MSDHVFAVAQQALPDSFTIHRLVADAMVRTAPDTTAVRIGGELLTYRQLDEQSDILSQAILRVASDSQLVGISCTRSLDMVVGVLAILKAGKAYLPLDPTYPDARLRQLINDSGVQHCLSTTADEPLFTELGLHVIRPDATQDGPSQAVTTQNETACVLYTSGSTGKPKGVCLTHMGLVNMLTNQVGRWAGQPGLQTLQFCHLSFDASFQEIFVPLLTGGTIHLVDDSYRLNAGRLLDYIEQERINRVFLPYVVLQYLTETAVASHRFPADLREIITGGELLKITPAIAQFFDALPGCALMNVYGPTEASVWVTENRLQGDALNWPQLPSIGRVVPGCGVIILNEQLEPVEEGEIGEIGIAGVCLANGYLNQPDRTADAFIDWQHPQYGPTRLYRTGDLARFMPDGTLDFHGRRDTQVKIRGNRVELGEIEVLLAQQPAVQQAVVVAREDIPGHKRLVAYVVVPATNFSVPLLRTALTERLPDFMLPTYYVRLDDLPRTTSGKVDKAQLPPPDHSRPDLTTLLRPARTALEKEIVGMWGEWLQLNPVGLDDNFFELGGNSLLAQQTIAALEQRGFTVPITKLYQYPTAGALAEFIQPTTSIRPGQPQPELTAPRRATADDTDVAVIGMSGRFPGASTIDELWSLLKEGRETTRFFTDAELDAAIPASVRENPQYVKARGVIDGADQFDARFFGLTPAIAQVMDPQQRIFLEIAYEALETTGYLPELYGGRVGVFAGCGNNTYYLNNVLANPDVVAQVGSFQAMTVNEKDYIASRTAYQLNLNGPAVSVYSACSTSLLAITQAVQSLRSGQCEVALAGGASITAPVSSGHLYQEGAMFSSDGHTRSFNADSTGTVFSDGAGVVLLKRLTDARRDGDTVYAVIKGIGVNNDGGNKGSFTAPNADGQAGSIRMALADAQVDPATISYVEAHGTATPVGDPIEIEGLTAAFGPQDRNQYCAIGSIKSNMGHLTQAAGVAGLIKAVLSLHYRQLPPSINYERPNPVIDFANSPFYVNATLRDWDQEQESTARRANSRRANPRRANPRRAGVSSFGVGGTNVHVVLEEFAETVTEPISDKPARPVQLLMWSAKSVASRHAFAQQLVARLQQPNAPALADVAFTLPLTRPGYVHRQFAVAASADELTQTLTSNPGINAQTLGRAPGDVVFLFPGQGAQFLNMGRALYEYEPTFRQAIDDCAEHLRPHLDVDIRKVLYPDTINLEVEQQLRNTRYTQAALFVTEYALARLWMSWGIEPSILCGHSVGEFVAAHLAGVFTLPDALRLVAARGRLVSEQPRGSMLSVRLGIDQLQPLLPDTLSVAAVNSRHLCVVAGQDEDIADFARLLDEREIPNRPLATSHAFHSAMMDPIVTQFAEIVKTVPLSRPQKPIVSTVTGTFMTDAQATDPAYWATHLRATVRFADALDTILTLDKPLLLEVGPGRSMATLARQHATGQAQPGSVLAGLATQADDKATYEALLTTLGQLYLHGLPIDWRAFYAGQNRRRVALPTYAFDRRRCWIDAPVSNPVLTELLPSYTTNQQASNSSTPPMRTPSLLNKIYQLLEDASGIEMADVAPETSFLELGFDSLLLTQMAITLRNEFGTPITFRQLTTDLTSPNDLAAFLDQQLPADQYAPAPVAVPAPVAAPVSQPAPMAEPVMPAMAPMPMAAAPALMPVGMVGGDSALGLIAQQLQLLARQVALMQGVPAQPAPVAPPVAVPPAPTPQPVAVQQPIAPPAPPIKPATLSVPTTGELTPEEAIEHKKPFGATAKIERQTQELTQPQQQFLAQLTQRYNSKTAGSKAYAQQHRAQMADPRVVSGFRPLTKEIVYPIVVNRSAGSRLWDVDGNEYIDVLNGFGSNMFGYQPDFIKKALHEQIEKGFEVGPQHELAGEVSQLVCELTGSERVALCNTGSEAVLGAMRVARTITGRSLIVAFAGSYHGIVDEVLVRGSKKLKTFPAASGIMANVVQNMLILDYGTDESLRIIRERADELAAVLVEPIQSRRPEFVPIDFLNELRSITTASGSALIFDEVITGFRMHLGGAQALLGIRADMATYGKVAGAGMSIGIIAGKRSFMDALDGGHWQYGDASAPEVGVTYFAGTFVRHPLALAAAKASMLHLREQGVGLQQALTRKTTYLADTLNTYLTERQLPMFIAHFGSLWKLKFTEDVPYAELLFTLMREKGIHIWDGFPCFMTEAHTDEELSTVIDAFCRSIDTMIDATFFPGKSVSTTPPVSAGSTLYQLEPPVAGARLGRDRAGNPAWFLPDPERPGAYLQVDLMA
>NZ_CP051677.1|WP_169551235.1|3212595_3213405_+|TolC-family-protein
MKSVLGRVSIGVLVGLLISQVSMGQAQQKSVRGLVSFGQATGVTGDTSFLDVDKDIAIQLLPFEELTKIATAYSPLLKYQGEIANSLDAGYQISKLQILQNMSAYGNYSAGNQAIVSSGVNIPSGVDPVSQIANGYRFGVDMRVTLYDLFGRKQQMKQAYSNYRASVLQKDIIAQEIRRSLIGIYQDMITAQQVLKTRLLDEQASLTAYRIAEAETQKGRGNAETLANALNRYAQAKSYSEQVKGEFLKNVRYFETLVGQPLQRLKRIN
>NZ_CP051677.1|WP_169551234.1|3211167_3212376_+|glycosyltransferase
MFVLESVYAIVLLYLGLSVLFLAVFAVAGRFGGTDDVSPAITPATYRKIGVLIPAYKEDAVIIESVRTNLRQKYPTDRFELIVIADSIHPSVLAQLAELPIRVIPVSFETSTVSKAINAALAQIPAGQYDVLMVADADNHMATDFLSRINLAFEQGWQAVQGHRVAKNTNTSVAVLDAISEEINNHLFRQGSRALGLASSIIGSGMAFEPELMRAGMASLHTMGGYDKELEMNIVLAGRPIAYLADAYIYDEKVASKAVFENQRTRWIAAQWQFLAHYFRPGLRELSASRMMSGFKMIQAMVLPRVLLLGVLTLLSALSLLATQPFFQLAAPALLLTLCLSLAISVPNYLWKRLTVRELLVLPVLMLRFARAMLNMRKAFRRFMHTPHTGTPDVQLQPNKSA
>NZ_CP051677.1|WP_169551233.1|3208916_3210848_+|CocE/NonD-family-hydrolase
MKKWLLSLSICVAVLPALAQTTPPRPNNTFVRDNFQKQEYDIPMRDGTKLHTNVYIPKDASAANKYPFLMQRTCYSVAPYGPDTYPNGLGPSGTLMRDKYIFVYQDVRGRWDSEGTWTNMTPTVTDQPSAADQKKRGKAPARQSAMAVDESSDTYDTIDWLLKNVPNNNGRVGQWGISYPGFYTIAGAVAAHPALKASSPQAPVSDFFFDDFHHNGAFIQAYMFTFPVFGIQHPGPTTKAWYEDQIINTGSKDGYQWQYDLGPLKNADKYYKDNFYWQETVNHPNYDEFWQKRSIIPHLKNIKHAVMTVGGWFDAEDLYGPLTIYKTVEKNNPGTYNTLVMGPFGHGRWSRETGHTMHSNVYFGDSIATFYQRNIEAKFFDHFLKGSGDGKSGLPEAYLFNTGRNEWKTFDKWPAPTAQPMQLGLRNSGKLDMGSKGSASAFSEFVSDPAKPVPYTEDNTTTLGFTPFNYMSEDQRFASRRPDVLTFQTDVLTDDVTLAGELMAKLNVSTTGTDADWVVKLIDVYPPNEPNHPYMPNKNITLGNYQQMVRSEVMRGRFRNSFEKPEPFVANQPTPVNVRLQDVLHTFKKGHRIMVQVQSTWFPLIDRNPQKYVDNIYKAEAADFQKATHRVYDDSVIEVSVLK
>NZ_CP051677.1|WP_169551232.1|3207798_3208824_+|LacI-family-DNA-binding-transcriptional-regulator
MTKEVTIYDIAKRLNYSPATVSRALNDHPAIRGETKELINATAQQMGYRSNTFASNLRRQKTSTLGIIVPRLNSNFMSRVLAGMEKAANDASYNLIITQSLESEIKEVANAKTLFDSRVDGLLVSVAYNTESNEHFETFIRRGVPVLFFDRVIQHPKCVSVSIDNEMAGYEATRHLLEQGCRRIAHITGIMRRNVYGDRLAGYRRALNEQALSVDDSLVVESDLSFEAGYQAGQAILAMPNRPDGIFVANDFCAAGCMLALKQAGISIPGDMAIVGFNDDPVAQVISPRLTTVHYAGEKMGEIAARSLINFLNGLQDIQATNRIVLRSELVVRESSVRRGK
>NZ_CP051677.1|WP_169551231.1|3204460_3207343_-|glycosyl-hydrolase
MKRLLFTLLILNLWIQSFAVTPGQYVATQAGKGRFPLTLKGQVAAMLTGPDEYAGVRRAMKSLEADIIRVTGAKPAPSPDSKDPKELILVGTLGKSPLIDKLVSDKKIDLSGLVGKWETYVTQVVDNPMPGVDPALVIAGSDKRGTIYGLYDLSAQIGVSPWHWWADVPVQTQKALYVLPGRHTAGTPAVKYRGIFINDEAPALSGWTKAKFGGFNHQFYEHVFELILRLKGNYLWPAMWGNAFYDDDPQNPKLADEYGVVIGTSHHEPLMRAHDEWRRYGKGPWNYQTNDSTLRAFWRKSVERMGTNESILSVGMRGDGDEPMSRETATALLEKIVADQRTIISDVTGKPAAETPQSWALYKEVQDYYDKGMRVPDDVTLLLCDDNWGNLRKLPTVGTPKRKGGYGIYYHYDYVGGPRNYKWLNTNTIARTREQMHLAYEHGVDQIWIVNVGDIKPMEFPIEFFLDYAWNPNAWPADKLTDYTRLWAQQQFGPKHAEAIARILTTYTQYNARRKPELLSPDTYSLTHYREAERVVADYNQLLSEAERIGKDLPTSYQDAYFQLVLHPVKASATLNELYVTAGRNRLYVKQGRSAANSLADRVKKLFERDAQITRFYNDTLAGGKWTHMMDQTHIGYTYWQQPNQNAMPKTETISVPTPADMGLTVEGSDDWFPGSAGSSLTLPTFDKYNQQTYYIDLFNRGQTPFTFQASAGAPWLTLSTTGGTVGQETRLLVGVNWKQAPAGTQQVPITLTGPNGQRVVVQAVVNNPASPLLDPAVGFVESNGYVSIDAEHPTHTTQTATATWQRLPDIGRTAGGMTSSPVTTPAIEQPGGQSPRLTYQVILADSGMVQVQTYVSPTLNFNDNKGLRFAISFDDETPQIVNMHANETGRVWEQSVANNIRILTTKHRLTKPGEHTLKYWLVDPAVVVQKFVIDRGGVKPSYLGPPESFRRDAPTMSHK
>NZ_CP051677.1|WP_169551230.1|3202155_3204261_-|alpha-glucuronidase
MNRLLLIGLLLLTHLTFADDGYRLWLKYDRLTDATVRSGYARSAQFIAVSGSSPVLKSATNELQLGLQGLLGTTVPTLPSAGTRQGGIVLTVGVSGADANELNEEGYRIVKRQGNILVMGKTDVGVLYGTFALLRQLQTGQSVDAINLVSSPKVKLRMLNHWDNPNGTIERGYAGGSLWKWSELPETIDPRYKDYARANASLGINGTVVNNVNASARMLTGEYLQKVAALAGVMRPYGIKVYLSVYFAAPKTLGGLKTSDPLDPEVRKWWTDKTAEIHRYIPDFGGFLVKANSEGEPGPQDYGRTHVDGANMLAAAMKPFPGVVIWRAFVYKADPTGDRFKAAYEEFTPFDGQFDPKVIVQVKNGPIDFQPREPFSPLFGAMPKTPLGIEFQLTQEYLGFATHLVYEAPVFKECLESDTYAAGKGSTVARVIDGSLHGYSQTLMAGVANTGSDRNWTGNPLAQANWYAFGRIAWDHTLTSAAIADEWVNMTLTRQPQAVSHVRAMLLRSRDIYVDYNAPIGLSRPWTGVHFAPEPWQNKSPRPDWTAVYYHRADSVGLGFDRTATGSNALAQYRPEVRRQWENVDNCPLPYLLWFHHVPWTKQLSTGRTLWDELCTRFYTSADSVRWLQQEWTLAKPALDPVLYTDVAGRLATQHREAIWWRDAWVLYLQEFAKKPVPKPFKQPEQTLDDVKKSVDIYLLR
>NZ_CP051677.1|WP_169551229.1|3201351_3202155_-|SDR-family-oxidoreductase
MTTNEQAADTALLTSAPAVFSLEGKRALITGGGSGIGFDIARCMTLAGADVIVTGRREQPLIDAVETLGPKANYMVNDVTVRAELDQLVDTIERQHGPIDILVNNAGINMKKPALDVTDDEFDRVVHTNLNAVFSLTRACATRMVERNSGVVIMISSMAAYYGIDRVAAYGASKSAVEGMVKILASEWSGKGVRVNAIAPGFIETAMSKTAMGGDPDRFARAMRRTPMGTFGQPSDIGWAAVFLASEAARYITGASLPVDGGNSIGF
>NZ_CP051677.1|WP_169551228.1|3200236_3201289_-|glycoside-hydrolase-family-43-protein
MKRIRISLALAALSCLSLSTFAQTETGKTPISQPLVSHIYTADPSAHVFNGKIYIYPSHDIDAKDVKEDDDGGHFAMRDYHILSMDKIGGPVKDNGVALDIKDIPWAGRQLWAPDAAYKNGTYYLYFPVKDKQDVFHLGVATSKSPVGPFKAEPQPMKGTYSIDPCVFQDTDGKSYLYFGGIWGGQLQRWDNNQYDAKGALKKPEEVAYLPRVARLAADMKELAEPVKAVQLLDENGKPFLEKDNDKRFFEAAWLHKYKGKYYFSYSTGDTHNLCYAMGDSPYGPFTYKGVLLKPVLGWTNHHSIIEKDGKWYLFYHDIQLSGKTHLRNVKVTEMTYNPDGTIKTIDAYK
>NZ_CP051677.1|WP_169551227.1|3198979_3200038_-|endo-1,4-beta-xylanase
MRFRSLLLLPLLSAMTAPEKGLKDYYKDYFPIGVAVNPRMVQPGPDAELIKAQFNSMTPENAMKIGPIHPEENRYNWKDADAIADFARQNNIKLRGHTLCWHNQTPAWLFVDSTGKTVSRDVLLARMKRHITDVMTRYKGTVYAWDVVNEAVPDTSTAIYRKTRFLEIIGEDYIEKMFQYAHEADPNAQLFYNDYNTETPSKRDRIFQLLKKLKAKGVPIDGVGLQAHWSIYEPTRSELEESITKFASLGLKVQFTEVDVSVYPKEHERRERRPTDKSEFTPAMNDQQAAQYKMLFEVFRKHRNTITGVTFWNLTDRYSWLDNFPVPGRKDYPLLFDQAGKPKKAYESVVRF
>NZ_CP051677.1|WP_169551237.1|3226727_3227294_-|pentapeptide-repeat-containing-protein
MEHYKQLYTTSDDLPSQWAGHTFEQCTFQKLSPTPTMLAGANFINCRFEQCMLIRCAVKQTQFNDVAFVGCAVQGVDFGTCNPFGFHADFQACQLDQSIFLNRRLVKAKFVECSIKSVLFIRCDMTGALFDRCDLELTKFDDNTLNQVDFSTSFNITLDPDVNRLKKAKFSLYSLPGLLDKHNLIVKS
>NZ_CP051677.1|WP_169551238.1|3227447_3228890_-|MOP-flippase-family-protein
MSNKDKAMNGGKWITIATVISTVFQFGQVAVLARLLVPADFGIVSISNLVIGFFTIFSSLGFSNSIIYKQESDRRVLSTLYYLNLIVGVIIFVAVYLSTPLIVSFYKEPKLAEVVHLSSYYFLIVYFGQLYLFLLQKELKFRAVAIIDILGTVIGSIATVTLAYNGYHELSLIIGSLINQTIKTVFQVIFGLPYFSPTLAFDMRNIGEHLRFGLFNLGDGLLGFIQSNADNIFIGGMLGVKLLGYYTIAYQLSIFPITKLNPIILQVAYPILAKMKESTVELKKSYLKILDFVSYCNMPLLAGLFITAESVVPLFYGPGWDKTIELIRIFVFVGWFTCLSHPLFTLAFTKGKPNLLFYLNVVTLIVKLPLVYFLGTYFGVMGIATAFLLATLFNLIANFGVVHYLIGDFFGAFLRNIAWPTVFCLVMVLVVYAYKQFVGYEGILNTIVQVGLGGLTYGLLTLNYKLSFAELKTYRQSLLS
>NZ_CP051677.1|WP_169551239.1|3228999_3229203_-|hypothetical-protein
MLTNDSQDPVQINVIGTTGQLYRSVRFSKPEPSLSARISLTGMAYGVCLLDIRQGKSRVVRKIIHVQ
>NZ_CP051677.1|WP_169551240.1|3229274_3231359_-|hypothetical-protein
MKKLFVTAVVALGALLLFTYWPQVLMASGSARPQLADAGKIPVTGPRWYQLNNVSNGLNGLFDGKTDEEVNTGYNKLLKNYDAYYPLRPGEQMTIDRIRMYDGSGTNVDAPLTISIITDSWERIPIARFIGDKYNAWVGPDPSQPDVLDLKTPISNARFLVINTSGAYPTELEFYGTYQPGPEPTLPSVRHTLLSQQLGVNAFEWNIESADAPWQVDETRIPLLKGFSAIRHYMDWEKLESTPGQYTFNPTFSGNWNYDAIYERMQSEGIEVLACLKTLPKWLENTYPEGQRDYENVPAIYGRDLTQPASYVEQAKVAFQYAARYGSNKSVDPGLVSVSPVKTWAGVNTVKIGLGLIRYIECDNERDKTWKGRKAYQTAREYAANLSAFYDGHKNTLGPGVGVKNADPAMIVAIGGLAASTTDYVRGMIDWCREFRGYKPDGSIDLCWDIINQHLYANDAGTSQDGGGTRGAAPELSGVGAQAAAFVKLSHELANDRPVWITEAGYDTNPGSPLRAIGVGGKTVQETQADWILRTALLYNRVGIDRLFFYQLYDEDPANPTQFSSMGLLSDDKTRKPAAEYLRQANALLGAYRFADTVAVTNGPARLIVDRYEPGPAVTSNGERRSAYVLLIGDEQGRSGTYALPVPRGDTVQLCVPTPGRSTMVRTRLVSQNGSVLIPVSETPIFVMPSAGPR
>NZ_CP051677.1|WP_169551241.1|3231420_3232368_-|T9SS-type-B-sorting-domain-containing-protein
MTRPLLLAWLVISGATLASQAQSCMGGPPELTVDETFGQVGSPSSLSNRTRYQFTTLTCPLDGQYALADHVDGTCYDNLWHAVPQDHTPGDSRGLMMIVNGSQGAGEVYTQPATGLCSQTTYEFSLWGINLLRPGICTNPLLPNLTLRVEAADGTVLQSIDFGSIPQSRTPSWQRFSTLFTTPNSTQGVVIKLINNQGDDGCGNDMAIDDVQVRQCTSCPPSPVFVPDAFTPNNDGTNDVLRVFTTNVASFTMTVFDRWGSPLFYTNTTDRFWDGMHSGQPCEPGSYSWLLSYQQVGADPNNTPIVQRGQVMLTR
>NZ_CP051677.1|WP_169551242.1|3232639_3233287_+|4'-phosphopantetheinyl-transferase-superfamily-protein
MAEPLGTLLAELSATDHSRANRYRQPADRLRFLYGRVLVGWVGAGLTGYTAQTVPLVIGPYGKPDLAAHTGWHINLTHAGDWVLLAVDRHPVGIDVENRRPDLPIATLLPTVCSPDEQARVWADTDPATAFLRSWTRKEALLKGIGHGLVDDLRVIPSLDGQSSLPPGLSDSDWQVQSFAVDSAHPAALAHQPTDISPVFYRLTASDLLTNLKWA
>NZ_CP051677.1|WP_169551243.1|3233364_3234321_+|hypothetical-protein
MQRLVLKFLYVVATLNYPRIRKDLRYFVRDNYYCRLNQLRYYRADYGRKQPYKVIDYHGEFDQELRYVLPFAYWHHCNGTLKQTISCTNTKPFYFFSPDHLETHEKRVWQAGYDYYDVPNMTHSPTFDFSKWKRVPLKAHYRNKLFRYDKPLLVIANKYNIEWDGPPRNFLDIPTLDHIISRCKTTHQIIYNRPLSSQIVLDNSEIMDLGEHAWLRENHPEVLLMNDLHEQHREQVSSFNHLQLMVYANCDRFISMHGGTAALASYFEGTNIILSRPGGGMEHHFDEYNTIFPALSGATIHHARTPEEVIQLVEQQYN
>NZ_CP051677.1|WP_169551244.1|3235398_3235890_+|acyltransferase
MDVVPFNVFQMGAGSTIEDFSVVNNGVGNVLIGNHCHLGLGSVVIGPVTLGNNIIIAQHVVMSGLNHVYDDVEMPIRHQPTVTKPIVLEDDCWIGANVTIVAGVTVGRHSVVAGGSVVTRDVQPFTVVGGNPARVLRRYDETTRQWVAASADKPAAPVAIPAQ
>NZ_CP051677.1|WP_169551245.1|3235873_3237052_-|glycosyltransferase
MTNFDSIICVGQTPWEGDFQKAIVQLMGELAVRHRVLYVDYQYTLKDLAMGLLNKQSVPVRSLTSRTNALITKKLATGAEVWVWQPPVMLPVNWLQPAMHDRLIQTNVDMLVRGLRSVMNQLGMRQPLVINGMNPVFGLPMLGKLNERGTIYYCFDEITVSNWMGRHGGRYEIDYLRRVNAVVTTSDALNNTKSQLQPKAFCVKNGVNFELFHQARLLADEQPPSRPVVGYLGTADNRVNIDLIEHSVRTMPDVVFRFVGEVPEEKLTQRLSVYPNVEFVPPHQPHQLPALLAQMTATIIPYVCNAHTKTIYPLKINEYLAAGLPVVSTSFANLNDFTGIIELADTPEAFADALRRALNDTNLTTRNQRVATARANSWARRAEEFEAVIAQV
>NZ_CP051677.1|WP_169551246.1|3237055_3238546_-|O-antigen-ligase-domain-containing-protein
MAEQLAHLADQLRDSRWFYGVLSVFVALLTGWLIGTFGVMGGAVMVALPLALAVFAGILIEPKFGLLIYVTLSFLIGFTRFIPGDTPLGLALDAVLVLTLMATFLNGKQMNWKRLRTPIFYLMAIWLFYSILEYFNPEVPNPVAWFYKVRSIAFSWFLLVILTLVMPITRRDILWFLRMWIGWSLLAAFWAFKQHYIGLANAEVQWLAAGAAKTHMLWGQLRCFSFYSDAAQFGAEMAGATLITIVLLTSTHSALHRLIYVGLLLIFFWAYALSGTRSALFVLLGGILAFIALRRSIKTIMWGVGIMAPIMVILLFTHIGDSNYQIWRMRTALHPKEDASFMVRIENQQRLKAYMKDLPFGAGLGTSGSWGARFAPDHPAAQIPPDSWYVELWIETGLVGTVLYILMLIAIMTIGTYQIWQLNDPWLRTTMIIFLAEFFGICVMSYSNATLGQFPTSTLLGITSVLFTTCYRWDLGAPTTNRFQPAPGSTTAWPTH

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Crispr_ID: NZ_CP051677_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP051677_4

3831576-3831812

Orphan

Consensus_repeat	Method
GGGGCGCTAGTAGTCCAGTGCTGACCAACTGCTCGTTTCTGGACAATTCATCTACA	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP051677_4

>merge|NZ_CP051677|4|3831576-3831812|PILER-CR
GGCGCTAGTAGTCCAGTGCTGATCAACTGCTCGTTTCAGGGCAATTCGTCTCTCAATGGGGCCGGAGCCATGGACAACGATGGGTCTCGTGGGGGCACTAGTAGTCCGGTGCTGACCAACTGCTCGTTTCTGGACAATTCAACTACAAATGGGGGTGGGGCCATAACCAATGATGGGTCCAGGGGCGCTAGTAGTCCAGTGCTGACCAACTGCTCGTTTCTGAATAACTCATCTAGA

>NZ_CP051677|4|1|3831576-3831812|PILER-CR
GGCGCTAGTAGTCCAGTGCTGATCAACTGCTCGTTTCAGGGCAATTCGTCTCTCAA	TGGGGCCGGAGCCATGGACAACGATGGGTCTCGTGGGGGC
ACTAGTAGTCCGGTGCTGACCAACTGCTCGTTTCTGGACAATTCAACTACAAATGG	GGGTGGGGCCATAACCAATGATGGGTCCAGGGGC
GCTAGTAGTCCAGTGCTGACCAACTGCTCGTTTCTGAATAACTCATCTAGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051677.1\|WP_169551707.1\|3818437_3818596_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169551714.1\|3836664_3837684_+\|formylglycine-generating-enzyme-family-protein	unknown	unknown	gnl\|CDD\|335469
NZ_CP051677.1\|WP_169551717.1\|3841469_3842576_+\|DUF4974-domain-containing-protein	unknown	unknown	gnl\|CDD\|226235
NZ_CP051677.1\|WP_169551713.1\|3835005_3836538_+\|sulfatase	unknown	unknown	gnl\|CDD\|293755
NZ_CP051677.1\|WP_169551703.1\|3814529_3814838_+\|cysteine-rich-CWC-family-protein	unknown	unknown	gnl\|CDD\|379586
NZ_CP051677.1\|WP_169551706.1\|3817256_3818438_-\|type-IV-secretory-system-conjugative-DNA-transfer-family-protein	unknown	unknown	gnl\|CDD\|238546
NZ_CP051677.1\|WP_169551711.1\|3825017_3826067_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169551704.1\|3814834_3815797_-\|rhodanese-related-sulfurtransferase	unknown	unknown	gnl\|CDD\|234663
NZ_CP051677.1\|WP_169551705.1\|3815853_3816495_+\|deoxynucleoside-kinase	unknown	unknown	gnl\|CDD\|224345
NZ_CP051677.1\|WP_169551710.1\|3823715_3824885_-\|PQQ-binding-like-beta-propeller-repeat-protein	unknown	unknown	gnl\|CDD\|274511
NZ_CP051677.1\|WP_169551715.1\|3837765_3840402_+\|glycosyl-hydrolase	unknown	unknown	gnl\|CDD\|225789
NZ_CP051677.1\|WP_169551709.1\|3822324_3823500_-\|DUF4249-domain-containing-protein	unknown	unknown	gnl\|CDD\|379442
NZ_CP051677.1\|WP_169551718.1\|3842669_3845978_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP051677.1\|WP_169553405.1\|3848060_3848732_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|130454
NZ_CP051677.1\|WP_169551720.1\|3848744_3850106_+\|HAMP-domain-containing-protein	unknown	unknown	gnl\|CDD\|273593
NZ_CP051677.1\|WP_169551719.1\|3845994_3847722_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_CP051677.1\|WP_169551708.1\|3818773_3822307_-\|TonB-dependent-receptor-plug-domain-containing-protein	unknown	unknown	gnl\|CDD\|372685
NZ_CP051677.1\|WP_169551702.1\|3813714_3814500_-\|5'/3'-nucleotidase-SurE	unknown	unknown	gnl\|CDD\|234732
NZ_CP051677.1\|WP_169551716.1\|3840839_3841421_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274357
NZ_CP051677.1\|WP_169551721.1\|3850777_3851611_+\|sterol-desaturase-family-protein	unknown	unknown	gnl\|CDD\|225546

Protein	Function_ID	Function_description	E-value
NZ_CP051677.1\|WP_169551714.1\|3836664_3837684_+\|formylglycine-generating-enzyme-family-protein	gnl\|CDD\|335469	pfam03781, FGE-sulfatase, Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.	2.14645e-82
NZ_CP051677.1\|WP_169551717.1\|3841469_3842576_+\|DUF4974-domain-containing-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	7.83563e-19
NZ_CP051677.1\|WP_169551713.1\|3835005_3836538_+\|sulfatase	gnl\|CDD\|293755	cd16031, G6S_like, unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS). N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.	0
NZ_CP051677.1\|WP_169551703.1\|3814529_3814838_+\|cysteine-rich-CWC-family-protein	gnl\|CDD\|379586	pfam14375, Cys_rich_CWC, Cysteine-rich CWC. This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 74 and 102 amino acids in length. It contains eight conserved cysteines, including a conserved CWC sequence motif.	1.08961e-06
NZ_CP051677.1\|WP_169551706.1\|3817256_3818438_-\|type-IV-secretory-system-conjugative-DNA-transfer-family-protein	gnl\|CDD\|238546	cd01126, TraG_VirD4, The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion. These proteins aid the transfer of DNA from the plasmid into the host bacterial chromosome. They contain an ATP binding domain. VirD4 is involved in DNA transfer to plant cells and is required for virulence.	1.21235e-64
NZ_CP051677.1\|WP_169551716.1\|3840839_3841421_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274357	TIGR02937, RNA_polymerase_sigma_factor, RNA polymerase sigma factor, sigma-70 family. This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.	2.86081e-24
NZ_CP051677.1\|WP_169551704.1\|3814834_3815797_-\|rhodanese-related-sulfurtransferase	gnl\|CDD\|234663	PRK00142, PRK00142, rhodanese-related sulfurtransferase.	2.85939e-158
NZ_CP051677.1\|WP_169551705.1\|3815853_3816495_+\|deoxynucleoside-kinase	gnl\|CDD\|224345	COG1428, COG1428, Deoxynucleoside kinases [Nucleotide transport and metabolism].	4.46655e-67
NZ_CP051677.1\|WP_169551710.1\|3823715_3824885_-\|PQQ-binding-like-beta-propeller-repeat-protein	gnl\|CDD\|274511	TIGR03300, assembly_YfgL, outer membrane assembly lipoprotein YfgL. Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking].	4.57027e-43
NZ_CP051677.1\|WP_169551715.1\|3837765_3840402_+\|glycosyl-hydrolase	gnl\|CDD\|225789	COG3250, LacZ, Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].	5.46343e-36
NZ_CP051677.1\|WP_169551709.1\|3822324_3823500_-\|DUF4249-domain-containing-protein	gnl\|CDD\|379442	pfam14054, DUF4249, Domain of unknown function (DUF4249). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 279 and 365 amino acids in length. There are two completely conserved residues (C and G) that may be functionally important.	5.15152e-34
NZ_CP051677.1\|WP_169551718.1\|3842669_3845978_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_CP051677.1\|WP_169553405.1\|3848060_3848732_+\|response-regulator-transcription-factor	gnl\|CDD\|130454	TIGR01387, Transcriptional_regulatory_protein_PcoR, heavy metal response regulator. Members of this family contain a response regulator receiver domain (pfam00072) and an associated transcriptional regulatory region (pfam00486). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc. Most members encoded by genes adjacent to genes for encoding a member of the heavy metal sensor histidine kinase family (TIGRFAMs:TIGR01386), its partner in the two-component response regulator system. [Regulatory functions, DNA interactions].	4.73243e-85
NZ_CP051677.1\|WP_169551720.1\|3848744_3850106_+\|HAMP-domain-containing-protein	gnl\|CDD\|273593	TIGR01386, Probable_sensor_protein_PcoS, heavy metal sensor kinase. Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.	7.43387e-45
NZ_CP051677.1\|WP_169551719.1\|3845994_3847722_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	1.0549e-24
NZ_CP051677.1\|WP_169551708.1\|3818773_3822307_-\|TonB-dependent-receptor-plug-domain-containing-protein	gnl\|CDD\|372685	pfam13715, CarbopepD_reg_2, CarboxypepD_reg-like domain. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.	6.59555e-17
NZ_CP051677.1\|WP_169551702.1\|3813714_3814500_-\|5'/3'-nucleotidase-SurE	gnl\|CDD\|234732	PRK00346, surE, 5'(3')-nucleotidase/polyphosphatase; Provisional.	1.01401e-124
NZ_CP051677.1\|WP_169551721.1\|3850777_3851611_+\|sterol-desaturase-family-protein	gnl\|CDD\|225546	COG3000, ERG3, Sterol desaturase [Lipid metabolism].	2.04303e-31

>NZ_CP051677.1|WP_169551711.1|3825017_3826067_-|hypothetical-protein
MNKIYGILLLICCGLLPAHAQPTRLEDLCQVFHLPSGKDTTTFIVFGTKDDLKVKKPLFLFRQGSPPTPFIIRDSSRYFLAGPFRFRDYKSEYHFAIIQKPGVRLVADQSYLDAYQKAIEQPDTPEEFISKKYLANNYRERYVEQCDQVINYLVKQPWVDARKVVYCGGSEGFTVGADLVANVNRHVTHTVLFSSNPNRRFEVIVQQIRAQIDRGEKSFDEGQEQIEKVYQVWADICANPTSIDKQFGDTYRAWYSFSQPVLPNLLAIRTPLYIAYGSADREVASGLDVVPLEFIARGKTNLTLKPYFDHDHMFFKLKRDTAGKIIGSEYNGDAVAKDWMNWLRTTPAH
>NZ_CP051677.1|WP_169551710.1|3823715_3824885_-|PQQ-binding-like-beta-propeller-repeat-protein
MSLPQLYLCTVLLLGLASCRTASELSVVPPPPDRPTPPVTTPTEVTLTNPTLYVGSFDSNLYAIDTTGKTSWTFRADTAIQSSPVVAYGRVYVGSNRNHIYAVDAQNGALQWQYQTGGAVVSSPTVAAGRLFAGCLDGKLYALDATTGNQLWTYQSTHGIYASPALSTNLLYVAGLSGRVDALDPASGTLRWFFTTGGYLLSSPIVENGVVYVGSADNTFYAIDAQTGTSRWTYKATAAFVGSPVVADGILYVVCSDWLLYAFNAVSGQSLWTFPLGDFNPGQQQQTSPVVANGRVYVGSRNHILYALDARTGTGLWQFTTNFDIYATPLVVNGIVYIGSTDRSLYALDGRTGQRRWSFKTGNILFSSPTSALKSSITGKYPTISGAGK
>NZ_CP051677.1|WP_169551709.1|3822324_3823500_-|DUF4249-domain-containing-protein
MPKLLSLLLIWLMLGCVSAYDPKLSLDADLVVVSGMITDLPETQTISLSRSRSKRDSADVVTPIRRAQVDVRVDEATTIRLTESQPGVYAFPADFRGKVGSRYQLRFTTEEGESYASTVESMTVAPAIQRAYDQFTPTGPTVRADGTPIPANDVYIDFQDPAGTRNFYLWRWRLYETQLWCATCKQGRYMVRDIGPVGAGPLDVVGCVPDQSLVYSNLYDYACRSQCWDIFYSTAIDTFSDIYTNGQTQVGHKVASIPIYQLDPALIVIEQLSISADAYRYYKLFADQVQNTGTLADSPPAPISGNVKNLNNVQENVVGYFTAASVAVSRYKLKRQNVTGAGRYQGLFYAQTGRLPNVDPGGGSTFGTGIPSALCVPSATRTDLIPEGWNQ
>NZ_CP051677.1|WP_169551708.1|3818773_3822307_-|TonB-dependent-receptor-plug-domain-containing-protein
MIQRFIPYRFRQIIWSLLLVLSMATATLAQTEIRLYNGPTLGGPTLGGPTLGGPTLGGPTLGGPTLGGPTLGAGLRPETTQPDRSFNRVVYNVSSPTLTAYLPDPARATGRSVLIFPGGGLSRLFIDEQGVFVAQQLAENGVAAFVVKYRLAQRPVGSSTDPLPQLPASVRDSALTRAVADGATALTYLRQHSTDLGIQPDRIGLLGFAAGGTIALRLGTTSDGTLRPAFLALIDPDITTQSTPTVQPTTPPLFLVTATNQTQPVLLAQSQLYQDWLRAGRPTEQHSYPANATDPNALSIPLDKWIDRLTTWIGELAASSPPPPVSPSATQTAPPTLPAIPPSVPASTPTTSPANSASTASAPATNSSPAALKPADKPVSSRRPEKQVVRQAPVYVSGPGGLVTGVVRDSATGTPLAGVAIVVDYRRHLTGTSTNDRGQYNIDLTAGEHVLVTRLVGYTPVRKIVQVSNTGALRVDINMVSVASQLEEVVVTTKGFDQTIRQPLLGVSQINIATLRKLPAALGEVDLLRGLQSLPGVTSVGEASNGVNIRGGTTDQNLILLDETPIFNPTHMFGLFSVFPTDVLSTVDLYKGNVPARFGGRAASVLDVSLRNPNLDQFQLSGGVSFVSNRLTADIPIVKGKLGLLVAGRGAFNDFLLPRISNRLAGIRARFGDGVTKLFWRIDDRNTLTATGYYSKDEFQTSLLASLPNVNGTTTRYDHQTINGMARWFHTFSPRTSLQTSAVWVDYVPKILAPELNSTNTVTLYSAVRQRQIKSNLNYQFTNQKLEVGLSGTQYRIQPGTLLPGASDRVNYITTPTENGLELAAYADYERSITPDLAVSAGLRYSHFLALGPSLVRRYLPGQPRDELSVIDSVRYGAGQVSKQYGGFEPRLGIRYSLSPTASVKFGYNLMRQYLQVVTNTTTPLPTSRWKTADANIRPQVSQLVSAGYFMTFHKDIYELTVEGYWRSTENSIDYRPGADFLLQPYPEAQLLQGRSRSYGVETMISKKRGEMTGWLNYTYARTFNQVYEGPTIEQNINGGAWYRANYDRPHTVNASLTFDVDKHNSFGFTFAYSTGRPYTAPTGYVTIDGAQYPYYGVRNQARLPDYHRLDFVWNIYNPSLQNRRWQGKWAFTIYNLYGRRNAYSVFFRTENGKTNSYQLQIFATPIASLSYNFIFK
>NZ_CP051677.1|WP_169551707.1|3818437_3818596_-|hypothetical-protein
MSFDVTPLLVGYKTDDPPASLPSTPITGFHRPRLPPTNPPRTIRFITMVRRT
>NZ_CP051677.1|WP_169551706.1|3817256_3818438_-|type-IV-secretory-system-conjugative-DNA-transfer-family-protein
MTVAPTGTGKGRGVVIPTLLTYPGSVVVLDPKGENYQVSARARREMGQHVIRLNPFGVNEKTSDALNVMDVFDLPGIDVETEAQLMAELFSQGQKGHKEPFWDITATSLLAGVIGYVATVCPPEERNLATVRDILFDSDVIYRLALILDTHGKQIPKAAYHQLSAFLAMPDQNTRPSTLATANSYLTAFLSEDVNRVTSQSSFKLVDFRDGKPLSIYIIVPPDKLVSHRALLKLWIGVLLKTITSRVTIPDQQTLFMLDEAGQLGHFAYLYSIITLCRGYGLKCWTIWQDFQQLESNFPDDWQTLMNNCGVLQFFGCKNTQIARRVEFVTGTPAHHVQKLRSDQQLLLLDGESIFSRKVNYLTDPAYQTRFDPNPFYQRSGSMGTDTTGPGRG
>NZ_CP051677.1|WP_169551705.1|3815853_3816495_+|deoxynucleoside-kinase
MHIAITGNIGAGKTTLAEQLARHYDWDVLYEAVAGNPYLADFYADMPRWAFSLQVYFLNSRFTQMRRIRALKQEPGGGRTVIQDRTIYEDSAIFARNLYQAGTMTERDYQTYRGVFDNMMSLVEPPDLMLYLRAGLPKLQQQIQKRGRSFEQSITADYLGRLNQLYDEFIATYTGGALLTIDVDQLDYVANPADFAAITAQIDAWLATRTRSA
>NZ_CP051677.1|WP_169551704.1|3814834_3815797_-|rhodanese-related-sulfurtransferase
MKPYRVLLYYIYSPIENPDQYRDEHHRLCLELNLLGRVIVAAEGLNGTVSGLAADCEQYMATLHADPRFAGIDFKVDESDVHAFQKLHVRTKAEIVHSDLPVDPLRQTGIHLEPAEFQRMKNDPDVVLVDMRSNYEHAVGKFSGAVTFDMENLRDLPDHVHELDHLRDKKIITYCTGGIKCEKASAYLLSQGFENVYQLHGGIIKYGMEAGGEGFDGECYVFDNRLAVPINEVNPTVISTCYRCGTPTSRLINCASPACNNHVTLCDDCGHTHEGTCTDACKEDPNRRPYDGTGYYSKQTQSYSPLQGYKSRQGQHGPLV
>NZ_CP051677.1|WP_169551703.1|3814529_3814838_+|cysteine-rich-CWC-family-protein
MQTYANTPERTGFTRERWQKKSGYTTMPKHAIDSCPRCGRLFTCKVNTVLHCDCQYVGLTKAETEYIRDVSLFDYDGECLCLACLNELKTEFQDNQPDEAAR
>NZ_CP051677.1|WP_169551702.1|3813714_3814500_-|5'/3'-nucleotidase-SurE
MPDRKPLILVTNDDGITSAGIRTLVELMQQLGTVVVVAPNSPQSGMGHAITISSPLRLYPSDLFTDATDVIAYECSGTPADCVKLAKHHVLKDQAPDLVVSGINHGSNTSISVLYSGTMSAAIEGALEGIPAIGFSLNDFTRQADFSHTHEHILTIARQVLERGLPKGTALNVNFPARAAEPIQGIKICRQANAKWQEEFDERRDPHGRRYFWLAGEFVNFDTHAEDTDEYAIAQNYTSVVPCQYDLTAYGLLDELAGWNM
>NZ_CP051677.1|WP_169551713.1|3835005_3836538_+|sulfatase
MKNTLLAGCTLVLITSLLAAFRPEVNAPTRPRNIIFILADDHRYDFMGFTGKVPGLQTPNLDRLAREGAHVRNAFVSTALCSPSRASILTGQYAHTHKVVDNFAPLTPGLRFFPQYLKKAGYKTAFLGKWHMGNTDDAPQPGFDYWLSFRGQGDYYNPTFNINGKRVSYTDSSYTTDLLTDYALKWLNTVDKSKPFCLYLSHKAVHAGFQPAKRHRNAFRNTPINYPETMYLTATDSSKVWGESTPGAKPVVSPDLKVNMADMPNWVKQQRYSWHGVDYLYHGTISFNDFYRQYCETLLGVDDSVGRVLAWLEQNGQLDNTMVVYMGDNGFSFGERGLIDKRHMYEESMRVPLLVRCPAVARPGTKLESVVQNIDLAPTFLAYAGLPKPAQMQGNSFLPLLKGERIPWRDRAFYEYYWEADFPQTPTMFGVRTDRYKYIFNHGVWDANELYDLQSDPQEVNNLIRSPAHQAIAKDMKDQVFTWLESTGGLQIPLHPIRQKRFDHRYEGNY
>NZ_CP051677.1|WP_169551714.1|3836664_3837684_+|formylglycine-generating-enzyme-family-protein
MLLMRLFGTVLTITTVALAACQSDTKRDTTATTVPAHRTATGSTAGMVWLPGGSFRMGSDEFADARPVHNVTVDGFWMDTHEVTNAEFAQFVKQTGYRTTAERPLDPADYPDVPADKLVQGSAVFTPPAQAVSLDNPLQWWQYVGGANWQHPAGPGSSIRGHENEPVVHVSYDDAMAYANWTGKRLPTEAEWEFAARAGREEQPYYWGNTQTPGGKWVSNIYQGDFPQRNTRADGFAGIAPVKSFPANPYGLYDMEGNVWEWCQDLYRPDYYSQSPTANPPGPADSYDPDEPGSVKRVQRGGSFLCSDQYCTRYKAGSRGKGEVSSGSNNLGFRCVRDK
>NZ_CP051677.1|WP_169551715.1|3837765_3840402_+|glycosyl-hydrolase
MNRFTIGRLIGLLVLVSYWANAQTTYELTAGWRCNPIGKTTGAGTAISTPTYALNGWQPAVVPGTVLTTMLANRQVPDPFYGMNNEAIPDIYRTGRDYYTYWFVNEFTEAPKTGQQVWLNFRGINYSCDVFLNGHKLNTKRFTGMFLRQSYNITPFLQKDGKNRLAVIVYPPDPVGNPNGGQGGDGTIARNVAHQYVAGWDWIQPMRDRNTGIWDKVTIEKTGAVNVRNPHVVTRVPGQRTPTGTQSPATIRPSAELENATGAMQTGTLRYTMNGQTVTKNVSLAPHTTTTVDLPALTLANPRLWWPNGYGEQYLYPASMQFVTGSQTVSDEEKLAVGVREMQTEWNSTTRSRQVSVNGQKVFIKGANWIVSDAMLRLSPERYNAEIRFHRDMNLNLMRVWGGALLERPEFYEACDRYGLLVMQDFWGSGDCNGRWVDPAKKDDQWTRRQYPDDHALFLTSAADQIKMIRNHASLAMWCGGNEITLPQDIMTPLRDSILPKLDGTRWFIDYSNSDEMSFNFLGGNGDGPYGIQPINRFWAYRTWPFNSEVGSVGVNDYASLERFMPDANRVAPVYVPGGKSVVDSVWQYHKYIGYDASIDPYGKATDIRDFTKKAQLVNYDQYRALMEGFSSHMWDWYTGTIIWKTQNPWTAMRGQMYDYYLDPNAGLYGLHHGSEPLHIMYNPVDSMVMVANNTFQYHRDMMMVIKVYDMAGRDTTLTQVFSEIGPTLVRPYVPINRAIRNLTRANGAFLNLQLLDLNRKPISDNLYWLPDSTGTHSGLQQLAKAPVRLSARQVAAGKVEVTLTNPAGGPVAFFNRLSLVDATTKKRLLPVFYSDNYVSVPPGQQKTITLDYTPGQVMPLVSLEGWNVPEQFAPVGQ
>NZ_CP051677.1|WP_169551716.1|3840839_3841421_+|sigma-70-family-RNA-polymerase-sigma-factor
MIVNEQELWQAFQAGDEGAYTQLYQQHIKAMYRYGMSLVAVSESFVLDCIHDVFTELWAKRTRLSTPDNIRYYLLRALKNRIMHLLERKERPLSPLLETDYDALWAEPDADLLDALETADNQQQRLQRLIAQLPPRQQEALKLRFVENMNYDQIGAVLAVNQQSAKNLVFRAVEKLRRLIISISLIFQLFFWV
>NZ_CP051677.1|WP_169551717.1|3841469_3842576_+|DUF4974-domain-containing-protein
MQPAYNTFTTTDFLLDDAFVDHLLAPTDQSNRFWADWLANHPHCRDTWQQAERLVRAIEAGLYDYAHTQLPDDTIRQLLTRIQQTNAQHTPVANPIVRPLRRVWWVAAASVLLVAGFGLWWYSRPVSIYTQQLAAQPDPVSEFVNDTKAVQQITLPDRSTVELAPASRISYPRTFGQKNRPVYLSGEATFAVTKNAAKPFLVYANEVVTKVLGTRFVVRAYTGESSVHVQVQSGQVAVYQNKPAETANKQHGVLLLPNQQVVFNRQSDQFIKQIVDLPQIVVRPSSRERTATPAFTYSDTPIPQVIQDLQDAYGIEIRYNKDALASCQLTASLVDESFASKLRIICATVGATYDMVDGQVVINGGTCQ
>NZ_CP051677.1|WP_169551718.1|3842669_3845978_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MEQISCYLPVYRRIVLVVALLLVQWARATQATDLPAPELLSRRISLSIERQSIKSVLRTLEQTAKVKFSYSPQVVRARQLISLRVQNSTLQDVLNKLLTPLQVSYTVAGEQIILARTVSEAMTIQLNEAGESIEVVADQTISGVVSDEKGAGLPGVTVAVKGSNRGAVTDASGTYRLTIPDGPQTLVFSFVGYASQEVAVSNQSTISVQLQPDVKSINEVVVVGYGSLNRKEVTSAVTHLSSGDLLRVGSNSPLMAVQGKVAGLSITNTAAGDPNSTPSIQLRGVSSRSAGLGPLFVINGIPGGNLDNINQNEIESIDVLKGGAASAIYGTRGSNGVIVITTKKGSDQSRIFYDGYSSFDFITNKLSVLSKDEFLANNRGVDLGGNTDWMKAVSRNPAFSQKHTLQFSGGNGKTNYFTSLDYRNATGVDLRSAKQEYGGRVNINHTSANNLYALTFSAAPRYAKTSNADYSGFNYALTLNPTQPIFDNTGKYAYITSGFFANNPVEQAKSVLSGSEIKYLDINASFKLNLLDNLSTLVTLGEVSSAFRNFGFTPSTLTTVVNGSGRNSGSQSLDENDQKSFEWTGNYALDAGKHSVKLLGGYSYQLFTSSGFNAGNENFPSNTLTYNNLGTGLWNLQAGINNVGSYRNSSKLIAFFGRVNYDFDQKYYLSASVRREGSSKFGYDNKWGYFPAASVGWRITQEKFAQNTGWLNELKLRADYGVTGNQDFGNYLSLDTYSGYGYYLYNGSSYQVWGPSQNTNYDLRWEKAINFNVGLDFDLFKNSRLTGSLNYYVRTNKDLLGSYTVPNPPNIQGSTFANVGTMQNSGLEIQLNAAIITGKDFRYNLTFAGATNSNKFVAFSNEAYQGQTYIDVLGMPAPGSPGNVQRLQENTRIGSFYALRSAGVNENGALLVYKKDGTVVQGNQANNDDRQFIGNGLPKFTGGLTNNFSYKKWDLTVFLRGTFGYQIFNTYAFYLGTPATQQNANTLKSAYDGGKYSKLTNPATYSNLSDYFLEPGSFVKVDNITLSYTQPLNVKYLRSARIYATTRNLATFTKYTGGDPDLVQTNGLYPGINQRVDNGNTVGTLNYFPSTTQLLLGLQLTF
>NZ_CP051677.1|WP_169551719.1|3845994_3847722_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MNRNRFFPTLLRTLGLSGLLLTAGCTNLDEVLYDRITSENFLQTRQDVTRDFLRAFEHAYWSIQGGSTYMLQENSSDELMTPNRQGDWFDGGQYQRVHYHTWTPNDGYTSDAWNALYGGVTLATNSLEDLQGITDPSRFSMTQAELDGMIAELRTLRAWFNIRLLDMYRNIVLVKKVKGETQGGPQVSPQEAFSYIEQELKESLPNLPTRQSLGANSIGRWTQGGAAALLTRLYLNAKVYTGTDHFADCATVCTDMLAGKYGQYALESRWDAPFDYTNSTSPETVFGFPGSFGLTHWQYDGGMYFWQLPVNATFYFGFTDFGTANPKYAIQPGRDVDSTEYSFALGKPYIKFRKYGDDVRLKTYKNLGNSKREGMFLKGYLPYTNSSGRVDTVRSTKGPYPLFFRDQVGMFLAAKPGTRIADKTSDMNHADQNSGLYPVKYPYYPSSDENKISSAYAEIRLAEIYYSLAECKYRAGDKAGAAALLNTVRARNYPANSPSLYKTDGSQLTDQEMLDEWGREFLVEGRRRTDLIRWGVFNTGTWWDKQPDADNHTAIFPIGQNVLNVSSQLKQNPGY
>NZ_CP051677.1|WP_169553405.1|3848060_3848732_+|response-regulator-transcription-factor
MKILVVEDEERAATFIRKGMSAEGYEVEIAYDGRTGLSLFRQNEYDIIILDVNLPHINGFDLCKLIRADNESVPVLMLTALDSITDKADGFNSGADDYLAKPFEFQELLLRVRALTRRNHNKPKQILQLADLELNLDTKTVTRSGKRIDLTTREYALMEYLMLNKGKVISRIDISERVWNLNFDSNTNVIDVYVSYLRKKIDKDFSPKLLHTIVGMGYVLRES
>NZ_CP051677.1|WP_169551720.1|3848744_3850106_+|HAMP-domain-containing-protein
MLIRNRLTIIFTGLAIAIQITLSLVVIYFYSLYRQEEFYSRLESKARVAGRVLISRRHLHDDFFKNMVRTDLLTIVDEQISIYDSNHNLVFTNRTLKESDYYKEKIPLLATNSLFEFRSGHFESIVIPFRDRGQQFYIFASGYDRIGFAKLTALEQILLLANLLGFALIVLAGWYFAGRVLKPISQIVDEVEQITATHLHKRVNEGNRQDEIAQLAMTFNRMLFRLEDAFVSQRSFVSHASHELRTPLNNTLGTLETSLRYDQNPVDWRDSMEVAVEELKKLISLTNGLLSLAKVSDGGVALSDIQVDDCLLTAIGQVQTKYPGRSLPLHFDAEDETSFTILGNATLLTTAFLNVLDNACKYSQAAVSVQLTLTNEQINITVTDQGRGISKADSIHVLDPLYRGNNVEGVPGYGIGLAITQKIIELHQGELVIDSQVDQGTTVTISLPGLEQA
>NZ_CP051677.1|WP_169551721.1|3850777_3851611_+|sterol-desaturase-family-protein
MIQSCSFATLSLTALLFFLVVFGRYVLFSLAFNWLFPQPATDGPPTRPPIQARRPKADQHWREIGWSALTSVIFAGIGLGVLIAFQAGYTRIYTDLHEYGLVWYGLSIGLVLLLQETYYYWLHRWMHKPGVYRWVHKTHHDSLTTSPWTAFSFHPIESTLQAILLPVLTFILPLHSTAIVLILMIMTVSGAINHLNTEIYPHAFNRHWLGKWLIGATHHSLHHSQFRYNYGLFFTFWDRWMRTESPDFDPLFAEKSRKENHHQNHTDAATVTDQECR

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Crispr_ID: NZ_CP051677_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP051677_5

4562420-4562565

Orphan

Consensus_repeat	Method
TGAACTGTGATTCCCGCTGATTGCACTGATGGACTGTGATTACT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP051677_5

>merge|NZ_CP051677|5|4562420-4562565|CRISPRCasFinder
TGAACTGTGATTCCCGCTGATTGCACTGATGGACTGTGATTACTCCCTTTTTCTGAATCAGCGAAATCACATAATCAGCGGGAATCACAGTTCAAGACGTCTTGAACTGTGATTCCCGCTGATTGCACTGATGGACTATGATTACT

>NZ_CP051677|5|4|4562420-4562565|CRISPRCasFinder
TGAACTGTGATTCCCGCTGATTGCACTGATGGACTGTGATTACT	CCCTTTTTCTGAATCAGCGAAATCACATAATCAGCGGGAATCACAGTTCAAGACGTCT
TGAACTGTGATTCCCGCTGATTGCACTGATGGACTATGATTACT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051677.1\|WP_169552230.1\|4569103_4570369_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_CP051677.1\|WP_169552224.1\|4560519_4561482_-\|alpha-E-domain-containing-protein	unknown	unknown	gnl\|CDD\|377234
NZ_CP051677.1\|WP_169552219.1\|4552347_4553859_+\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|173803
NZ_CP051677.1\|WP_169552223.1\|4559676_4560435_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169552229.1\|4567893_4569009_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274350
NZ_CP051677.1\|WP_169552228.1\|4567017_4567713_-\|cyclase-family-protein	unknown	unknown	gnl\|CDD\|224790
NZ_CP051677.1\|WP_169552231.1\|4570380_4570734_+\|nucleotidyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|143393
NZ_CP051677.1\|WP_169552225.1\|4561630_4562401_+\|NIPSNAP-family-protein	unknown	unknown	gnl\|CDD\|311781
NZ_CP051677.1\|WP_169552227.1\|4564239_4566132_+\|DNA-polymerase-III-subunit-gamma/tau	unknown	unknown	gnl\|CDD\|237874
NZ_CP051677.1\|WP_169552233.1\|4571160_4571514_+\|nucleotidyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|143393
NZ_CP051677.1\|WP_169552221.1\|4554584_4556240_+\|putative-maltokinase	unknown	unknown	gnl\|CDD\|274141
NZ_CP051677.1\|WP_169552217.1\|4550871_4551654_-\|peptidoglycan-editing-factor-PgeF	unknown	unknown	gnl\|CDD\|376831
NZ_CP051677.1\|WP_169552232.1\|4570730_4571129_+\|HEPN-domain-containing-protein	unknown	unknown	gnl\|CDD\|224807
NZ_CP051677.1\|WP_169552218.1\|4551824_4552220_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169553443.1\|4557556_4559518_+\|1,4-alpha-glucan-branching-protein-GlgB	unknown	unknown	gnl\|CDD\|235445
NZ_CP051677.1\|WP_169552234.1\|4571534_4571918_+\|HEPN-domain-containing-protein	unknown	unknown	gnl\|CDD\|224807
NZ_CP051677.1\|WP_169552226.1\|4562750_4564103_+\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP051677.1\|WP_169552220.1\|4554246_4554501_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376918
NZ_CP051677.1\|WP_169552235.1\|4571914_4572391_+\|2-C-methyl-D-erythritol-2,4-cyclodiphosphate-synthase	unknown	unknown	gnl\|CDD\|376811
NZ_CP051677.1\|WP_169552222.1\|4556405_4557239_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|187632

Protein	Function_ID	Function_description	E-value
NZ_CP051677.1\|WP_169552230.1\|4569103_4570369_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	1.84318e-69
NZ_CP051677.1\|WP_169552224.1\|4560519_4561482_-\|alpha-E-domain-containing-protein	gnl\|CDD\|377234	pfam04168, Alpha-E, A predicted alpha-helical domain with a conserved ER motif. An uncharacterized alpha helical domain containing a highly conserved ER motif and typically found as a tandem duplication. Contextual analysis suggests that it functions in a distinct peptide synthesis/modification system comprising of a transglutaminase, a peptidase of the NTN-hydrolase superfamily, an active and inactive circularly permuted ATP-grasp domains and a transglutaminase fused N-terminal to a circularly permuted COOH-NH2 ligase domain.	6.36274e-132
NZ_CP051677.1\|WP_169552227.1\|4564239_4566132_+\|DNA-polymerase-III-subunit-gamma/tau	gnl\|CDD\|237874	PRK14971, PRK14971, DNA polymerase III subunit gamma/tau.	0
NZ_CP051677.1\|WP_169552228.1\|4567017_4567713_-\|cyclase-family-protein	gnl\|CDD\|224790	COG1878, COG1878, Kynurenine formamidase [Amino acid transport and metabolism].	6.11855e-61
NZ_CP051677.1\|WP_169552229.1\|4567893_4569009_-\|hypothetical-protein	gnl\|CDD\|274350	TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.	0.00687928
NZ_CP051677.1\|WP_169552235.1\|4571914_4572391_+\|2-C-methyl-D-erythritol-2,4-cyclodiphosphate-synthase	gnl\|CDD\|376811	pfam02542, YgbB, YgbB family. The ygbB protein is a putative enzyme of deoxy-xylulose pathway (terpenoid biosynthesis).	9.62642e-97
NZ_CP051677.1\|WP_169552231.1\|4570380_4570734_+\|nucleotidyltransferase-domain-containing-protein	gnl\|CDD\|143393	cd05403, NT_KNTase_like, Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.	3.36898e-11
NZ_CP051677.1\|WP_169552225.1\|4561630_4562401_+\|NIPSNAP-family-protein	gnl\|CDD\|311781	pfam07978, NIPSNAP, NIPSNAP. Members of this family include many hypothetical proteins. It also includes members of the NIPSNAP family which have putative roles in vesicular transport. This domain is often found in duplicate.	9.14556e-17
NZ_CP051677.1\|WP_169552219.1\|4552347_4553859_+\|S8-family-serine-peptidase	gnl\|CDD\|173803	cd07477, Peptidases_S8_Subtilisin_subset, Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	1.60399e-61
NZ_CP051677.1\|WP_169552233.1\|4571160_4571514_+\|nucleotidyltransferase-domain-containing-protein	gnl\|CDD\|143393	cd05403, NT_KNTase_like, Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.	1.48854e-11
NZ_CP051677.1\|WP_169552221.1\|4554584_4556240_+\|putative-maltokinase	gnl\|CDD\|274141	TIGR02457, trehalose_synthase, trehalose synthase-fused probable maltokinase. Three pathways for the biosynthesis of trehalose, an osmoprotectant that in some species is also a precursor of certain cell wall glycolipids. Trehalose synthase, TreS, can interconvert maltose and trehalose, but while the equilibrium may favor trehalose, physiological concentrations of trehalose may be much greater than that of maltose and TreS may act largely in its degradation. This model describes a domain found only as a C-terminal fusion to TreS proteins. The most closely related proteins outside this family, Pep2 of Streptomyces coelicolor and Mak1 of Actinoplanes missouriensis, have known maltokinase activity. We suggest this domain acts as a maltokinase and helps drive conversion of trehalose to maltose. [Energy metabolism, Biosynthesis and degradation of polysaccharides].	6.29514e-107
NZ_CP051677.1\|WP_169552217.1\|4550871_4551654_-\|peptidoglycan-editing-factor-PgeF	gnl\|CDD\|376831	pfam02578, Cu-oxidase_4, Multi-copper polyphenol oxidoreductase laccase. Laccases are multi-copper oxidoreductases able to oxidize a wide variety of phenolic and non-phenolic compounds and are widely distributed among both prokaryotes and eukaryotes. There are two main active catalytic sites with conserved histidines that are capable of binding four copper atoms.	9.4559e-86
NZ_CP051677.1\|WP_169552232.1\|4570730_4571129_+\|HEPN-domain-containing-protein	gnl\|CDD\|224807	COG1895, COG1895, Uncharacterized conserved protein related to C-terminal domain of eukaryotic chaperone, SACSIN [Function unknown].	1.18189e-19
NZ_CP051677.1\|WP_169553443.1\|4557556_4559518_+\|1,4-alpha-glucan-branching-protein-GlgB	gnl\|CDD\|235445	PRK05402, PRK05402, 1,4-alpha-glucan branching protein GlgB.	0
NZ_CP051677.1\|WP_169552234.1\|4571534_4571918_+\|HEPN-domain-containing-protein	gnl\|CDD\|224807	COG1895, COG1895, Uncharacterized conserved protein related to C-terminal domain of eukaryotic chaperone, SACSIN [Function unknown].	6.079e-17
NZ_CP051677.1\|WP_169552226.1\|4562750_4564103_+\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	4.55183e-73
NZ_CP051677.1\|WP_169552220.1\|4554246_4554501_+\|hypothetical-protein	gnl\|CDD\|376918	pfam02745, MCR_alpha_N, Methyl-coenzyme M reductase alpha subunit, N-terminal domain. Methyl-coenzyme M reductase (MCR) is the enzyme responsible for microbial formation of methane. It is a hexamer composed of 2 alpha (this family), 2 beta (pfam02241), and 2 gamma (pfam02240) subunits with two identical nickel porphinoid active sites. The N-terminal domain has a ferredoxin-like fold.	0.00709654
NZ_CP051677.1\|WP_169552222.1\|4556405_4557239_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|187632	cd05374, 17beta-HSD-like_SDR_c, 17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs. 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	6.92149e-62

>NZ_CP051677.1|WP_169552225.1|4561630_4562401_+|NIPSNAP-family-protein
MVSFYTLLTMSLLAFSSLTAAPAPTPAKPGTKLYEVRIYHPTPGNYANIVDRFRQYTTKLFEKHGMENIGYWTPTDTTDKRLIYILAYPDRTARDASWKAFGSDPDWKAVVAKTEANGKIVAKVDQIFMSEADISPALKLKKASPTRVFEMRTYFPAPGKLADLLSRFRDHTIKLFSKHGMTNVAYWLTEDKDADGQSKLVYILAHPSEAEGKQHFDEFRKDSKWVKAKADSEKNGSLTTKVESVYMVPTDYSPIQ
>NZ_CP051677.1|WP_169552224.1|4560519_4561482_-|alpha-E-domain-containing-protein
MLSRVANSVYWMHRYIERAENYARFMSVNFNLELDLPPTVNQQWEPLLIATADNHLFDKYYDAPTRENVIQFMTFEKRNPNSIISCLSNARENARTIREVISKEMWEHLNQFYLMVRDTDPRQQQEQTQTQTYFNEIRNAIQLFYGIIDATITRNDAWHFGRLGRFLERADKTSRFLDVKYFTLLPQVEAVGSTLDLMIWSAVLKSVSAYNMHRQQYRALTPTSIVEFLILSKAFPRSVAHCIRQAELSLYEISGNNITNGFGNAAERRLSKLRTEIEFTETTDIFKKGLHQYLDSFQTQTNEVGAAIFETYFDLKPVEV
>NZ_CP051677.1|WP_169552223.1|4559676_4560435_+|hypothetical-protein
MKKFLLAVCLLGTVTSFAQSPVSARLSSGYDLGMGYSTNRYNPSIQYYQLLNIGERKLVSLGWNFRLGAFYGDNIDCYTAPARLTREKTGFSALGAPLVPANIDTLRFDFVSMTSASIGVRAQINLGRVELGASADLVGLTLGRTRTGRVTSSTGRYRVDSTTTSPFTGANADQSARPSRLNARLLGDNNLGTLSTDVYARIRVSQRVGIKVGYQWLTSEVRMSNRDVIADNDRFRNRSGLAYLAVTLPIFQ
>NZ_CP051677.1|WP_169553443.1|4557556_4559518_+|1,4-alpha-glucan-branching-protein-GlgB
MPDPVQEPVPATDSPAPAPESAGSYSRFTDFDVHLFRSGKHQRLYEKFGSHVVEHNGVTGTYFAVWAPSARYVAVIGDFNGWNKGSHSMAVRWDSSGIWEIFIPNVGRGTVYKYFIVHEGGRELEKGDPYAHSWEVPPKTASVVTDTYYEWNDQDWMANRGAKNSLNAPISVYEMHLASWRRDPGNPERELSYGEIADALVPYIQDMGFTHVEFMPVMQYPYAPSWGYQITGYFAPSSRFGTPQEFMHLVERLHQAGIGVLLDWVPSHFPGDAHGLYEFDGSHLYEHPDPRKGYHPDWKSYIFNYGRPEVRSFLLSNALFWLDRCHADGLRVDAVASMLYLDYSRNAGEWEPNMFGGRENLDAISLFKEINEAVYAAFPDTQTIAEESTSFPGVSRPLYTGGLGFGMKWMMGWMNDTLRYFERDPAFRKFHQNELTFSTIYAFTENFMLPLSHDEVVYGKHSLVGKMPGDEWQRFANLRLLFSYMFTHSGTKLLFMGGEFGQTEEWKYDSSLDWHLLQYAPHSGMAACVKALNQLYRNEPGLYDRNFTANGFEWIDTSDQENSVITYARNGNRPEDTLLIVLNMTPVPRHGYRIGVPTGGTYHEIFNSDATEFYGSGVTNPNAINSDEQGWQGRMQSLQLNIPPLGAVVLKMK
>NZ_CP051677.1|WP_169552222.1|4556405_4557239_+|SDR-family-NAD(P)-dependent-oxidoreductase
MSTLKNHVIIITGAGSGIGRQLAIQAAATGAPVIATDINLNGLAETNRLAGGAVTTRQLDVSDAASIQRFADETIPALGNRPLILVNNAGVALSSGPFATTELDDFEWLLSINLWGVIRMTKAFLPYMTEHNAGHIVNLSSVFGLAGVMNQSAYSTAKFGVRGFSDVLRMELLDTPIKVTCVHPGGIKTAIASSARQGKNTPVTDAMKQNAVSSFEKAARTTPDEAARQIWRGVEQDKARVLIGADARQIEWLTRLLPTRYVQIIRSKIERTFNTEG
>NZ_CP051677.1|WP_169552221.1|4554584_4556240_+|putative-maltokinase
MTTSPPFASPVAWSDAGQHTDIWSDLCQTLLPPYINTCRWFAGKARQQTGLQMRAVMPLLIDAESGKVAYLTILTVSYADGNPESYLLPLSFVSDRATKERTFGVADVPDKGRIGEVQLAGKAGLLIDAIYDERFRNALFNAIYDNQTMAMPEGQIRFQRGQGLDEGDRSLPSRVLPVDSSNSAMTFGDKYFMKLYRKLFRETNPEVDMVAFLTDVGQFTHIPAFGGSFVWERDGIADVTLGMVQRMVPNDKDSWGQTGDYLNDFLYAVPQRLFTIREDVFEKAELLGRRTGEMHNALYNPTASADFAPEPFTDEYRTFIINRFESLLEQRYTLLIDRYTELDPLAQRLAWVFMEAREMIEAFINDFRTRPLGSLRTRIHGDYHLGQVLATDTDFVIIDFEGEPESSITDRKIKHSPLKDVAGMIRSYHYAVSAKLFNSAETEDLDPAYLQRVSDRWFHLIRDTYLDAYFDTFGSPHPLFRNNNEINFLLLIYLLEKAVYELGYEISYRPSWVKIPLKGIIDVVTEIEKIRLSDGVTLSPDIPMLQKGLLR
>NZ_CP051677.1|WP_169552220.1|4554246_4554501_+|hypothetical-protein
MARYLLAFNGPLPLPPDDLRLIGQQAQLLDTSRRTVLVETDADHRIHKLASQLPNWTISPETITPLPTTRPAIRKGTNEGGSIT
>NZ_CP051677.1|WP_169552219.1|4552347_4553859_+|S8-family-serine-peptidase
MANLPPRNYILLPRTGIQFSDATPTTRDAIKSLTVDTRLRDVLAGDLTNVAVVLDSTDGQGAKLVQLSESELPLLRAQLPGVLIVPEVFYYPQLFRESIRTVARPLQGQAKVALKIQLVEAKTTKPVAGATVVAFTNFADRTGEQATSDAQGVVSFKNITNQKIDQLYVYPKVGYWSYWKQKVTLKTGDKLPIQPVKLDYQNAKSFFYPAPADGEPNGSGLTVGVIDTGAGPHPDLNIAGGACTVTGDDPKDFADVDEHGSHVSGIIAAQGTPPTGVRGIAPGATLRAYRVFGRNSNGASNFAIIKAIEQAVADKCDLLNMSLGGGPVDTATQEAITFAYQNGTLCFVATGNDGRQPVSFPASFSLSLAVSAMGRKGTFPANTTDAPNVAAPFGTDKKNFIAAFSNVGSSVDFTGPGVGIVSTVPGGYSPLSGTSMACPAATGIAARLLSGHPDLVKMPRNAARSDAMIQQLAKYVRPMGFGPTFEGTGMLLLPDGTTPPTVS
>NZ_CP051677.1|WP_169552218.1|4551824_4552220_+|hypothetical-protein
MKTLVTSLLVAFTLVSSAVSFCEAKPIVRPVKQAAAYEVSMYTATNGNLRLALDKQKGGRVTVSMKNDKGNTLFTQYVGKRETQSRFMFDISALPDGVYTVEISNGAETKTQELTINTPKEQLPARQIALN
>NZ_CP051677.1|WP_169552217.1|4550871_4551654_-|peptidoglycan-editing-factor-PgeF
MLSYTPAEAQQLPLYRVPGLFTSIDGLIAAESTRHGGVSPAPFAALNLGINTADDPANVDENRLRFFSAIGTTEFGFASAHQVHGTAVLHVTEAGRYEGYDALMTNVSDLLIGVTVADCVPILIYDSGQRAVAAVHAGWRGTVGRIVQETITQMQQQFGTQPADCHIYIGTCIDQHAFDIGPEVATQFDASLLGTNPQTGRTCADLKRANMNLCLAMGVPASQIEVSPFSTVANNDDYFSYRAEQGQTGRMLAVIGLKNT
>NZ_CP051677.1|WP_169552226.1|4562750_4564103_+|Gfo/Idh/MocA-family-oxidoreductase
MKQMDHLSRSQFLSVTGRGLAIGAMSSALASCAKQVAQPVTAQTQPTPSGPVPKLPPVSPPATVPSDPARPIVLEQIEAKTEQEKPPTPTPLPPDQRVGFAVVGLGHLTLDEILPALSMSKKSKLVALVSGSPEKMKKVAEQYGVRKEYCYSYADYDKLRDNKDVQVIYIVLPNGMHAEYTIRGAQAGKHILCEKPMANSLAECQAMIDACKQANVKLMIAYRIQYEPHNRKVREMVQTNQFGKVKSIIANNGQNSDNPKHWRFNKALAGGGSLPDVGLYCLNTIRFVLAEEPTEVSAFIHSTPGDPRFTEVEEQVNWLMKFPSGVQASCATSYGHHDDKSYRVLADTGWIKMDPAFPYQGLKLMTSQAQGKQNLITEHDMGQKNHFMSEMDHFSTCVTGNKTPFTPGEEGLQDQRIMDAIYQSAREGKPVKLAKIDKKDAFRGTPPADE
>NZ_CP051677.1|WP_169552227.1|4564239_4566132_+|DNA-polymerase-III-subunit-gamma/tau
MENFVVSARKYRPATFDTVVGQEHITTTLKNAIRTNHLASAFLFCGPRGVGKTTCARILAKTINCQNLTEDGEACDQCDSCVSFNQSASFNIHELDAASNNSVEDIRNLIDQVRYPPQSGKYKIYIIDEVHMLSSAAFNAFLKTLEEPPSYAIFILATTEKHKILPTILSRCQIFDFNRIQPQHIAGHLAKIAGAENIEAEPEALALIAQKADGGLRDALSMFDLNVTFAADRVIRYKEVLDNLHILDYDYYFKLTEQLLAGNLVQSLLTTDEILRKGFDGHQFVVGLCRHFRDLLVAKDAATVQLLQVTENVRKQYLEQAMQAPMSFLLSALSLGGQCDMNYKQAKDQRLHTELWLMKLANLRNVLDWDALPAQPVSGTRSNAPAAPVITEAAVPNGVPLPDGAEKKNDSPQPSPDHGLTAQHPITSEPVNGYQSAPSPAPQPVASASTVAPPVAPAQQPATAMRQPIAMPARPASSRLRSTVSLNTSPVQATSEPSVVAVLAPARPDRPFDFDDLQTCWRTFTKLRLQQNDSATEQLVLNRQLVLDGTTISLTLDNTLQVGYLTDIKPELMMYLREQLQNSQIQLEHTVTVQETKKMIYSSQDKYNFMANKNPALHELRQALNLEVDY
>NZ_CP051677.1|WP_169552228.1|4567017_4567713_-|cyclase-family-protein
MTPANANREANSLIDLSHTIEDGLITYKGLPAPVVCDYLSREDSRQLYAEGTEFQIGKIEMVTNTGTYIDSPFHRYADGKDLSQIGLERFAELEGVVVRIPYTDTLEITDEHFKKYAVSNRAVLIHTGWDSHWNTDSYYENHPYLTAEAATYLRDQGAILVGIDSHNIDNTTGKQRPVHTTLLGAEILIVEHLCNLAQLPDEGFLFSAVPPKFRGVGTFPVRAMASVYGVR
>NZ_CP051677.1|WP_169552229.1|4567893_4569009_-|hypothetical-protein
MFQLSRFLPLLCLVCLLLPVRAQVMTDPAAQQTVQKALDHIYNMEFTQADGLIRQLQTRYPQHPVASMLRATQLDIQNLPMAENNAAMAQFGQAVNQGMTLAKRMLDKNENDPEGVFFTLSAYSYMASLYHNQGESLKAVGESKKAYSYLRDGAKLLDKGSDFYFTTGLYNYYVERYPLDHPVVRPFMFFFADGDMPLGLKQMDIATRKAVFMRPVANYYLAHILIKHESNPVKANVYTTYLTEKYPKNPLFAMIQAESLLLSGRYADARPAVQQLRQFSNKLVPLAYQTFSGMLAEQADKNDKAATDFYEAALKLPANEAYTKEYKAFAYSGLARIAARANDHARAKAYYKKALDTAEYKTTVREAKAFK
>NZ_CP051677.1|WP_169552230.1|4569103_4570369_+|insulinase-family-protein
MIHYEQFVLDNGLNVFVHQDDSTPMAAVNILYNVGSRDEDPARTGFAHLFEHLMFGGSQHIPSYDEPLQKVGGENNAFTSPDITNYYITLPAANLETAFWLESDRMMSLSFDPQVLDVQQKVVIEEFKQRYLNQPYGDVWLKLRPLAYREHPYRWATIGKDISHIENATLDDVRSFFFKYYLPNNANLVVAGNVTVEQVKELCAKWFAPIPAGPAYVRALPNEVRQTEARHEEASAKVPLDALYKAWHMPGRFEPGYYSADLLSDMLGRGKSSRLYQRLLRDNPLFSNIGAYSTSSLDPGLLVVQGTLNEGVSLEEADAAVSAIIQEFIDQPVADDELSKVKNQAEATLAFSEIELLNRAMNLAYAANAGNPDLVNEEAAMIQAITADDIQATARQVLRPDNCSTLFYRRANAENPDEVAA
>NZ_CP051677.1|WP_169552231.1|4570380_4570734_+|nucleotidyltransferase-domain-containing-protein
MNLTYTPHALTPEQLTALSQELKQALTDLYGPRLDRLVLYGSYARGDYHAESDVDFLVVLRDEPVRAGREVRQMAAVVGPLALKYGVEVSVFPTGSHRYTADETLFLRSATTDGIPL
>NZ_CP051677.1|WP_169552232.1|4570730_4571129_+|HEPN-domain-containing-protein
MNDLNRAEAHLQKAAEDLREARSLLDAGFPDGTCNRAYYALFHAIIALLYTTDGPIPKTHTGAHTEFRRQFIRPGLFADSFSNTITLLFNLRQGSDYEIEFDTTLDDAQDAVNKAAEFLSKAEAYMKTIQPR
>NZ_CP051677.1|WP_169552233.1|4571160_4571514_+|nucleotidyltransferase-domain-containing-protein
MNLTYTPHALTPEQLTALSQELKQALTDLYGPRLDRLVLYGSYARGDYHAESDVDFLVVLRDEPVKSRQEINFMIDPVYDLTEKYDVLVMVKPSSTHKYESSDLFFYDQVRTDGITI
>NZ_CP051677.1|WP_169552234.1|4571534_4571918_+|HEPN-domain-containing-protein
MVMAEQCIDDANALFQLGSDRGALNRAYYGFFDAVRALLLTKAIFTKSHQATRSLFSEHFVKEGPFTAKDAKDFHILFNLRQDSDYETDDPTDSVAVKQIIDTAAEFVLQAGAYLREQPNTNQPKTE
>NZ_CP051677.1|WP_169552235.1|4571914_4572391_+|2-C-methyl-D-erythritol-2,4-cyclodiphosphate-synthase
MKIRVGQGYDVHRLEAGRPFWLGGIQIPCDFGPVGHSDADVVCHVLCDALLGAANMRNIGYHFSDKDPRWKGVDSKLLLAEVLRMVREAGYEISNVDVTVVLQEPKLNPHIPAMKTCLSGVMRIPEDDISIKATTSEHIGFVGRSEGIAAHCVALIFR

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Crispr_ID: NZ_CP051677_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP051677_6

4681322-4681399

Orphan

Consensus_repeat	Method
GTGTCAGGTCCCTGACCTGACAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP051677_6

>merge|NZ_CP051677|6|4681322-4681399|CRISPRCasFinder
GTGTCAGGTCCCTGACCTGACACATTTCCGGGCGAAGCGAGTTGCTGTCGCATCTGTGTCAGGTCCCTGACCTGACAC

>NZ_CP051677|6|5|4681322-4681399|CRISPRCasFinder
GTGTCAGGTCCCTGACCTGACAC	ATTTCCGGGCGAAGCGAGTTGCTGTCGCATCT
GTGTCAGGTCCCTGACCTGACAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051677.1\|WP_169552315.1\|4672321_4672990_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169552318.1\|4674366_4674900_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|312075
NZ_CP051677.1\|WP_169552323.1\|4681432_4682521_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|379862
NZ_CP051677.1\|WP_169552316.1\|4673016_4673298_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197666
NZ_CP051677.1\|WP_169552322.1\|4678170_4681296_-\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|226220
NZ_CP051677.1\|WP_169552321.1\|4677336_4678155_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP051677.1\|WP_169552328.1\|4688867_4689563_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_CP051677.1\|WP_169552329.1\|4689610_4691029_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379441
NZ_CP051677.1\|WP_169552314.1\|4671356_4672214_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187578
NZ_CP051677.1\|WP_169552325.1\|4685635_4685947_+\|DUF1206-domain-containing-protein	unknown	unknown	gnl\|CDD\|377695
NZ_CP051677.1\|WP_169552317.1\|4673485_4673863_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319911
NZ_CP051677.1\|WP_169552319.1\|4675098_4676064_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223757
NZ_CP051677.1\|WP_169552320.1\|4676364_4677336_+\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381302
NZ_CP051677.1\|WP_169552327.1\|4687503_4688871_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP051677.1\|WP_169552326.1\|4686682_4687258_-\|cupin-domain-containing-protein	unknown	unknown	gnl\|CDD\|369571
NZ_CP051677.1\|WP_169552330.1\|4691456_4691894_+\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP051677.1\|WP_169553446.1\|4684191_4685391_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340951
NZ_CP051677.1\|WP_169553445.1\|4670919_4671318_-\|acetyltransferase	unknown	unknown	unknown
NZ_CP051677.1\|WP_169552324.1\|4682790_4684059_-\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_CP051677.1\|WP_169553447.1\|4685874_4686459_+\|DUF1206-domain-containing-protein	unknown	unknown	gnl\|CDD\|377695

Protein	Function_ID	Function_description	E-value
NZ_CP051677.1\|WP_169552328.1\|4688867_4689563_-\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	4.49293e-79
NZ_CP051677.1\|WP_169552318.1\|4674366_4674900_-\|hypothetical-protein	gnl\|CDD\|312075	pfam08448, PAS_4, PAS fold. The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.	0.000737656
NZ_CP051677.1\|WP_169552323.1\|4681432_4682521_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|379862	pfam16576, HlyD_D23, Barrel-sandwich domain of CusB or HlyD membrane-fusion. HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.	3.55443e-49
NZ_CP051677.1\|WP_169552316.1\|4673016_4673298_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|197666	smart00342, HTH_ARAC, helix_turn_helix, arabinose operon control protein.	9.10427e-27
NZ_CP051677.1\|WP_169552322.1\|4678170_4681296_-\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|226220	COG3696, COG3696, Putative silver efflux pump [Inorganic ion transport and metabolism].	0
NZ_CP051677.1\|WP_169552321.1\|4677336_4678155_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	1.00948e-20
NZ_CP051677.1\|WP_169552329.1\|4689610_4691029_-\|hypothetical-protein	gnl\|CDD\|379441	pfam14052, Caps_assemb_Wzi, Capsule assembly protein Wzi. Many bacteria are covered in a layer of surface-associated polysaccharide called the capsule. These capsules can be divided into four groups depending upon the organisation of genes responsible for capsule assembly, the assembly pathway and regulation. This family plays a role in group 1 capsule biosynthesis. It is likely to be involved in the later stages of capsule assembly. It is likely to consist of a beta-barrel structure.	1.5397e-20
NZ_CP051677.1\|WP_169552314.1\|4671356_4672214_-\|SDR-family-oxidoreductase	gnl\|CDD\|187578	cd05269, TMR_SDR_a, triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs. TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	1.6918e-78
NZ_CP051677.1\|WP_169552325.1\|4685635_4685947_+\|DUF1206-domain-containing-protein	gnl\|CDD\|377695	pfam06724, DUF1206, Domain of Unknown Function (DUF1206). This region consists of two a pair of transmembrane helices and occurs three times in each of the family member proteins.	1.91712e-07
NZ_CP051677.1\|WP_169552317.1\|4673485_4673863_+\|VOC-family-protein	gnl\|CDD\|319911	cd07247, SgaA_N_like, N-terminal domain of Streptomyces griseus SgaA and similar domains. SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.	3.14203e-08
NZ_CP051677.1\|WP_169552319.1\|4675098_4676064_-\|hypothetical-protein	gnl\|CDD\|223757	COG0685, MetF, 5,10-methylenetetrahydrofolate reductase [Amino acid transport and metabolism].	1.21922e-06
NZ_CP051677.1\|WP_169552320.1\|4676364_4677336_+\|aldo/keto-reductase	gnl\|CDD\|381302	cd19076, AKR_AKR13A_13D, AKR13A and AKR13D families of aldo-keto reductase (AKR). Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.	4.51297e-127
NZ_CP051677.1\|WP_169552327.1\|4687503_4688871_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	4.94614e-50
NZ_CP051677.1\|WP_169552326.1\|4686682_4687258_-\|cupin-domain-containing-protein	gnl\|CDD\|369571	pfam07883, Cupin_2, Cupin domain. This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).	6.56354e-14
NZ_CP051677.1\|WP_169552330.1\|4691456_4691894_+\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	9.43672e-15
NZ_CP051677.1\|WP_169553446.1\|4684191_4685391_-\|MFS-transporter	gnl\|CDD\|340951	cd17393, MFS_MosC_like, Membrane protein MosC and similar proteins of the Major Facilitator Superfamily of transporters. The gene encoding Sinorhizobium meliloti membrane protein MosC is part of the mos locus, which encodes the biosynthesis of the rhizopine 3-O-methyl-scyllo-inosamine. MosC belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.81287e-93
NZ_CP051677.1\|WP_169552324.1\|4682790_4684059_-\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	3.73691e-14
NZ_CP051677.1\|WP_169553447.1\|4685874_4686459_+\|DUF1206-domain-containing-protein	gnl\|CDD\|377695	pfam06724, DUF1206, Domain of Unknown Function (DUF1206). This region consists of two a pair of transmembrane helices and occurs three times in each of the family member proteins.	1.02933e-05

>NZ_CP051677.1|WP_169552322.1|4678170_4681296_-|efflux-RND-transporter-permease-subunit
MSRFIRTIVGFSLKNRFFVFFMTGVLVIAGVVSYLRTPLEAFPDVTNTQIVVVTQWHGRSAEEVERFVTVPIEVAMNSVQRKSNVRSTTMFGLSVMKIIFDDGVEDFFARQQVNNLLQNVSLPDGVGPEIQPPYGPTGEIFRYTLESKTRDSRELLTLQNWVIDRQLRSVPGVADIVAFGGRDKIYELRVNPTQLAKYDITPLEVYQAVTRSNVNVGGDVIERNGQAYVVRGIGLLTSIPDIENILIEEAGGNPVLVKHVAEVIESELPRVGQVGLDAQDDVVEGIVVMRKGENPSEVLGRVKTKINELNTSVLPSDVNMATFYDRDNLIEFCTQTVLHNLTEGIVLVTVIVFLFMADWRTTVIVSIIIPLALLFAFMCLRLRGMSANLLSMGAVDFGIIIDGAVVMVEGIFVALDHKAHKVGMARFNQLAKLGLIRKTGGELGKAVFFSKLIIITALLPIFSFEKVEGKMFSPLAWTLGFALLGALLYTLTLVPVLCSMLLNKNVREKSNPLVRFFDRVVMRGFGWCFRHRRTSLVAALGFMVATFFSASMLGTEFLPQLNEGALWVTAELPMSMSLPESVKMTKTIRADLQKFPEVRQVLSQVGRSNDGTDPNGFYFCQFQVDLKPKKEWSRTITTEQLTDEMDARLKNYAGVLYNYSQPIVDNVAEAVAGYKASNGIKIFGPDVYELEKYAAQAMAAIEGVPGIKDLGIIRNVGQPEISVLLHDRQMALYGVSTADAQAVIEMAIGGKTASVLYEGERKFDIRVRFLPEYRQSEADIMRLMVPTMSGGKIPLKEIATIRQVTGPAFIYRDLNKRFIGVKFSIRGRDLGSTIAEAQQRVRAKLQPAREYSVDWVGEFENQVRATDRLSQVVPISIGAIFVILFVLFGNAKDAGLVLLNVPFALIGGILALHVTGMNFGISAGVGFIALFGICVQNGVILITVFNNNRKERLPLDQAIREGVQSRVRPVVMTALMAAIGLLPAAVSTGIGSETQKPLAIVVIGGLITATILTLLVFPIIYRLFYRKDTKTIEPEPAVALS
>NZ_CP051677.1|WP_169552321.1|4677336_4678155_+|helix-turn-helix-transcriptional-regulator
MTSPAEILPGVLFYSYHSAKPNEKVCVWNHHTLILQVYGQLVLQTAGQRLSMSDGELMLIGKNQVGTLTKTPPPGGHYETIVISLQEELLRRIALEDHVQADRRHLGAPNSLIPINDFLRGYFQSIVPYARSSGASMTDELGILKLKEGVKLLLLTLPDLRNQLFDFSVSHKIDLEKFMLNNFQFNVPIEKFAQLTGRSLAAFKRDFVKTFGAPPRHWLQEKRLSEARHLIENSQQKPSAIYLKLGFESISHFSHSFKKKFGVTPTALLQEP
>NZ_CP051677.1|WP_169552320.1|4676364_4677336_+|aldo/keto-reductase
MKNIPTIQLGQRGPSVSRLGLGCMRMSSIWGGATPDETESLATIQEALDSGINFLNTGDFYGAGHNELLIGRAINGRRDDAFISVKFGAIFHNGQPIGMDLRPVSIKNFINYSLTRLGIDTIDLYQPSRIDNSVPLEDIIGTVADLVQEGKVRYIGVSEITAGQLRRAHAVHPISALEIGYSLADRQIERDLLPTAAQLGIAVVAFANTAEGLLTGDLPVPLAPNDYRQVFSRFQGDNLRHNLEKVDVLKQIARDKGCTPTQLAIAWVKEQGKQIMPLVSMSRRSRLPENIAALDLVITSDEMNLLNTTFAIGAIRGDTYLQR
>NZ_CP051677.1|WP_169552319.1|4675098_4676064_-|hypothetical-protein
MFLEKIKSAESGILLYGITPPKASTQPERIAEIARNTLDRLTSLDIDALVVYDVQDESARTADERPFPFLPALDPFVFASGYLTALAIPKLIYRPAGKFSPQELTDWLQQLHQHRFYPVFVGVPAPNFPVKTTLADAYQIWSRHQETSVVGAVTIPERHNLLNDEDSRILDKMSCGVSYFVSQCVFNVDYARQVIDDLATRCHAQQVAPPTIIFTLTACGSEKTLHFMEWLGIHVPDTVKETLKTSADMLETSVQLCLAIADSLTAFCMERSIPFGFNIESVAIRKAEIEASVYITTKIGQMLSEKGLRKSPVAHSVSIDR
>NZ_CP051677.1|WP_169552318.1|4674366_4674900_-|hypothetical-protein
MLEATLDSSFNFIQVFKAVRDQSGQIIDFVWVLTNRRWQQAYGDIIGKSLLELNPAVVQTGVFARLVDVTQTGVAQTHEHYYPFEQFNGWFHQTLTKLQDGVVLTTEDITIRKQAEILQAFLLTLSDHLGQMVDDLLDVSRISQGKIQLKKKCLDLGQLVEQALESIRAVANPEVRS
>NZ_CP051677.1|WP_169552317.1|4673485_4673863_+|VOC-family-protein
MNKVTGLGGIFFKCDDPTLMNEWYARHLGLPVAEYGTLFKWRDAHDPSKERTTVWATFDKDTSYFAPSTKDFMISYRVEQLEELVEELKRAGVTVVDEIAEYDYGKFVHILDPEGNSIELWEDVA
>NZ_CP051677.1|WP_169552316.1|4673016_4673298_+|helix-turn-helix-transcriptional-regulator
MIGNLVEAPPLTELAQLVGMSLSKLKRLFRQVFGCGPYGYYQTMRMNEAASLLREKRLSVSEVGYALGFSNLSHFSRVFEEHIGMKPKKFSAS
>NZ_CP051677.1|WP_169552315.1|4672321_4672990_+|hypothetical-protein
MDRQLTAIDGDNFLDAFAQTVGSSVENGRVTIPPPYGSGYVMGFLFGSHLRLLVRHYALHDDLLIKRQSVNLPDSMIQIGISGILKEEQSEDVAGGTPKRALPSVTISTHGLDTEVHIPRGVRFNLIKLAVDPAYLRELLAGEAENLVLKTLLDNRQPLVFEELVSLRLQEIVLDMMDRPIPASLQRFFYKVKAEELICCLLMELVQRQDHSLPFTQSTRLI
>NZ_CP051677.1|WP_169552314.1|4671356_4672214_-|SDR-family-oxidoreductase
MIVITGATGSIGSELCRLLAADNTPCRAIYRKESQQPFFDALELEAVRADFDDIDSMRRAMQDCTNLFLLTAPDQRHVEREIVMIRLAVESGVQHIVKVSTANTNQSSALAYARSHAQIDHYLRGQPIDWTILRPTGFMQNFIEYAHPIGKGILPHMLGDGQISYIDLRDIALVARHVLTQPGHANATYYLTGPAALTVSDVAAELTAGLGHPVRAVNQSEADTRQALIYAGLDAWYTDALIEQFRIGANGGEIDTTGEVARLTGRAPRTLRQFVRDYKNQFTNQ
>NZ_CP051677.1|WP_169553445.1|4670919_4671318_-|acetyltransferase
MITLVALWTTVGSYIFDWNDTHIYNPAWPPHARFHNAQTMLLGTVIGLTAGWVLWVPKANALYRLQVASALASYYWITQAGSLLFPGTALVDPQFAYPGQPPAQLIVDAVTLVLLTIGFVLERDRLKRNPQL
>NZ_CP051677.1|WP_169552323.1|4681432_4682521_-|efflux-RND-transporter-periplasmic-adaptor-subunit
MKNKLSLLLISLTLLTACSPDKAETGEGAEKVFRLSDTMMRRIKLDSVVTRPVRSELTLVGKVMADENRVIKVFPLVGGDVEAVNVELGDYVRKGQALASIRSGEVADLERQGIQARSDLLLAEKNLRVAQDLFETKLNSQREVVAAQKEVEKAQADVNRVSAVSRIYGIGKSSMYTVKAPIDGYVIEKNVNRGTQLRSDNADNLFTIGQISDVWVLANVNESDIGRVRTGMDASIQTLSYPNDLFRGKVDKIYSVLDPNTKAMTVRIRLPNPGSKLKPEMHATVTLRYEDGGQLATVPAQSVIFERSKQYVMVFRDRTNIETREVTVLKSLGDVAYIRQGVQPGERIISNDQLLIFNALNK
>NZ_CP051677.1|WP_169552324.1|4682790_4684059_-|TolC-family-protein
MRLLIALFFLTLTIPRLSLARTLPPADSLPLTLRQADSLFLRNNLLLLAERFRIDASQAQVLQAGLYDNPTATLELSTYNPETRRVPDIGRQGQKIVSVQQLLYTAGKRNKRVALASEATRLTEYELLDLLRSLRFDLRSRFYAIYFQQQTLSRFDQQINTLQTTVSAYEVQYGRNNVSLRELLRLKALLFELNNQRTAIRFQLADGQQQLQTLLSITTPVRPVVTDATLTRYRLPTLPDDSLRQQALRSRPDLRAAESLTRQAELNHTLQRALAVPDLRVGGTYDQAGSYVPNYVGLSVSADLPVFNRNQGAIRAAKSQIGYQRELQRQRAIQITNEVDAVLAKVREVEGRMQTMEPQFTDQFEQLNRGVVVSFQKGNLSLIEFVDLIEAYNDSVQQLNRLKADRVSAYEELNYLVGQELF
>NZ_CP051677.1|WP_169553446.1|4684191_4685391_-|MFS-transporter
MNTDTTVLPDAVTKARTATQLVFLVCGLGMASWAPMVPFAKDRLGLDDATLGLLLLLLGAGAMVMMPTSGWLVSRLGSRVVIAGAALLMALTLPLLMVLTSPAAMAVTLFLFGAGVGAIDVAMNAHGVQVQNLYGRPIMSSLHGLFSVGGLFGSLGLGFLVRMGLNPLYAISSIAALMVLIVLTQYNQLFPANTERQVMARFAEDTGQSTAEKTRFGWLKGSVLFLGMMCFAVFLSEGAILDWSAIYLRDTKGVDPTLAGTGYAAFSVAMAIMRLVGDKLVARLSGKAVVVGGSLLGAAGLAMAVLVPGTYGALAGFVLLGLGVANIVPIFFSAAGRLPGVAPTVSIPAITTIGYTGLLTGPALLGFIAQQFSLSVALGFVSVLLILVALSYQLKGQTN
>NZ_CP051677.1|WP_169552325.1|4685635_4685947_+|DUF1206-domain-containing-protein
MVVADKVKDKSIQGIEWLARGSYLAKGILYGTIGVFTLELAFGPHSADPNRKEVLTQLTGNTMGHLLLALMVLALAGHTLWRIVEIWNDPYDKGWGRGASCTA
>NZ_CP051677.1|WP_169553447.1|4685874_4686459_+|DUF1206-domain-containing-protein
MAHRGNLERPLRQGLGPWGILYRLNYLLSGITYASLGITAFRLLTGQGSGPDDAKKLWVTRLLQIDGGDWLIITVGVILLIWAGLQAYKGVSGKVYKSLELPQESNRYVCAFLRFCSFAGFLTVAGTLTVTGWYLIKGALKKDPDWIRGTDDLLKAMEHFPGGWGVQLAAALGFLLMSVFMLAMARWFPLKAVD
>NZ_CP051677.1|WP_169552326.1|4686682_4687258_-|cupin-domain-containing-protein
MQRANFLKASLATATLLASPFVWAADTLKRYRVDKGFKVDAGKDRFNQAISLFDGDTFMTKVSTKDTNGDLYVYESRRVKEGGPALHVHFEQDELWYVLEGEFLIKVGDVIHQVKAGDTVFGPRNVPHCFAKVGSGEGRLLMTFQPAGKMEECFQQISAGVLKTMNEAQQDAFREAHGFKRVGPPINQLKQ
>NZ_CP051677.1|WP_169552327.1|4687503_4688871_-|HAMP-domain-containing-histidine-kinase
MTIRNRIALQFSLIVASILIVFSVVIYVVSATYRREEFYDRLKNKGRTTVRFLVEVKEVDRDLLKIIDRNTLTALFNEKVLVFDQHNRLIYSSVDDQVIDYSPALLAEVRREKDIETHSGSNELVGLLYRQNGRDLVILASAYDEFGRSKLENLQLTLGWGLFVGISITIGLGIFFAGQSLRPISQLNEQVTTITAGNLQQRLDEGNRQDEIARLAINVNDLLRRLQRAFEQQRSFVSQTSHELRTPLAALKSEIQLGLLHPLTVAEHETILQNLLSDADRLIGLTNSLLQLARTLETIDLLPLHPIRTDDSLFAARDELTTARPSYQIAIDYGNIPESETETLVAGNEELLKQVFSNLLDNACKYSADHTARVRISTDATHCRIAVSDRGIGMTEAEIARIFEPFYRAETALGYPGFGIGLSITARLIDLHHGTLTVESAPGQGSTFTVSLPHL
>NZ_CP051677.1|WP_169552328.1|4688867_4689563_-|response-regulator-transcription-factor
MKKILIIEDDRRIAQNISRGLQQEGYATEVVYEGINGRQMALQPGIDLLILDINLPGINGFEVCRSVRAERPHLPIILLTALDEIDDKVEGLALGADDYLVKPFDFRELIARVATCLRRSALLGDVADPAETILQLANLTVDLARKEVRRNNTTIDLTAREFALLEYLLRNRGRVLSKPDIAEAVWDLNFDTGTNVVEVYINYLRKKIDRDFEPKLIHTRPGMGYVLKEEA
>NZ_CP051677.1|WP_169552329.1|4689610_4691029_-|hypothetical-protein
MPFWLRSNQWGAVPLAGSAGTIRAGIWGDHNGNAPDSTTTRPKFGWNYGLDVVANSGLNGKVLLPEAYAGIRFGKFELFAGRRRQIVGLCDTLLTSGSYIWSGNALPLPKIQFGTIGYVPIFKGVLAFNAIYNHGWFANKDASGRELIVRNSYLHQKTLYVRLGKPSWAFRLYGGVNHQVQWGGYAPSLPSGLANKGYLPSSLRAYQYVVSAQAYPDFTIDPNLTEIDVDNRVGNHLGSIDVGADVNIGSFNLLMYRQSLVESGSIFYLTSIADGLNGIRLRNNQPGDGFLTLDNVLFEFFYSKSQGGPEFVINDPQRRGKVNYFNHGQYQDGWIYENHTIGTPFLTPQTDVRPNLRTGRAIVNNRVALWHGGLSGRVAQRVQWQMKLSYSQNLGTYDSPYPANTNQFSGILSASSPLTLPVLGDCDLSASVAYDQGQLFYNSTGVFASLRKTVRMRRQPSSASSEWRVPTR
>NZ_CP051677.1|WP_169552330.1|4691456_4691894_+|MarR-family-transcriptional-regulator
MHKNYRNEHQRLIGNLHRTDGYIFNHFSQKLAPFDLSVQQYIVLRLLSYEYPNSLSAGELKERMTDMNSDVTRLTDRLVAKNLIVREIDPQNRRRVNLRLTEESKQFVDTVAVEFSDFESIVSHLTDDEVTTLNTLLDKIRNKPQ

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Crispr_ID: NZ_CP051677_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP051677_7

5551946-5552039

Orphan

Consensus_repeat	Method
AATCAAAAAATCAAAAAAATCACAGTTCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP051677_7

>merge|NZ_CP051677|7|5551946-5552039|CRISPRCasFinder
AATCAAAAAATCAGGGAAATCAAAAAATCAAAAAAATCACAGTTCAGACAATCGGCAATCAGCGGAATCAGTAAATCAGAAAAATCATAGTTCA

>NZ_CP051677|7|6|5551946-5552039|CRISPRCasFinder
AATCAAAAAATCAGGGAAATCAAAAAATC	AAAAAAATCACAGTTCAGACAATCGGCAATCAGCGG
AATCAGTAAATCAGAAAAATCATAGTTCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051677.1\|WP_169553049.1\|5553372_5555778_+\|LysM-peptidoglycan-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|381615
NZ_CP051677.1\|WP_169553040.1\|5545407_5545800_-\|GxxExxY-protein	unknown	unknown	gnl\|CDD\|275083
NZ_CP051677.1\|WP_169553046.1\|5550411_5551764_+\|magnesium-transporter	unknown	unknown	gnl\|CDD\|225148
NZ_CP051677.1\|WP_169553053.1\|5565306_5565684_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169553056.1\|5566833_5567040_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169553039.1\|5544746_5545220_-\|nucleoside-triphosphate-pyrophosphohydrolase-family-protein	unknown	unknown	gnl\|CDD\|212137
NZ_CP051677.1\|WP_169553041.1\|5546075_5546651_-\|MarC-family-protein	unknown	unknown	gnl\|CDD\|225006
NZ_CP051677.1\|WP_169553042.1\|5546688_5547720_-\|alanine--glyoxylate-aminotransferase-family-protein	unknown	unknown	gnl\|CDD\|223153
NZ_CP051677.1\|WP_169553043.1\|5547819_5548242_-\|type-II-3-dehydroquinate-dehydratase	unknown	unknown	gnl\|CDD\|376496
NZ_CP051677.1\|WP_169553054.1\|5565766_5566342_+\|DUF3109-family-protein	unknown	unknown	gnl\|CDD\|378636
NZ_CP051677.1\|WP_169553037.1\|5543114_5543441_-\|BrnT-family-toxin	unknown	unknown	gnl\|CDD\|225481
NZ_CP051677.1\|WP_169553052.1\|5560500_5560872_+\|DUF3471-domain-containing-protein	unknown	unknown	gnl\|CDD\|371817
NZ_CP051677.1\|WP_169553050.1\|5558810_5559197_+\|response-regulator	unknown	unknown	gnl\|CDD\|381099
NZ_CP051677.1\|WP_169553044.1\|5548366_5549272_+\|site-specific-tyrosine-recombinase-XerD	unknown	unknown	gnl\|CDD\|274043
NZ_CP051677.1\|WP_169553038.1\|5543492_5544740_-\|peptidase-T	unknown	unknown	gnl\|CDD\|235484
NZ_CP051677.1\|WP_169553055.1\|5566400_5566802_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051677.1\|WP_169553051.1\|5559590_5560448_+\|ThuA-domain-containing-protein	unknown	unknown	gnl\|CDD\|377643
NZ_CP051677.1\|WP_169553045.1\|5549602_5550415_+\|16S-rRNA-(adenine(1518)-N(6)/adenine(1519)-N(6))--dimethyltransferase-RsmA	unknown	unknown	gnl\|CDD\|234708
NZ_CP051677.1\|WP_169553047.1\|5552085_5552538_+\|D-tyrosyl-tRNA(Tyr)-deacylase	unknown	unknown	gnl\|CDD\|235383
NZ_CP051677.1\|WP_169553048.1\|5552644_5553286_+\|O-methyltransferase	unknown	unknown	gnl\|CDD\|226607

Protein	Function_ID	Function_description	E-value
NZ_CP051677.1\|WP_169553049.1\|5553372_5555778_+\|LysM-peptidoglycan-binding-domain-containing-protein	gnl\|CDD\|381615	cd16894, MltD-like, Membrane-bound lytic murein transglycosylase D and similar proteins. Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).	2.48957e-43
NZ_CP051677.1\|WP_169553040.1\|5545407_5545800_-\|GxxExxY-protein	gnl\|CDD\|275083	TIGR04256, conserved_hypothetical_protein, GxxExxY protein. Members of this protein family average about 130 residues in length and include an almost perfectly conserved motif GxxExxY. Members occur in a wide range of prokaryotes, including Proteobacteria, Perrucomicrobia, Cyanobacteria, Bacteriodetes, Archaea, etc.	9.65416e-53
NZ_CP051677.1\|WP_169553046.1\|5550411_5551764_+\|magnesium-transporter	gnl\|CDD\|225148	COG2239, MgtE, Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism].	2.45209e-109
NZ_CP051677.1\|WP_169553039.1\|5544746_5545220_-\|nucleoside-triphosphate-pyrophosphohydrolase-family-protein	gnl\|CDD\|212137	cd11530, NTP-PPase_DR2231_like, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs. This family includes a MazG-like NTP-PPase from Deinococcus radiodurans (DR2231), a putative NTP-PPase YP_001813558.1 from Exiguobacterium sibiricum and their bacterial homologs. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It can hydrolyze dUTP into dUMP. DR2231-like proteins contain a well conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for the all-alpha-helical NTP-PPase superfamily. Unlike normal dimeric dUTPase-like proteins with a central four-helix bundle forming the active site, YP_001813558.1 displays a very unusual interlaced segment-swapped dimer. It potentially prefers to hydrolyze dCTPs or its derivatives. YP_001813558.1-like proteins contain a variant divalent ion binding motif, EXXEX(12-28)AXXD.	5.74786e-29
NZ_CP051677.1\|WP_169553041.1\|5546075_5546651_-\|MarC-family-protein	gnl\|CDD\|225006	COG2095, MarC, Multiple antibiotic transporter [Intracellular trafficking and secretion].	1.15381e-24
NZ_CP051677.1\|WP_169553042.1\|5546688_5547720_-\|alanine--glyoxylate-aminotransferase-family-protein	gnl\|CDD\|223153	COG0075, COG0075, Serine-pyruvate aminotransferase/archaeal aspartate aminotransferase [Amino acid transport and metabolism].	1.37233e-30
NZ_CP051677.1\|WP_169553043.1\|5547819_5548242_-\|type-II-3-dehydroquinate-dehydratase	gnl\|CDD\|376496	pfam01220, DHquinase_II, Dehydroquinase class II.	1.9563e-84
NZ_CP051677.1\|WP_169553054.1\|5565766_5566342_+\|DUF3109-family-protein	gnl\|CDD\|378636	pfam11307, DUF3109, Protein of unknown function (DUF3109). This bacterial family of proteins has no known function.	1.6604e-109
NZ_CP051677.1\|WP_169553037.1\|5543114_5543441_-\|BrnT-family-toxin	gnl\|CDD\|225481	COG2929, COG2929, Uncharacterized protein conserved in bacteria [Function unknown].	6.73656e-12
NZ_CP051677.1\|WP_169553052.1\|5560500_5560872_+\|DUF3471-domain-containing-protein	gnl\|CDD\|371817	pfam11954, DUF3471, Domain of unknown function (DUF3471). This presumed domain is functionally uncharacterized. This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 98 to 114 amino acids in length. This domain is found associated with pfam00144.	9.13407e-07
NZ_CP051677.1\|WP_169553050.1\|5558810_5559197_+\|response-regulator	gnl\|CDD\|381099	cd17546, REC_hyHK_CKI1_RcsC-like, phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC. This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	3.35e-32
NZ_CP051677.1\|WP_169553044.1\|5548366_5549272_+\|site-specific-tyrosine-recombinase-XerD	gnl\|CDD\|274043	TIGR02225, Tyrosine_recombinase_XerD, tyrosine recombinase XerD. The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This model represents XerD, one of two closely related chromosomal proteins along with XerC (TIGR02224). XerC and XerD are site-specific recombinases which help resolve chromosome dimers to monomers for cell division after DNA replication. In species with a large chromosome and with homologs of XerD on other replicons, the chomosomal copy was preferred for building this model. This model does not detect all XerD, as some apparent XerD examples score below the trusted and noise cutoff scores. XerC and XerD interact with cell division protein FtsK. [DNA metabolism, DNA replication, recombination, and repair].	9.05882e-126
NZ_CP051677.1\|WP_169553038.1\|5543492_5544740_-\|peptidase-T	gnl\|CDD\|235484	PRK05469, PRK05469, tripeptide aminopeptidase PepT.	0
NZ_CP051677.1\|WP_169553051.1\|5559590_5560448_+\|ThuA-domain-containing-protein	gnl\|CDD\|377643	pfam06283, ThuA, Trehalose utilisation. This family consists of several bacterial ThuA like proteins. ThuA appears to be involved in utilisation of trehalose. The thuA and thuB genes form part of the trehalose/sucrose transport operon thuEFGKAB, which is located on the pSymB megaplasmid. The thuA and thuB genes are induced in vitro by trehalose but not by sucrose and the extent of its induction depends on the concentration of trehalose available in the medium.	4.75426e-70
NZ_CP051677.1\|WP_169553045.1\|5549602_5550415_+\|16S-rRNA-(adenine(1518)-N(6)/adenine(1519)-N(6))--dimethyltransferase-RsmA	gnl\|CDD\|234708	PRK00274, ksgA, 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase RsmA.	3.07512e-102
NZ_CP051677.1\|WP_169553047.1\|5552085_5552538_+\|D-tyrosyl-tRNA(Tyr)-deacylase	gnl\|CDD\|235383	PRK05273, PRK05273, D-tyrosyl-tRNA(Tyr) deacylase; Provisional.	1.10744e-85
NZ_CP051677.1\|WP_169553048.1\|5552644_5553286_+\|O-methyltransferase	gnl\|CDD\|226607	COG4122, COG4122, Predicted O-methyltransferase [General function prediction only].	3.88952e-57

>NZ_CP051677.1|WP_169553046.1|5550411_5551764_+|magnesium-transporter
MTFELTQDYLDQLHAYIEAGDDERLRAEMEELYPADISEILNELDAEQAHYLLSLLDESVGAEILANLDTADRTDFLKTFTSEQLAPLVNEMDSDDAVDMLNEQPIQVREEVIGLLEDREQARFIIDLLHYDDGVAGSLMQKELIKINVNLTVNACIEEIRQQAEDVENVYAIYVVDDQGKLLGLVSLKKIVLSQKYVKIADIYDDDIVFVETYRPVDEVAELMQKYDLDAIPVVNVQQRLLGRITIDDVVDVITEQAEEDRQVISGLAGEVEEDDSVWLRSKVQLPWLVAGAVGSLMAATVINGFQSELGKIAALAAFIPIIGSTGGNVGIQTSSLILQSLADTSGLTTTLGRRLLRTLAVALINGLVVGLIAGTYTFLIGEPRLFFVVATSLLSVVLLASFMGTVTPLLLSKTGINPAVASGPFITTANDLIGIGVYFLIAQWLLSEL
>NZ_CP051677.1|WP_169553045.1|5549602_5550415_+|16S-rRNA-(adenine(1518)-N(6)/adenine(1519)-N(6))--dimethyltransferase-RsmA
MSVKPKKELGQHFLIDLSIAQDIASLLTGHAGPGQAPYREILEIGPGMGVLTQFLLQDNRFDTYVIEIDRESVEYLNQHFPALSGRILPSDFLNIRPDLLPTKQPDSTTPFAVIGNFPYNISTQILFKVLDMRDRVPELVGMFQREVAQRVASGPGNKDYGILSVLLQAWYDIKYEFTVPPDVFNPPPNVFSGVISLKRNDKTELGCNERKFTQVVKHGFSQRRKTLRNALKPLNPTEAALASPFMNKRAEQLSVADFVQLTNLMQQADQ
>NZ_CP051677.1|WP_169553044.1|5548366_5549272_+|site-specific-tyrosine-recombinase-XerD
MWQSYINAFKNYLRLERSLAGNSVEAYLHDAEKLYQYILLTDPARTPMDVSERELMGFLVYLGELGLTAHSQARILSGLKSFFKYLLLEGLIQHDPTQLLEAPKLGRKLPDTLSFPEIEAILDTIDLSTPGGTRDRAMLEVLYSSGLRVSELLGLRLTNCYFDEGFVRVLGKGDKVRLVPIGQDAMHYTRIYVNHVRSQLDVQKGDEDTIFLNLRGKHLSRISVFTTIKKLADLVGIQKNISPHTFRHSFATHLIEGGADLRAVQQMLGHESITTTEIYTHLDRDYLRQTLREFHPRAQKK
>NZ_CP051677.1|WP_169553043.1|5547819_5548242_-|type-II-3-dehydroquinate-dehydratase
MKQILIINGPNLNLLGKREPGIYGSQSFEAYFETLQASFPDVQLTYFQSNHEGALLDKIHDFGFDGDGIVINAGAYTHTSVAIGDALAAITAPTVEVHISNVHARESFRHHSYLSAKSKGVIVGLGLMGYELAIRYLIDL
>NZ_CP051677.1|WP_169553042.1|5546688_5547720_-|alanine--glyoxylate-aminotransferase-family-protein
MITFYPGPSKVYPQVADYAAQAVRDGIVSMNHRSPGFMAIVERAFALLREKLALPADYHIALVSSATECWEIVAQSLTASTSLHPSGGAFGDKWREYAHKIKPMIAPNLADTLCVVQNETSNGTQVSMDTLAGFRRDFSALIAVDAVSSMAGIAFDWILADVWFASVQKCFGLPAGLAVLIYSPAALKRAQAIGENDHYNSLLFLHENFSKFQTPYTPNGLGIYCLMRVLEQVPPIAEVDALTRQHAAEWYTFFERDMADSRFRLLIPPTTPERPATRSDTVIAVSGSEADISAVKKAAQQAGIMLGNGYGNWKNTTFRIANFPAITQAERDQLRDFLRSYRP
>NZ_CP051677.1|WP_169553041.1|5546075_5546651_-|MarC-family-protein
MFNFREIISVTLILFSVIDIVGSLPVIIDLRKKVGKIESEQATFASGALMVSFLFVGERILKLFGVDVASFAVAGGLIIFLIGLEMILGRTIFKSEVEAGGATHIVPIAFPLIAGAGTLTTIISLRAEYQTLNIIVGIVINLMLIYIVLKSSEWLEARMGPGGLAVLRKIFGIILLAISIKLIKTNLIPGF
>NZ_CP051677.1|WP_169553040.1|5545407_5545800_-|GxxExxY-protein
MINERYKYSELTGLIIGCAMEVHRRLGNGFQEVIYQRALAIELTEASIPYRRELEMPIFYKDHNIGSRRVDFYIDDCVSVELKAIIQLEDVHLAQAINYLEAYNLEVGLLINFGARSLQHKRVVNRKKDR
>NZ_CP051677.1|WP_169553039.1|5544746_5545220_-|nucleoside-triphosphate-pyrophosphohydrolase-family-protein
MQSPDSLNQVAQFHHTFHAPVLDSPQIPDAGRCQLRVALLAEELDELREAIDAQDIVAVADALCDLQYVLSGAVLEFGLGDRFKALFDEVQRSNMSKACQTVEEAEATVAQYRSKGVDCHYTESAGTYLVFRDADRKTLKSVNYSPADLETILNENA
>NZ_CP051677.1|WP_169553038.1|5543492_5544740_-|peptidase-T
MTDYPYTVVDRFLRYVQIDTQSDPQSKTNPSTEKQKDLSRVLVEELLAMGVADAELDEWGYVYATIPANTDKPDVPTICFCSHVDTSPDVTGAGVKPIIHASYDGSDLVLPDDPAQVIRASDHPDLAQQLGNDIITASGTTLLGADNKAGVAEIMDATNYLLTHPDVKHGRIRLLFTPDEEVGRGTEKVDMAKLGAQYGYTIDGESLGTLEDETFSADAVSIQIHGVSTHPGFAKGKLENALKIAADLLALLPKDHLSPETTEDRQGFIHPTRMEGNQDKATVEFIIRDFTEVGLQEKETYLQNQLNEVLKQYPGSSATLTVHQQYSNMKQVLDDHPAVVENALEALSRAGLSARQRSIRGGTDGSRLSFMGLPCPNIFAGEHAFHSRQEWVSVQDMQHAVDVIVNVAQVWEERG
>NZ_CP051677.1|WP_169553037.1|5543114_5543441_-|BrnT-family-toxin
MILFQWDDGNTKHILRDYPERDNSISEVESVFADPFVMIKEVRSSNDGEARFQAVGLSNRFRVCSVVFVVRNSQIRPISCWPSKAKVRNQYAENTEKRKQEASGRNQK
>NZ_CP051677.1|WP_169553047.1|5552085_5552538_+|D-tyrosyl-tRNA(Tyr)-deacylase
MIAVIQRVSRASVTIDKQVKGQIGAGFLVLLGVTHADTPDDVEWLSRKIVGMRVFGDADDKMNLDLASIGGSILLISQFTLHASTKKGNRPSFVEAARPEVAIPLYEAMIRQLSADLGRPIQTGEFGADMKVELLNDGPVTIVIDTKNRI
>NZ_CP051677.1|WP_169553048.1|5552644_5553286_+|O-methyltransferase
MDFLPADLTAYAETHTSPESTLLQQLNRNTRAQVMAPRMLSGHLQGRLLSMIAHMIRPRRILEIGTYTGYSALCLAEGLTDDGLLITLEQNEELEDFARSYWQQSPLGAKIDLRIGSAADIIPALDETFDLVFIDADKRNNQLYYELIFDKLRPGGFILADNVLWSGKVVAPVKTNDTDTKTVLAFNQLVQNDPRVENILLPIRDGIMLIRKR
>NZ_CP051677.1|WP_169553049.1|5553372_5555778_+|LysM-peptidoglycan-binding-domain-containing-protein
MLKRTPFLFFILWLTAAFTMAQTPAPNVPDRLTFADISVRLDDNARRIVQQDVNSLLANRQYWTAKLDRVALYFPIIEAILIQEDVPTDFKYLAVQESSLTPDAVSSSAAVGYWQFKRETATGLGMRVDEGVDERKSITASTHGAAQYMKRSNAQFNNWIASLYSYYLGAGGIAKLIPPDWAYAREIALDGRTDRYILRFFAHKLAIENALKSHQTSNRIALLEYPGSANKTFKEVADELSVDEFELRKYNRWLTDEAVPADKDYVMVVPVPTDQINDVRQKIVSVTPRKAADAGQIDVGFPVLRRVTTGLKDDPFLYEINGLPGIQAQAGDNAATLARKSKISMSSFLRYNDLDESDPIIVGDVYYLAKKRKKALVPFHTVRAGETARSISQRYGLRLKRLLRYNRVDRTLKLATGRVMWLRERRPASKPVEIINAPTPAVYDQTPTPPARTDIADGSLQPTRTVAGGNSVPRTMAERKKYQPKLVGGGVTPNDGTSQPAAPQPAIEVQSLGGDGWSTGSTGSGMSKKKTPRTTPAGTTVSQPAGADGSQRLVIVRTPTGDAGQPETRAVPVATTPERTQPVSAAPAAVEKPASKPTASVEMSAPVRATKPKSVSDDDLQPAEPRTVSRPATPKPESRPAEPVVVKSTPEPKPAPAEPAPISRPATPVDRSATTHIVEPKETYYSIARMHGLTVDELLTINGLTANDPLPAGKKLSLKATGAGTTTPKAQTPKPTVGSAAPASGAAASSAKTVYHTVGKGETMYRISRDYGVTVQQIQEWNSLTDTNVKEGQKLKIEKSE
>NZ_CP051677.1|WP_169553050.1|5558810_5559197_+|response-regulator
MRNDLSDTRILLVDDNPLNLMLIRKLVTKWGASVDTAENGEKAVELSRDGTANRLPYQAIIMDLQMPVMDGATACQLIRQFDSSVAILASSATALPQAELDASGFTGSVVKPFESAQLRQQLLSILSE
>NZ_CP051677.1|WP_169553051.1|5559590_5560448_+|ThuA-domain-containing-protein
MKKGLKIALWSLLGLVVLLFVAGGLFLYKVKNGFPVSYETDRPAINFPANKPAVLLFSKTTGFRHGESIDASKPVFQQLAQRNGWFVYETEEGGVFTPEQLKQFKAVVFDNSTGRVLNDEQQQALSEYVEAGGSLVGIHGSGDDSHHWPWYETNLLGAKFSHHPLNPQLQQADVHVNANVDSTLTRRLPASWKHTDEWYVFFTQPRGVRVVSYIDGDKIIPSGNVLFIKDKNFGMGHNHPVAWYRTVGRGKTFYTSMGHNAAVWQDTDFVQLLTNALQWAMASPK
>NZ_CP051677.1|WP_169553052.1|5560500_5560872_+|DUF3471-domain-containing-protein
MKSIVFTLACALSLTTLYAAPHTAPAPIKPPVYRADSIDLNQYVGKYKFEGLPFEFVTIAVKDGQLTIDTGSEAGAMTPIKNTLDAFDAAGRATLTFKRDDTRKVTGVTLDAQGRSFEGKKEN
>NZ_CP051677.1|WP_169553053.1|5565306_5565684_+|hypothetical-protein
MELSQVVRHDNRLEATWTSVCTFLRQYSLGMSKQYGTVFESLTRAATPFGGNVLAGAYKQSRTRMYLSQQEIREQVERLTREITQLNTRVASMDTPAQSQPTTAHQTQTVGIDRFRQESPNTPAA
>NZ_CP051677.1|WP_169553054.1|5565766_5566342_+|DUF3109-family-protein
MILIDNTCISDDIAEKFFVCNLDKCKGACCVEGDMGAPLEGDEPAILDRIYPDIKPFLSPEGIAEIERRGGGYEPDGEGGYVTNTINNRECVYATWDERGILKCGIEEAYNHGKVDWKKPISCHLYPIRVTKYESFHALNYDRWPICSPACGFGEQLNVPIYKFVREALVRAYGAPWYDQLTKAIEEKEVQ
>NZ_CP051677.1|WP_169553055.1|5566400_5566802_-|hypothetical-protein
MASLLCPSSTARPGAALFGVQTATGQIEYLDEPVIIDQTFVDKARQGRAPEERFRFASNCAKSGCGHWDSGQAGCSLVGKIVDAMNRKADDTLVACAIRTNCRWYHQEGARACASCDEVVRNVRTQETLALAG
>NZ_CP051677.1|WP_169553056.1|5566833_5567040_-|hypothetical-protein
MKNQITDKIDALKSEAVSQEAFMNQLAQLDEQGQANPELLDQVNGGIAANQLPFPVLGLWLDPDTIKF

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP051677_6	6.1\|4681345\|32\|NZ_CP051677\|CRISPRCasFinder	4681345-4681376	32	NZ_LR594664	Variovorax sp. RA8 plasmid 3	277376-277407	7	0.781

1. spacer 6.1|4681345|32|NZ_CP051677|CRISPRCasFinder matches to NZ_LR594664 (Variovorax sp. RA8 plasmid 3) position: , mismatch: 7, identity: 0.781

atttccgg--gcgaagcgagttgctgtcgcatct	CRISPR spacer
--ctcaggccgcgatgcgagtggctgtcgcatcc	Protospacer
  .** **  **** ****** ***********.

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

1298708 : 1309864

Pseudomonas_phage(50.0%)

holin

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_169549825.1\|1298708_1300370_+\|holin	choline dehydrogenase	A0A1V0S9J5	Catovirus	5.3e-65	33.2
WP_169549826.1\|1300364_1301477_-	hypothetical protein	A0A125RNN9	Pseudomonas_phage	1.5e-23	30.4
WP_169549827.1\|1301529_1302711_-	hypothetical protein	A0A125RNN9	Pseudomonas_phage	1.6e-18	25.3
WP_169549828.1\|1302719_1304165_-	MBOAT family protein	A0A125RNP0	Pseudomonas_phage	1.0e-67	36.1
WP_169549829.1\|1304436_1305474_+	SGNH/GDSL hydrolase family protein	NA	NA	NA	NA
WP_169549830.1\|1305591_1306227_-	hypothetical protein	NA	NA	NA	NA
WP_169549831.1\|1306270_1306900_-	MgtC/SapB family protein	G3MA03	Bacillus_virus	4.1e-18	43.9
WP_169549832.1\|1306984_1309864_+	excinuclease ABC subunit UvrA	A0A1B1IVR3	uncultured_Mediterranean_phage	1.9e-219	42.6

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage

2. NZ_CP051678

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP051678_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP051678_1

121159-121255

Orphan

Consensus_repeat	Method
GTTTGAGCCTCACCTTCTAATACCTTACT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP051678_1

>merge|NZ_CP051678|1|121159-121255|CRISPRCasFinder
GTTTGAGCCTCACCTTCTAATACCTTACTGGAAATCAAAAATACGCAGGGCCTGCTCAACGAGCGGAAGTTTGAGCCTCATCTTCTAATACCTTACT

>NZ_CP051678|1|1|121159-121255|CRISPRCasFinder
GTTTGAGCCTCACCTTCTAATACCTTACT	GGAAATCAAAAATACGCAGGGCCTGCTCAACGAGCGGAA
GTTTGAGCCTCATCTTCTAATACCTTACT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP051678.1\|WP_169553593.1\|116661_117768_+\|FecR-family-protein	unknown	unknown	gnl\|CDD\|377406
NZ_CP051678.1\|WP_169553597.1\|125675_126260_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274376
NZ_CP051678.1\|WP_169553701.1\|114708_115569_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_CP051678.1\|WP_169553702.1\|127368_127824_-\|DUF305-domain-containing-protein	unknown	unknown	gnl\|CDD\|367619
NZ_CP051678.1\|WP_169553590.1\|111907_113026_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051678.1\|WP_169553603.1\|138683_139595_+\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP051678.1\|WP_169553599.1\|128246_128453_-\|copper-chaperone	unknown	unknown	gnl\|CDD\|270194
NZ_CP051678.1\|WP_169553592.1\|115996_116332_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP051678.1\|WP_169553699.1\|109890_111420_-\|TolB-family-protein	unknown	unknown	gnl\|CDD\|223893
NZ_CP051678.1\|WP_169553596.1\|122889_125391_+\|glycoside-hydrolase-family-2-protein	unknown	unknown	gnl\|CDD\|225789
NZ_CP051678.1\|WP_169553598.1\|126588_126966_-\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319911
NZ_CP051678.1\|WP_169553600.1\|128707_129256_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|237125
NZ_CP051678.1\|WP_169553601.1\|130410_130623_+\|transposase	unknown	unknown	gnl\|CDD\|379098
NZ_CP051678.1\|WP_169553588.1\|105897_106809_-\|TonB-family-protein	unknown	unknown	gnl\|CDD\|367555
NZ_CP051678.1\|WP_169553700.1\|113022_113655_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224054
NZ_CP051678.1\|WP_169553591.1\|114114_114669_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP051678.1\|WP_169553602.1\|130911_131094_+\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|222853
NZ_CP051678.1\|WP_169553595.1\|121267_122725_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|185760
NZ_CP051678.1\|WP_169553698.1\|108683_109196_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378331
NZ_CP051678.1\|WP_169553589.1\|107332_108217_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP051678.1\|WP_169553593.1\|116661_117768_+\|FecR-family-protein	gnl\|CDD\|377406	pfam04773, FecR, FecR protein. FecR is involved in regulation of iron dicitrate transport. In the absence of citrate FecR inactivates FecI. FecR is probably a sensor that recognizes iron dicitrate in the periplasm.	2.20814e-17
NZ_CP051678.1\|WP_169553597.1\|125675_126260_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	6.53645e-24
NZ_CP051678.1\|WP_169553701.1\|114708_115569_+\|alpha/beta-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	8.43461e-30
NZ_CP051678.1\|WP_169553702.1\|127368_127824_-\|DUF305-domain-containing-protein	gnl\|CDD\|367619	pfam03713, DUF305, Domain of unknown function (DUF305). Domain found in small family of bacterial secreted proteins with no known function. Also found in Paramecium bursaria chlorella virus 1. This domain is short and found in one or two copies. The domain has a conserved HH motif that may be functionally important. This domain belongs to the ferritin superfamily. It contains two sequence similar repeats each of which is composed of two alpha helices.	1.40564e-11
NZ_CP051678.1\|WP_169553599.1\|128246_128453_-\|copper-chaperone	gnl\|CDD\|270194	cd14675, PH-SEC3_like, PH-like domain of Sec3-like protein. Fungal Sec3, as well as its homolog in higher eukaryotes Exocyst complex component 1 (EXOC1) are part of the exocyst is a conserved octameric complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.	0.0071378
NZ_CP051678.1\|WP_169553598.1\|126588_126966_-\|VOC-family-protein	gnl\|CDD\|319911	cd07247, SgaA_N_like, N-terminal domain of Streptomyces griseus SgaA and similar domains. SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.	4.89277e-06
NZ_CP051678.1\|WP_169553699.1\|109890_111420_-\|TolB-family-protein	gnl\|CDD\|223893	COG0823, TolB, Periplasmic component of the Tol biopolymer transport system [Intracellular trafficking and secretion].	9.73918e-33
NZ_CP051678.1\|WP_169553596.1\|122889_125391_+\|glycoside-hydrolase-family-2-protein	gnl\|CDD\|225789	COG3250, LacZ, Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].	7.26131e-66
NZ_CP051678.1\|WP_169553600.1\|128707_129256_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|237125	PRK12519, PRK12519, RNA polymerase sigma factor; Provisional.	2.42377e-23
NZ_CP051678.1\|WP_169553601.1\|130410_130623_+\|transposase	gnl\|CDD\|379098	pfam13276, HTH_21, HTH-like domain. This domain contains a predicted helix-turn-helix suggesting a DNA-binding function.	2.85067e-09
NZ_CP051678.1\|WP_169553588.1\|105897_106809_-\|TonB-family-protein	gnl\|CDD\|367555	pfam03544, TonB_C, Gram-negative bacterial TonB protein C-terminal. The TonB_C domain is the well-characterized C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance.	1.77956e-07
NZ_CP051678.1\|WP_169553700.1\|113022_113655_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	3.25787e-35
NZ_CP051678.1\|WP_169553591.1\|114114_114669_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	3.94011e-05
NZ_CP051678.1\|WP_169553602.1\|130911_131094_+\|IS3-family-transposase	gnl\|CDD\|222853	PHA02517, PHA02517, putative transposase OrfB; Reviewed.	9.07789e-13
NZ_CP051678.1\|WP_169553595.1\|121267_122725_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|185760	cd08977, SusD, starch binding outer membrane protein SusD. SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.	2.19735e-35
NZ_CP051678.1\|WP_169553698.1\|108683_109196_+\|hypothetical-protein	gnl\|CDD\|378331	pfam09970, DUF2204, Nucleotidyl transferase of unknown function (DUF2204). This domain, found in various hypothetical archaeal proteins, has no known function. However, this family was identified as belonging to the nucleotidyltransferase superfamily.	0.00314466
NZ_CP051678.1\|WP_169553603.1\|138683_139595_+\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	1.65809e-43

>NZ_CP051678.1|WP_169553593.1|116661_117768_+|FecR-family-protein
MQYKDALYQQLLEDQRFVRWATGEAPQDDEHWKNWAREDSSRLDTMELARQTLLAIQGGPVDLSQADIDYQIQRALYTAKQREMQTRIPVGREHRLARFNWVAAASLLFLLGFGWYGYLNRTTLTRSLSVKKTQPTTDPLLVSNRLQCVANTDRPARHVLLPDGSSVVLYKNSQVSYAFAFNGPRREVYLSGEAFFEVTKDPAKPFFVYADGLVTKVLGTSFTVKAHQQAEQVIVVVRTGKVAVFAQADPTADAIRTNLELTGLVLTPNQQATFERTNAHLSRTETDAPTGQPSFEFRATPAADVFAALEKAYGVTIRFDRDVMAHCSLSATLGDEPLQQKLQWICTILEATYQVKDQQISITGKPCQ
>NZ_CP051678.1|WP_169553592.1|115996_116332_-|hypothetical-protein
MKLRSADQVKPVFKWKNSAKFGALNADAQWFSMLRSTKMGRVGRQRVAAWEAQNLPMAIREATAPIAGGRTLLVVGAAHKPFIEAYLHSFTDVEIVSAPALLASQPVDCLN
>NZ_CP051678.1|WP_169553701.1|114708_115569_+|alpha/beta-hydrolase
MDNELVKRLPGFTSHYLTVNDVQLHYIIGGQGEPLVLLPGWPQTWWSYHKIMPTLVDRYQVIAVELRGMGSSDKPMGGYSKKVMASDVAALLDQLGIGRSSIAGHDIGAAVAFSFAAHFPHKTKKLILLDTPHPDENMYRLPMLPTGLGLHPWWVAFNQVRHLPEQLLENRFHLVQDWLFDQLLVDKTAVSSFDRQVYAQAYASQDAIRASNGWYQAFAEDIDDIKGKRIEVPTMGIAGPAGFELFSYALPPYVDQLTLKEVKGSGHFVQEERPLETSEFIRDFLS
>NZ_CP051678.1|WP_169553591.1|114114_114669_+|TetR/AcrR-family-transcriptional-regulator
MKDTRQALIQAAVVALNSDESATIEHIADQAGVTRRTVHRYFNDRNTLLQECKQTMLRVCNHSMITAYQSSQQPAVQLENMFYAALEVGIQYSFVKKVAKRQQYADLLDNQELAYDDVKTNWFKLVEQLQQQGAISSKLSIPWIYNLFGGMVDIAIEAHQAGDVARNDIKSFSWASFKGSIGLQ
>NZ_CP051678.1|WP_169553700.1|113022_113655_-|ATP-binding-cassette-domain-containing-protein
MLHLHAFRKAHHQHLVLQIDAFTIRPGVYWLRGRNGSGKSSLLTALAGITAFEGNVHLDQVSLRQQPVAYRRLVNFAEAEPIFPPFLTGTELIQLVKAAKQAPAHQEVFYLDSMGMNDYVNQPVGSYSSGMLKKLSLVLAFLGQPRCLLLDEPLTTLEVDALPVLYDWIARLSQQTQAVVLLSSHQPLEAGGLLTGPAIVVAQTTIRFTA
>NZ_CP051678.1|WP_169553590.1|111907_113026_-|hypothetical-protein
MSRPLTRVLINVIAADFYRQHTGLLLSLFILLVSNFFYTSVLNQTHLTQPQIIQHALKLVLTSVSEPLGVVILVGICWLYCHKCWQYVTGRLHRPDVYFLRYTATALPRRRQHQSWAWVQLIMMLPLWSIGLFASVIGFRFGHWLVPTLLPLYLSGLVGYSGWRYSRLLDAPTQQPSPGKLDWFRGWPKPFFSLFLYELVLNRRLSYGLAKLASFASIGLAYSILANDLTGLRLVGLLSVCSAVSHAMLLYQSREFERFYLRFGRNLPYSRWQVFGQQGAQLGVLLLPELLGLVGVGGLADGLWAGSLLLGLSLLFRSLLYRLGSQSVVYLRWVFGLFIGCLVGLLFDLTVWLALGSVVIAGALSYYYDEQV
>NZ_CP051678.1|WP_169553699.1|109890_111420_-|TolB-family-protein
MKPTWLIYLISLLLSGPGCSHAQSPKLGLFTGHQDIGKVHQPGAARYDARTHQYHMAGSGYNVWFDHDEFQFMYKPINGDFILYARAALLGNGVDPHRKVGWMVRSSLDTNSAHINAVVHGDGLTSLQYRPTTGANTQEIRATITHADVIQLERKGTTYTMRVAKFGEPFVTQQVTDLALGEQVYVGLFISSHNKDVLEQGVFRDVRISVPAPESLVPYRQYLASNLEILDVTTGTRQLIYTNPNSIQAPNWTPDGKTLLYNSQGLMYRFDLAKRTPKVLPTGAVTNNNNDHVLSFDGQLLGLSSGVSERGGSVIYTVPVRGGTPTLITPQGPSYLHGWSPDKRHLVFTGSRQDEYDIYRVPSAGGPEVRLTQAKGLDDGPEYSPDGQYIYFNSARTGTMQLYRMKADGSEQQALTNGEYQDWFPHVSPDGKWLVFLSFLKEEVKADDHPFYKHVYLRLLPVSGQGQPRVIAYVYGGQGTINTPSWSPDSRRVAFISNTAEGSLSLVEQ
>NZ_CP051678.1|WP_169553698.1|108683_109196_+|hypothetical-protein
MGYSTDIKIFSTLQKYDVDYLIIGGTAVSFYGEYRKSRLANGQVVETADYDFWYNPNLGNYYRLLSAVEELGKDVARYRDETPDPKKDVFKFEFEEENYTIDFLPHIMVPISFREAFERRTMVERDGIVAYFIGLDDLINDKQALGRQKDFDDIDNLRKHNPDSFPPPHP
>NZ_CP051678.1|WP_169553589.1|107332_108217_+|hypothetical-protein
MLSEAMPGEQVMGLEAYAAYHGNAGQYGGPTLEMAKTAQVQLQLSAAQALVRADSLVAKGNLSPAQRRQLAVWFVAAAEPFSATVQWLRLAPAERIAEDGVSASLVKRLNRFAGLRSELTSIAARLAADVGLERLYGAGDHASDVSLPASADMAAAVAAEPGLTDLFNHRTAAFAAVPEDTMKLRSAAQVMPLFKWKNSDKFGALDADAQWFSMLRSTKMGRLGRQRVAAWEAQNLQMAVAVREATAPIAGGRALLIVGAAHKPFIEAYLRSFTDVEIVSVPALLNSRTGDCPN
>NZ_CP051678.1|WP_169553588.1|105897_106809_-|TonB-family-protein
MVDCRLIWCIIALLCPVLPSLGQADKQALITQLDAIAQDDQRYRNDSLRQTTTSQQEDDANMAKQAVLDRFNLTKIERIIARYGYPGRSLVGEQRQAIAFLVIQHSELETQEKYLPLLTEAAAKGELKAASLAIFTDRVRVGRGQKQLYGSQLRETKQGVKVMPIEDEAQVNQRRAAVGLAPLEDYLRHWHIVYQVPTADHANPDSVYYKSVVTAPASVDLIGGWSNLYQRIVCPPTEKGLKGSVTVQLTVDKNGLPKDLQVVRSLGAAYDKEALRVLGQARFVNPLGEDHEIRTNLPFSCSR
>NZ_CP051678.1|WP_169553595.1|121267_122725_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKRTLLCLLLTLAGCTNYLDEVPQGQVVGTNAIQDVAGLEAALTGTYKGMLRTWARGFLTSALEAYVMGADDVTSLSGGNKAEFRQTDQFDVVSSNSRLAQIWSGCYKTIQGANNIITNYKTVSGDQTTINAIVGEAYFLRALGYYWLVRGYGNIPLVTSADFTNDLLTLQKSAPADIYKLIESDLLQAEQLVPNTKRDAGRPNKGSVKALLADVYLTEGGWPIKDASKYALAATKAKEVIDNKTTYGFDLVPDLATLWSGTPASVGTSEEIFSFQTSVNYGGSANAFYGSSATPGDENGWDDFFAEVGFFNRFPAGKRKDITFYTEFTKSDGTTISWQNSQSKHPYYRKFRLADNTNYQSSMPVHMIRYAHVLLVYAEAQARSGNSVSTDAYTAVNAVRKRAGLADLTGLSATNFAAAVVDERAWEFAGEWTRWFDLQRLEQVEAANAPDKKGADDLKPLKSITKANYWYPVPIGDANINPNL
>NZ_CP051678.1|WP_169553596.1|122889_125391_+|glycoside-hydrolase-family-2-protein
MKQLVLLLGVMGTLTGRAQQASLVWPSAVNSTARTQLFDQDWRFLRDSVPGAEQPSYQDDTWRRLTLPHDWSIEDLPPQQAGTVAGPFARSSAGATSTGYAVGGTGWYRKTFTLPPATGAKRVSVRFDGVYRNADVWLNGHHLGFHPYGYTPFVYDLTPYLRHPGQPNSLAVRVRNGGQNTRWYTGSGIYRHVWLTIAESIHVAPWGITVTTPQVSDSAAQVQVRTVVVNQGSIAAPVTVQVLLQTADGRVVNSTRKTATVAAAGRTDVTQTLTLAQPKRWSVETPYRYRAVVTIRQGSRTVDSLSTPFGVRTIHFNAQTGFTLNGKRVWLKGGCVHHDNGPLGAVALDRAEERKVELLKANGFNAVRSSHNPPSPAFLDACDRLGMLVIDEAFDMWQRPKKPDDYHLDFDAWWERDLTAMIERDRNHPAVILWSVGNEISERADSSGLAITRKLVDAVHRLDPTRPTTEAICRFWEYPGTPWEASAKAFALLDIGGYNYEWKHYESDHRQAPNRIMVGTETFAKEAYENWQQVETHPYVIGDFVWTALDYMGETAIGHSLLQPRTDKDSLAAVLPWPWFNAFCGDLDLIGTKKPQSYYRDVVWRNSPVEMAVHVPIPDGMKETVTSWGWPDERQSWTWSGPDGSGLDGSGFGAAGKPLQVRVFTRSQKVRLLLNGKHVGEQSLPDSSIVVVFTVPYQPGTLEAISLNDGQETGRVSLTTASSPHRIRLTADRPTLRADQQDLSFLTAEVVDAQGRVVPDAALPLTFQVSGAGSLAAVGSGNPTDMASFQQPTRTTYRGRCLAVIRATATKGSITVRASAAGLVPAEVTLSTQ
>NZ_CP051678.1|WP_169553597.1|125675_126260_+|sigma-70-family-RNA-polymerase-sigma-factor
MDDQALWQLLRTGSEEAYSVLAQRYYAKLVHYGQKFTPNRQLVEDALQDLLIRLWLGRQRLSDTPSVKFYLLKAFRHQLFKTLNKSLRHSEVEEADMAELMVFSVEDQYIELESDLRFTSELTERLTHLPTRQREVIYLRFFQGLTIEEIADLLVIQTQSVSNLLQRALTNLRSSWFITTPVILALAYRLIPLL
>NZ_CP051678.1|WP_169553598.1|126588_126966_-|VOC-family-protein
MGKVIGLGGIFFTCDDPQAINQWYAYHLGLPVAEYGTLFKWRDTNNPSQERTTVWATFGKDTGYFAPSPKEFMINYQVDQLESLVEQLKRDGVAVIDEITVYEQGKFVHILDPEGNKIELWEEIN
>NZ_CP051678.1|WP_169553702.1|127368_127824_-|DUF305-domain-containing-protein
MTKGNYTRFFLMLGVSFVVMHLTMYLNTEQADHLYLSVNRLYMTTLMISSMSLIMLGFMRSMYRNVRLNQLIVTGSVGLFVAALVGVRNQTFIDDKLFMHSMIPHHSIAILVSKRANLKDPEVKQLAQNIIDAQEREIAQMKRILARLETK
>NZ_CP051678.1|WP_169553599.1|128246_128453_-|copper-chaperone
METLNFKTNIQTSNDVAAVTQPLNDIEQVDGWNLNTDSPDFLLTVQTTDNRIADQVEEAIRKRVLRLL
>NZ_CP051678.1|WP_169553600.1|128707_129256_-|sigma-70-family-RNA-polymerase-sigma-factor
MFADKSELELIKQISLGDQVAFGHLYRRYRRALLHSITLIVKEPMAAEDALHDTYLKVWQKATSYDPQRGGVYNWLLNLARNTAIDTLRHRNRLDQLELTEANTAELFTQWPSVEDIGLRFYIDQRLTSRQRHLLELRYWQDQTLSDIAGQLTLPLGTVKTTLRQTLRMLRPLLAADYALSR
>NZ_CP051678.1|WP_169553601.1|130410_130623_+|transposase
MKQRQLLADIRQIRTQSQGRYGSPCIADELREQGVKASRNRVALLMCQAAIHSIMYKKYWVQATDSRHDI
>NZ_CP051678.1|WP_169553602.1|130911_131094_+|IS3-family-transposase
MKGLPVVQSMTGPPAGRKGNCWDNAVAKSFFKTFKSELVNHVAFQTRAEARLATFEYIEG
>NZ_CP051678.1|WP_169553603.1|138683_139595_+|HAMP-domain-containing-histidine-kinase
MENPPTQQPYENDPVNRHLIRLEQMNQELIQQITNCRQELDQAQSALGEARIVLAQRYRLEVEQDRLLTQERGLNELKSNFITLASHEFRTPMMTILSSASLIGRYSGSEEGDERERHVQRIKAAVNSLTTMLNDFLAISQIDQYVPDSSTQSLDVTALCREVIMAVQTTAKPQQRFHYQPQTGPLQLQLDRQLLERILVNLLTNASKYSPDDTDIQLTSTIWNRRVLFTVADQGIGIPDSDKDRLFTHFFRSRNANHMQGVGLGLYLAKRYAELLGGSITFTSKLEQGTTFTVELPLLTGRA

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP051678_1	1.1\|121188\|39\|NZ_CP051678\|CRISPRCasFinder	121188-121226	39	NZ_CP051678	Spirosoma sp. CJU-R4 plasmid unnamed1, complete sequence	121188-121226	0	1.0

1. spacer 1.1|121188|39|NZ_CP051678|CRISPRCasFinder matches to NZ_CP051678 (Spirosoma sp. CJU-R4 plasmid unnamed1, complete sequence) position: , mismatch: 0, identity: 1.0

ggaaatcaaaaatacgcagggcctgctcaacgagcggaa	CRISPR spacer
ggaaatcaaaaatacgcagggcctgctcaacgagcggaa	Protospacer
***************************************

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site	Prophage annotation

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP051677

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NZ_CP051678

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection