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
NC_011027	Chlorobaculum parvum NCIB 8327, complete genome	4 crisprs	csx15,cas10,csm2gr11,csm3gr7,csm4gr5,csm5gr7,csx1,cas6,cas3,csa3,Cas9_archaeal,DEDDh	0	0	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NC_011027_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_011027_1

87152-88366

TypeIII

Consensus_repeat	Method
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CRISPRCasFinder
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CRT
AATACGCTAAAGCGTGCAATGAAATGAAAT	PILER-CR

16 spacers

cas1,csx15,cas10,csm2gr11,csm3gr7,csm4gr5,csm5gr7,csx1,cas6

The CRISPR arrays of NC_011027_1

>merge|NC_011027|1|87152-88366|CRISPRCasFinder,CRT,PILER-CR
GCTTCGATACGCAAAAGCGTGCAATGAAATGAAATACGTGTACCATGCAAAGGCCCAGGCGACGAACTATGACTTGTCGCAATACGCTAAGGCGTGCAATGAAATGAAATAGAAACCAGTACTTGAATCACTCAAACGATACGCAAAGTTGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATGTTGCAGGCGTGGCGAGACGGCTTTTCCGTCGAAGGGTCGCAATACGCAAAAGCGTGCAATGAAATGAAATCATTGGATACGTAACTATCAGGGGGCGGGAATACCGATGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATGTATGCTGATGTGTCGCTGCCGGAGCTTCAGAGGGAGCTGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATTTTCGGGTTTGTGATTCCGTCAGGTACGGTGTCAGAGGACGGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATCAGAATGCTATCGATAGCATCGATAGATAGCGTCCGACAAGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATCGTCGGTGATGATGGAACGCAGTATTGGCCAATCTTCATGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATCCGTATGTCAATTACCGCATCCACGTGGTCGGCACTGGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATCGTGGTATTTCGAACTGACGAGGCGGCTCGAAAGGGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATTATCGAGATCGGCACGCTCATGGGCGGCCTGACGAAAGGGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATCCCTTGCCTAACCCTGACGATTGTCCGGTAATTCCAGTCATGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATCCCCTGTCTGCAGAACGCCGAATATCGTCTGCATTTGGCTGCTGTAATACGCTAAAGCGTGCAATGAAATGAAATAATGAAAAAAATGAACATCGCCACTCTCTTTTTCCTGCGCTGTAATACGCTAAAGCGTGCAATGAAATGAAATCACTCCACCATATCCGAACGCACCAAACCACCCGGATAGTCGCAATACGCTAAAGCGTGCAATGAAATGAAATCGCCTACGCATTTCGCCTCGCGCTTATATCGGTAGGCATGTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT

>NC_011027|1|1|87152-88366|CRISPRCasFinder
GCTTCGATACGCAAAAGCGTGCAATGAAATGAAAT	ACGTGTACCATGCAAAGGCCCAGGCGACGAACTATGACTT
GTCGCAATACGCTAAGGCGTGCAATGAAATGAAAT	AGAAACCAGTACTTGAATCACTCAAACGATACGCAAAGTT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	GTTGCAGGCGTGGCGAGACGGCTTTTCCGTCGAAGG
GTCGCAATACGCAAAAGCGTGCAATGAAATGAAAT	CATTGGATACGTAACTATCAGGGGGCGGGAATACCGAT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	GTATGCTGATGTGTCGCTGCCGGAGCTTCAGAGGGAGCT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	TTTCGGGTTTGTGATTCCGTCAGGTACGGTGTCAGAGGACG
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CAGAATGCTATCGATAGCATCGATAGATAGCGTCCGACAA
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CGTCGGTGATGATGGAACGCAGTATTGGCCAATCTTCAT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CCGTATGTCAATTACCGCATCCACGTGGTCGGCACTG
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CGTGGTATTTCGAACTGACGAGGCGGCTCGAAAGG
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	TATCGAGATCGGCACGCTCATGGGCGGCCTGACGAAAGG
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CCCTTGCCTAACCCTGACGATTGTCCGGTAATTCCAGTCAT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CCCCTGTCTGCAGAACGCCGAATATCGTCTGCATTTGGCT
GCTGTAATACGCTAAAGCGTGCAATGAAATGAAAT	AATGAAAAAAATGAACATCGCCACTCTCTTTTTCCTGC
GCTGTAATACGCTAAAGCGTGCAATGAAATGAAAT	CACTCCACCATATCCGAACGCACCAAACCACCCGGATA
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CGCCTACGCATTTCGCCTCGCGCTTATATCGGTAGGCAT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT

>NC_011027|1|1|87152-88366|CRT
GCTTCGATACGCAAAAGCGTGCAATGAAATGAAAT	ACGTGTACCATGCAAAGGCCCAGGCGACGAACTATGACTT
GTCGCAATACGCTAAGGCGTGCAATGAAATGAAAT	AGAAACCAGTACTTGAATCACTCAAACGATACGCAAAGTT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	GTTGCAGGCGTGGCGAGACGGCTTTTCCGTCGAAGG
GTCGCAATACGCAAAAGCGTGCAATGAAATGAAAT	CATTGGATACGTAACTATCAGGGGGCGGGAATACCGAT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	GTATGCTGATGTGTCGCTGCCGGAGCTTCAGAGGGAGCT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	TTTCGGGTTTGTGATTCCGTCAGGTACGGTGTCAGAGGACG
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CAGAATGCTATCGATAGCATCGATAGATAGCGTCCGACAA
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CGTCGGTGATGATGGAACGCAGTATTGGCCAATCTTCAT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CCGTATGTCAATTACCGCATCCACGTGGTCGGCACTG
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CGTGGTATTTCGAACTGACGAGGCGGCTCGAAAGG
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	TATCGAGATCGGCACGCTCATGGGCGGCCTGACGAAAGG
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CCCTTGCCTAACCCTGACGATTGTCCGGTAATTCCAGTCAT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CCCCTGTCTGCAGAACGCCGAATATCGTCTGCATTTGGCT
GCTGTAATACGCTAAAGCGTGCAATGAAATGAAAT	AATGAAAAAAATGAACATCGCCACTCTCTTTTTCCTGC
GCTGTAATACGCTAAAGCGTGCAATGAAATGAAAT	CACTCCACCATATCCGAACGCACCAAACCACCCGGATA
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT	CGCCTACGCATTTCGCCTCGCGCTTATATCGGTAGGCAT
GTCGCAATACGCTAAAGCGTGCAATGAAATGAAAT

>NC_011027|1|1|87232-88366|PILER-CR
AATACGCTAAGGCGTGCAATGAAATGAAAT	AGAAACCAGTACTTGAATCACTCAAACGATACGCAAAGTTGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	GTTGCAGGCGTGGCGAGACGGCTTTTCCGTCGAAGGGTCGC
AATACGCAAAAGCGTGCAATGAAATGAAAT	CATTGGATACGTAACTATCAGGGGGCGGGAATACCGATGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	GTATGCTGATGTGTCGCTGCCGGAGCTTCAGAGGGAGCTGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	TTTCGGGTTTGTGATTCCGTCAGGTACGGTGTCAGAGGACGGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	CAGAATGCTATCGATAGCATCGATAGATAGCGTCCGACAAGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	CGTCGGTGATGATGGAACGCAGTATTGGCCAATCTTCATGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	CCGTATGTCAATTACCGCATCCACGTGGTCGGCACTGGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	CGTGGTATTTCGAACTGACGAGGCGGCTCGAAAGGGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	TATCGAGATCGGCACGCTCATGGGCGGCCTGACGAAAGGGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	CCCTTGCCTAACCCTGACGATTGTCCGGTAATTCCAGTCATGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	CCCCTGTCTGCAGAACGCCGAATATCGTCTGCATTTGGCTGCTGT
AATACGCTAAAGCGTGCAATGAAATGAAAT	AATGAAAAAAATGAACATCGCCACTCTCTTTTTCCTGCGCTGT
AATACGCTAAAGCGTGCAATGAAATGAAAT	CACTCCACCATATCCGAACGCACCAAACCACCCGGATAGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT	CGCCTACGCATTTCGCCTCGCGCTTATATCGGTAGGCATGTCGC
AATACGCTAAAGCGTGCAATGAAATGAAAT

Protein	Signature genes	Signature genes Name	Protein_function
NC_011027.1\|WP_012501336.1\|81183_83295_-\|ATP-dependent-metallopeptidase-FtsH/Yme1/Tma-family-protein	unknown	unknown	gnl\|CDD\|273520
NC_011027.1\|WP_012501343.1\|93086_93956_+\|type-III-A-CRISPR-associated-RAMP-protein-Csm3	csm3gr7	cd09684_csm3gr7_CAS-III-A:CAS-III-D	gnl\|CDD\|187815
NC_011027.1\|WP_156773330.1\|86598_86892_+\|hypothetical-protein	unknown	unknown	unknown
NC_011027.1\|WP_012501344.1\|93969_95070_+\|hypothetical-protein	csm4gr5	cd09663_csm4gr5_CAS-III-A	gnl\|CDD\|380071
NC_011027.1\|WP_012501342.1\|92597_93071_+\|type-III-A-CRISPR-associated-protein-Csm2	csm2gr11	pfam03750_csm2gr11_CAS-III-A	gnl\|CDD\|367635
NC_011027.1\|WP_012501333.1\|77808_79170_-\|RIP-metalloprotease-RseP	unknown	unknown	gnl\|CDD\|272878
NC_011027.1\|WP_012501332.1\|76712_77786_-\|peptide-chain-release-factor-1	unknown	unknown	gnl\|CDD\|234801
NC_011027.1\|WP_012501347.1\|96917_98453_+\|hypothetical-protein	csx1	cd09747_csx1_CAS-III	gnl\|CDD\|187878
NC_011027.1\|WP_083762329.1\|95358_96921_+\|hypothetical-protein	csm5gr7	cd09662_csm5gr7_CAS-III-A	gnl\|CDD\|224251
NC_011027.1\|WP_012501340.1\|89395_89974_+\|hypothetical-protein	csx15	cd09766_csx15_CAS-I:CAS-III	gnl\|CDD\|187735
NC_011027.1\|WP_012501345.1\|95071_95386_+\|hypothetical-protein	unknown	unknown	unknown
NC_011027.1\|WP_083762327.1\|88616_89336_-\|CRISPR-associated-endonuclease-Cas1	cas1	cd09634_cas1_CAS-I:CAS-II:CAS-III:CAS-V	gnl\|CDD\|187766
NC_011027.1\|WP_012501330.1\|74840_75872_-\|potassium-channel-protein	unknown	unknown	gnl\|CDD\|367001
NC_011027.1\|WP_041466077.1\|79336_80485_-\|1-deoxy-D-xylulose-5-phosphate-reductoisomerase	unknown	unknown	gnl\|CDD\|235472
NC_011027.1\|WP_012501341.1\|90204_92598_+\|type-III-A-CRISPR-associated-protein-Cas10/Csm1	cas10	cd09680_cas10_CAS-III	gnl\|CDD\|187811
NC_011027.1\|WP_012501331.1\|75908_76520_-\|DUF1997-domain-containing-protein	unknown	unknown	gnl\|CDD\|370453
NC_011027.1\|WP_012501338.1\|84521_86366_+\|glutamine--fructose-6-phosphate-transaminase-(isomerizing)	unknown	unknown	gnl\|CDD\|234729
NC_011027.1\|WP_012501337.1\|83605_84430_+\|orotidine-5'-phosphate-decarboxylase	unknown	unknown	gnl\|CDD\|234651
NC_011027.1\|WP_012501335.1\|80899_81178_-\|acylphosphatase	unknown	unknown	gnl\|CDD\|172921
NC_011027.1\|WP_012501348.1\|98479_99271_+\|CRISPR-associated-endoribonuclease-Cas6	cas6	COG1583_cas6_CAS-I:CAS-III:CAS-IV	gnl\|CDD\|187889

Protein	Function_ID	Function_description	E-value
NC_011027.1\|WP_012501336.1\|81183_83295_-\|ATP-dependent-metallopeptidase-FtsH/Yme1/Tma-family-protein	gnl\|CDD\|273520	TIGR01241, ATP-dependent_zinc_metalloprotease_FtsH, ATP-dependent metalloprotease FtsH. HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides].	0
NC_011027.1\|WP_012501343.1\|93086_93956_+\|type-III-A-CRISPR-associated-RAMP-protein-Csm3	gnl\|CDD\|187815	cd09684, Csm3_III-A, CRISPR/Cas system-associated RAMP superfamily protein Csm3. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; RAMP superfamily protein.	3.85324e-65
NC_011027.1\|WP_012501344.1\|93969_95070_+\|hypothetical-protein	gnl\|CDD\|380071	pfam17953, Csm4_C, CRISPR Csm4 C-terminal domain. Clustered, regularly interspaced, short palindromic repeat (CRISPR) loci play a pivotal role in the prokaryotic host defense system against invading genetic materials. The CRISPR loci are transcribed to produce CRISPR RNAs (crRNAs), which form interference complexes with CRISPR-associated (Cas) proteins to target the invading nucleic acid for degradation. The interference complex of the type III-A CRISPR-Cas system is composed of five Cas proteins (Csm1-Csm5) and a crRNA, and targets invading DNA. This entry represents the C-terminal domain found in Csm4. Csm4 structurally resembles Cmr3, a component of the type III-B CRISPR-Cas interference complex. Studies indicate that Csm3-Csm4 complex binds single-stranded RNA in a non-sequence-specific manner. Structural analysis show, Csm3 and Csm4 have one and two ferredoxin-like folds (also known as an RRM-like fold), respectively. The long beta-hairpin inserted into the C-terminal ferredoxin-like fold of Csm4, is well-conserved in the Cmr3 structure. The corresponding beta-hairpin of Cmr3 binds the D1 domain of Cmr2, as observed in the Cmr2-Cmr3 complex structure. Furthermore, it is suggested that the hairpin of Csm4 is responsible for the interaction with Csm1 (ortholog of Cmr2).	1.36203e-21
NC_011027.1\|WP_012501342.1\|92597_93071_+\|type-III-A-CRISPR-associated-protein-Csm2	gnl\|CDD\|367635	pfam03750, Csm2_III-A, Csm2 Type III-A. Clusters of short DNA repeats with non-homologous spacers, which are found at regular intervals in the genomes of phylogenetically distinct prokaryotic species, comprise a family with recognisable features. This family is known as CRISPR (short for Clustered Regularly Interspaced Short Palindromic Repeats). A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-associated) proteins. This entry represents Csm2 Type III-A, a family of Cas proteins also known as TM1810/Csm2.	3.05147e-14
NC_011027.1\|WP_012501333.1\|77808_79170_-\|RIP-metalloprotease-RseP	gnl\|CDD\|272878	TIGR00054, Putative_zinc_metalloprotease_slr1821, RIP metalloprotease RseP. Members of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by a match to the full length of the seed alignment; the model also detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain. [Protein fate, Degradation of proteins, peptides, and glycopeptides].	4.03867e-81
NC_011027.1\|WP_012501332.1\|76712_77786_-\|peptide-chain-release-factor-1	gnl\|CDD\|234801	PRK00591, prfA, peptide chain release factor 1; Validated.	0
NC_011027.1\|WP_012501347.1\|96917_98453_+\|hypothetical-protein	gnl\|CDD\|187878	cd09747, Csx1_III-U, CRISPR/Cas system-associated protein Csx1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Protein of this family often fused to HTH domain; Some proteins could have an additional fusion with RecB-family nuclease domain; Core domain appears to have a Rossmann-like fold; loosely associated with CRISPR/Cas systems; also known as Cas02710 family.	5.83614e-20
NC_011027.1\|WP_012501338.1\|84521_86366_+\|glutamine--fructose-6-phosphate-transaminase-(isomerizing)	gnl\|CDD\|234729	PRK00331, PRK00331, isomerizing glutamine--fructose-6-phosphate transaminase.	0
NC_011027.1\|WP_012501340.1\|89395_89974_+\|hypothetical-protein	gnl\|CDD\|187735	cd09766, Csx15_I-U, CRISPR/Cas system-associated protein Csx15. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Small protein loosely associated with CRISPR/Cas systems; some are fused to AAA ATPase domain, also known as TTE2665 family.	7.16906e-42
NC_011027.1\|WP_083762327.1\|88616_89336_-\|CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|187766	cd09634, Cas1_I-II-III, CRISPR/Cas system-associated protein Cas1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas1 is the most universal CRISPR system protein thought to be involved in spacer integration; Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain.	1.18444e-62
NC_011027.1\|WP_012501330.1\|74840_75872_-\|potassium-channel-protein	gnl\|CDD\|367001	pfam02254, TrkA_N, TrkA-N domain. This domain is found in a wide variety of proteins. These protein include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.	1.00871e-32
NC_011027.1\|WP_041466077.1\|79336_80485_-\|1-deoxy-D-xylulose-5-phosphate-reductoisomerase	gnl\|CDD\|235472	PRK05447, PRK05447, 1-deoxy-D-xylulose 5-phosphate reductoisomerase; Provisional.	0
NC_011027.1\|WP_012501341.1\|90204_92598_+\|type-III-A-CRISPR-associated-protein-Cas10/Csm1	gnl\|CDD\|187811	cd09680, Cas10_III, CRISPR/Cas system-associated protein Cas10. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; signature gene for type III; also known as Csm1 family.	2.05554e-89
NC_011027.1\|WP_083762329.1\|95358_96921_+\|hypothetical-protein	gnl\|CDD\|224251	COG1332, COG1332, CRISPR system related protein, RAMP superfamily [Defense mechanisms].	2.28132e-05
NC_011027.1\|WP_012501331.1\|75908_76520_-\|DUF1997-domain-containing-protein	gnl\|CDD\|370453	pfam09366, DUF1997, Protein of unknown function (DUF1997). This family of proteins are functionally uncharacterized.	0.000579826
NC_011027.1\|WP_012501337.1\|83605_84430_+\|orotidine-5'-phosphate-decarboxylase	gnl\|CDD\|234651	PRK00125, pyrF, orotidine 5'-phosphate decarboxylase; Reviewed.	2.21721e-83
NC_011027.1\|WP_012501335.1\|80899_81178_-\|acylphosphatase	gnl\|CDD\|172921	PRK14445, PRK14445, acylphosphatase; Provisional.	2.15596e-53
NC_011027.1\|WP_012501348.1\|98479_99271_+\|CRISPR-associated-endoribonuclease-Cas6	gnl\|CDD\|187889	cd09759, Cas6_I-A, CRISPR/Cas system-associated RAMP superfamily protein Cas6. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6 is an endoribonuclease that generates crRNAs, predicted subunit of Cascade complex; RAMP superfamily protein; Possesses double RRM/ferredoxin fold.	1.73642e-42

>NC_011027.1|WP_156773330.1|86598_86892_+|hypothetical-protein
MPIILGVAKNPERFVAVTKWMLHDAALYSERQNHLSTLLLKLRVSAIGWERQLHELVIPFLKQLCIIIGLVACQSVIPAKAGIHVLFPDSGFPPARQ
>NC_011027.1|WP_012501338.1|84521_86366_+|glutamine--fructose-6-phosphate-transaminase-(isomerizing)
MCGIIGYIGKREAAPLLLNGLKRLEYRGYDSAGMAVMNGSMQVLKQKGSVGNLEELLNVSGSVMLGATIGIAHTRWATHGDPSDRNAHPHMNISDDIALIHNGIIENYTTLKKELISQGYEFESDTDSEVLVHLIDRVWKADPSIGLEGAVRQALRHVEGAYGICVVSSREPDKIVVARKGSPLVIGLGDGEYFIASDAAPIVEHTNKVVYLLDGEMAVVTHENYTVKTIENVEQEKRVTELDFSLEKIEKGGFEHFMLKEIFEQPEVMRDVMRGRIRVDEGRVQLGGIEDYLDRLKQAKRIVICACGTSWHAGLIGEYLIEEYARIPVEVDYASEFRYRNPIVTADDVVIVISQSGETADTLAALRLAKEKGALVMGICNVVGSTIARETLCGMYTHAGPEVGVASTKAFTAQVIVLFMLAMALSKGRTISQEEIKLNLRDLADVPEKVARILEQNDVIKELAAKLKDARNALYLGRGYNFPVALEGALKLKEISYIHAEGYPAAEMKHGPIALIDEDMPVIVIATRDNTYAKILSNIEEVRSRKGRVIAIASEGDREIAELTPDVIYIPQASAALLPLLTVIPLQLLSYHVATMRGCNVDRPRNLAKSVTVE
>NC_011027.1|WP_012501337.1|83605_84430_+|orotidine-5'-phosphate-decarboxylase
MNSSRNKANERIASLRSMLCVGLDSDPAKIPALFQSMQHPVQEFNRAVIRATRDHAAAYKVNTAFYESRGLAGMRDLEETLQALPPECLSIADAKRADIGNTSRQYAKAFFEAWPFDAITVAPYMGFDSLEPFFEYEDKLVFVLCLTSNPGSRDFEERIVEDGRPLYRSVLERVSAWQRNGNAGVVVGATKPGLLQELRRDAPDLFFLIPGVGAQGGSMQEAVSHGADPEGRSAVVNVSRALIFPDGEFSSVEQFEAAVNREAGKLHESMIGML
>NC_011027.1|WP_012501336.1|81183_83295_-|ATP-dependent-metallopeptidase-FtsH/Yme1/Tma-family-protein
MANNPFKLNNPYDNEQDNGPRKPRFSIFYYMAVILLLIGFQLAFFWSGSTKEIPYSEFRQLILQNKVESVKIAPEKIYVNLKKDGTVPAADKQQEQPKLTLPGASTNEPETEVTVNPVRDEGLIPLLESSGIKYEAIPGNSWIGELLQWILPFGLLIGIYFFMFRRMGGPGSQFMNISKNKAALYENLDEHTRISFKDVAGLDEAKGEVMEVVDFLKDPKKYTKLGGKLPKGVLLVGPPGTGKTLLAKAVAGEADVPFFSISGSDFVEMFVGVGAARVRDLFKQAKEKAPCIIFIDEIDAVGRSRGKGFMMGANDERENTLNQLLVEMDGFATDKGVILMAATNRADVLDTALLRPGRFDRQIVVDKPDLKGRIDIFKVHTKELSLSGDVNLKALASQTPGFAGAEIANAANEAALLASRRGKQSIEMRDFEDAIERVIAGLEKKNKVINPKEKEIVAYHEAGHAIVSWLMPENDPVQKISIVPRGVSALGYTLNIPLEDRYLMTKAELIARICGLLGGRIAEEVVFGEISTGAQNDLERVTEIAYNMVMVYGMSDKIGYLSFVDSNNPYTGGPSLDKKYGDETARMIDLEVKSIVEEARNKVFKMLSENREQLETLAKELLSKEIVQYCRIEEILGKRPAGKFSEHLECQNNIELPAADPTAEPATDAPQTKPESATLSDRELEELEAAVQRLKESRNLSSN
>NC_011027.1|WP_012501335.1|80899_81178_-|acylphosphatase
MTEKRVHIIVRGLVQGVGFRMFVHREASARNLAGWTRNLPDGTVEIEAQGNAGMVDELVKQARIGPSRSQVNSIAVREIAPDNAENDFSIRY
>NC_011027.1|WP_041466077.1|79336_80485_-|1-deoxy-D-xylulose-5-phosphate-reductoisomerase
MKSLSILGSTGSIGLSTLDVVRRHPGRFSVAALAEGHDVELLSQQIAEFRPSLVSVRDEESRERLKGLLGEHKPEILCGLDGAAEVASVDGADMVVSAIVGAAGLVPTVRAIEAGKDIALANKETLVVAGQLVSDLVKKHGVKLLPVDSEHSAIFQSLVGHRTEDIDRIILTASGGPFRKTPAEELKNVGPEQALKHPQWSMGAKITIDSATLMNKGLEVIEAHWLFNMPAEKIGVVVHPQSIIHSMVEYLDGCVIAQLGVPDMRAPIAYALSYPERCETGIGKLDLAKVGTLTFEEPDMERFPALRLAFDALKAGQTYPAVLNAANEIAVAAFLDKKIGFTAIADTVDKTMQAHEAWTPVTLDEYIQADKWARETAKQLIG
>NC_011027.1|WP_012501333.1|77808_79170_-|RIP-metalloprotease-RseP
MDLLSTIFYFIIAIFILVTAHEFGHFITARIFGMRVDRFFIGFDFFGTTLWKKKIGETEYGIGAFPLGGYVKIAGMVDESMDTDYVQSEAKPWEFRAKPVWQRLIVLAGGVAMNMVLAAVIFISITAMFGESQTSIKTPSYVEPNSVFASMGFRDGDRLISINGTKLQYWEDALDPEKLSSSSVRFTVMRDGQELTFTAPKDFMSQLNESRSLGIGPAMPPVIGEVLPNNPAEKAGILPGSLITAINGQPITDWSQVLDIVSSNAGKPLAITWMHLDKHEDSPLNANRIRSEGKSFTTEVTPNTSGKIGISLKQTIESERITVPFPEAVVSGINQTWKASVMTVQGFAKIFTGKEDFRKSVGGPIKIAKIANQSAEQGPISFMYFVAVLSISLAIINILPIPALDGGQFVLNAIEGVMGREIPFELKMRIQQVGMTLLLTLFAYFMINDLLNP
>NC_011027.1|WP_012501332.1|76712_77786_-|peptide-chain-release-factor-1
MFDKLQSIKDKYLTIEQQLSDPEVAADQNRFRKLNKEYSGLREIVRAYDNWRSAKQQLDETLAMQKSEEDPEMRALAAAEAEELQERLPELEQNLKILLLPKDEADTRNAIIEIRAGTGGDEAGLFAADLMRMYQRYAERQGWSCQTLDVSEGSVPGSLKEVSLEVSGHDVYGILKFESGVHRVQRVPETETQGRIHTSAASVAVLPEAEEVDVEIRKDDLQMDTFRSGGKGGQNVNKVETAVRITHVPSGIVVACQEERSQLQNRERAMKMLRSKLYDIKITEQLQSRADLRRSMVATGDRSAKIRTYNFPQSRVTDHRIGFTTHALPQVMQGELEPIIDALRMHDQAERLKAETN
>NC_011027.1|WP_012501331.1|75908_76520_-|DUF1997-domain-containing-protein
MEMDATGKSKGQWVFHGTFDRTVDYLSDHARILEFNPFCHKVEPLDRDEAYRWHFRVTDPQNNPFDVIFNIQQETELLLELPEELGTMHPDELTDAMIEQYTIGRKISWRHLPASETIAMPEKYLFEGKATADLLILPLQGERTKVDFDLRIDVQFILYPAFRIIPEQIIRTMTNAGMSLVMQTATNKMFQSISSDFGTIRQL
>NC_011027.1|WP_012501330.1|74840_75872_-|potassium-channel-protein
MSKDAQQISAIRRFSASIISVALLVISGTVGYMYLENMSPLDALYMTVITVATVGFSEVRPLDDVGKIFTMTLIVGGTGIFFFTLTNVAVFFVSGEWREHWEQQRNERMLRKLNDHFIICGFGRLGSNVAEEFRIKSIPFMVIDNMIDNVLRARDEGYLAIKGNAADEGVLIDAGLQRAKGLIAAAGNDAENVFIVLTARNLKPSLHIVARADCEESENKLLRAGAQKVVMLYRSAGKRMANILIEPELEEYLDELSDANNLNLRIAQFIVNENSALVGKSFQEVDLYNNHRINVVGYKLPGGELHTTPRPAEIIQKNGTIIAIGQGGDLEMLNHLTQGEAQK
>NC_011027.1|WP_083762327.1|88616_89336_-|CRISPR-associated-endonuclease-Cas1
MSISNPKIRNSRTLIRKRRAMAWEHNGELKERFDNHLGALSALAGHAQRCESMDALRGFEGKAAALYFELFGLLFKKELPFYTEAFRRVRRPPTDPVNSLLSFGYSLLHTNMFSLVRMKGMNPYIGFLHAEDKGNPALINDLVEEFRTIIDSLALYMLNKGILRNKDFYYHKDRLGCFLTDKARKTFLTVFERRMWENAVDQETGKAMNIRRHMEHQVHKLKEVLEGKRPVYEPYRVSR
>NC_011027.1|WP_012501340.1|89395_89974_+|hypothetical-protein
MQELLSQLTISEWAIIISGISTIAVVFQQALELIFTRNIPWLIRLLQKGWRWLKRLVRGRLTGVRTLILNCSGHPVHPAQKSAIEKLMHWQDAEVLDVELGNVPEDRHFVPSIEKAIDRLGLTSKEWEQPIVVIPAGYPPACSAIQSILHGRLGHFPDVVRLRRVDPVDGVRYEVAEIMPLQQLRHDSRGKR
>NC_011027.1|WP_012501341.1|90204_92598_+|type-III-A-CRISPR-associated-protein-Cas10/Csm1
MSSQHPVIECGIRLLKSPEGELKTGWTEQGGKELAEACSLLNIKLDEPLTLQALQSVFLEENSPEAAPMWFKPCELKAGPLPALVETPEPDQLTLRNTLQGLRQTGNGEAAFSDPLTELEHYGSFIATSAHASTPLFDLFKSLAALYDCLKQGTPETPCLMVSCDFSGIQDTVYTITSKGALKTLRARSFMLELLCEHLIYEILHMARSDRHAVIYSGGGGFSLLLPNIEQSHDSDGGIIEKIEEYRETINKWALKEFEGRLFIALDAKPFDKEKLRDQASFQEIRQSQADALDRLKRRKFSDHLETLFTPSMPEQVTVKKECQITHRDDLTDDEMFDLNELKKCVSMASVDADKRDSDDYLWVSESCYHQFKLGDKLVGATGIFRYTTAIDRSKNPGTLVLPSASGGMVSYTVEEVADATPATQWSINSWDGQRLFLYANYVRKHGELSAYARQEEKEQLLEEGRRSVKADDTASFAGLAASSCGADLIGALRMDVDNLGKLFSSISNIAQLSARSRMLNLFFKLHLNHICANRSFDLLKKNQAEHEEWGKPGRNVSIIYAGGDDLFIVGAWDETVELAFDIQEEFECFTAALPKGANGISGGLTLHQPKFPLYQMARLSAEAEAYAKGDRDAEELKPKKNRISLFYDHSKVNRKRRLGDRELSQRYMLSMQWGLANAFLRSLMKVYQRCFKQTAFQSEERKGIEIEKFSYGTIEKWFAVIKKYQQSNQLYLPTMARVMKDVEREFSDDDKDDKDDKAELFKNLVSYLYTTEENKRNWISHLHIALNWLTYLRRKV
>NC_011027.1|WP_012501342.1|92597_93071_+|type-III-A-CRISPR-associated-protein-Csm2
MAGKEFDFIKELGELPKLDEVKKRLERVNTFSSASSEIKESLYLYAAAIAKQMSADVTPTQLRRYYSYIKSIELVNRDQKDDAPQIIDKYKLSFLLPKIAGSSERKKLESLYDVMKVCLSNNNGGKIKTVADLRLFVEFFEAILDYHASIEKSVNHN
>NC_011027.1|WP_012501343.1|93086_93956_+|type-III-A-CRISPR-associated-RAMP-protein-Csm3
MSDPKQPKTIKLLGYVKIYGEIEAVTGLHIGGTADAIDKGGIDSPVIKNPITNEPYIPGSSLRGRMRSLLEKKNGKPLTEMTKGIWMEIYEDDKKEDAEDGNKKKAKDSEVCRVFGNAHTGLPSILIVRDALYTEETKNNGYIESDLPVTEAKMEIAVDRITAQALPRTIERVPSGARFDFSMVYRVQQDENHPNPTDTLEKDLKNILEALKDIEEFDGLGGNTARGHGQVKFHLKPLQVTVLEPKQQSSEILGENPDAKGFYDLKKMATKGAKVAGEFGPAPSKAPTT
>NC_011027.1|WP_012501344.1|93969_95070_+|hypothetical-protein
MNTEKTYLIRLYFKNALRVGAARSGVGIEASQDYIHSDSFWAALANYWALLGSAGGISFAEFLEGFRVGSTSSGASSGVPPLFTISSVFPFARSSGMRRYWLPKPLSVPFDLSTSNSKESRDSERENYGKALKQARLLSDKTFTNWQAFEHQVGYEVGNEKDFSSTGKNNVRPQSSLDRITSQSNLFHSGISYLNPNDNDEGLYVLVKTSDERVKEALEEVLDVIRDAGGLGGDISSGCGELVNYSIELIGSNDKKWAFLRECDGANARCLLSLCLPSDPKTISTKLVAYDTVLRKGWTGSLTASLQRKRQTLYMLSEGTVLSVEEQGQMATITPASTKTPDWTGQHPVYRYGYAFSVPIKITFED
>NC_011027.1|WP_012501345.1|95071_95386_+|hypothetical-protein
MDKTTKSKETAIIELETLTPLFIKGKDPDYGEGMYFFPNENKAYLLDNDKLCKFIYDKTYDKDGNILVDGKDYVALYSELLANEGGEKEIAGLYDKFSRFQAQR
>NC_011027.1|WP_083762329.1|95358_96921_+|hypothetical-protein
MFSVPGSKIDSSLDDIPKQDKERLKGKSIQYFLDNLDLLEKNKKSEIERLSRGVTTLHLSNKNKKFIQNGCGERFLPGSSIKGAIRNALLWKMLNADMGLKLKFSKFAYDKFQWCEEWTQAKVLEYINGLSGLSPQKQEEEKERYKKKKPREFASRFSRKDDDAPTSLAQASLDSITLAAFSPEFAGNKALVTPKYIKEYNEQWGKATDIHRDLSRIIRITDANFIERAKWKKIDIATYNLRGERFQKRDNTFAKLEATDKTTKAWFRITLDHDLAREFFGNSIPTYLQSIENILKTVSEFFYAVAREELDFYGKATHVGPVHAVKKWYEELLRSAELEGQEGAQLFRLGWGGGMMTKTQFLHLDEKDRKRSRDLMNPRDETVAPQSRCLQTEKVNGNNNRNQEDKALHPLGWCTLRYLGSNIAKAKDASANAEAKRQATEPAPPGCVRATIMDDESFPIKIKIEEGEYQNSNTNLKIMELQDLQNTQFKKGVVVFVQLNEQQGKKGKKSLRNATYRGKP
>NC_011027.1|WP_012501347.1|96917_98453_+|hypothetical-protein
MIDAIYINRRVEKLSKNEPEKVQWRNLLRNLSDDQDNISNHADSEKRITKYFGVNAEFHPDNKTFFKSPFSKSLKAFRALYSIDYPTDEGDSCDLLMSIVGFSLEPIMHTVLTLRPKNLLFLFSKESSLIGSKDVNAFDRLQALIACHGDGYNPKIDQEILEVADAPHVFSVVRDAITKASSPERVAIDVTGGKKSMDASAFLAASLFEKVAIYYVDYASYDTDKGFPVWGSEFLNKLENPYKVFGVREEKLIKEFWDKADFPAVVKFIKLCIDKLKPEIAKKYRLTEKINQLELVKKAAECYTEWRIFDYQKAKDKPFKGCDKHHSNVLEELAKCSTLEADQNINNQQSAQLALALAIDRYRRGSDAYEHEKHSTAILCYAQSVEILLRFCCKKDWNELKQKRNCKGIKMLGDLRRVLFKDNPFYFNAPGFGERLNENVNKARNAIAHYNCISSSENSDIKIDAECMREVVDELFFLFVNKHGLAEGLINEYKQSLSFCSLNENLELYKP
>NC_011027.1|WP_012501348.1|98479_99271_+|CRISPR-associated-endoribonuclease-Cas6
MRITLELSHRRSFVTVPINHSSLISSLIYNVIDRSSSEYAERLHEQGYRLENRAFKLFTFSPLNPGHHRKWVMHENGTMSTGEKRLYLTISSPKEEFIEHLILGLLHEPFVSVGKERFRVETVRKLDAPLFSGDMRFVMLSPLVCATKSEADQYPQYLFPGDPDFKRVLVANLCRKYEVLHGKPIACDENDVMFELDRDYVAKVHGKVQKLITLKEGRSDESKVKGTLAPFRLVAPTELIEVGYECGFGEKNAQGFGMVKAIN

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Crispr_ID: NC_011027_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_011027_2

331893-331991

Orphan

Consensus_repeat	Method
GGCACTACGATAACCGGTACGACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_011027_2

>merge|NC_011027|2|331893-331991|CRISPRCasFinder
GGTACGACGATAACTGGCACTACGATAACCGGTACGACGATAACCGGTACGACAGGAACGTTTACGAATCTGGCCGGCACTACGATAACCGGTACTACG

>NC_011027|2|2|331893-331991|CRISPRCasFinder
GGTACGACGATAACTGGCACTACG	ATAACCGGTACGACGATAACCGGTACGACAGGAACGTTTACGAATCTGGCC
GGCACTACGATAACCGGTACTACG

Protein	Signature genes	Signature genes Name	Protein_function
NC_011027.1\|WP_041466097.1\|341003_341810_+\|RNA-methyltransferase	unknown	unknown	gnl\|CDD\|349982
NC_011027.1\|WP_012501579.1\|340197_341007_+\|hypothetical-protein	unknown	unknown	unknown
NC_011027.1\|WP_041466093.1\|328503_329358_+\|DUF4349-domain-containing-protein	unknown	unknown	gnl\|CDD\|379526
NC_011027.1\|WP_012501575.1\|336045_336813_-\|NADH-ubiquinone-oxidoreductase	unknown	unknown	gnl\|CDD\|224852
NC_011027.1\|WP_012501577.1\|337700_338780_-\|hydrogenase	unknown	unknown	gnl\|CDD\|131956
NC_011027.1\|WP_156773338.1\|329339_330161_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|212492
NC_011027.1\|WP_012501568.1\|326989_328462_+\|transport-protein	unknown	unknown	gnl\|CDD\|214950
NC_011027.1\|WP_012501574.1\|334781_336056_-\|Ni/Fe-hydrogenase-subunit-alpha	unknown	unknown	gnl\|CDD\|225798
NC_011027.1\|WP_012501565.1\|323669_324098_+\|peptidylprolyl-isomerase	unknown	unknown	gnl\|CDD\|223976
NC_011027.1\|WP_012501571.1\|330324_330582_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377801
NC_011027.1\|WP_049755817.1\|341944_342994_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|130981
NC_011027.1\|WP_156773339.1\|330565_330964_+\|hypothetical-protein	unknown	unknown	unknown
NC_011027.1\|WP_012501567.1\|325965_326973_+\|SPFH-domain-containing-protein	unknown	unknown	gnl\|CDD\|259806
NC_011027.1\|WP_012501566.1\|324341_325847_+\|sodium-dependent-transporter	unknown	unknown	gnl\|CDD\|271366
NC_011027.1\|WP_012501564.1\|322403_323501_+\|mechanosensitive-ion-channel	unknown	unknown	gnl\|CDD\|366370
NC_011027.1\|WP_156773446.1\|334649_334745_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235840
NC_011027.1\|WP_041466231.1\|336822_337647_-\|oxidoreductase	unknown	unknown	gnl\|CDD\|99817
NC_011027.1\|WP_012501578.1\|338889_340128_-\|U32-family-peptidase	unknown	unknown	gnl\|CDD\|223896
NC_011027.1\|WP_012501582.1\|343022_343856_-\|universal-stress-protein	unknown	unknown	gnl\|CDD\|238182
NC_011027.1\|WP_012501563.1\|321205_322396_+\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224153

Protein	Function_ID	Function_description	E-value
NC_011027.1\|WP_041466097.1\|341003_341810_+\|RNA-methyltransferase	gnl\|CDD\|349982	cd18109, SpoU-like_RNA-MTase, SAM-dependent RNA methylase related to SpoU-TrmH. RNA 2'-O ribose methyltransferase catalyzes the methyltransfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH group of ribose in tRNA or rRNA. It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.	3.59844e-63
NC_011027.1\|WP_041466093.1\|328503_329358_+\|DUF4349-domain-containing-protein	gnl\|CDD\|379526	pfam14257, DUF4349, Domain of unknown function (DUF4349). This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 282 and 353 amino acids in length. There is a single completely conserved residue D that may be functionally important.	3.70061e-57
NC_011027.1\|WP_012501577.1\|337700_338780_-\|hydrogenase	gnl\|CDD\|131956	TIGR02910, anaerobic_sulfite_reductase_subunit_A, sulfite reductase, subunit A. Members of this protein family include the A subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. Note that any one of these enzymes may have secondary substates such as NH2OH, SeO3(2-), and SO3(2-). Heterologous expression of the anaerobic sulfite reductase of Salmonella confers on Escherichia coli the ability to produce hydrogen sulfide gas from sulfite. [Central intermediary metabolism, Sulfur metabolism].	5.05713e-43
NC_011027.1\|WP_156773338.1\|329339_330161_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|212492	cd05327, retinol-DH_like_SDR_c_like, retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs. Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. 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.	6.83974e-60
NC_011027.1\|WP_012501568.1\|326989_328462_+\|transport-protein	gnl\|CDD\|214950	smart00978, Tim44, Tim44 is an essential component of the machinery that mediates the translocation of nuclear-encoded proteins across the mitochondrial inner membrane. Tim44 is thought to bind phospholipids of the mitochondrial inner membrane both by electrostatic interactions and by penetrating the polar head group region.	1.1827e-11
NC_011027.1\|WP_012501565.1\|323669_324098_+\|peptidylprolyl-isomerase	gnl\|CDD\|223976	COG1047, SlpA, FKBP-type peptidyl-prolyl cis-trans isomerases 2 [Posttranslational modification, protein turnover, chaperones].	1.19639e-39
NC_011027.1\|WP_012501571.1\|330324_330582_-\|hypothetical-protein	gnl\|CDD\|377801	pfam07277, SapC, SapC. This family contains a number of bacterial SapC proteins approximately 250 residues long. In Campylobacter fetus, SapC forms part of a paracrystalline surface layer (S-layer) that confers serum resistance.	1.1463e-10
NC_011027.1\|WP_049755817.1\|341944_342994_+\|hypothetical-protein	gnl\|CDD\|130981	TIGR01926, peroxid_rel, uncharacterized peroxidase-related enzyme. This protein family with length of about 200 amino acids. One member, from Myxococcus xanthus, is a selenoprotein, with an otherwise conserved Cys replaced by Sec. This family is drawn narrowly enough to suggest that These proteins contain a domain described by TIGR00778, with a CxxCxxxHxxxxxxxG motif. Some members of that family are known to act as peroxidases or correlate with resistance to oxidative stress.	2.66932e-07
NC_011027.1\|WP_012501575.1\|336045_336813_-\|NADH-ubiquinone-oxidoreductase	gnl\|CDD\|224852	COG1941, FrhG, Coenzyme F420-reducing hydrogenase, gamma subunit [Energy production and conversion].	3.58952e-44
NC_011027.1\|WP_012501567.1\|325965_326973_+\|SPFH-domain-containing-protein	gnl\|CDD\|259806	cd03408, SPFH_like_u1, Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.	7.66072e-78
NC_011027.1\|WP_012501566.1\|324341_325847_+\|sodium-dependent-transporter	gnl\|CDD\|271366	cd10334, SLC6sbd_u1, uncharacterized bacterial and archaeal solute carrier 6 subfamily; solute-binding domain. SLC6 proteins (also called the sodium- and chloride-dependent neurotransmitter transporter family or Na+/Cl--dependent transporter family) include neurotransmitter transporters (NTTs): these are sodium- and chloride-dependent plasma membrane transporters for the monoamine neurotransmitters serotonin (5-hydroxytryptamine), dopamine, and norepinephrine, and the amino acid neurotransmitters GABA and glycine. These NTTs are widely expressed in the mammalian brain, involved in regulating neurotransmitter signaling and homeostasis, and the target of a range of therapeutic drugs for the treatment of psychiatric diseases. Bacterial members of the SLC6 family include the LeuT amino acid transporter.	0
NC_011027.1\|WP_012501574.1\|334781_336056_-\|Ni/Fe-hydrogenase-subunit-alpha	gnl\|CDD\|225798	COG3259, FrhA, Coenzyme F420-reducing hydrogenase, alpha subunit [Energy production and conversion].	2.09825e-103
NC_011027.1\|WP_156773446.1\|334649_334745_+\|hypothetical-protein	gnl\|CDD\|235840	PRK06599, PRK06599, DNA topoisomerase I; Validated.	0.000964991
NC_011027.1\|WP_041466231.1\|336822_337647_-\|oxidoreductase	gnl\|CDD\|99817	cd06221, sulfite_reductase_like, Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.	6.70354e-136
NC_011027.1\|WP_012501578.1\|338889_340128_-\|U32-family-peptidase	gnl\|CDD\|223896	COG0826, COG0826, Collagenase and related proteases [Posttranslational modification, protein turnover, chaperones].	5.58755e-101
NC_011027.1\|WP_012501564.1\|322403_323501_+\|mechanosensitive-ion-channel	gnl\|CDD\|366370	pfam00924, MS_channel, Mechanosensitive ion channel. Two members of this protein family of M. jannaschii have been functionally characterized. Both proteins form mechanosensitive (MS) ion channels upon reconstitution into liposomes and functional examination by the patch-clamp technique. Therefore this family are likely to also be MS channel proteins.	8.80388e-17
NC_011027.1\|WP_012501582.1\|343022_343856_-\|universal-stress-protein	gnl\|CDD\|238182	cd00293, USP_Like, Usp: Universal stress protein family. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, athough Usp lacks ATP-binding activity.	1.51178e-11
NC_011027.1\|WP_012501563.1\|321205_322396_+\|FAD-dependent-oxidoreductase	gnl\|CDD\|224153	COG1232, HemY, Protoporphyrinogen oxidase [Coenzyme metabolism].	5.81721e-30

>NC_011027.1|WP_156773339.1|330565_330964_+|hypothetical-protein
MSSFSTKKGFRRNLRQAAPPEAPPAKVGVELQHDPSRHTECRREVCCRGAVHYYQIHDDAQSCRVGEVLQLFAEEANGRVVNSLFILFSHLLPQADVFELFGGDAPFVVVGELLVALPADADSRLYFLEHTA
>NC_011027.1|WP_012501571.1|330324_330582_-|hypothetical-protein
MENEDKRTESYLPAYLHRCPFITTAQNGEQEPMVYFDKAYGGFNTKDGAGLFEDSAPSETLQKQKVMLTFGDDSPKNLTDLGSRR
>NC_011027.1|WP_156773338.1|329339_330161_+|SDR-family-NAD(P)-dependent-oxidoreductase
MEAEEVKKLTLCITGSTDGIGLAAAKRFAADGHRVIVHGRDESRISDACAAIVQSTGVEAVGFVEADFTDLDAVCSMGRELVERYPGLDLLINNAAVYMPTRTFVQEGFETTFCVNYLAPVLLTSVVRPVLIANGGSVLNVSSMDHHSAVFDPVNMQGERSYSGYEAYARSKLFNIMLTIDLASGDDAIRSNSLDPGVIATKLLHAGWALAGDDVSVGGDDVFETVMEIARNDYNGEYFENARPAICSSVAQEPVARQELRELTGEMLSRFVP
>NC_011027.1|WP_041466093.1|328503_329358_+|DUF4349-domain-containing-protein
MKTPARYFLSLFLLLAMMACSGQSKRYEAENADFPASSSRIVAESFMPQPAPEVAGQDGGGPATEQNLVQKISQQIIRDGQAVFETNDLKKTKTWIESLVQKHKAYLSLDEQSKGSDRIEQRMIVRIPADRFDAFVADLEKGVVKFDSKSITATDVTEEFIDVSQRLRLKKETEERYIALLEKAKSVQDVLETEKYIGQVRAEIESLEGRLKYLQNRIGLSTLNITFYQLKPEVQEFTSRIGLAFSEGWNNFLFFLLGVISLWPFLLAGVLLVGTVRFLWKLRK
>NC_011027.1|WP_012501568.1|326989_328462_+|transport-protein
MRTGFFSRFLVSATIAVLGLPCFSAELLARAGGGGGGGGIGDGGGFSGGGGNGIDYAFNGSRGYGAPGQFDFSVVFTVFFILFILFAFFSVVAKFRKKSNENAFGEPVPEATPDARIDNTPLFPGAPPGFDQSAFLAKVRKAFLEVQRAWSAQSTDMMRRFISDGVYQRFNTQFKMMRLLQQGNPLSNINISMAWVDRIEQDGRYDIVHAGIKASMTDRFICALNHDLDEEGTNEFVEYWSFIRKRGAAGKDMYETEQCPNCGAPLPKDMGEVCKCNYCNATINSGEFDWVLAEITQQDDYRRDGDRAEKMPGLDAKVAEMVTVYGDFSVQLVEDKASNAWMQMMTAKAMHNPAIMRRFVADDLFRQLAPKYEQNREIFNRIFLNRVTLIKAEQRDGKNILTFALTASIQRASLTGNSVRLIDPEIVEREEIMTLTRDATAGAGKGSIYQHTCPACGAPVKDTLDLKCAFCGSTLNSTANDWVVSGLTGR
>NC_011027.1|WP_012501567.1|325965_326973_+|SPFH-domain-containing-protein
MALWNSVTGQLRSVIEWKNPAPGVLFERWTDNGDEIKNASKLIVGPGQGVIFVYEGKPQAAITEPGMTDLKTANIPFWTTITKFMQAFQSEHKVGIYFFRTAEILNQGWGTPGPIKYLDPQYKFPVGMRGYGNFSFRITDAGSFFVNIMGQRDELTIDELRTAIVARLVQPLTDFLAEAKFGYNEIDANRNEIADGVKEKVAPIFATLGFGLTDFRVENTDFDDDTKRRVGRVADMQAEAQAAQAVGVDFAKLQQLAALRDAAQNEGGAAGAGVGLGAGVGLGQAMAGMMSGMNTPQPATEDPVAKLSQLKQMLDNQLISQEEYDAKKQQILSQL
>NC_011027.1|WP_012501566.1|324341_325847_+|sodium-dependent-transporter
MKRSEWGSRVGFVLAAIGSAIGLGNIWRFPYLCYENGGGAFLIPYLVALFTAGIPLLILEFGVGHERIGSAPLAFRKIGKQWEWLGWWPLLFTMFGIVLYYSVVIAWCIDFLFYSVKLAWGADSEAFFFKQFLQVSSGPTEISTIRTPILFGLLAVWALTWVIIMRGVSKGVELANMIFMPLLFVLTLVLVFWSLNLEGSMTGIVAYLKPDFSKLMDPKVWVSAYGQIFFTLSLGFGIMITYASYMPEKSNMTGSALITALVNSGFSLISGFGVFSILGFMATTQNVPVDEVVKESIGLAFIVYPKAISMIGDFGPMFGMLFFLSLTVAGVSSAISIVEAFASGLEDKFSINRKMLATLLCFLGFTGGVIFTTNGGLFWLDIVDHFINNYGLVLAGILECIVVGWFFNLDQIRKHLNKVSKIQLGPWWNWIIKLFLPLSLSVILLNQLIRELTTAYGGYTWASLIGIGWSWIVITFLVAFILAAQPWRTENHLEKGRGDEL
>NC_011027.1|WP_012501565.1|323669_324098_+|peptidylprolyl-isomerase
MAQVKQGDKVRVHYTGTYDDGTVFDSSVERDPLEVTVGTGMVIQGFDRALVDMEPGQKKNVNIPAAEAYGPRAEELVAEIPRERIPENIQLEVGQQLQLSLADGGEAIVMIVDLSEKTVTLDANHPMAGMDLNFELELVEIL
>NC_011027.1|WP_012501564.1|322403_323501_+|mechanosensitive-ion-channel
MNTLDSIIGLLQSQLGIWLGPILFVFLAVVLYLGANSLFKRSVAFFRKQGLVGSLPFERLVWPFRLIVVLAGSALFLDYVSLPDVSLRLLKHLFLILSIVTAAWFIMRMLAVLEQFILSHYQSRSGQSEIAAKKVATNVSLARKILNALIIVLAVSGVLMTFDTVRQVGLSILASAGIAGVILGFAAQKSLGTLIAGIQIAISQPISIDDVVIVEGEWGRIEEITLTYVVVLIWDQRRMIVPITWFLDKPFQNWTRTSTELLGTVYLYVDYAIPVESIRQELESIVASTPLWDKRVVRLHVTKATDKTVELRALMSAANSSDLWELRCLVRERLIDFIRINYPAGLPKVRMEVEGGAPVAVAVQE
>NC_011027.1|WP_012501563.1|321205_322396_+|FAD-dependent-oxidoreductase
MAKEVVIIGGGISGLSMAFYCSQAGMKTTLIEKDNKVGGSFASHQYASDNDRFWLEMGAHTCYSSYQNLLGIVEECGIMDTIIPREKVPFTLLKNGKVSSIMSGLNLFELLTHAPKIFSLKKEGKTVRSYYSQIVGENNYRNTISHFFNAVPSQPTDDFPADMMFKSREKRKDVLKNYTFKNGLQSVALTIAERKGIDVRTGSAAQSLANSDGKYVVKTADGQEVSADSLVIAVPSAPAARLLQDINPAIADHFTRLKFADVDSVGVVIRKNNVSLKPVAAIISPNDTFFSMVSRDTVPDDNFRGFAFHFRPGLSEKDKFKRINEVLGVGMEKIEHTTTRMNVVPSLRINHKDWADKTDQMLAGMRGLYMTGNYYGGMAIEDCVSRSHDEFNRMNR
>NC_011027.1|WP_156773446.1|334649_334745_+|hypothetical-protein
MALRTAKTGKNAGKQFWGCTGYPDCKEVVRV
>NC_011027.1|WP_012501574.1|334781_336056_-|Ni/Fe-hydrogenase-subunit-alpha
MKVDFNIDIHHLPRVEGHGDIRISVRDGKLVDAKWAVVETPRFFEVMVKGLSAERVPFLTSRICGICSISHSLASIRSLERAMQITPPETARIIRLLAMHGETLQSHALHLFFLAAPDFAGTPSAVPLLQSHPEVVEAGLMLKELGNELSIATTGRATHPVSLVLGGVSKAPSKQRLAEIKQMIVDRKPMLDKATEFFKTLTIPDFVRETEFISLFDGESYPYIGGDLVTTDGVRRDENDYLAMTNEYTVEFATTKFTKVSRESSAAGALARFNNNYDLLHPQAKAAAEAFGLKPVCHNPFMNNVAQLVECHHLVADAEEIIDCLLDDDLRDIKADYKPRAGAATGAVEAPRGVLYHYMETDENGKVVKGDCIIPTTQNNANIHYDLHALAEQALAQGKGEKEVEKLCEMLVRSYDPCISCSVH
>NC_011027.1|WP_012501575.1|336045_336813_-|NADH-ubiquinone-oxidoreductase
MNHLGFDIEKLKIGSFDFTCCEGCQLQLANKESTLPEFLALLDIRNFREISSERLDDYDIALVEGSITRQDEVERLKAIRAQAKVLVAYGTCACFGGMNAQKNKFDKEECIRTVYGDKEIDTMQESHKISDFVKVDYSIPGCPVNKEEVERIVVSIATRSPISLPKYPVCVECKQRLNTCLFDLGEVCLGPISRAGCDAVCPSGKTVCLGCRGPADDINYDSFVQLVREHGLSEDEMKEKLAFYNGFAEYLNHEG
>NC_011027.1|WP_041466231.1|336822_337647_-|oxidoreductase
MVTDHGYKCRITNIVPLSEHEKLFQLRIVDPHERALFTFRPGQFLMLDVPGYGEAPISISSATSNREFIELCIRKAGHVTSALFEAKQGAFIAVRGPFGTSFPMEAMQDSDVLLIAGGLGIAPLRAPLFWINDHRDHYRNVSFLYGAKEPSQMLFTYQFEEWKTVSHIDLHTIVEKPSDEWTGRTGMITSLFDDITIDPKNTWAIVCGPPVMFKFVCTHLDKLGIPMNRMFVSLERRMHCGMGKCCRCMVGSTFTCLDGPVFDYWSVMNLKEAI
>NC_011027.1|WP_012501577.1|337700_338780_-|hydrogenase
MIYKVISKPEFRAFVDALVRANTSYGPRQVDTDHNGEPIYQFMPVASADEIAFDYTVTTSSAKHLLMPFREELSKFSFKDKNWDQEVEYDAPPIVLFGLRPCDINAINILDEVMLKGPYPSPYYLARRKNTFIIGMDHLPLPDCFCRSMNKHTTDHGFNVFASDIGENYFLSINSSKAFNFLKEFETSDPTYEDDCKLIERRKLIKQSFKTNVEVTGLPMFLDLEFDSPIWEKWGDKCLNCGTCAMVCPTCYCYNMEEHLATDLESSSREKRLYSCNLIDFAEVTGGHNFRPKNGDRLKYRYYHHYRGFAVNDNQQICVGCNRCGRACLAGINPKDVINDLRLEKESCVTCVLPSPEKS
>NC_011027.1|WP_012501578.1|338889_340128_-|U32-family-peptidase
MPVTKPELISPAGDWTSMRAALDAGANAVYFGAEGFNMRAASKGFAPGDFGGIARLCRSHGAKAYLALNSVIYDAELGEVDRTVATAKAAGLDAVICWDLAVVEACRRHAMPIHLSTQASVSNISALRFYASLGARMIVLARELTLEQTAAITKCIAAEKLPVTVESFVHGAMCVAVSGRCFLSQELFGRSANRGECVQPCRRSYRIADVEEGFELELGSDYVMSPKDLCTLPFLDKLFDAGIGAFKIEGRNRSPEYVATTTAAYRKAIDFIAEHRDDENFDEAYRTLTDGLQDDLARVYNRGFSEGFFFGKPADAWTKHSGSVATETKSYVGVVRKYFPKAGVAEILVHAPSVDSGVTLSIQGSATGLVTVPDAELHLDGDPANRIGQGQVFTVRCNRVRKNDKVYVLLKK
>NC_011027.1|WP_012501579.1|340197_341007_+|hypothetical-protein
MNQRLVAGVLAGLSLAFIAAELLVATLGGFDTGWMVLLLSFYAGLVGLLFGVRTLSEGRREVVESVSERRARAKRDGLVGDLLDDYEIDEEFIGRGKRKFSASKPATSQPSASPSSGASGDRPLDDDELKSAITAHADMMGGLGNLRTRIEAMDDLDFYSMARKVGMAGVSRTRALAVVTELVSASGGAMLDEASPLSLSIDKGSFDDYIKRCMNNPDTRVDDEANDSESFSVGLDAGDLSSQPGTPPTEFSHDPKAVIERFKRSAGKR
>NC_011027.1|WP_041466097.1|341003_341810_+|RNA-methyltransferase
MRRETYPPLSKTMLGRLAKLSRKKYRDSEGLFLAEGLRTVSELLDSLPDLSMLHALVLDEAAAGQLDGLKRFAGKVWLGDADAFKRLAQTASPQGVCAAFRKPEMGEFRPAERSFVVALDDVQDPGNVGTIIRTAAWFGAEAVICGPGTADPWNAKTVRSTAGSIFALRIIDVPDLAAELKRLQAAGFTVAAAALDGQDYRSFGEWPDRRALVIGNEANGISEKVLALADSRLLIPHAGTHPAVESLNASVSAGILMARIALRANYEC
>NC_011027.1|WP_049755817.1|341944_342994_+|hypothetical-protein
MLRSVEQFIFRHLTPLSIRWLPAPDIERASGLAAEVYRQLDEEFMTVPPVTLHHLNSQLMAGVWSACRESLVAGPDRALKELIAVAVSQSNRCPYCVQAHSSMLQDANDRPALDAVSSGERANDDLSNLAAWASATGRKAALASVPPPFTKPQAPAFMATAVLFHYINRMVNIFLDDTMMPVVGKVPVIGDQAFRLFSSVTSGRIVRIDAKPGVFLTGSPAMKLPEEFGWAGDDPAVAGGLLRFADAVRAIADSVDSGVQSLVKRHVVAWQGEPPGIDKGWLEDAVRTLPEKLKPQARLALLAAMASWAVDSGEIASCRRAGLDDRALLETSAWGAYLATERIASWLSR
>NC_011027.1|WP_012501582.1|343022_343856_-|universal-stress-protein
MTHRIIHSIAVAIDCSPHSKASLEAAAEMASRLKAELIGIFVEDINLLHMAGLPFAEEIRLYTATTEKLDTAQLERLLRHQAQQAREMLEHIAQPRTLRHTFRVLRGLVPEQVMQAALEADMLVLGRSGRSPSCRKGLGSTARSALDKGSVNVMLMRPGVTAAEGPLLVLYDGSDASKRALATALEIAGPTSTLNLLITDPAPEAMERCKQETDAVVREKGLETEYYHLPFTDSRQLVSFIRMIDSGLLIIGKGMNLPEETVRELIDTIDYPVLVVR

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Crispr_ID: NC_011027_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_011027_3

356934-357033

Orphan

Consensus_repeat	Method
AACCCGACGGACATTCGACTCTTACATTGCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_011027_3

>merge|NC_011027|3|356934-357033|CRISPRCasFinder
AACCCGACGGACATTCGACTCTTACATTGCCGTTCAGTTGCCCCGGCTTCTTATACTCAGGAGAGTTTTAACCCGACGGATATTCGACTCTTACATTGCC

>NC_011027|3|3|356934-357033|CRISPRCasFinder
AACCCGACGGACATTCGACTCTTACATTGCC	GTTCAGTTGCCCCGGCTTCTTATACTCAGGAGAGTTTT
AACCCGACGGATATTCGACTCTTACATTGCC

Protein	Signature genes	Signature genes Name	Protein_function
NC_011027.1\|WP_156773340.1\|366060_366366_+\|hypothetical-protein	unknown	unknown	unknown
NC_011027.1\|WP_012501596.1\|360732_361386_+\|YukJ-family-protein	unknown	unknown	gnl\|CDD\|378365
NC_011027.1\|WP_012501583.1\|343872_346299_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|379314
NC_011027.1\|WP_012501591.1\|354501_355419_+\|decarboxylating-6-phosphogluconate-dehydrogenase	unknown	unknown	gnl\|CDD\|236582
NC_011027.1\|WP_012501600.1\|363760_365512_+\|L,D-transpeptidase-family-protein	unknown	unknown	gnl\|CDD\|225536
NC_011027.1\|WP_012501585.1\|347507_348896_+\|aldehyde-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|143406
NC_011027.1\|WP_012501587.1\|349915_350383_+\|YbaK/EbsC-family-protein	unknown	unknown	gnl\|CDD\|239824
NC_011027.1\|WP_012501595.1\|358550_360575_-\|transketolase	unknown	unknown	gnl\|CDD\|223100
NC_011027.1\|WP_012501590.1\|352810_354244_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|367817
NC_011027.1\|WP_156773448.1\|363117_363744_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379310
NC_011027.1\|WP_012501584.1\|346458_347211_-\|TerC-family-protein	unknown	unknown	gnl\|CDD\|223930
NC_011027.1\|WP_012501601.1\|365521_365989_+\|SRPBCC-family-protein	unknown	unknown	gnl\|CDD\|176861
NC_011027.1\|WP_012501586.1\|348900_349680_+\|patatin-like-phospholipase-family-protein	unknown	unknown	gnl\|CDD\|132844
NC_011027.1\|WP_012501593.1\|357120_357552_-\|IS200/IS605-family-transposase	unknown	unknown	gnl\|CDD\|376616
NC_011027.1\|WP_012501594.1\|357738_358554_-\|6-phosphogluconolactonase	unknown	unknown	gnl\|CDD\|238694
NC_011027.1\|WP_049755818.1\|351752_352823_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|349474
NC_011027.1\|WP_156773447.1\|361527_362214_+\|DUF541-domain-containing-protein	unknown	unknown	gnl\|CDD\|225516
NC_011027.1\|WP_012501598.1\|362246_362813_+\|hypothetical-protein	unknown	unknown	unknown
NC_011027.1\|WP_012501592.1\|355415_356837_+\|glucose-6-phosphate-dehydrogenase	unknown	unknown	gnl\|CDD\|235579
NC_011027.1\|WP_012501588.1\|350533_351664_+\|glycosyltransferase-family-1-protein	unknown	unknown	gnl\|CDD\|340842

Protein	Function_ID	Function_description	E-value
NC_011027.1\|WP_012501596.1\|360732_361386_+\|YukJ-family-protein	gnl\|CDD\|378365	pfam10042, DUF2278, Uncharacterized conserved protein (DUF2278). Members of this family of hypothetical bacterial proteins have no known function.	1.42772e-59
NC_011027.1\|WP_012501583.1\|343872_346299_-\|AAA-family-ATPase	gnl\|CDD\|379314	pfam13654, AAA_32, AAA domain. This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.	0
NC_011027.1\|WP_012501591.1\|354501_355419_+\|decarboxylating-6-phosphogluconate-dehydrogenase	gnl\|CDD\|236582	PRK09599, PRK09599, NADP-dependent phosphogluconate dehydrogenase.	0
NC_011027.1\|WP_012501600.1\|363760_365512_+\|L,D-transpeptidase-family-protein	gnl\|CDD\|225536	COG2989, COG2989, Uncharacterized protein conserved in bacteria [Function unknown].	7.18254e-122
NC_011027.1\|WP_012501585.1\|347507_348896_+\|aldehyde-dehydrogenase-family-protein	gnl\|CDD\|143406	cd07087, ALDH_F3-13-14_CALDH-like, ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins. ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.	0
NC_011027.1\|WP_012501587.1\|349915_350383_+\|YbaK/EbsC-family-protein	gnl\|CDD\|239824	cd04332, YbaK_like, YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, ProX, and PrdX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express an INS homolog in trans (e.g. YbaK, ProX, or PrdX).	1.36652e-30
NC_011027.1\|WP_012501595.1\|358550_360575_-\|transketolase	gnl\|CDD\|223100	COG0021, TktA, Transketolase [Carbohydrate transport and metabolism].	0
NC_011027.1\|WP_012501590.1\|352810_354244_-\|hypothetical-protein	gnl\|CDD\|367817	pfam04107, GCS2, Glutamate-cysteine ligase family 2(GCS2). Also known as gamma-glutamylcysteine synthetase and gamma-ECS (EC:6.3.2.2). This enzyme catalyzes the first and rate limiting step in de novo glutathione biosynthesis. Members of this family are found in archaea, bacteria and plants. May and Leaver discuss the possible evolutionary origins of glutamate-cysteine ligase enzymes in different organisms and suggest that it evolved independently in different eukaryotes, from an ancestral bacterial enzyme. They also state that Arabidopsis thaliana gamma-glutamylcysteine synthetase is structurally unrelated to mammalian, yeast and Escherichia coli homologs. In plants, there are separate cytosolic and chloroplast forms of the enzyme.	0.000264478
NC_011027.1\|WP_156773448.1\|363117_363744_+\|hypothetical-protein	gnl\|CDD\|379310	pfam13645, YkuD_2, L,D-transpeptidase catalytic domain. This family is related to pfam03734.	6.34117e-97
NC_011027.1\|WP_012501584.1\|346458_347211_-\|TerC-family-protein	gnl\|CDD\|223930	COG0861, TerC, Membrane protein TerC, possibly involved in tellurium resistance [Inorganic ion transport and metabolism].	1.40808e-73
NC_011027.1\|WP_012501601.1\|365521_365989_+\|SRPBCC-family-protein	gnl\|CDD\|176861	cd07819, SRPBCC_2, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.	1.45439e-53
NC_011027.1\|WP_012501586.1\|348900_349680_+\|patatin-like-phospholipase-family-protein	gnl\|CDD\|132844	cd07205, Pat_PNPLA6_PNPLA7_NTE1_like, Patatin-like phospholipase domain containing protein 6, protein 7, and fungal NTE1. Patatin-like phospholipase domain containing protein 6 (PNPLA6) and protein 7 (PNPLA7) are included in this family. PNPLA6 is commonly known as Neuropathy Target Esterase (NTE). NTE has at least two functional domains: the N-terminal domain putatively regulatory domain and the C-terminal catalytic domain which shows esterase activity. NTE shows phospholipase activity for lysophosphatidylcholine (LPC) and phosphatidylcholine (PC). Exposure of NTE to organophosphates leads to organophosphate-induced delayed neurotoxicity (OPIDN). OPIDN is a progressive neurological condition that is characterized by weakness, paralysis, pain, and paresthesia. PNPLA7 is an insulin-regulated phospholipase that is homologus to Neuropathy Target Esterase (NTE or PNPLA6) and is also known as NTE-related esterase (NRE). Human NRE is predominantly expressed in prostate, white adipose, and pancreatic tissue. NRE hydrolyzes sn-1 esters in lysophosphatidylcholine and lysophosphatidic acid, but shows no lipase activity with substrates like triacylglycerols (TG), cholesteryl esters, retinyl esters (RE), phosphatidylcholine (PC), or monoacylglycerol (MG). This family includes subfamily of PNPLA6 (NTE) and PNPLA7 (NRE)-like phospholipases.	4.82359e-74
NC_011027.1\|WP_012501593.1\|357120_357552_-\|IS200/IS605-family-transposase	gnl\|CDD\|376616	pfam01797, Y1_Tnp, Transposase IS200 like. Transposases are needed for efficient transposition of the insertion sequence or transposon DNA. This family includes transposases for IS200 from E. coli.	1.26743e-26
NC_011027.1\|WP_012501594.1\|357738_358554_-\|6-phosphogluconolactonase	gnl\|CDD\|238694	cd01400, 6PGL, 6PGL: 6-Phosphogluconolactonase (6PGL) subfamily; 6PGL catalyzes the second step of the oxidative phase of the pentose phosphate pathway, the hydrolyzation of 6-phosphoglucono-1,5-lactone (delta form) to 6-phosphogluconate. 6PGL is thought to guard against the accumulation of the delta form of the lactone, which may be toxic through its reaction with endogenous cellular nucleophiles.	8.78811e-82
NC_011027.1\|WP_049755818.1\|351752_352823_-\|hypothetical-protein	gnl\|CDD\|349474	cd06256, M14_ASTE_ASPA-like, Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup. A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.	1.62417e-99
NC_011027.1\|WP_156773447.1\|361527_362214_+\|DUF541-domain-containing-protein	gnl\|CDD\|225516	COG2968, COG2968, Uncharacterized conserved protein [Function unknown].	3.59012e-37
NC_011027.1\|WP_012501592.1\|355415_356837_+\|glucose-6-phosphate-dehydrogenase	gnl\|CDD\|235579	PRK05722, PRK05722, glucose-6-phosphate 1-dehydrogenase; Validated.	0
NC_011027.1\|WP_012501588.1\|350533_351664_+\|glycosyltransferase-family-1-protein	gnl\|CDD\|340842	cd03814, GT4-like, glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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. The members of this family are found mainly in bacteria and eukaryotes.	2.85632e-144

>NC_011027.1|WP_012501592.1|355415_356837_+|glucose-6-phosphate-dehydrogenase
MNGKPGNLTIVIFGADGDLASRKLFPSIFQLDRWGHMPEHFRVIGVGRRDLTHGVFRDFVRDRLLEHSPEAAGDDEQLKAFCDLFFYVNVDLRKPEAYQELREKIMEDETSSNLLFYLSIPPSLAPPVVRNLAEAGLGGREPNVPGWRKLVAEKPYGHDLESAHELNRVIDEAFDESQVYRIDHYLGKEPVQNIMVFRFSNGIFEPLWNRQYIAQVQITIAEDFGIRDRGGYYEEAGLLRDIIQNHGLQLLAAIAMEPPVDLSADGIRDEKSKILRSIRHFSPDTISDTAVVGQYEGYHSEKGVAPDSRVETFAAVKFHIDNWRWSGVPFYMKAGKNLAKHVTEIIITFKCPPQNYYGASAAACSTPNQVVLGIQPDETVAIRFGTKRPGEQMVTDPVFMKFDYRETFPGEQLTPYHRLLLDAIEGNQMNFIRKDSVETSWQIIDSLRDSLDGITPERYPPHSWGPDASHLYG
>NC_011027.1|WP_012501591.1|354501_355419_+|decarboxylating-6-phosphogluconate-dehydrogenase
MKIGFIGLGKMGFNMVEHLLELGHEVTAFDLSAEAVAAIAEKGATAASSLQHVVGDLPKPRVVWMMVPAGKAVDAVLDGLLPFLDKGDIVIDGGNSRYTDSVARAEKLRQQGVRMLDIGTSGGLDGARHGACMMAGGEREAYDVVEPMLRDLCVENGYGYMGASGAGHFVKMVHNGIEYGMMQAIGEGFDLLRASGFDLDNQNVARVWSNGSVIRGWLMDLAGKAFAQDNDLGWLGSKVADSGEGRWTVEAAIDLGVAVPIISGSLFRRFRSQSEENFSDKVVAALRHEFGGHAYEKPGDGEGKA
>NC_011027.1|WP_012501590.1|352810_354244_-|hypothetical-protein
MGREIEKTEFSEADFQQFRQNLRKETKLLMDWFTSSGFETEGVLCGLEVEAWLIDEAFAPVPKNEEFLQRVNNPLVVAELSKYNFEINVAPHPLNRNLASFLCQQLRTLWDTCSTHARDMGCQTLMTGILPTLQDRMLTLENISQLQRFHALNREILKSRSRHPLKIHIEGANDKLDVLHHDVMAEAATTSLQIHFQVPLSKAAAFYNVAHVLSAPMAALTANSPFLFGKELWHETRIPLFEQAVNTPSFVDREGRPVSRVTFGHDYVRNSLLEVFLENLDGYPALLPVNFDADPQMLEHLRLHNGTIWRWNRPLIGFGPDGKPHLRIEHRVPPAGPSIPDMVANILFFYGSMLNLQPEVPQAAISFEQARANFYAAARFGLDAEITWTNGKRLPVRDVLLQHLIPGAVLSLAAMGLDSSELRHYLIDILAKRVASGRNGAAWQKAFIANYGPDFRAMTQVCLENQSQNIPVHQWKL
>NC_011027.1|WP_049755818.1|351752_352823_-|hypothetical-protein
MEIVNEHYAPPELHLFDRLPDGFADVPLERLGSVLPGPSLIRIAGEEGPPLFVSVLLHGNETTGFYAMQRIISAYGAPEKPLPRPVLLFVGNVAAAEKGLRKLDGQADYNRIWQGNHHPEHRLAEKVMEEVRKAEPLAGIDLHNNTGKNPHYGCVNRLDCASLSLARRFSKIIVYFTEPHEVLSLAFSQICPTVTLECGVSGDEAGTNHVENYLRHCLELPEETLFTPPPNHLNEIYHTTARIIVPEGLDVGFGECTDGLDICFRKDLELLNFEPVPAGTELGKFNGEATALRVIDNRNRDVTERYLSFTDGRILTRVPVIPSMFTLDTKIIMDDCLGYVMETYRGKNEISSGSEG
>NC_011027.1|WP_012501588.1|350533_351664_+|glycosyltransferase-family-1-protein
MKVALYAGTYVKDKDGAVRSIYQLVASMVKSGHTVVVWTPDFTPGEDGMVPVNKVPSVPIPLYPDYKLGFFNAVVERQLDAFAPDIIHISTPDIVGRKFLQYARNRGIPVGSAYHTDFPSYLSYYRLGFAEPAVWKFLRKFYNACDVTLAPNEIVRQRLTGKGIERVELWSRGIDKELFDPSRRSEAMRRQWNAEGRTVIVYAGRFVLYKDIEVVMSLYQRFADEELGDKVRFVMIGSGPEEEQMRARMPEAVFTGYLTGTALPEAYASGDVFLFPSTTEAFCNVVLEALASGLPAVVSDIGGCMELVKRSDGGIVAKAGDIDEFFAACRKLIDDRDTYEAMKARGIAFAEDKSWAAVNGALIDRYRGMIAAKALG
>NC_011027.1|WP_012501587.1|349915_350383_+|YbaK/EbsC-family-protein
MPIRKLREFLDSHHIKYFVFSHSPAYTAQEIAESAHVSGKEMVKTVMVNIDGRMAMALLPASRQLDFDKLRMLCGTRDVKLAEEEEFSDLFPECEIGAMPPFGNLYAMEVYADEALDEDVDIAFNAGAHTELLRMGWEDYKRLAAPVIAPISVGL
>NC_011027.1|WP_012501586.1|348900_349680_+|patatin-like-phospholipase-family-protein
MDKANSESNLTGLAFGGGAVLGAAHIGVLKAMHETGFRADCVAGTSIGSFVAALHAFGKSWEEIEQIAVDLDWFDLSGLALSSYGLLSNRKFGRLVLKKLGRKRIEDAPIPLAIVATDICTGEKVVMRKGSVATAVMASSSIPGIFNPVKQKQMLLVDGLLTENVPVSPLKEMGASRIVCIDLLGRHSYRKPEHLAMLLMNAFYSAMRTMSEIQMEAADLVIRPNLSDFSLVDISAVPEIFEAGYREALPLLETWMAKA
>NC_011027.1|WP_012501585.1|347507_348896_+|aldehyde-dehydrogenase-family-protein
MPDFYDATTHAGLQRYFDSGATRSFEWRREQLRGLDAFLHEREAAIAEAVHADLGKPVAETWLTETGYLCTEIRYALRNLRRWMRPKRVGVPLHYQFARAFVEREPVGVALIIGAWNYPLQLCLAPLIGALAGGNCALLKPSELAPATSALLASELGRYVDPQAIRIVEGDGELSARLLEHRFDHIFFTGSRRTGQAVMQAAARHLTPVTLELGGKCPVIVTEQADLRVAARRIVWAKFLNAGQTCVSPDYLLVHHAVEERLLALMKEALATFYGPDPKLSPHYGRIVDERNFHRVKALQHEGSLVTGGGAELSSCCIEPTIVRNVPADSDLMSEEVFGPVLPVRAFSSFDEVAGLVASMPDPLALYLFSRDRSERRELMRRIRSGTVCCNDLLFQASIPGLPFGGRGMSGMGRYHGKAGFDTFTSERSVLCRSGFPDPDLRYPPYTACRFGLLKRIVTFFS
>NC_011027.1|WP_012501584.1|346458_347211_-|TerC-family-protein
MEWITSPEAWIALLTLTTLEIVLGIDNIIFLTIIVSRMPAEQQKSGRVLGLGLAMLSRIALLLSITWVMSLTNELFTAFGHAVTGRDLILLGGGLFLLAKSTHEIHQSLEGTEEVIKERSASNFVMTLIQIALIDIVFSLDSVITAVGLAKDIPVMILAIMIAVGIMMVAAQTIGEFVERHPTIKMLALSFLILVGATLVAEGAGFEFPRGYVYFAMAFSVSVEMLNLRLRKREAEPVHLRKAIEEEEAA
>NC_011027.1|WP_012501583.1|343872_346299_-|AAA-family-ATPase
MPVPEKLRPEQLFNRCDPDAFEFNTTADLDGTAEIAGQERALEAIRLGMGIRRDGFNLFALGPAGTGKQSTVLQFLNNLAPGEARPDDWCYVYNFDKPRNPKALRLPPGRACKLSDDMAHLVETLFSVMPSAFSSEEYQTREKEIEESIHEQQASAIEALEQDAKEHSISLIRTPGGFAFAPLKKGEVIKPDDYMRLKEAERAKIEEQIDRLRDVLQSIMAQFPKWQRETAEKIKELNREVSAFALKPLMDEIRAKYKDLDEVLKYLDDVQNDIIENFIQFLEKESSEQGAMTMLASLRTAGQRQTMIRYRVNVMIDNSELNGAPVILEDKPASQNLIGDIEHSAQMGTLVTDFTLIKPGALHRANGGYLILDARRLLLEPFAWEALKKAIRTRQIRIESLAQLYSLVSTISLEPEPIPLEIKVILLGERSLYYLLSSYDPDFNELFKIAADFENDMPRNDETQLAYARLIGSMAELDKLLPFDRTAVARIIEHGSRMAGDATRLTSNLQNIRDLAHEADHHAAQNGRKEVVAEDVEAMLEAQRYRASRIQERLRDNMMQGTILIDTDSEKTGQINGLSVYSLGDQSFGSPSRITARVRLGKGVVIDIEREVEMGGPIHSKGVMILSGFLGSRYAAEQPLSLSATLVFEQSYGGVEGDSASSAELYALLSAISGIPIRQWLAVTGSVNQHGEVQAIGGVNEKIEGFFDLCNERGLDGRHGVLIPASNVKHLMLRQDIVKAVESGLFSIWPVSHIDEGIELLTGIPAGEMDETGAWPEGTVNAKVYERLKTMAEKQKSFGKKQGDEPDK
>NC_011027.1|WP_012501593.1|357120_357552_-|IS200/IS605-family-transposase
MPFIKIWIHCVWATKNRSAMMDHSVRTNLFSHIANYAGNQGIFIDRINGGNDHVHLLISLGSNQNIARVIQTLKGESSCWMNKSGMLPFRFGWQDDYFAVSVSESQLDTVRAYIDGQIEHHRVKTFADEYQEFIEKFGFADRL
>NC_011027.1|WP_012501594.1|357738_358554_-|6-phosphogluconolactonase
MTHWISAPHDELLEKAVAAITDLAYRAVAERGRFTLVLSGGHTPAALYLKLARGIKEERYLELGYTLPDEARRPVRNPESIILPWPQTLLFQGDERYLPPSHPDSNYGMARKTLIRYICIKPADIHRMPTESGDPEADARRYEALIRGLFHKRGSDEAPPSFDLILLGLGDDGHTASLMPDDKAALNEKERWVIAVEAPNGKPPGTRLTLTLPVINEAKNVLFLVPPSRKDFARSISNGERPELPSGMVRPRSGDVWWFVEESQKQNQEML
>NC_011027.1|WP_012501595.1|358550_360575_-|transketolase
MTNTPSIEQQAISTIRLLAVDMVEKAKSGHPGLPLGAAPMAYTLFTKIMRFNPSNPEWPNRDRFVLSAGHGSALLYSLLHLCGYGLGMDELKQFRQLGSRTPGHPEYGETPGVEMTTGPLGQGIATAVGMAAAERFLAAKLNTPERALIDHFTYVLCGDGDLMEGVSSEASSLAGHLKLGKLICLYDSNHISIEGSTKLAFTENVAQRYEAYGWHVISHIDGNDTAAIEQAVRDAQEIDDRPSLIIVTTTIGYGSPHKQGTASAHGEPLGPDEAKLVKRAFGFPEDESFGVPEEVRDHFRTIAERGIGLEAEWKKLWKAFEREEPDLAAALTDLLAGRFPASWLPDMPEFTAGEKLATRQASKKVLGAIAEKIPLLAGGSADLAPSNGTLLGTAFEARSYDGSTFHFGVREHAMGAMVNGLALSNMMVPYGATFLVFADYMKPALRLAALMQSPSLFIFTHDSIGLGEDGPTHQPIEQLAMLRAMPGMDVYRPADANETKAAWLLALERRKPAALVLTRQGLPVIDDTDGRIRAGVPKGAYVLADWADGAEEQPGNCAIIVATGSEVHPALEAKARIEKEGYAVRVVSMPSKELFAEQSAAYRNSVLPANVTKRVVVEAATTFGWHDVAGSDGIVIGLDRFGASGPGPQVMEHFGFTASNIAAQTLELLKTGEA
>NC_011027.1|WP_012501596.1|360732_361386_+|YukJ-family-protein
MPLFDGYGVLAGTLLRYGCDNRQDETHYYHCSLLVRARASVYRCVVDLDSKHRRDGIQWKTVDLPHLRAAALTDRPDGWHDLEMEEHSGALDYYRSEWLGPSAECVRAGCEESASRMCWKYGTGHDAYRDLEPLLRRGRRIFVFGEPFRRGKGVHNIHQNQGDPPGSRWAAENGPWQDGSVMVERPDGSVVAFLSKFSTQRFCLDEHSATVSEADGR
>NC_011027.1|WP_156773447.1|361527_362214_+|DUF541-domain-containing-protein
MLLCFGVWPASLHAEVPAISVTASSTVRYEPDTAEFTTSVSATEKDASKAAARVAELWKSLQQSLRSAGIPAPDASSIAYSVNPQWEYNRTTGSRSLKGYTAQHTVRVTVRDLRKLGGAIDAVAGAGASTIQGLRYSSSRYDQFRTEALAEAVRNARHDAEVMAKAAGGRIGTVLDLAYTAQRPVIPVMRTMMAASPQAEESTELQPGEQEVTVSVSSRWQFLSVKGK
>NC_011027.1|WP_012501598.1|362246_362813_+|hypothetical-protein
MKEKILERYDRTDDNRVIIDVSASKVEELYEDFDKQAPYHRKDLDEELASYLVDCVREIGAADFVIRITLDRPLSAELQARIRTSLYKFFMYQRELEVASVKRILKRSLMLLFVGFALLFLSFRLHGDSVRPFYQNVLIEGVTIAAWVSLWESLSIALFNWWPSHHRIRLNFRIANAELLFQAQSSRL
>NC_011027.1|WP_156773448.1|363117_363744_+|hypothetical-protein
MSSMMRAIERNNDINPQALRLALQGYWNLYSEGQLRRKDVLTVIDFSKPSDTKRLFIIDVSQGKILQSSLVAHGRNSGGVYATNFSNRPGSYQSSLGFYLTSNTYDGKHGYSLVLKGIDRGINDNAEQRNIVLHGADYVSEQFIRCNGRLGRSLGCPAVPMEERFEVIDKIKDGSCLFIYHDGRDYASRSAVLNPEMASRIAQSDNPA
>NC_011027.1|WP_012501600.1|363760_365512_+|L,D-transpeptidase-family-protein
MRSIVRFWLVVFSFLHVATPAALHAAENDNEAAAPRLTIVGEQLKESLDRLQRSAGSISPARSVIVGQMQRFYDSLEYRIAWTNRKAIARLIEVIRQSADDGLDPSDYHLEEIRAAYDNPPTSPALQVRADLLMTDGLFTLLSHMRAGKVVPKSLDSNWNLPLSGPAKNSDDMLKSAVMDAKFPEMIASLRPSTPEYRLLRKGLAKYRKVAAAGGWKPVPAGPRIGDVGQIDERMPLIRKRLVVTGDLIEDGLTISAPANSADSTAARQAFVYTAELFDAVKAFQERHGLEVDGIIGTETAGAMAVPVEEWIDQIRINLERYRWYSSSLGSTYVMVNIPSFSVEFVRDDSVRWKSRVIVGKPNLQTPVFKAEIQSVIFNPRWVIPSGILAKEALPAIKKNLDYLSRHQLTVVNNQGKPVDPSSVNWAAYQGRGFPYRLVQASGDDGALGRIKFNMPNRFTVYMHDTPTKPLFERSYRAFSHGCVRVQNPNELGVLLFNDPVKWDMNRIEAMIDTGKTRTINLPERIPVYFMYQTAFPDGDNIDFRYDVYDRDPDLQKALDSTRERVIVEEALRPVMSSVVTKP
>NC_011027.1|WP_012501601.1|365521_365989_+|SRPBCC-family-protein
MSFTVTLDVSKSFETSAQPDKVFELLADVPRSASYFPDVEKLEPLGDNSYRWIMERIALGDHTLQQTIYACTYRSDPATLSVDWTPVDGEGNARVEGSWRIEPAGTGTKVQLHTKGTLEVDLPGFLQFLLSPLIELAFVQKIERYISNLQAAFEG
>NC_011027.1|WP_156773340.1|366060_366366_+|hypothetical-protein
MRPFAIFSVTTLVTFVLMLVANILALPVVFDTQGVGWSAAPFRSALVFVGNLLQWPMVAIYSLAGNRSNDGMVAIVVLSIIYGTGAVGIWAFWGRYRKVRK

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Crispr_ID: NC_011027_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_011027_4

2034621-2034757

Orphan

Consensus_repeat	Method
TCTCCATGCACTGCGACACCTGG	CRISPRCasFinder

2 spacers

The CRISPR arrays of NC_011027_4

>merge|NC_011027|4|2034621-2034757|CRISPRCasFinder
CCTCGATGCACTGTGACACGTGGGATCCAGACAAACCGACAGCACAGCCCGGAAAAATCTCCATGCACTGCGACACCTGGACGCCTGACGAACCGTCAAAACGCACCAGCAGGCTCTCCATGCATTGCGACACCTGG

>NC_011027|4|4|2034621-2034757|CRISPRCasFinder
CCTCGATGCACTGTGACACGTGG	GATCCAGACAAACCGACAGCACAGCCCGGAAAAA
TCTCCATGCACTGCGACACCTGG	ACGCCTGACGAACCGTCAAAACGCACCAGCAGGC
TCTCCATGCATTGCGACACCTGG

Protein	Signature genes	Signature genes Name	Protein_function
NC_011027.1\|WP_012503068.1\|2026334_2026826_-\|HEPN-domain-containing-protein	unknown	unknown	gnl\|CDD\|214800
NC_011027.1\|WP_012503075.1\|2033411_2034251_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187576
NC_011027.1\|WP_012503082.1\|2041218_2041431_-\|cysteine-rich-CWC-family-protein	unknown	unknown	gnl\|CDD\|379586
NC_011027.1\|WP_012503079.1\|2037988_2039824_+\|B12-binding-domain-containing-radical-SAM-protein	unknown	unknown	gnl\|CDD\|223963
NC_011027.1\|WP_012503070.1\|2027119_2027377_-\|DUF4160-domain-containing-protein	unknown	unknown	gnl\|CDD\|379344
NC_011027.1\|WP_156773524.1\|2025585_2025939_-\|peptidase-M4	unknown	unknown	gnl\|CDD\|377032
NC_011027.1\|WP_012503078.1\|2036207_2037992_+\|YcaO-like-family-protein	unknown	unknown	gnl\|CDD\|376866
NC_011027.1\|WP_012503084.1\|2043054_2043864_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213232
NC_011027.1\|WP_012503086.1\|2044652_2045390_-\|DNA-metabolism-protein	unknown	unknown	gnl\|CDD\|274851
NC_011027.1\|WP_012503083.1\|2041450_2042902_-\|glycerol-kinase-GlpK	unknown	unknown	gnl\|CDD\|198361
NC_011027.1\|WP_083762347.1\|2034817_2036200_+\|radical-SAM-protein	unknown	unknown	gnl\|CDD\|223714
NC_011027.1\|WP_012503080.1\|2039839_2040175_-\|cytochrome-c	unknown	unknown	gnl\|CDD\|376999
NC_011027.1\|WP_012503069.1\|2026865_2027123_-\|DUF2442-domain-containing-protein	unknown	unknown	gnl\|CDD\|378424
NC_011027.1\|WP_156773423.1\|2025449_2025608_-\|hypothetical-protein	unknown	unknown	unknown
NC_011027.1\|WP_012503085.1\|2043799_2044645_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|130314
NC_011027.1\|WP_012503081.1\|2040354_2041185_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293799
NC_011027.1\|WP_012503074.1\|2032868_2033339_+\|hypothetical-protein	unknown	unknown	unknown
NC_011027.1\|WP_012503071.1\|2027642_2029019_+\|TrpB-like-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|237087
NC_011027.1\|WP_012503073.1\|2030119_2032669_-\|ATP-dependent-Clp-protease-ATP-binding-subunit	unknown	unknown	gnl\|CDD\|223616
NC_011027.1\|WP_012503072.1\|2029173_2029863_-\|porin-family-protein	unknown	unknown	gnl\|CDD\|226163

Protein	Function_ID	Function_description	E-value
NC_011027.1\|WP_012503068.1\|2026334_2026826_-\|HEPN-domain-containing-protein	gnl\|CDD\|214800	smart00748, HEPN, Higher Eukarytoes and Prokaryotes Nucleotide-binding domain.	0.00572536
NC_011027.1\|WP_012503075.1\|2033411_2034251_-\|SDR-family-oxidoreductase	gnl\|CDD\|187576	cd05266, SDR_a4, atypical (a) SDRs, subgroup 4. Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended 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.	1.39987e-77
NC_011027.1\|WP_012503082.1\|2041218_2041431_-\|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.	5.88689e-05
NC_011027.1\|WP_012503079.1\|2037988_2039824_+\|B12-binding-domain-containing-radical-SAM-protein	gnl\|CDD\|223963	COG1032, COG1032, Fe-S oxidoreductase [Energy production and conversion].	1.27786e-25
NC_011027.1\|WP_012503070.1\|2027119_2027377_-\|DUF4160-domain-containing-protein	gnl\|CDD\|379344	pfam13711, DUF4160, Domain of unknown function (DUF4160).	1.1509e-20
NC_011027.1\|WP_156773524.1\|2025585_2025939_-\|peptidase-M4	gnl\|CDD\|377032	pfam03413, PepSY, Peptidase propeptide and YPEB domain. This region is likely to have an protease inhibitory function (personal obs:C Yeats). This model is likely to miss some members of this family as the separation from signal to noise is not clear. The name is derived from Peptidase & Bacillus subtilis YPEB.	2.20292e-10
NC_011027.1\|WP_012503084.1\|2043054_2043864_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213232	cd03265, ABC_DrrA, Daunorubicin/doxorubicin resistance ATP-binding protein. DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.	6.36845e-128
NC_011027.1\|WP_012503086.1\|2044652_2045390_-\|DNA-metabolism-protein	gnl\|CDD\|274851	TIGR03915, putative_DNA_metabolism_protein, probable DNA metabolism protein. This model represents a conserved hypothetical protein that almost invariably pairs with an uncharacterized radical SAM protein. The pair occurs in about twenty percent of completed prokaryotic genomes. About forty percent of the members of this family occur as fusion proteins, where the C-terminal domain belongs to the uracil-DNA glycosylase family, a DNA repair family (because uracil in DNA is deamidated cytosine). The linkage by gene clustering and correlated species distribution to a radical SAM protein, and by gene fusion to a DNA repair protein family, suggests a role in DNA modification and/or repair.	3.47397e-93
NC_011027.1\|WP_012503083.1\|2041450_2042902_-\|glycerol-kinase-GlpK	gnl\|CDD\|198361	cd07786, FGGY_EcGK_like, Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases. This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases.	0
NC_011027.1\|WP_083762347.1\|2034817_2036200_+\|radical-SAM-protein	gnl\|CDD\|223714	COG0641, AslB, Arylsulfatase regulator (Fe-S oxidoreductase) [General function prediction only].	2.06587e-40
NC_011027.1\|WP_012503080.1\|2039839_2040175_-\|cytochrome-c	gnl\|CDD\|376999	pfam03150, CCP_MauG, Di-haem cytochrome c peroxidase. This is a family of distinct cytochrome c peroxidases (CCPs) that contain two haem groups. Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c-type haem as an oxidisable substrate. However, since they possess two, instead of one, haem prosthetic groups, bacterial CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two haem groups have significantly different redox potentials. The high potential (+320 mV) haem feeds electrons from electron shuttle proteins to the low potential (-330 mV) haem, where peroxide is reduced (indeed, the low potential site is known as the peroxidatic site). The CCP protein itself is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. This family also includes MauG proteins, whose similarity to di-haem CCP was previously recognized.	5.06741e-08
NC_011027.1\|WP_012503069.1\|2026865_2027123_-\|DUF2442-domain-containing-protein	gnl\|CDD\|378424	pfam10387, DUF2442, Protein of unknown function (DUF2442). This family of bacterial and fungal proteins has several members annotated as being putative molybdopterin-guanine dinucleotide biosynthesis protein A; however this could not be verified. Hence the function is not known. This family also includes the DUF3532 that was found to be related and was merged into this family. Members of this family also fall into the NE0471 N-terminal domain-like superfamily, a family of proteins with a unique fold in SCOP:143880.	1.54558e-08
NC_011027.1\|WP_012503078.1\|2036207_2037992_+\|YcaO-like-family-protein	gnl\|CDD\|376866	pfam02624, YcaO, YcaO cyclodehydratase, ATP-ad Mg2+-binding. YcaO is an ATP- an Mg2+-binding protein involved in the peptidic biosynthesis of azoline. There three motifs involved in the binding are, in UniProtKB:P75838, 71-79: Sx3ExxER, 184-203: Sx6Ex3Qx3ExxER, and 286-290: RxxxE. Three slightly different functional families are represented in this family, proteins involved in TOMM (thiazole/oxazole-modified microcin) biogenesis, non-TOMM proteins such as UniProtKB:P75838, and TfuA-associated non-TOMM proteins involved in trifolitoxin biosynthesis. UniProtKB:P75838 hydrolyzes ATP to AMP and pyrophosphate.	8.07082e-33
NC_011027.1\|WP_012503085.1\|2043799_2044645_+\|ABC-transporter-permease	gnl\|CDD\|130314	TIGR01247, drrB, daunorubicin resistance ABC transporter membrane protein. This model describes daunorubicin resistance ABC transporter, membrane associated protein in bacteria and archaea. The protein associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other].	3.53378e-36
NC_011027.1\|WP_012503081.1\|2040354_2041185_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293799	cd07713, DHPS-like_MBL-fold, Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain. This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.	1.24503e-119
NC_011027.1\|WP_012503071.1\|2027642_2029019_+\|TrpB-like-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|237087	PRK12391, PRK12391, TrpB-like pyridoxal phosphate-dependent enzyme.	0
NC_011027.1\|WP_012503073.1\|2030119_2032669_-\|ATP-dependent-Clp-protease-ATP-binding-subunit	gnl\|CDD\|223616	COG0542, clpA, ATP-binding subunits of Clp protease and DnaK/DnaJ chaperones [Posttranslational modification, protein turnover, chaperones].	0
NC_011027.1\|WP_012503072.1\|2029173_2029863_-\|porin-family-protein	gnl\|CDD\|226163	COG3637, COG3637, Opacity protein and related surface antigens [Cell envelope biogenesis, outer membrane].	1.90705e-11

>NC_011027.1|WP_012503075.1|2033411_2034251_-|SDR-family-oxidoreductase
MSEKQRISILGCGWLGLPLARFLVGEGYAVKGSTTSEAKIAKMKEAGVEPFRIAIGESIEGDIASFLQSDILVVNIPPQRRPDVVEYHVGQISLLIDALADSPVKHVIFVSSTSVYPATGGEVVEADATDPDEADSPAGRALMYVEEMLRSESAFNTTVVRFGGLIGPGRNPAEFIQRMTEITSPAHPVNLIHLDDCVHVIAEIIRQGSWGEVFNACAPQHPTRGELYKAAAESHGFASLPEEASSNSHFKIVNSDWLVKKLDYKFLHPDPLGMARGGN
>NC_011027.1|WP_012503074.1|2032868_2033339_+|hypothetical-protein
MTVTHILLDDQNPLHRELPIYRSGKIGAVRLADKSYKVYDSMEISAHDYTALFHYGVIEQLNALPFISESNNGLDSWDEAFLPSGAIGRMIEIIDEFVGEISGKSPEKVMLGWQDDPERIAYWREIDPEKTIDFLRKFQEFATKVQEEEYDLEFIL
>NC_011027.1|WP_012503073.1|2030119_2032669_-|ATP-dependent-Clp-protease-ATP-binding-subunit
MEGNFSNRVQDVIRLSREEALRLGHDYIGTEHLLLGLIREGEGIGAKILKNLKVDLFKLKQKIEENTHPKVPATQMGNVPLTKQAEKVLKITYLEAKICKSTIIGTEHLLLSILKGDDNIAAQILEQFGVTYDQVRDELMTITTGRSEADEPPMEGSYSTGSASERPSKKSESKRGERTKTPVLDNFGRDITRLAMEDKLDPIIGREKEIERVAQVLSRRKKNNPVLIGEPGVGKTAIAEGLALKIVQRKVSRVLYDKRVVALDLAALVAGTKYRGQFEERMKALMNELERSRDVILFIDELHTIIGAGGASGSLDASNIFKPALARGELQCIGATTLDEYRQYIEKDGALDRRFQKIMVEPTTVEETIQILNNIKNKYEAHHHVQYSEEAIEKAVKLSERYITDRFLPDKAIDVMDEAGARVHLSNIHVPQDILELEKGIEEVKAEKNKVVKMQNFEEAARLRDKEKNMLEALDHAKQEWEEESAESVYDVTENDISSVIAMMTGIPVVRVAQSESKKLLNMEAELKKEVIGQDEAIKKITKAIQRTRAGLKDPMRPIGSFIFLGPTGVGKTELAKALTRYLFDSEDALIRADMSEYMEKFSVSRLVGAPPGYVGYEEGGQLTEKVRRKPYSVVLIDEIEKAHPDVFNILLQVLDEGVLTDGLGRKVDFRNTIIIMTSNIGAKEIKSFGTGMGFSAPEDTTGNYKAMKSTIEDALKRVFNPEFLNRIDDTIVFHQLEKSDIFQIIDITAGKLFKRLKEMGIDVRIDEKAKEFLVEKGYDQKYGARPLKRALQKYVEDPLAEEMLKGRFTEGSVIQITFDEKEKELRFSEGTAEPPAKKGKKEEKLDKE
>NC_011027.1|WP_012503072.1|2029173_2029863_-|porin-family-protein
MKKKLLALVAVLLATGAWSSTGYSAGNYVSANAGISWFGDAKLTDNADDEENFCVDLDSGIALTGAYGHDYGDYRIEAELGYQRNDIAKSIDYLYGSVYDEYSMTGNMSVISLMGNAYYDINLTDDLELFLTAGAGAAFVSFNDVGDVDDDFRYDKVTATAFAYQLGAGLSYKVAENLRLEARYRYFATADFTIDDTANFWDDYAEDDYMNTVKNISSSSVMLGLRLSL
>NC_011027.1|WP_012503071.1|2027642_2029019_+|TrpB-like-pyridoxal-phosphate-dependent-enzyme
MSTEPTKILLGEDELPRQWYNIQADLPSPMPPPVGLDGNPIGPDALAKVFPMNLIEQEVSTERWIDIPEEILGILKLWRPSPLYRARRLEAALGTPAKIYYKNEGVSPAGSHKPNTAVAQAWYNREFGIKYLTTETGAGQWGSALAMSCKLIGIECKVFMVRISFDQKPFRKIMMKTWGAECIPSPSPQTAIGRKILEEMPDTPGSLGIAISEAIEQAVERDDTRYALGSVLNHVMLHQTIIGLEAKKQFDKIGRYPDIVIGCAGGGSNFAGISFPFLYDKIHGRDVRVIGTEPEACPTLTRAPYAYDSGDVAMMTPLLPMHSLGHTFIPPAIHAGGLRYHGMAPLVSHTKQLGLIEATALPQTECYEAALLFAHTEGFIPAPETSHAIAQTIREAKQAKEEGKEKVILMNWSGHGLMDLQGYDAYLSGKISDYPLPEELLQRSLTASLAGLPKVPGV
>NC_011027.1|WP_012503070.1|2027119_2027377_-|DUF4160-domain-containing-protein
MFYGILIRMFFRDTEKHHLPHIHADYQGKVAVYSIIDGMLLAGELPPNKHKLVVAWIEIHQEDLLADWNLAVNGKKPFPIKGLDQ
>NC_011027.1|WP_012503069.1|2026865_2027123_-|DUF2442-domain-containing-protein
MRIAELHPQSDWVLSIVAEDGRVGIFDVSPYLEYEAFEALRDHEEFMKVSNGGYFIEWECGADLSADTIEARWQVVGEDAERITA
>NC_011027.1|WP_012503068.1|2026334_2026826_-|HEPN-domain-containing-protein
MKIHLGTVDLAGKGPGTFSMGTFKLSKDYRIDIFSSARQFLAAAEFCLNNGEIIEGKPMLLVPGVVCAAFACELCLKWLIYNETEEEVKGHRLTELYGLLSQDMQNHISAFQSAFSDFLQRNDDVFIKARYHHESELFAFRETEILQFAQFLVSTMESKNESA
>NC_011027.1|WP_156773524.1|2025585_2025939_-|peptidase-M4
MMIMKRYGYVAVGVMLSAWMFGGMFARSAYAADAGNDALTLQKPAISLSQAVNAAEKFTRGRAVRAELETHDGRPVYDVEVVDGMKVMDVRVDKDNGRVLAANIDKADHDDAHDAED
>NC_011027.1|WP_156773423.1|2025449_2025608_-|hypothetical-protein
MPMMQKIKGQQIRLPFLPERLRYPGKGFYERLDAAMVNRLMERSFRATCSFF
>NC_011027.1|WP_083762347.1|2034817_2036200_+|radical-SAM-protein
MASCRRQRLVMITALQPSPLSRSTTQTTAKGADSEMPAYSIEQKGDITFLQPSSGKFFVALDNRCGRWQMFDGNASEAQKAEIAASLKESPTPDLMEPDDDYLEVVIFITDRCNLGCVYCKYADLTQLSEVRGTDVEQICRTLEKLIRGKKQVRITFQGGEPLLMHREIDQICAFLTGNFSEIEFSFALQSNGTLLNDAILEMLKQYEITVGITIDGPASQHDLSRPFKNGEGSFATITSNLERLQKNNVRCGVLSVIRDPDELEALFRFNREELGLNSFYLKPLEFADSGAESSEEFSAYYGKLADRQLELIQELIRIHTTSGERIHEQMLKTVLGKMFRPSFYNDGCIRTPSCGSNERYKSMNCDGSVQWCAHLKNQQDEAVKQRSKERYGFCADCPISSICLSFCPAVIPGYRHGDPEACYLPLAKRFCTYRRQMMMSLFELMHENMQAVTACFMQK
>NC_011027.1|WP_012503078.1|2036207_2037992_+|YcaO-like-family-protein
MSSALEQMRVALRSTGMEVCEKTRQGSELPFFTTMLFAGKTPDDDSLPLVSGQGITAEASLLSAYGEFFERLQNNFIIAGYRYACASNGGYDRLPERCRQRLDRQGGPLDFFIAPDETWIAADRFGAAENPDLMPRHQMPASSGVDGDTLLCVPFYSVFDDSVRLCPIERMLFASGSTGCAAGRTLEQAIAKALFEICERHVFHRIFSDEPPLPLIPRELLRNTEADRIIEAIEERSTSVTLLDCSLGARFPVVAMLLIDRQRQRYNCNLGAAATLSGAVIGALKELYDGGNDFHALPLSGLDNPFAATTADESHRLRFANYYAAKASSTGLWPKSLFASRNSASQWIDETWSDELAGRPLKVLLERFASWTPTLYIRDVSWLGIPSVYCYAPGLSEVNYTTGRNELTMLLELRAESERLQSSGEMEMKRLLRIMELHRSLKRITLPASVRLLNSFACPNLPGSARQREATLLAALAQLFGDKTPHDESLLDRCIRDSKQLADESCNAAEINSQLRQFYPDSVVDLAARCRQAPAEVIENALHSIELPGNESACDDCHFLKTVETARRLQKRQITNLPDQRRLAEILTTARNET
>NC_011027.1|WP_012503079.1|2037988_2039824_+|B12-binding-domain-containing-radical-SAM-protein
MTIALTIFPCFSDKTLPLGLACLKSVLDGEGIESEVFDFDLLLSIEDPALYYQLHRLGASPGAALDDRMINFIGYRPDLTLAALFTPPEEARKRFETDGLEQLFDKLDHFLERAVTRLLATEPEQIWLSTYISNLWVSMLAARKLRERTEATIVFGGPAVFPEEVQRFLIVNGLADRVVVGEGELTARELIRANGRPVAGAAQMIEGEFRYEPRHEWLRPEEFPMPDFKGFPFADTPFDAYLRRRFEGLPVSFSRGCVNGCIYCSEKQIWKRFRHLSPEASVERLAAYKQRFGIGLFYICDSLINFSEAWLSEFCDLILSSDLQPLFTFAFCDLKHLKPELTAKMAAAGFTRITFGLESASENVLTRMHKKLDLDLARENIVAATRNGLSIHVSTIINFPGEQTADALDTIRFFREIDRELAGNNLPMTHLPRRSLSNRFRLEPASAIYLHPEHYGIRMETTGASWTPLAEESAFLAKRWRSSDDQEQLEWNAYLLSGFSKNPRPWHLHDSQYRKQAEAIAPLIDKEKHRFTLSPHVVLRQSTPENGLILHDYREEFQLDDWQSQVIRLLAKKASLHEITEKITALTEAKSAGAIRDFVLFLYVRGIARIT
>NC_011027.1|WP_012503080.1|2039839_2040175_-|cytochrome-c
MMKSVKTAMLVAAMVGMGTAAQAAQTPSVELGKKLFNDPTLGGATGTKTCASCHPNGKGVENAWQNPKLVQQINTCIAGALRGKPLPLESVEMKSLILYHQSLNPSSSLGK
>NC_011027.1|WP_012503081.1|2040354_2041185_+|MBL-fold-metallo-hydrolase
MKLTILTDNQAAPGLACEHGFAVLIETGGKRILFDTGQLGAFDANCRALGIDLSDIDIIVLSHGHYDHTGNLADVLRIADRATLYLHPSALVERYSIRNGKPKPIDMPEAAKQAIDELPKERIVWVSEPTRLTDGVFLTGPVPRQTTFEDTGGPFFFDPDGKTPDPIEDDLSLWIEKPEGLTVLAGCCHSGIVNTLDYIESITGQKRIATLIGGMHLSAASPERLDRTVASLAERDIARLIPCHCTGEAAAERFSKELPYPVEAGYAGMVVELGKK
>NC_011027.1|WP_012503082.1|2041218_2041431_-|cysteine-rich-CWC-family-protein
MTHNDHPGEGVPKTVVCPMCGEQFTCGMSTSCWCATRVVPDSVRNYLAERYETCVCSTCLDRLIAEAKGE
>NC_011027.1|WP_012503083.1|2041450_2042902_-|glycerol-kinase-GlpK
MAILSIDQGTTGTTCMIYDRSGNVLARAYRELTQCYPQAGWVEHDPKEIWQTVVECVVEVRGAYSGHIEAIGITNQRETTVVWDRRNGEPVHRAIVWQCRRTAELCNRYRGEEAAIRAKTGLPVDAYFSATKIRWILDAHPEADPSNLLFGTIDTWLIWKLTGGEVHATDLTNASRTLLFDIHERRWDAELCELFGVPLSMLPEVRPSMGGFGAVRAIPELDGVPIAGVAGDQQAALFGQCCFESGSVKNTYGTGCFMVMNTGDKCVSSSHGLLTTLALDGAGRSCYAVEGSVFIGGAVMQWLRDGLQLIGSAAESEAIARSVESNGGVYVVPAFVGLGAPHWNMEVRGTITGLTRGSSRVHIVRAALESIAYQSHDVFRAMVADTGIQPQSLTVDGGAVSNEFLMQFQADLLGVPVHRPRNIESTALGAACLAGLEAGVWNSADELRALNGVERVFTPAMPEAERETLLAGWQKALRQTLVS
>NC_011027.1|WP_012503084.1|2043054_2043864_+|ATP-binding-cassette-domain-containing-protein
MPQPTTDIAIQTDRLTRSFGSLVAVNELNLTVRSSEIFGLLGPNGAGKTTTIKMLTTMLPPTSGAATVAGHSILGDSIGVRKRIGYVSQMISADGALTGFENLLLFARIYNVPRRERTRRIDEALAFMGLTDARDKLVRTYSGGMIRRLEIALSMLHRPEVLFLDEPTIGLDPAARLQVWKRLKELLKTFGTTILLTTHDMEEAEELCDRIAIMKEGVIAAEGSAKELKHRAGTDSMNQVFIHFAGEFSDSKPNFRDINRTRRTAKRLG
>NC_011027.1|WP_012503085.1|2043799_2044645_+|ABC-transporter-permease
MTASQTSATSTALAGRPNGWAEKFDPAGFLRDTAAIVATELAKLRRDPSEILSRSIQPALWLLVFGQVFGRMRAIPTGKLDYFSFLAPGILAQSVLFIAIFYGINVIWEKDLGILQKLLASPAPRSALVFGKAVSAGMRAIAQAAIVYLMALVAGVHLNWSPLALGGVLVAIVLGAALFSTFSLMIACLVRSRERFMGIGQVMTMPLFFASNAIYPISIMPTWLKIVAHINPLSYQVDLLRALMVVGGTSTFGIGMDFLMLIGMLVALIVVTSKLYPTIVQ
>NC_011027.1|WP_012503086.1|2044652_2045390_-|DNA-metabolism-protein
MNKYLYDGTPEGLVSAIGAILESGDDPEKTVLGIRQDTLFEEGLFLRTDSAFAEALFGRLRQRAPDAVQTLWYFTMAETSELETSLLRYIALAFEHGDRVNGYLTHPDVKAVVAIARKAGRELHRMKGLLRFEQLRDGSWLARMEPDHNVIQPLARHFSRRLRAQEWFIYDARRHSAAHWNGHALSFGNLEQFSRPKLSPEERVVQQHWQTFFKTIAIPERKNPRLQQSNMPAKYWKYLTEKQGE

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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

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

1888106 : 1896903

Enterobacteria_phage(50.0%)

tRNA

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_012502951.1\|1888106_1891349_-\|tRNA	isoleucine--tRNA ligase	A0A2I2L3Y0	Orpheovirus	5.9e-169	33.5
WP_012502952.1\|1891530_1891752_-	hypothetical protein	NA	NA	NA	NA
WP_012502953.1\|1891875_1893285_-	mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase	A0A1V0SH58	Hokovirus	1.5e-55	29.3
WP_012502954.1\|1893333_1894383_-	dTDP-glucose 4,6-dehydratase	I7HTA3	Enterobacteria_phage	2.8e-88	50.3
WP_012502955.1\|1894467_1895343_-	dTDP-4-dehydrorhamnose reductase	I7HXC9	Enterobacteria_phage	9.8e-34	37.5
WP_012502956.1\|1895377_1895935_-	dTDP-4-dehydrorhamnose 3,5-epimerase	A0A291LA62	Escherichia_phage	1.3e-47	54.2
WP_012502957.1\|1896021_1896903_-	glucose-1-phosphate thymidylyltransferase RfbA	I7I009	Enterobacteria_phage	5.6e-106	62.5

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. NC_011027

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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