CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP016348	Vibrio natriegens strain CCUG 16371 chromosome 2, complete sequence	0 crisprs	csa3,DEDDh,cas3	0	0	1	0
NZ_CP016347	Vibrio natriegens strain CCUG 16371 chromosome 1, complete sequence	2 crisprs	cas3,RT,DinG,csa3,csx1,DEDDh	1	1	3	0

Results visualization

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CRISPR-Cas detection and classification

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

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

113970 : 122108

Bacillus_virus(33.33%)

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_014235081.1\|113970_114822_-	ATP-binding cassette domain-containing protein	G3M9Y6	Bacillus_virus	4.4e-31	36.9
WP_020335006.1\|114851_115883_-	taurine ABC transporter substrate-binding protein	G3M9Z0	Bacillus_virus	1.8e-07	27.7
WP_065300593.1\|116098_117514_-	aminotransferase class III-fold pyridoxal phosphate-dependent enzyme	A0A1V0SKB7	Klosneuvirus	2.4e-21	24.5
WP_065303164.1\|117693_119169_+	PLP-dependent aminotransferase family protein	A0A1X9I5H2	Streptococcus_phage	1.2e-15	26.9
WP_065303165.1\|119361_120087_+	TSUP family transporter	NA	NA	NA	NA
WP_065303166.1\|120106_120883_+	SDR family NAD(P)-dependent oxidoreductase	F2NZ12	Diadromus_pulchellus_ascovirus	2.6e-06	29.8
WP_065303167.1\|121412_122108_+	ABC transporter ATP-binding protein	G9BWD6	Planktothrix_phage	1.6e-23	30.4

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_CP016347

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP016347_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016347_1

2620518-2620849

Orphan

Consensus_repeat	Method
TCTTCAGCATCACGTTTCGCTTTTTCTTCAGC	CRISPRCasFinder

4 spacers

The CRISPR arrays of NZ_CP016347_1

>merge|NZ_CP016347|1|2620518-2620849|CRISPRCasFinder
TCTTCAGCCTTACGCTTAGCTTCTTCTTCCTGACGACGTTTAAGCTCGTCGGCCTCTTTTCGCGCTGCTTCTTGCTTAATTTTCTCTTCAGCATCACGTTTCGCTTTTTCTTCAGCTTCACGTTGTGCATTCGTATCAACGTCTCGTTTCGCTTTTTCTTCAGCTTCACGTTTCGCTTTTTCTTCAGCGTCACGTTTCGCTTTTTCTTCAGCTTCACGTTTTGCAGCTTCTTCAGCTTCACGCTTTGCGGCTTCTTCAGCTGCGCGTTTTGCTGCTTCTTCTGCTTCACGTTTTGCCGCTTCTTCAGCGTCACGTTTCGCTTCATCTTCAAT

>NZ_CP016347|1|1|2620518-2620849|CRISPRCasFinder
TCTTCAGCCTTACGCTTAGCTTCTTCTTCCTG	ACGACGTTTAAGCTCGTCGGCCTCTTTTCGCGCTGCTTCTTGCTTAATTTTC
TCTTCAGCATCACGTTTCGCTTTTTCTTCAGC	TTCACGTTGTGCATTCGTATCAACGTCTCGTTTCGCTTTT
TCTTCAGCTTCACGTTTCGCTTTTTCTTCAGC	GTCACGTTTCGCTTTTTCTTCAGCTTCACGTTTTGCAGCT
TCTTCAGCTTCACGCTTTGCGGCTTCTTCAGC	TGCGCGTTTTGCTGCTTCTTCTGCTTCACGTTTTGCCGCT
TCTTCAGCGTCACGTTTCGCTTCATCTTCAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016347.1\|WP_020333900.1\|2610488_2611367_+\|U32-family-peptidase	unknown	unknown	gnl\|CDD\|237968
NZ_CP016347.1\|WP_065302838.1\|2626426_2628406_-\|ATP-dependent-zinc-metalloprotease-FtsH	unknown	unknown	gnl\|CDD\|182683
NZ_CP016347.1\|WP_065297335.1\|2624179_2625520_-\|phosphoglucosamine-mutase	unknown	unknown	gnl\|CDD\|236787
NZ_CP016347.1\|WP_014232894.1\|2629655_2630129_-\|transcription-elongation-factor-GreA	unknown	unknown	gnl\|CDD\|234693
NZ_CP016347.1\|WP_014232888.1\|2623614_2623953_-\|preprotein-translocase-subunit-SecG	unknown	unknown	gnl\|CDD\|235881
NZ_CP016347.1\|WP_005456065.1\|2622699_2623155_-\|ribosome-maturation-factor-RimP	unknown	unknown	gnl\|CDD\|234627
NZ_CP016347.1\|WP_014232886.1\|2621175_2622663_-\|transcription-termination/antitermination-protein-NusA	unknown	unknown	gnl\|CDD\|236410
NZ_CP016347.1\|WP_014232882.1\|2616568_2616838_-\|30S-ribosomal-protein-S15	unknown	unknown	gnl\|CDD\|180170
NZ_CP016347.1\|WP_065302834.1\|2611421_2612768_-\|MATE-family-efflux-transporter	unknown	unknown	gnl\|CDD\|236576
NZ_CP016347.1\|WP_014232875.1\|2606416_2606944_-\|SCP2-domain-containing-protein	unknown	unknown	gnl\|CDD\|225696
NZ_CP016347.1\|WP_065302839.1\|2630663_2631686_+\|porin	unknown	unknown	gnl\|CDD\|225744
NZ_CP016347.1\|WP_014232881.1\|2614099_2616235_-\|polyribonucleotide-nucleotidyltransferase	unknown	unknown	gnl\|CDD\|236995
NZ_CP016347.1\|WP_065302837.1\|2625540_2626374_-\|dihydropteroate-synthase	unknown	unknown	gnl\|CDD\|183230
NZ_CP016347.1\|WP_014232877.1\|2609454_2610468_+\|U32-family-peptidase	unknown	unknown	gnl\|CDD\|223896
NZ_CP016347.1\|WP_014232884.1\|2617930_2618326_-\|30S-ribosome-binding-factor-RbfA	unknown	unknown	gnl\|CDD\|234787
NZ_CP016347.1\|WP_065302833.1\|2607296_2609336_+\|bifunctional-diguanylate-cyclase/phosphodiesterase	unknown	unknown	gnl\|CDD\|236645
NZ_CP016347.1\|WP_014232883.1\|2616986_2617931_-\|tRNA-pseudouridine(55)-synthase-TruB	unknown	unknown	gnl\|CDD\|235333
NZ_CP016347.1\|WP_065302835.1\|2612983_2613901_-\|lipoprotein-NlpI	unknown	unknown	gnl\|CDD\|236875
NZ_CP016347.1\|WP_005380066.1\|2629282_2629579_+\|ribosome-assembly-RNA-binding-protein-YhbY	unknown	unknown	gnl\|CDD\|182393
NZ_CP016347.1\|WP_014232893.1\|2628514_2629144_-\|23S-rRNA-(uridine(2552)-2'-O)-methyltransferase-RlmE	unknown	unknown	gnl\|CDD\|183025

Protein	Function_ID	Function_description	E-value
NZ_CP016347.1\|WP_020333900.1\|2610488_2611367_+\|U32-family-peptidase	gnl\|CDD\|237968	PRK15447, PRK15447, putative protease; Provisional.	0
NZ_CP016347.1\|WP_065302838.1\|2626426_2628406_-\|ATP-dependent-zinc-metalloprotease-FtsH	gnl\|CDD\|182683	PRK10733, hflB, ATP-dependent zinc metalloprotease FtsH.	0
NZ_CP016347.1\|WP_065297335.1\|2624179_2625520_-\|phosphoglucosamine-mutase	gnl\|CDD\|236787	PRK10887, glmM, phosphoglucosamine mutase; Provisional.	0
NZ_CP016347.1\|WP_014232894.1\|2629655_2630129_-\|transcription-elongation-factor-GreA	gnl\|CDD\|234693	PRK00226, greA, transcription elongation factor GreA; Reviewed.	1.06832e-79
NZ_CP016347.1\|WP_014232888.1\|2623614_2623953_-\|preprotein-translocase-subunit-SecG	gnl\|CDD\|235881	PRK06870, secG, preprotein translocase subunit SecG; Reviewed.	6.78181e-25
NZ_CP016347.1\|WP_005456065.1\|2622699_2623155_-\|ribosome-maturation-factor-RimP	gnl\|CDD\|234627	PRK00092, PRK00092, ribosome maturation protein RimP; Reviewed.	3.52252e-81
NZ_CP016347.1\|WP_014232886.1\|2621175_2622663_-\|transcription-termination/antitermination-protein-NusA	gnl\|CDD\|236410	PRK09202, nusA, transcription elongation factor NusA; Validated.	0
NZ_CP016347.1\|WP_014232882.1\|2616568_2616838_-\|30S-ribosomal-protein-S15	gnl\|CDD\|180170	PRK05626, rpsO, 30S ribosomal protein S15; Reviewed.	4.02139e-54
NZ_CP016347.1\|WP_065302834.1\|2611421_2612768_-\|MATE-family-efflux-transporter	gnl\|CDD\|236576	PRK09575, vmrA, MATE family efflux transporter.	0
NZ_CP016347.1\|WP_014232875.1\|2606416_2606944_-\|SCP2-domain-containing-protein	gnl\|CDD\|225696	COG3154, COG3154, Putative lipid carrier protein [Lipid metabolism].	2.72884e-66
NZ_CP016347.1\|WP_065302839.1\|2630663_2631686_+\|porin	gnl\|CDD\|225744	COG3203, OmpC, Outer membrane protein (porin) [Cell envelope biogenesis, outer membrane].	4.7926e-48
NZ_CP016347.1\|WP_014232881.1\|2614099_2616235_-\|polyribonucleotide-nucleotidyltransferase	gnl\|CDD\|236995	PRK11824, PRK11824, polynucleotide phosphorylase/polyadenylase; Provisional.	0
NZ_CP016347.1\|WP_065302837.1\|2625540_2626374_-\|dihydropteroate-synthase	gnl\|CDD\|183230	PRK11613, folP, dihydropteroate synthase; Provisional.	2.63369e-154
NZ_CP016347.1\|WP_014232877.1\|2609454_2610468_+\|U32-family-peptidase	gnl\|CDD\|223896	COG0826, COG0826, Collagenase and related proteases [Posttranslational modification, protein turnover, chaperones].	1.22731e-112
NZ_CP016347.1\|WP_014232884.1\|2617930_2618326_-\|30S-ribosome-binding-factor-RbfA	gnl\|CDD\|234787	PRK00521, rbfA, 30S ribosome-binding factor RbfA.	1.08353e-51
NZ_CP016347.1\|WP_065302833.1\|2607296_2609336_+\|bifunctional-diguanylate-cyclase/phosphodiesterase	gnl\|CDD\|236645	PRK10060, PRK10060, cyclic di-GMP phosphodiesterase.	6.13392e-112
NZ_CP016347.1\|WP_014232883.1\|2616986_2617931_-\|tRNA-pseudouridine(55)-synthase-TruB	gnl\|CDD\|235333	PRK05033, truB, tRNA pseudouridine synthase B; Provisional.	0
NZ_CP016347.1\|WP_065302835.1\|2612983_2613901_-\|lipoprotein-NlpI	gnl\|CDD\|236875	PRK11189, PRK11189, lipoprotein NlpI; Provisional.	4.43714e-168
NZ_CP016347.1\|WP_005380066.1\|2629282_2629579_+\|ribosome-assembly-RNA-binding-protein-YhbY	gnl\|CDD\|182393	PRK10343, PRK10343, ribosome assembly RNA-binding protein YhbY.	1.27415e-41
NZ_CP016347.1\|WP_014232893.1\|2628514_2629144_-\|23S-rRNA-(uridine(2552)-2'-O)-methyltransferase-RlmE	gnl\|CDD\|183025	PRK11188, rrmJ, 23S rRNA (uridine(2552)-2'-O)-methyltransferase RlmE.	4.15765e-155

>NZ_CP016347.1|WP_014232884.1|2617930_2618326_-|30S-ribosome-binding-factor-RbfA
MSKEFSRTQRVSQQLQKELAMILQREVRDSRLGMVTISDVEVSRDLAYAKVFVTFLCVGEQTPESCLAALREHEVHIRMMLGKRIRLRLTPEIRFHYDNTLVEGMRMSNLVSEVVSADKQKQKDSGREDEE
>NZ_CP016347.1|WP_014232883.1|2616986_2617931_-|tRNA-pseudouridine(55)-synthase-TruB
MARRRKGRPINGVILLDKPTGISSNDALQKVKRIYFAEKAGHTGALDPLATGMLPICLGEATKFSQFLLDSDKRYRVIAKLGERTNTSDSDGEVVETRPVDVDLEKLEACIDKFRGESDQVPSMFSALKYQGKPLYEYARKGIEVPRESRKITVYEIILHRFEGDEVEMEVHCSKGTYIRTIVDDLGEMLGCGAHVTMLRRTGVAKYPYEKMVTLEQLNELLEQAHRQEVAPRELLDPLLMPMDTAVEDLPEVNLIPELADMVQHGQPVQVSGAPTEGSLRLTMGEERLFIGVGEMNNDGKIAPKRLVVFRDEE
>NZ_CP016347.1|WP_014232882.1|2616568_2616838_-|30S-ribosomal-protein-S15
MSLNAETKAAIVAEYAQSEGDTGSPEVQVALLTASINHLQGHFKAHKGDHHSRRGLLRMVSRRRKLLDYLKGKNLARYQDLIKRLGLRR
>NZ_CP016347.1|WP_014232881.1|2614099_2616235_-|polyribonucleotide-nucleotidyltransferase
MFEKPVVKTFQYGNHTVTLETGVIARQATAAVMVTMDDTAVFVSVVGKKEAVAGQDFFPLTVNYQERTYAAGKIPGGFFKREGRPSEGETLTARLIDRPIRPLFPDAFKNEVQVIATVVSVNPDVQPDIPTMIGTSAALAISGIPFNGPIGAARVGHIDGQLVLNPSQTELDASRLDLVVAGTESAVLMVESEADNLTEEEMLAAVVYGHDQQQVVINAINEFKAEVATPAWDWVAPEENTVLKNKIAELAEAKLVEAYQITEKMARYDRIHAIAAEVNEVLLAEDPEADTKEIHTIFHDLEKTVVRRSIIAGNPRIDGREKDMVRALDVRTGILPRTHGSALFTRGETQAIVTATLGTQRDAQIIDELTGERKDHFLLHYNFPPYCVGETGFVGSPKRREIGHGKLAKRGIAAVMPSVDEFPYTVRVVSEITESNGSSSMASVCGTSLALMDAGVPIKSSVAGIAMGLVKEGDDFVVLSDILGDEDHLGDMDFKVAGTNTGVTALQMDIKIEGITKEIMQIALNQAQGARKHILSVMDEAISGARDDISEFAPRIHTMKISAEKIKDVIGKGGAVIRALTEETGTTIEIEDDGTIKIAATEGAAAKEAIRRIEEITAEVEVGRIYTGKVARLADFGAFVTVLPGKDGLVHISQIAEKRVEKVSDYLTEGQEVQVKVLEIDRQGRVRLSMKEAVEKPAEEAAAEAPAAKDE
>NZ_CP016347.1|WP_065302835.1|2612983_2613901_-|lipoprotein-NlpI
MKWFQTASLCVAIVLTGCANTSQQSAMQWVYPPMAVPLQPSVQQEVQIARLSQLLQRPDLSDEVRAKMHYERGNYYDSVGLRDLARLDFNQSLQLNPAQPDIFNLLGVYFTQVGEFDAAYEAFDSTLELAPDNTYAERNRAIALYYGGRIELALEDMNKHYEEMPSDPFRALWLYIIEAEQDPEQAKVNLKKHYKRDRSEEWGWVLVAIMLRDVSDEQALKLIMDGTRENYRLAERLTETYFYLGKRHQLQGDLASAISLYKLAISFNVYDYVEHRYSFLELAQIYEQLQQDRMAKLKAEQQPDN
>NZ_CP016347.1|WP_065302834.1|2611421_2612768_-|MATE-family-efflux-transporter
MQGSIYRQFWKYTIPTVAAMLVNGLYQVIDGIFIGRYVGADGLAGINVAWPVIGTILGVGMMVGVGTGALVSIKRGEQDQDGAKRILSTGLLLLAALMPVVATVLFYFSDDFIRWQGAQGQVYELGLQYLQILIVSCIFTLGSIAAPFLLRNDDSPNLATILMVTGAAINISLDYVFIAWLGWELTGAAIATALAQMVVTVLGIGYFFSSKAKLRLRFSDLQIQFEFVPKVVMIGSSSFFMYAYGSIMVALHNSLFAQYGSALLIGAYAILGYIVTVYFLVAEGIANGMQPLVSYNHGARNPQNIRKLLKIAMGTAVLGGFAFVTLLNVFPYEVVSVFNSSDQQLIESAVMGIRFHMFALFLDGFLMVSAAYYQSMNKGSKAMFITVGNIMVQLPFLFIMPKIFGVVGIWIAFPLSNIALSLVVMSMLWRDVKKLLSESPVEPSMQSS
>NZ_CP016347.1|WP_020333900.1|2610488_2611367_+|U32-family-peptidase
MKYALGPLLYFWPKQDVEAFYQEAKESTADIIYLGETVCSKRREMKPAHWFDIAKELSAAGKQVVLSTMALLEAPSEVNIMKKYIDNGDFAIEANDVSAVQLASEHRVPFVVGPAINTYNAHTLNLFLKQGMTRWCMPVELSRDWLRDTLAQCESLGIRNKFEVEVFSHGYLPLAYSARCFTARAENRAKDDCETCCIKYPTGIQVSSQEGQEVFNLNGIQTQSGYCYNLINDLPGMQGLVDVVRLSPLGISTLSELDQFRANEQGEKPQKLEDRQCNGYWHQLAGLDVKNI
>NZ_CP016347.1|WP_014232877.1|2609454_2610468_+|U32-family-peptidase
MELLCPAGNLPALKTAIDCGADAVYIGFKDDTNARHFAGLNFHGKKLEKAVQYVHDRNKKIHVALNTFAHPNGFERWTNAVDNAASLGVDALIVADIAVLEYAARKYPELELHLSVQASATNVAAIEFYKQNFNVKRVVLPRVLSIHQVKQLSRNITSDVELEVFAFGSLCIMSEGRCYLSSYMTGESPNTVGACSPAKYVRWQETEQGLESRLNNILIDRYSEGENAGYPTLCKGRFEAEIEGEKKRYHALEEPTSLNTLSMLPELFAANVASVKIEGRQRSPAYVEQVTRTWRAAIDRYQANPAAYQVEEAWNATLANVSEGTQTTLGAYHRQWQ
>NZ_CP016347.1|WP_065302833.1|2607296_2609336_+|bifunctional-diguanylate-cyclase/phosphodiesterase
MPSQQLQHWFATLTSNSPFFFAILDKKHNYRMVSDRYCDIAGLSNAEIIGLNDVHVLGEQFYKKLAPYYQRAFDGTHIEAEITLDETDLETSLHFSLSPVYEGNEIRHVVFHAVDTSEKQILVRSLEESESKFAKLTQLLPDGLLLIEEDVIISANPASARLLGINSPHDLLGEKLSRLFIDENTKKVFGHPLSTLISDKPFLCLTSARCGFERKVQLHADSTAILGSASQIILIQDADTAPKNLSASLGEDANIDSLTKLYNRFGFTKRLEQLIKKQTPLLLFYLDIDNFKNINDSLGHHIGDKVIQEVSARLKRLLPSQAILGHLGSDEFGILLPEPENARMAEILSDRIISLINQPFDLHHFSKRLACSIGSVRYPEDGQDARILLQNADTAMYEAKDRGRNRLIKFNDQMNKEARMRLWLEIELQKALQQNGLEVWYQPKVNARDFSINGAEALVRWKHPVEGYISPGAFIPVAERAGLIEHLGRVVMRDVFNTVKRWKQQSVLPGRVAINLSPEQFGNPQLIDFMEKLLRTTELDPSCITFELTESAVMSDSEHTLQMLNAIKKLGFALSIDDFGTGYSSLSYLARFPIDELKIDRAFISDIDTLPKQVTVIENIINLGKSLDLSVVAEGVETHQQATLLSNLQCHSIQGFHFYRPQPKHEIEELFVQNRRHKN
>NZ_CP016347.1|WP_014232875.1|2606416_2606944_-|SCP2-domain-containing-protein
MLNKIRSQLVKNAANILRSPVQLLPQTVQKKALLEGLKMIFKEALEDGDFEFLEDKWLKVAIKDLNLAWYISYQDENLLVAEKPVQEDVSFSGNLNDLVLIAGRKEDPDTLFFQRRLSIEGDTELGLEVKNLMDSVDLEQLPKAMQVALNQLADFVQKGVQEPAQQPGVANAYSN
>NZ_CP016347.1|WP_014232886.1|2621175_2622663_-|transcription-termination/antitermination-protein-NusA
MSKEILAVAEAVSNEKAVPRERIFEALEIALATSTKKKYEIEIDVRVAIDRKTGEFVTYRRWLVVDNVENPTKEISLEAAQYDDDSVELGDYVEDEIQSVTFDRITTQTAKQVIVQKVREAERAQIVEQFIDNEGDLITGVVKKVNRDTIVLDLGNNAEAVILRDDQLPRENFRPGDRVRGLLYKVAPEARGFQLFITRSKPEMLAELFRVEVPEIAEDIIELKGAARDPGSRAKIAVKTNDKRIDPVGACVGMRGARVQAVSGELGGERIDIVLWDDNPAQFVINAMAPADVASIIVDEDAHAMDIAVEADNLAQAIGRNGQNVRLASQLTGWELNVMTVADLQKKHAEESQASIENFMKYLDIEEDFAQLLVEEGFSTLEEVAYVPVNELLEVDGLNEELIEELRGRAKDALTTIALAQEESFEGLEPAEDLLGLEGLEREMAFKLAAKGVATLEDLADQGIDDLEGIEGLTEERAGELIMAARNICWFGEEA
>NZ_CP016347.1|WP_005456065.1|2622699_2623155_-|ribosome-maturation-factor-RimP
MTGLERQLTEMLEAPVEASGYELVGLEFIRAGAHSTLRIYIDHENGINVDDCAEVSHQVSAVLDVEDPISVAYSLEVSSPGLERPLFKAAHYEQFIGHEVSIVLKMAVANRRKWKGIIHGVDGETVTVTVEGQQEEFALSNISKANLIPKF
>NZ_CP016347.1|WP_014232888.1|2623614_2623953_-|preprotein-translocase-subunit-SecG
MFTVLLVIYLLAALGVIGLVLIQQGKGADMGASFGAGASNTVFGASGSGNFLTRTTAILATVFFVISLLLGRMSTHKTESQWVDPTLGQPVVEQVKDAASEVPAPAGDEIPQ
>NZ_CP016347.1|WP_065297335.1|2624179_2625520_-|phosphoglucosamine-mutase
MSDKRRYFGTDGVRGKVGQYPITPDFVLKLGWAAGRVLAKQGTKKVIIGKDTRISGYMLESALEAGLAAAGLKATFTGPMPTPAVAYLTQTFRAEAGIVISASHNPYYDNGIKFFSSEGTKLPDDIELAIEAELDKEIECVESAELGKATRLNDAAGRYIEFCKSTFPSTLSLASLKIVVDCAHGATYHIAPNVFKELGAEVIAMGVEPNGTNINDQVGATDVRALQKRVVEEQAHLGLAFDGDGDRIIMVDHLGNKVDGDQIAYIIARDALRRGELKGGVVGTLMTNLGMENGLKQLGIPFVRAAVGDRYVMEQLLAKGWKIGAENSGHVILLDKVTTGDAIVAALQVLASIVGSDMSLHDLSQGMTLYPQVLENVRFSGDANPLEAKAVLDSVAEVEAELGDKGRVLLRKSGTEPLIRVMVEGEDAELVQSSALKIADAVKASF
>NZ_CP016347.1|WP_065302837.1|2625540_2626374_-|dihydropteroate-synthase
MIIKVKNKSLDLSRPHVMAILNVTPDSFSDGGKFNSLDSALARVEKMIKAGVSIIDVGGESTRPGAPEVTLEDELERVIPVVRAIRAHYPDVWISVDTSKAEVIRQSVEAGADLINDIRSLTEPGALEVAAKANVPVCIMHMKGQPKTMQQNPQYDDLMQEVEQFLVERMAVCEAAGIARENIILDPGFGFGKTIEHNYHMLAHLEKFHKFGLPILAGLSRKSMIFKLLDKPAAECTNASVVCATIAAMKGAQIIRVHDFEETLEAMKVVEMTKNNI
>NZ_CP016347.1|WP_065302838.1|2626426_2628406_-|ATP-dependent-zinc-metalloprotease-FtsH
MAKNLILWLVIAVVLMSVFQSFGPGESNGRTVDYTTFVQEVGQGQIQEATFKDGEISFVRRGGGAKMVTYMPVYDQKLLDDLINQNVKVQGTPPEEQSLLGTIFISWFPMILLIGVWIFFMRQMQGGGGKGAMSFGKSKARMMSEEQIKTTFADVAGCDEAKEDVKELVDYLRDPSRFQKLGGKIPTGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAVPCIIFIDEIDAVGRQRGAGVGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRKVPLAGDVEPSLIARGTPGFSGADLANLVNEAALFAARGNKRNVSMVEFELAKDKIMMGAERRSMVMSEETKASTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMYLPEQDRVSMSRQHLESMISSLYGGRLAEELIYGADKVSTGASNDIERATDIARKMVTQWGFSEKLGPLLYAEDEGEVFLGRSVTQTKHMSDDTAKLIDDEVRQIIDRNYDRAKKILQDNMDIMHAMKDALMKYETIDAHQIDDLMERKAEIREPAGWGDNPSNKPQVDDKPQAAPAAKEEEKKADADNDAEQSTSQEAASADAPEKKDSE
>NZ_CP016347.1|WP_014232893.1|2628514_2629144_-|23S-rRNA-(uridine(2552)-2'-O)-methyltransferase-RlmE
MSKQKHSASSGRWLKEHFDDKYANEARKKGYRSRAYFKIDEIQTKDKLLKPGMTVVDLGAAPGGWSQYAAKIVGDSGQIIACDLLPMDPIAGVSFLQGDFRDDAVLDALLERIQPSMVDVVMSDMAPNIAGNNSVDQPRAMYLVELALDMCRQVLAPNGSFVVKVFQGEGFDQYVKEVRDMFKVVKVRKPDSSRARSREVFVVATGYKG
>NZ_CP016347.1|WP_005380066.1|2629282_2629579_+|ribosome-assembly-RNA-binding-protein-YhbY
MNLSTKQKQHLKGLAHSLKPVVLMGANGLTEAVLAEIEIALNHHELIKVKVASEDRETKQLIIDAIVRETGAEKVQTIGKVLVLYRQSEERKIEIPRK
>NZ_CP016347.1|WP_014232894.1|2629655_2630129_-|transcription-elongation-factor-GreA
MEKVPMTLRGEQMLREELDRLLKLRPQISAAIAEARELGDLKENAEYHAAREEQGICEAQIRDIEYKLSVAQVIDVTKMENTGKVIFGTTVTLIDVDTDEEKTYQIVGDDEADIKAGRISVSSPIARGLIGKMEGDEVVIETPGGAKDFEIDRVEYL
>NZ_CP016347.1|WP_065302839.1|2630663_2631686_+|porin
MKKTLIALSVSAAAMATGVNAAELYNQDGTSLEMGGRAEARLSMKDGDASDESRIRLNFLGKQQVSDNLYGVGFWEGEFTTADFDENGKDISGEDSLDTRLAYAGLGGAWGEFSYGKNEGALGVITDFTDIMAYHGNSAADKLAVADRADNMMSYKGQFENLSVKASYRFADRVENANGDFSDNDQDGYSLSAIYAVANTGLELGAGYADQDEANEYMLAASYTMGDLYFAGVFTDGEKMTDTFDGTVDYTGYELAGAYTVGQTVFTTSYNNAETNNETSADNIAIDASYYFKPNFRGYVSYNFNLIDSGDKFGSTTGQNATATKIDAEDELALGLRYDF

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Crispr_ID: NZ_CP016347_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP016347_2

2814664-2814921

Orphan

Consensus_repeat	Method
GTGCCTCCTTAGCTCAGTAGGTAGAGCAACGGACTGATAATCCGC	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP016347_2

>merge|NZ_CP016347|2|2814664-2814921|PILER-CR
GTGCCGACTTAGCTCAGTAGGTAGAGCAACTGACTTGTAATCAGTAGGTCACCAGTTCGATTCCGGTAGTCGGCACCATTCTTTTGCCTCGATAGCTCAGTCGGTAGAGCAGAGGATTGAAAATCCTCGTGTCGGTGGTTCGATTCCGCCTCGAGGCACCATTATTTGGTGCACTTGCTTAATTTAATTGATTAGCAAGACACAAACAGAATAGTTCCTCCTTAGCTCAGTTGGTAGAGCGACGGACTGTTAATCCGC

>NZ_CP016347|2|1|2814664-2814921|PILER-CR
GTGCCGACTTAGCTCAGTAGGTAGAGCAACTGACTTGTAATCAGT	AGGTCACCAGTTCGATTCCGGTAGTCGGCACCATTCTTTTG
CCTCGATAGCTCAGTCGGTAGAGCAGAGGATTGAAAATCCTCGTG	TCGGTGGTTCGATTCCGCCTCGAGGCACCATTATTTGGTGCACTTGCTTAATTTAATTGATTAGCAAGACACAAACAGAATAGTT
CCTCCTTAGCTCAGTTGGTAGAGCGACGGACTGTTAATCCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP016347.1\|WP_065300225.1\|2809493_2810522_-\|DNA-methylase	unknown	unknown	gnl\|CDD\|223971
NZ_CP016347.1\|WP_065302903.1\|2826537_2827212_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP016347.1\|WP_065302902.1\|2824979_2826233_-\|HD-GYP-domain-containing-protein	unknown	unknown	gnl\|CDD\|225116
NZ_CP016347.1\|WP_065302897.1\|2805681_2805972_+\|YggU-family-protein	unknown	unknown	gnl\|CDD\|179931
NZ_CP016347.1\|WP_065303111.1\|2807229_2808405_+\|radical-SAM-family-heme-chaperone-HemW	unknown	unknown	gnl\|CDD\|235550
NZ_CP016347.1\|WP_065302899.1\|2811456_2812533_+\|A/G-specific-adenine-glycosylase	unknown	unknown	gnl\|CDD\|182805
NZ_CP016347.1\|WP_020334002.1\|2806046_2806478_+\|DUF4426-domain-containing-protein	unknown	unknown	gnl\|CDD\|379616
NZ_CP016347.1\|WP_065302900.1\|2812916_2814059_+\|membrane-bound-lytic-murein-transglycosylase-MltC	unknown	unknown	gnl\|CDD\|183271
NZ_CP016347.1\|WP_065302903.1\|2837452_2838127_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP016347.1\|WP_014233043.1\|2812552_2812825_+\|oxidative-damage-protection-protein	unknown	unknown	gnl\|CDD\|180059
NZ_CP016347.1\|WP_065302904.1\|2838265_2839204_-\|bile-acid:sodium-symporter-family-protein	unknown	unknown	gnl\|CDD\|223462
NZ_CP016347.1\|WP_065302898.1\|2806609_2807212_+\|XTP/dITP-diphosphatase	unknown	unknown	gnl\|CDD\|234648
NZ_CP016347.1\|WP_065302901.1\|2815219_2816845_+\|methyl-accepting-chemotaxis-protein	unknown	unknown	gnl\|CDD\|214599
NZ_CP016347.1\|WP_065300231.1\|2840218_2840884_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|187643
NZ_CP016347.1\|WP_065302905.1\|2841062_2842331_+\|DUF2254-domain-containing-protein	unknown	unknown	gnl\|CDD\|378351
NZ_CP016347.1\|WP_014233041.1\|2810533_2811253_-\|tRNA-(guanosine(46)-N7)-methyltransferase-TrmB	unknown	unknown	gnl\|CDD\|234649
NZ_CP016347.1\|WP_065302904.1\|2827350_2828289_-\|bile-acid:sodium-symporter-family-protein	unknown	unknown	gnl\|CDD\|223462
NZ_CP016347.1\|WP_065300231.1\|2829303_2829969_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|187643
NZ_CP016347.1\|WP_014233039.1\|2808484_2809405_-\|glutaminase-B	unknown	unknown	gnl\|CDD\|234880
NZ_CP016347.1\|WP_065302902.1\|2835894_2837148_-\|HD-GYP-domain-containing-protein	unknown	unknown	gnl\|CDD\|225116

Protein	Function_ID	Function_description	E-value
NZ_CP016347.1\|WP_065300225.1\|2809493_2810522_-\|DNA-methylase	gnl\|CDD\|223971	COG1041, COG1041, Predicted DNA modification methylase [DNA replication, recombination, and repair].	1.57202e-08
NZ_CP016347.1\|WP_065302903.1\|2826537_2827212_+\|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.	1.70864e-56
NZ_CP016347.1\|WP_065302902.1\|2824979_2826233_-\|HD-GYP-domain-containing-protein	gnl\|CDD\|225116	COG2206, COG2206, c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms].	2.57514e-68
NZ_CP016347.1\|WP_065302897.1\|2805681_2805972_+\|YggU-family-protein	gnl\|CDD\|179931	PRK05090, PRK05090, hypothetical protein; Validated.	1.93848e-60
NZ_CP016347.1\|WP_065303111.1\|2807229_2808405_+\|radical-SAM-family-heme-chaperone-HemW	gnl\|CDD\|235550	PRK05660, PRK05660, radical SAM family heme chaperone HemW.	0
NZ_CP016347.1\|WP_065302899.1\|2811456_2812533_+\|A/G-specific-adenine-glycosylase	gnl\|CDD\|182805	PRK10880, PRK10880, adenine DNA glycosylase.	0
NZ_CP016347.1\|WP_020334002.1\|2806046_2806478_+\|DUF4426-domain-containing-protein	gnl\|CDD\|379616	pfam14467, DUF4426, Domain of unknown function (DUF4426). Members of this entry are found mostly in g-proteobacteria, especially in Vibrio. Strangely enough, there seems to be one eukaryotic homolog in Nematostella vectensis (NEMVEDRAFT_v1g226006), where the PA0388-like domain is fused with a domain homogous to the Methionine biosynthesis protein MetW (see below). In several Pseudomonas species, but also in Vibrio vulnificus and Azotobacter vinelandii PA0388 homologs are genomic neighbors of Nucleoside 5-triphosphatase RdgB (dHAPTP, dITP, XTP-specific) (EC 3.6.1.15) and Methionine biosynthesis protein MetW. On the other hand, in most Vibrio species it appears as a part of a conserved operon involved in possible response to stress.	3.41423e-65
NZ_CP016347.1\|WP_065302900.1\|2812916_2814059_+\|membrane-bound-lytic-murein-transglycosylase-MltC	gnl\|CDD\|183271	PRK11671, mltC, membrane-bound lytic murein transglycosylase MltC.	3.91385e-145
NZ_CP016347.1\|WP_065302903.1\|2837452_2838127_+\|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.	1.70864e-56
NZ_CP016347.1\|WP_014233043.1\|2812552_2812825_+\|oxidative-damage-protection-protein	gnl\|CDD\|180059	PRK05408, PRK05408, oxidative damage protection protein; Provisional.	3.33891e-59
NZ_CP016347.1\|WP_065302904.1\|2838265_2839204_-\|bile-acid:sodium-symporter-family-protein	gnl\|CDD\|223462	COG0385, COG0385, Predicted Na+-dependent transporter [General function prediction only].	2.58816e-83
NZ_CP016347.1\|WP_065302898.1\|2806609_2807212_+\|XTP/dITP-diphosphatase	gnl\|CDD\|234648	PRK00120, PRK00120, dITP/XTP pyrophosphatase; Reviewed.	8.62002e-124
NZ_CP016347.1\|WP_065302901.1\|2815219_2816845_+\|methyl-accepting-chemotaxis-protein	gnl\|CDD\|214599	smart00283, MA, Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer). Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.	8.21655e-59
NZ_CP016347.1\|WP_065300231.1\|2840218_2840884_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|187643	cd08939, KDSR-like_SDR_c, 3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR. These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical 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 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.	2.64531e-69
NZ_CP016347.1\|WP_065302905.1\|2841062_2842331_+\|DUF2254-domain-containing-protein	gnl\|CDD\|378351	pfam10011, DUF2254, Predicted membrane protein (DUF2254). Members of this family of bacterial proteins comprises various hypothetical and putative membrane proteins. Their exact function, has not, as yet, been defined.	1.66711e-118
NZ_CP016347.1\|WP_014233041.1\|2810533_2811253_-\|tRNA-(guanosine(46)-N7)-methyltransferase-TrmB	gnl\|CDD\|234649	PRK00121, trmB, tRNA (guanine-N(7)-)-methyltransferase; Reviewed.	4.68784e-109
NZ_CP016347.1\|WP_065302904.1\|2827350_2828289_-\|bile-acid:sodium-symporter-family-protein	gnl\|CDD\|223462	COG0385, COG0385, Predicted Na+-dependent transporter [General function prediction only].	2.58816e-83
NZ_CP016347.1\|WP_065300231.1\|2829303_2829969_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|187643	cd08939, KDSR-like_SDR_c, 3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR. These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical 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 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.	2.64531e-69
NZ_CP016347.1\|WP_014233039.1\|2808484_2809405_-\|glutaminase-B	gnl\|CDD\|234880	PRK00971, PRK00971, glutaminase; Provisional.	0
NZ_CP016347.1\|WP_065302902.1\|2835894_2837148_-\|HD-GYP-domain-containing-protein	gnl\|CDD\|225116	COG2206, COG2206, c-di-GMP phosphodiesterase class II (HD-GYP domain) [Signal transduction mechanisms].	2.57514e-68

>NZ_CP016347.1|WP_065302900.1|2812916_2814059_+|membrane-bound-lytic-murein-transglycosylase-MltC
MKKIVFIVAALLLTAGCSREVVEKFYDVEYEPTNRFANNLAELPGQFEKDTAALDSLINSFSGNIQKKWGKREVKLAGKSNYVKYIDNYLSRAEVDFQKGVITIETVSPTEPQKHLKNAIITTLLTPDEPANVDLFSSKDIKLEGQPFLYKQVVDQDNKPIQWSWRANRFADYLINHEIKTKDVDFKKAYYVEIPMVEDHFIQRSYQYANIVRRTAEKYDIPEDLIYAIIKTESSFNPYAVSWANAYGLMQVVPKTAGRDVFALVKNRSGQPSPEYLFNPENNIDTGTAYFYILKNRYLKEVSHPTSLEYSMISAYNGGTGGVLNTFNRSDRKRAMRDLNSLQPNQVYWALTKKHPNAEARRYLEKVTNFKKEFNSVQTF
>NZ_CP016347.1|WP_014233043.1|2812552_2812825_+|oxidative-damage-protection-protein
MSRTVFCARLKKEGEGLDFQLYPGELGKRIFDNISKEAWAEWQHKQTMLINEKKLNMMDPEHRKLIETEMVNFLFEGKDVHIDGYTPPSE
>NZ_CP016347.1|WP_065302899.1|2811456_2812533_+|A/G-specific-adenine-glycosylase
MTPFASAILKWYDAYGRKDLPWQQNKTAYSVWLSEIMLQQTQVTTVIPYYQRFLERFPTVVDLANAEQDEVLHLWTGLGYYARARNLHKAAKEVAQTYNGEFPLDIEQMNALPGIGRSTAAAVLSSVHKQPHAILDGNVKRTLSRCFAVEGWPGQKKVENQLWEIAEAHTPQTDVDKYNQAMMDMGAMVCTRSKPKCTLCPVADLCVAKKQGNILDYPGKKPKKDKPVKQTRFVMLHHKNANGHEVWLEQRPQTGIWGGLFCFPQTEHVDVESDIDLLLEQRGIQTNDIKEQQTLITFRHTFSHYHLDITPILIDLSKQPDVIMEGNKGLWYNLSKPEEVGLAAPVKLLLETLPHELR
>NZ_CP016347.1|WP_014233041.1|2810533_2811253_-|tRNA-(guanosine(46)-N7)-methyltransferase-TrmB
MSEVTTNEYNEDGKLIRKIRSFVRREGRLTKGQESAMNECWPTMGIDYKAELLDWKEVFGNDNPVVLEIGFGMGASLVEMAKNAPEKNFIGIEVHSPGVGACLADAREAGLTNLRVMCHDAVEVFEHMIPNDSLATLQLFFPDPWHKKRHHKRRIVQLEFAEMVRQKLIPNEGIFHMATDWENYAEHMIEIMNQAPGFENIAEEGDFVPRPEERPLTKFEARGHRLGHGVWDIKFKRTA
>NZ_CP016347.1|WP_065300225.1|2809493_2810522_-|DNA-methylase
MYHYAILANPGHNRIYFDSAMTIACSELKAMLASEGVEVTEIGSKDVGLPAALVFSCAEALNEAQARKIAASSIYYALFEVREDGLLRPIQAPAFNTFPESMSQILRYTGKTNEQFTRLMVNLGVSAANTDSAQLTLMDPMCGKGTTLFEGLIHGLNVVGVEINQKWVQEIQTFVVKFMKNGRFKHKVSKEKRTSGGKKVADGFVVEAAATKEDYNQGNLQTMKLYSADTRIADQVVKKNSVDVMVSDLPYGVQHGSKNAKDSKLNRSPLELLKEALPAWKVVLKKQGSVVLSFNEFTLKWKDVAALFEEQGWKVLSEDPYIGYLHRVDQSINRNIIVAVKP
>NZ_CP016347.1|WP_014233039.1|2808484_2809405_-|glutaminase-B
MKPTVEILTDILTEVRPLIGQGKVADYIPALAKVPSNKLGIAVYTNDGEVIKAGDADEPFSIQSISKALSLTLAMCLYKQEEIWARVGKEPSGQAFNSLIQLEMEQGIPRNPFINAGAIVVADLLQSRLSAPRQRLLEFVRQLSGDTHIVYDKVVAASEMMHGDRNAAIAYLMRSFGNFENEVIPVLQNYFHACALKMSCVDLAKTFSYLANKGTSVHTGKPIVSPTQTKQLNALLATCGLYDGAGEFAYRVGMPGKSGVGGGIIAVVPGDMTIAVWSPELDPAGNSLAGTKALELLSERIGRSIF
>NZ_CP016347.1|WP_065303111.1|2807229_2808405_+|radical-SAM-family-heme-chaperone-HemW
MLTPPALSLYVHIPWCVQKCPYCDFNSHELKAEIPEEQYINALLEDLDTDIEKYRLNDAPRPLHSIFIGGGTPSLISAQGIERLLKGIEERIPFKTDIEITMEANPGTIEAERFAGYRKAGVTRISIGVQSFEQEKLERLGRIHGKDEAVNAANLAHQIGLNSFNLDLMHGLPDQSIEQALADLDKAIELAPPHLSWYQLTIEPNTMFYYKPPTLPDDDDLWDIFELGHKKLAAAGYVQYEISGYSKPGFQCQHNLNYWRFGDYLGIGCGSHGKLSFADGRIIRTTKVKHPRGYLAAYQNMVKPYLHTEQFVEDEDRPFEFFMNRFRLMEACPKQDFIDTTGLPLSSIQETINWALDLGYLSETDTHWQITEKGKLFLNDLLEAFMAEEDE
>NZ_CP016347.1|WP_065302898.1|2806609_2807212_+|XTP/dITP-diphosphatase
MKKIVLATGNQGKVREMADLLSDFGFEVLAQSEFNVSEVAETGTTFIENAIIKARHAAQETGLPAIADDSGLEVDYLNGAPGIYSARYAGEGSTDQENLEKLLKAMEGVPEAERTARFHCVLVLMRHKDDPTPVVCHGKWEGRILTEAHGENGFGYDPVFFVPEDDCASAELEPARKKQLSHRGKALKSLFAQLSEQAAQ
>NZ_CP016347.1|WP_020334002.1|2806046_2806478_+|DUF4426-domain-containing-protein
MNKWITALLISLLSFPTFAEQFKNMKDIEVHYVAFNSTFLTPKIARSYDIKRNGYLAIINISVLDRASLGKPALEAQVAGQAKNLIGQTQQLTFREVKEGDAIYYLAELPVTHEETFTFDIDVKSGNKGSGKLQFTQKFYVEE
>NZ_CP016347.1|WP_065302897.1|2805681_2805972_+|YggU-family-protein
MSAAVWRDGEDIVLRLYIQPKASRDKIVGLHGEELKIAITAPPVDGKANAHLTKFLAKQFKVAKGLVHIEKGELGRHKQIRIESPTQIPTDIKAIL
>NZ_CP016347.1|WP_065302901.1|2815219_2816845_+|methyl-accepting-chemotaxis-protein
MKLKTQAYLLSAIILLALLALTATGLWTLRVASNLDNKARVTELFKSAYSILTEVEAMAASGELPEDEAKALATRLLRNNIYKDNEYVYVADENMIFVAAPLDPQLHGTSFHDFKDSNNNSVGQLILDILDNKTGQIVEYTWSQTQTDGSIEEKHSIAEKTPHWGWVVGTGIGFNEVNARFWATAQWQLVLCLFIAGAILTSLIIAIRKMLNVLGGEPHDVRQAVQAVSQGNIQTSFDTVAPKDSIYDAVQNMSQSLAIMVTNLDSSMLALRSELSAVESRSGTIADLTLSQQESTAMIATAMTEMASSANQVATSANDTARNTDEADKQSQQTQSLIYSTVDNIQGLANQLSTASLAVANLDQDVNNIVKVLDVIGDIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAGRTQDSTKEIQNMISNLQQGSRHAIQTMEICAETSQSTVTQSQSASEALQQIVTALEAITTMSQQIATAAAEQTHVSDDIAHRINLIEESGYQLNSVVTESQSSTQSLASLANDLEGWVNKFSVKH
>NZ_CP016347.1|WP_065302902.1|2824979_2826233_-|HD-GYP-domain-containing-protein
MAAIKLTVDRIQPGLHIRLPLKWNDHPFLLNSFKIKDQGQVEMIRHLGVKFVYFNPEQSDSLPLPVNQDREDKVKSDDSLDLETQALWQEKQKRIEKLSAYRRRVIQCEKEFERSLARMRSVMMKIRNRPVAAVNEAKQLTEDIVDKLMCDDNVTLHLMNGKNEYEDIYFHSLNVAVIAMMIGRAKGYSANQLKELSFAALFHDMGKVKIPTAILRKQEPLTVPEENYLKLHTKYGLDLANQIEDFPETAKTVIEQHHELRDGSGYPKGLQGDEINEFAQIIIVANAFDNLCHTRITSEQKIPYTALSHLYKNCKHLYKEENLKLLIKFMGVFPPGTVVQLTNNMIGLVISVNASNLLFPNVLVYDPSVPRTQAPILDLASKDLRIVNAIHPSKLPENIKEYLNPRSRISYFFDTDA
>NZ_CP016347.1|WP_065302903.1|2826537_2827212_+|SDR-family-oxidoreductase
MKILVTGASSGIGFELVKQLCAGHHDVFATGRNKNKLTELHQLTGCKFASYDLTESQQVMDMFKQATEELDGLDVLINNAGMNTRKCAIDEFSLEEFEQQYAINLRAPAILCREALSLMKEQKSGYIINVTSTVAKRASETMAVYTTMKQGLAGFTGVLMKEAQPHGIKVTNLFPGGTDTNFRAASRPEYMHPESVARTILGLLKLPEDVVVHEMVFRPLVELE
>NZ_CP016347.1|WP_065302904.1|2827350_2828289_-|bile-acid:sodium-symporter-family-protein
MIGRLTQLFPVWAVIFALTAYFSPSIFVDLKSQIVPLLTIIMLAMGISLSPSDFLNVLKHKKAVGVGVFLQFLIMPLAALLISFLLGFSTELTVGMVLVGSVAGGTSSNVMVFLAKGDVALSISMTAISTLLGVILTPLLVEGLIGQSVDVPVSGMLMSLVKIVLLPVSIGVIINTFIPKAVAKVNAILPLISMLAIVVIIAIVVALNAENLNTIGPLVALAVILHNGLGLTAGYYCCRLLGFNESTCRTIAFEVGLQNSGLATALAMKFFSPASAIAGTIFSVWHNISGSLLAGYWASKKARKAKAVTNSL
>NZ_CP016347.1|WP_065300231.1|2829303_2829969_-|SDR-family-NAD(P)-dependent-oxidoreductase
MILITGASSGLGAELAKLYDCDGQPTYLTGRSEGKLSEITNRLSNNIGYQACDLSLHQDVEQLFDQLGQPPQTVIHSAGSGYFGLLEDQEPEQIQKLINNNLNSAINVLRELVKRYKDHSVNVVVIMSTASQQPKAQESTYCAVKWAVKGLIESVRLELKGKPMKIIAVYPGGMATEFWETSGKSLDLSSFMQAEDAAQMIHDAVSSIGNGYVSDITVNRL
>NZ_CP016347.1|WP_065302902.1|2835894_2837148_-|HD-GYP-domain-containing-protein
MAAIKLTVDRIQPGLHIRLPLKWNDHPFLLNSFKIKDQGQVEMIRHLGVKFVYFNPEQSDSLPLPVNQDREDKVKSDDSLDLETQALWQEKQKRIEKLSAYRRRVIQCEKEFERSLARMRSVMMKIRNRPVAAVNEAKQLTEDIVDKLMCDDNVTLHLMNGKNEYEDIYFHSLNVAVIAMMIGRAKGYSANQLKELSFAALFHDMGKVKIPTAILRKQEPLTVPEENYLKLHTKYGLDLANQIEDFPETAKTVIEQHHELRDGSGYPKGLQGDEINEFAQIIIVANAFDNLCHTRITSEQKIPYTALSHLYKNCKHLYKEENLKLLIKFMGVFPPGTVVQLTNNMIGLVISVNASNLLFPNVLVYDPSVPRTQAPILDLASKDLRIVNAIHPSKLPENIKEYLNPRSRISYFFDTDA
>NZ_CP016347.1|WP_065302903.1|2837452_2838127_+|SDR-family-oxidoreductase
MKILVTGASSGIGFELVKQLCAGHHDVFATGRNKNKLTELHQLTGCKFASYDLTESQQVMDMFKQATEELDGLDVLINNAGMNTRKCAIDEFSLEEFEQQYAINLRAPAILCREALSLMKEQKSGYIINVTSTVAKRASETMAVYTTMKQGLAGFTGVLMKEAQPHGIKVTNLFPGGTDTNFRAASRPEYMHPESVARTILGLLKLPEDVVVHEMVFRPLVELE
>NZ_CP016347.1|WP_065302904.1|2838265_2839204_-|bile-acid:sodium-symporter-family-protein
MIGRLTQLFPVWAVIFALTAYFSPSIFVDLKSQIVPLLTIIMLAMGISLSPSDFLNVLKHKKAVGVGVFLQFLIMPLAALLISFLLGFSTELTVGMVLVGSVAGGTSSNVMVFLAKGDVALSISMTAISTLLGVILTPLLVEGLIGQSVDVPVSGMLMSLVKIVLLPVSIGVIINTFIPKAVAKVNAILPLISMLAIVVIIAIVVALNAENLNTIGPLVALAVILHNGLGLTAGYYCCRLLGFNESTCRTIAFEVGLQNSGLATALAMKFFSPASAIAGTIFSVWHNISGSLLAGYWASKKARKAKAVTNSL
>NZ_CP016347.1|WP_065300231.1|2840218_2840884_-|SDR-family-NAD(P)-dependent-oxidoreductase
MILITGASSGLGAELAKLYDCDGQPTYLTGRSEGKLSEITNRLSNNIGYQACDLSLHQDVEQLFDQLGQPPQTVIHSAGSGYFGLLEDQEPEQIQKLINNNLNSAINVLRELVKRYKDHSVNVVVIMSTASQQPKAQESTYCAVKWAVKGLIESVRLELKGKPMKIIAVYPGGMATEFWETSGKSLDLSSFMQAEDAAQMIHDAVSSIGNGYVSDITVNRL
>NZ_CP016347.1|WP_065302905.1|2841062_2842331_+|DUF2254-domain-containing-protein
MTGSKWQWLLKQVTRKLWVRTSLFALLAVATALMSIVLNEFVVLPPAINVSSDLLNNILNILATSMLAVTTFSLNIMVSAYTAASAGVTPRATKLLMEDSTTQNALATFLGSFLFSLVGIIALGVGAYHEQARIYLFIVTMVVIVMIILTLLRWIQHLSVLGRVSETTSKVEQALISAIRKRGNEPWLGARPWSHPEHKPRGSKPIYSQEIGYLQHIDMHHLDSIAEENQCTIYIERQPGNFVYLGQPIAWLCGELKEESEVSAAFTIRTERSFDQDPRFGLVVLAEIASRALSPAVNDNGTAIDVLGRAIRALSLWGELLKQRPIKTRFPRLFVPSLSCQDLFDDVFLPIAHDGAAQLQVQIRLQKSLLAISSMHPKLFASPAQKLSEKALELALSQHYTEDEKHQLSQLSHQVVDQKFHG

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NZ_CP016347.1	2814330-2814370	0	1.0

1. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to position: 2814330-2814370, mismatch: 0, identity: 1.0

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccattctt	Protospacer
*****************************************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	LN997803	Escherichia coli phage phi467	15124-15164	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NZ_CP041417	Escherichia coli strain STEC711 plasmid pSTEC711_1, complete sequence	296497-296537	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NZ_LN868946	Salmonella enterica subsp. enterica serovar Senftenberg strain NCTC10384 plasmid 4, complete sequence	103819-103859	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	KU052038	Escherichia phage SerU-LTIIb, partial genome	1162-1202	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	KU052038	Escherichia phage SerU-LTIIb, partial genome	3068-3108	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NZ_CP022660	Salmonella enterica subsp. enterica strain RM11060 plasmid pRM11060-2, complete sequence	52076-52116	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NZ_CP045061	Salmonella enterica subsp. enterica serovar Muenchen strain LG26 plasmid pLG26p2, complete sequence	52082-52122	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NZ_CP045054	Salmonella enterica subsp. enterica serovar Muenchen strain LG24 plasmid pLG24p2, complete sequence	52087-52127	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NZ_CP045058	Salmonella enterica subsp. enterica serovar Muenchen strain LG25 plasmid pLG25p2, complete sequence	52086-52126	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NZ_CP023526	Cedecea neteri strain FDAARGOS_392 plasmid unnamed, complete sequence	1925-1965	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NC_021742	Serratia liquefaciens ATCC 27592 plasmid unnamed, complete sequence	35426-35466	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	MH791411	UNVERIFIED: Escherichia phage Ecwhy_1, complete genome	13643-13683	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	MH494197	Escherichia phage CMSTMSU, complete genome	196770-196810	4	0.902
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NZ_CP054057	Scandinavium goeteborgense strain CCUG 66741 plasmid pSg66741_1, complete sequence	85815-85855	5	0.878
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	KY653118	Morganella phage IME1369_01, complete genome	696-736	5	0.878
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NC_049942	Escherichia phage JLK-2012, complete sequence	23522-23562	8	0.805
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	NC_027364	Escherichia phage PBECO 4, complete genome	207830-207870	9	0.78
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	LC494302	Escherichia phage SP27 DNA, complete genome	76609-76649	9	0.78
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	LT603033	Escherichia phage vB_Eco_slurp01 genome assembly, chromosome: I	17115-17155	9	0.78
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	MK817115	Escherichia phage vB_EcoM_phAPEC6, complete genome	52943-52983	10	0.756
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	MH383160	Escherichia phage UB, complete genome	272122-272162	10	0.756
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	MK327931	Escherichia phage vB_EcoM_G17, complete genome	77927-77967	10	0.756
NZ_CP016347_2	2.1\|2814709\|41\|NZ_CP016347\|PILER-CR	2814709-2814749	41	KM507819	Escherichia phage 121Q, complete genome	77936-77976	11	0.732

1. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to LN997803 (Escherichia coli phage phi467) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccatatgc	Protospacer
************************************* . .

2. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NZ_CP041417 (Escherichia coli strain STEC711 plasmid pSTEC711_1, complete sequence) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccatatgc	Protospacer
************************************* . .

3. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NZ_LN868946 (Salmonella enterica subsp. enterica serovar Senftenberg strain NCTC10384 plasmid 4, complete sequence) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccatcaag	Protospacer
*************************************.

4. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to KU052038 (Escherichia phage SerU-LTIIb, partial genome) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccatatgc	Protospacer
************************************* . .

5. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to KU052038 (Escherichia phage SerU-LTIIb, partial genome) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccatatgc	Protospacer
************************************* . .

6. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NZ_CP022660 (Salmonella enterica subsp. enterica strain RM11060 plasmid pRM11060-2, complete sequence) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccacttac	Protospacer
************************************.*. .

7. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NZ_CP045061 (Salmonella enterica subsp. enterica serovar Muenchen strain LG26 plasmid pLG26p2, complete sequence) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccacttac	Protospacer
************************************.*. .

8. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NZ_CP045054 (Salmonella enterica subsp. enterica serovar Muenchen strain LG24 plasmid pLG24p2, complete sequence) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccacttac	Protospacer
************************************.*. .

9. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NZ_CP045058 (Salmonella enterica subsp. enterica serovar Muenchen strain LG25 plasmid pLG25p2, complete sequence) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccacttac	Protospacer
************************************.*. .

10. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NZ_CP023526 (Cedecea neteri strain FDAARGOS_392 plasmid unnamed, complete sequence) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccagaatg	Protospacer
************************************   *

11. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NC_021742 (Serratia liquefaciens ATCC 27592 plasmid unnamed, complete sequence) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagccggcaccaatcaa	Protospacer
***************************.******** **

12. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to MH791411 (UNVERIFIED: Escherichia phage Ecwhy_1, complete genome) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcacaaatcag	Protospacer
********************************** * **

13. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to MH494197 (Escherichia phage CMSTMSU, complete genome) position: , mismatch: 4, identity: 0.902

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcacaaatcag	Protospacer
********************************** * **

14. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NZ_CP054057 (Scandinavium goeteborgense strain CCUG 66741 plasmid pSg66741_1, complete sequence) position: , mismatch: 5, identity: 0.878

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgattccggtagtcggcaccaaatgc	Protospacer
************************************  . .

15. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to KY653118 (Morganella phage IME1369_01, complete genome) position: , mismatch: 5, identity: 0.878

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
agtaggtcaccagttcgactccggtagccggcaccatatta	Protospacer
******************.********.********* .*

16. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NC_049942 (Escherichia phage JLK-2012, complete sequence) position: , mismatch: 8, identity: 0.805

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
atcaggtcgccagttcgattccggtagccggcaccatatgc	Protospacer
* .*****.******************.********* . .

17. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to NC_027364 (Escherichia phage PBECO 4, complete genome) position: , mismatch: 9, identity: 0.78

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
gaaaggtcaccagttcgattccggtagtcggcacaaaataa	Protospacer
.. ******************************* *  .

18. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to LC494302 (Escherichia phage SP27 DNA, complete genome) position: , mismatch: 9, identity: 0.78

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
gaaaggtcaccagttcgattccggtagtcggcacaaaataa	Protospacer
.. ******************************* *  .

19. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to LT603033 (Escherichia phage vB_Eco_slurp01 genome assembly, chromosome: I) position: , mismatch: 9, identity: 0.78

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
gaaaggtcaccagttcgattccggtagtcggcacaaaataa	Protospacer
.. ******************************* *  .

20. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to MK817115 (Escherichia phage vB_EcoM_phAPEC6, complete genome) position: , mismatch: 10, identity: 0.756

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
gaaatgtcaccagttcgattccggtagtcggcacaaaataa	Protospacer
.. * ***************************** *  .

21. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to MH383160 (Escherichia phage UB, complete genome) position: , mismatch: 10, identity: 0.756

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
gaaatgtcaccagttcgattccggtagtcggcacaaaataa	Protospacer
.. * ***************************** *  .

22. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to MK327931 (Escherichia phage vB_EcoM_G17, complete genome) position: , mismatch: 10, identity: 0.756

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
gaaatgtcaccagttcgattccggtagtcggcacaaaataa	Protospacer
.. * ***************************** *  .

23. spacer 2.1|2814709|41|NZ_CP016347|PILER-CR matches to KM507819 (Escherichia phage 121Q, complete genome) position: , mismatch: 11, identity: 0.732

agtaggtcaccagttcgattccggtagtcggcaccattctt	CRISPR spacer
gaaatgtcaccagttcaattccggtagtcggcacaaaataa	Protospacer
.. * ***********.***************** *  .

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

741531 : 748185

Staphylococcus_phage(66.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_014231006.1\|741531_742671_+	glutamate 5-kinase	A0A1X9I5D0	Streptococcus_phage	1.7e-62	41.7
WP_065302035.1\|742688_743939_+	glutamate-5-semialdehyde dehydrogenase	A0A1X9I5D4	Streptococcus_phage	3.6e-98	47.7
WP_014231008.1\|744055_744505_+	transcriptional regulator NrdR	NA	NA	NA	NA
WP_065302036.1\|744511_745630_+	bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD	A0A2H4PQS8	Staphylococcus_phage	2.9e-46	37.7
WP_020333699.1\|745647_746301_+	riboflavin synthase	A0A2H4PQS5	Staphylococcus_phage	3.1e-32	37.0
WP_014231011.1\|746436_747546_+	bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II	A0A2H4PQS2	Staphylococcus_phage	2.7e-65	39.3
WP_014231012.1\|747714_748185_+	6,7-dimethyl-8-ribityllumazine synthase	A0A2H4PQS3	Staphylococcus_phage	3.7e-32	48.0

DBSCAN-SWA_2

2234286 : 2254032

Vibrio_phage(85.19%)

capsid,tail,portal,head,terminase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_065302669.1\|2234286_2234889_-	hemolysin	A0A2I7RNJ4	Vibrio_phage	1.2e-102	85.5
WP_065302670.1\|2234875_2236063_-	hypothetical protein	A0A2I7RNJ7	Vibrio_phage	6.7e-195	83.0
WP_065302671.1\|2236062_2236404_-	DUF2590 family protein	A0A2I7RNH9	Vibrio_phage	4.0e-44	80.9
WP_065302672.1\|2236403_2238290_-\|tail	phage tail tape measure protein	A0A1D9C9V3	Salinivibrio_phage	1.1e-220	58.7
WP_162836293.1\|2238301_2238442_-	hypothetical protein	Q1I0Y8	Pasteurella_virus	1.5e-05	51.2
WP_031429742.1\|2238483_2238747_-	hypothetical protein	A0A1D9C9R9	Salinivibrio_phage	1.1e-17	54.1
WP_045607483.1\|2238743_2239028_-	hypothetical protein	NA	NA	NA	NA
WP_065302673.1\|2239030_2239261_-	hypothetical protein	NA	NA	NA	NA
WP_065302674.1\|2239257_2239755_-	hypothetical protein	A0A2I7S7C4	Vibrio_phage	5.7e-23	48.8
WP_065302675.1\|2239751_2239970_-	molecular chaperone DnaK	A0A2I7RNJ6	Vibrio_phage	1.2e-22	72.1
WP_025605246.1\|2239982_2240432_-	DUF2597 family protein	A0A2I7RNI0	Vibrio_phage	9.6e-78	96.0
WP_065302676.1\|2240435_2241566_-	DUF2586 family protein	A0A2I7RNI8	Vibrio_phage	1.3e-179	83.5
WP_065302677.1\|2241569_2242226_-	virion morphogenesis protein	A0A2I7RNI6	Vibrio_phage	1.6e-97	81.7
WP_065302678.1\|2242209_2242701_-\|tail	phage tail protein	A0A2I7RNH2	Vibrio_phage	6.8e-77	85.6
WP_065302679.1\|2242697_2243117_-\|head	head completion/stabilization protein	A0A2I7RNH7	Vibrio_phage	2.7e-50	74.1
WP_065302680.1\|2243231_2243948_-\|terminase	terminase	A0A2I7RNJ0	Vibrio_phage	1.2e-103	84.4
WP_065302681.1\|2243958_2244963_-\|capsid	phage major capsid protein, P2 family	R9TPZ5	Vibrio_phage	3.9e-111	62.7
WP_065303097.1\|2244962_2245820_-\|capsid	phage capsid protein	A0A2I7RNH1	Vibrio_phage	2.5e-98	66.1
WP_065302682.1\|2245986_2247762_+\|terminase	terminase	A0A2I7RNI3	Vibrio_phage	1.4e-305	90.2
WP_065302683.1\|2247758_2248787_+\|portal	phage portal protein	A0A2I7RNI9	Vibrio_phage	1.1e-148	74.1
WP_045607465.1\|2248865_2249117_+	ogr/Delta-like zinc finger family protein	R9TNQ2	Vibrio_phage	1.1e-30	75.9
WP_065299985.1\|2249111_2249375_-	hypothetical protein	Q8HA64	Vibrio_phage	9.8e-14	56.9
WP_065302684.1\|2249456_2251337_-	replication endonuclease	A0A218M4H2	Erwinia_phage	7.4e-63	38.2
WP_025517534.1\|2251342_2251579_-	hypothetical protein	NA	NA	NA	NA
WP_065302685.1\|2251575_2251803_-	hypothetical protein	U3PIK2	Vibrio_phage	9.6e-18	54.7
WP_065302686.1\|2251814_2252222_-	hypothetical protein	A0A2I7RNG1	Vibrio_phage	3.0e-38	60.9
WP_065302687.1\|2252218_2252422_-	hypothetical protein	A0A2I7RNH0	Vibrio_phage	1.2e-11	67.3
WP_065302688.1\|2252450_2252990_-	transcriptional regulator	A0A2I7RNI1	Vibrio_phage	3.7e-52	57.5
WP_045607456.1\|2253104_2253317_-	hypothetical protein	U3PFJ1	Vibrio_phage	3.0e-13	52.9
WP_065302689.1\|2253405_2254032_+	phage repressor protein CI	A0A2I7RNF9	Vibrio_phage	2.4e-34	38.9

DBSCAN-SWA_3

2733718 : 2744881

uncultured_Mediterranean_phage(28.57%)

tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_065302875.1\|2733718_2736301_-\|tRNA	alanine--tRNA ligase	A0A1V0SK38	Klosneuvirus	6.6e-78	37.7
WP_065297372.1\|2736443_2736911_-	recombination regulator RecX	NA	NA	NA	NA
WP_014232974.1\|2737025_2738072_-	recombinase RecA	A0A2D1GPX2	Mycobacterium_phage	1.4e-111	60.7
WP_065302876.1\|2738262_2738754_-	nicotinamide-nucleotide amidase	B5TK85	Pseudomonas_phage	1.4e-26	46.8
WP_065302877.1\|2738838_2741400_+	DNA mismatch repair protein MutS	A0A1V0SC35	Catovirus	3.7e-33	23.5
WP_020333966.1\|2742541_2743429_-	peptidoglycan DD-metalloendopeptidase family protein	D7RWE0	Brochothrix_phage	1.8e-06	36.4
WP_014232979.1\|2743478_2744105_-	protein-L-isoaspartate(D-aspartate) O-methyltransferase	A0A1B1IU40	uncultured_Mediterranean_phage	6.7e-37	52.7
WP_014232980.1\|2744104_2744881_-	5'/3'-nucleotidase SurE	A0A1B1ITZ2	uncultured_Mediterranean_phage	1.7e-66	50.6

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP016348

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NZ_CP016347

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection