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
NZ_CP023681	Zymomonas mobilis subsp. mobilis strain ZM4 substr. 2032 plasmid pZM39, complete sequence	0 crisprs	NA	0	0	0
NZ_CP023680	Zymomonas mobilis subsp. mobilis strain ZM4 substr. 2032 plasmid pZM36, complete sequence	0 crisprs	NA	0	0	2
NZ_CP023679	Zymomonas mobilis subsp. mobilis strain ZM4 substr. 2032 plasmid pZM33, complete sequence	0 crisprs	NA	0	0	0
NZ_CP023678	Zymomonas mobilis subsp. mobilis strain ZM4 substr. 2032 plasmid pZM32, complete sequence	0 crisprs	NA	0	0	0
NZ_CP023677	Zymomonas mobilis subsp. mobilis strain ZM4 substr. 2032 chromosome, complete genome	4 crisprs	cas1,cas3f,cas8f,cas5f,cas7f,cas6f,DinG,csa3,PD-DExK	1	5	2

Results visualization

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CRISPR-Cas detection and classification

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

2696 : 14768

Burkholderia_phage(27.27%)

tail,plate

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_062339727.1\|2696_3614_+	hypothetical protein	R4JDM0	Burkholderia_phage	5.9e-66	46.4
WP_062339728.1\|3610_4162_+\|tail	phage tail protein I	V9IQK7	Stenotrophomonas_phage	5.4e-38	41.5
WP_062339731.1\|4161_6666_+	hypothetical protein	V9IQX0	Stenotrophomonas_phage	7.1e-37	50.3
WP_108128663.1\|6689_7148_+	hypothetical protein	NA	NA	NA	NA
WP_081094487.1\|7376_7913_+\|plate	phage baseplate assembly protein V	NA	NA	NA	NA
WP_012954685.1\|7997_8339_+	GPW/gp25 family protein	A0A077K8R5	Ralstonia_phage	8.5e-18	43.4
WP_012954684.1\|8338_9496_+\|tail	tail sheath protein	S4TRX2	Salmonella_phage	2.2e-86	46.1
WP_012954683.1\|9515_10028_+\|tail	phage major tail tube protein	R4JEU1	Burkholderia_phage	1.8e-24	37.6
WP_012954682.1\|10111_10492_+\|tail	phage tail assembly protein	R4JJY8	Burkholderia_phage	3.5e-12	45.3
WP_012954681.1\|10500_10635_+\|tail	GpE family phage tail protein	A0A2H4JFK5	uncultured_Caudovirales_phage	2.4e-08	61.5
WP_160327983.1\|10624_13243_+\|tail	phage tail tape measure protein	A0A088FV68	Escherichia_phage	2.7e-23	27.5
WP_062339739.1\|13242_13788_+\|tail	phage tail protein	Q9ZXJ9	Pseudomonas_virus	2.5e-19	32.0
WP_062339740.1\|13784_14768_+	hypothetical protein	A0A0F7LDR0	Escherichia_phage	3.9e-39	29.8

DBSCAN-SWA_2

28793 : 36436

Burkholderia_phage(37.5%)

head,portal,tail,capsid

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_062339711.1\|28793_29444_+	AAA family ATPase	K7R2R7	Vibrio_phage	4.5e-36	40.7
WP_062339713.1\|29436_29664_+	hypothetical protein	NA	NA	NA	NA
WP_012954703.1\|30021_31041_-\|portal	phage portal protein	E5FFI9	Burkholderia_phage	3.2e-84	48.2
WP_062339714.1\|31040_32816_-	oxidoreductase	E5FFI8	Burkholderia_phage	1.8e-164	50.4
WP_062339716.1\|32948_33758_+	hypothetical protein	Q01088	Escherichia_phage	6.5e-24	34.2
WP_063630122.1\|33799_34951_+\|capsid	phage major capsid protein, P2 family	Q9ZXM3	Pseudomonas_virus	5.5e-77	46.1
WP_062339718.1\|34953_35745_+	hypothetical protein	E5E3W7	Burkholderia_phage	5.7e-33	46.5
WP_062339719.1\|35741_36227_+\|head	head completion/stabilization protein	A0A0M3LPQ0	Mannheimia_phage	3.9e-24	38.5
WP_012954697.1\|36223_36436_+\|tail	tail X family protein	A0A077K8R0	Ralstonia_phage	1.6e-06	42.2

Anti-CRISPR protein detection

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

2. NZ_CP023677

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP023677_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023677_1

113783-114170

Orphan

I-F

Consensus_repeat	Method
TTTCTAAGCTGCCTATGCGGCAGTGAAC	CRT
TTTCTAAGCTGCCTATGCGGCAGTGAAC	PILER-CR

6 spacers

The CRISPR arrays of NZ_CP023677_1

>merge|NZ_CP023677|1|113783-114170|CRT,PILER-CR
ATTTGATGCTGCCTGTGCGGCAGTGAACATACCGAGAACGATTATTGCCCGTAGTGTAAATTTCTAAGCTGCCTGTGCGGCAGTGAACGTTTGCTGCCATAAAATGCTCCTGCCGTGCAATTTCTAAGCTGCCTATGCGGCAGTGAACTGAAAAAGGGTGACCCTATCAAAGTAGGGGCTTTTCTAAGCTGCCTATGCGGCAGTGAACCAAAACTGTCATATCGTAGCTAATATCTTCACTTTCTAAGCTGCCTATGCGGCAGTGAACACAGCTAAAACCCTTTTACCTTTACTGTCGGCTTTCTAAGCTGCCTATGCGGCAGTGAACTGAAAAAGGGTGACCCTATCAAAGTAGGGGCTTTTCTAAGCTGCCTATGCGGCAGTGAAC

>NZ_CP023677|1|1|113783-114170|CRT
ATTTGATGCTGCCTGTGCGGCAGTGAAC	ATACCGAGAACGATTATTGCCCGTAGTGTAAA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	GTTTGCTGCCATAAAATGCTCCTGCCGTGCAA
TTTCTAAGCTGCCTATGCGGCAGTGAAC	TGAAAAAGGGTGACCCTATCAAAGTAGGGGCT
TTTCTAAGCTGCCTATGCGGCAGTGAAC	CAAAACTGTCATATCGTAGCTAATATCTTCAC
TTTCTAAGCTGCCTATGCGGCAGTGAAC	ACAGCTAAAACCCTTTTACCTTTACTGTCGGC
TTTCTAAGCTGCCTATGCGGCAGTGAAC	TGAAAAAGGGTGACCCTATCAAAGTAGGGGCT
TTTCTAAGCTGCCTATGCGGCAGTGAAC

>NZ_CP023677|1|1|113843-114170|PILER-CR
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	GTTTGCTGCCATAAAATGCTCCTGCCGTGCAA
TTTCTAAGCTGCCTATGCGGCAGTGAAC	TGAAAAAGGGTGACCCTATCAAAGTAGGGGCT
TTTCTAAGCTGCCTATGCGGCAGTGAAC	CAAAACTGTCATATCGTAGCTAATATCTTCAC
TTTCTAAGCTGCCTATGCGGCAGTGAAC	ACAGCTAAAACCCTTTTACCTTTACTGTCGGC
TTTCTAAGCTGCCTATGCGGCAGTGAAC	TGAAAAAGGGTGACCCTATCAAAGTAGGGGCT
TTTCTAAGCTGCCTATGCGGCAGTGAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023677.1\|WP_014500662.1\|122738_124106_+\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP023677.1\|WP_160327976.1\|122579_122729_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023677.1\|WP_011240087.1\|106316_107483_+\|Na+/H+-antiporter-NhaA	unknown	unknown	gnl\|CDD\|377746
NZ_CP023677.1\|WP_012817485.1\|111116_112700_-\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|223510
NZ_CP023677.1\|WP_011240092.1\|112712_113186_-\|Cys-tRNA(Pro)-deacylase	unknown	unknown	gnl\|CDD\|237976
NZ_CP023677.1\|WP_011240083.1\|102403_103015_+\|aminodeoxychorismate/anthranilate-synthase-component-II	unknown	unknown	gnl\|CDD\|235552
NZ_CP023677.1\|WP_011240096.1\|119336_120281_-\|metallophosphoesterase	unknown	unknown	gnl\|CDD\|277347
NZ_CP023677.1\|WP_011240099.1\|125250_125751_+\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP023677.1\|WP_011240088.1\|107643_108711_+\|dihydroorotate-oxidase	unknown	unknown	gnl\|CDD\|239204
NZ_CP023677.1\|WP_011240084.1\|102980_103817_+\|aminotransferase	unknown	unknown	gnl\|CDD\|238800
NZ_CP023677.1\|WP_017466460.1\|120788_121607_+\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP023677.1\|WP_011240086.1\|104520_106158_+\|hydroxylamine-reductase	unknown	unknown	gnl\|CDD\|235391
NZ_CP023677.1\|WP_011240095.1\|118384_119179_-\|phosphatase-PAP2-family-protein	unknown	unknown	gnl\|CDD\|239491
NZ_CP023677.1\|WP_011240089.1\|108978_110328_+\|replication-associated-recombination-protein-A	unknown	unknown	gnl\|CDD\|237355
NZ_CP023677.1\|WP_017466461.1\|121837_122560_+\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP023677.1\|WP_011240090.1\|110562_110850_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023677.1\|WP_017466287.1\|124243_125068_+\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP023677.1\|WP_011240094.1\|115569_118062_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP023677.1\|WP_011240085.1\|104016_104454_+\|Rrf2-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224870
NZ_CP023677.1\|WP_011240093.1\|114592_115552_-\|S1/P1-Nuclease	unknown	unknown	gnl\|CDD\|367008

Protein	Function_ID	Function_description	E-value
NZ_CP023677.1\|WP_011240087.1\|106316_107483_+\|Na+/H+-antiporter-NhaA	gnl\|CDD\|377746	pfam06965, Na_H_antiport_1, Na+/H+ antiporter 1. This family contains a number of bacterial Na+/H+ antiporter 1 proteins. These are integral membrane proteins that catalyze the exchange of H+ for Na+ in a manner that is highly dependent on the pH.	2.89579e-139
NZ_CP023677.1\|WP_012817485.1\|111116_112700_-\|ATP-binding-protein	gnl\|CDD\|223510	COG0433, COG0433, HerA helicase [Replication, recombination, and repair].	1.16328e-14
NZ_CP023677.1\|WP_011240092.1\|112712_113186_-\|Cys-tRNA(Pro)-deacylase	gnl\|CDD\|237976	cd00002, YbaK_deacylase, This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's.	4.97033e-68
NZ_CP023677.1\|WP_014500662.1\|122738_124106_+\|sel1-repeat-family-protein	gnl\|CDD\|276807	sd00010, SLR, Sel1-like repeat. Sel1-like repeats (SLRs) share similar alpha-helical conformations with Tetratricopeptide repeats (TPRs), but with different consensus sequence lengths and superhelical topologies. SLRs contain 36 to 44 amino acids and are present in bacteria and eukaryotes but not in archaea. SLR proteins are involved in a variety of functions, and many serve as adaptor proteins for the assembly of macromolecular complexes. The SLR family was named after the Caenorhabditis elegans Sel1 protein which is predicted to fold into 11 SLRs, a transmembrane domain, and an N-terminal signal sequence. The human Sel1L protein contains an additional fibronectin type-II domain and an N-terminal PEST sequence. Its downregulation is associated with the development of breast and pancreatic carcinomas.	5.46246e-41
NZ_CP023677.1\|WP_011240096.1\|119336_120281_-\|metallophosphoesterase	gnl\|CDD\|277347	cd07402, MPP_GpdQ, Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain. GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	1.68496e-18
NZ_CP023677.1\|WP_011240099.1\|125250_125751_+\|sel1-repeat-family-protein	gnl\|CDD\|276807	sd00010, SLR, Sel1-like repeat. Sel1-like repeats (SLRs) share similar alpha-helical conformations with Tetratricopeptide repeats (TPRs), but with different consensus sequence lengths and superhelical topologies. SLRs contain 36 to 44 amino acids and are present in bacteria and eukaryotes but not in archaea. SLR proteins are involved in a variety of functions, and many serve as adaptor proteins for the assembly of macromolecular complexes. The SLR family was named after the Caenorhabditis elegans Sel1 protein which is predicted to fold into 11 SLRs, a transmembrane domain, and an N-terminal signal sequence. The human Sel1L protein contains an additional fibronectin type-II domain and an N-terminal PEST sequence. Its downregulation is associated with the development of breast and pancreatic carcinomas.	1.00785e-38
NZ_CP023677.1\|WP_011240088.1\|107643_108711_+\|dihydroorotate-oxidase	gnl\|CDD\|239204	cd02810, DHOD_DHPD_FMN, Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.	6.73801e-102
NZ_CP023677.1\|WP_011240084.1\|102980_103817_+\|aminotransferase	gnl\|CDD\|238800	cd01559, ADCL_like, ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.	9.40565e-68
NZ_CP023677.1\|WP_017466460.1\|120788_121607_+\|sel1-repeat-family-protein	gnl\|CDD\|276807	sd00010, SLR, Sel1-like repeat. Sel1-like repeats (SLRs) share similar alpha-helical conformations with Tetratricopeptide repeats (TPRs), but with different consensus sequence lengths and superhelical topologies. SLRs contain 36 to 44 amino acids and are present in bacteria and eukaryotes but not in archaea. SLR proteins are involved in a variety of functions, and many serve as adaptor proteins for the assembly of macromolecular complexes. The SLR family was named after the Caenorhabditis elegans Sel1 protein which is predicted to fold into 11 SLRs, a transmembrane domain, and an N-terminal signal sequence. The human Sel1L protein contains an additional fibronectin type-II domain and an N-terminal PEST sequence. Its downregulation is associated with the development of breast and pancreatic carcinomas.	1.18005e-40
NZ_CP023677.1\|WP_011240086.1\|104520_106158_+\|hydroxylamine-reductase	gnl\|CDD\|235391	PRK05290, PRK05290, hybrid cluster protein; Provisional.	0
NZ_CP023677.1\|WP_011240095.1\|118384_119179_-\|phosphatase-PAP2-family-protein	gnl\|CDD\|239491	cd03397, PAP2_acid_phosphatase, PAP2, bacterial acid phosphatase or class A non-specific acid phosphatases. These enzymes catalyze phosphomonoester hydrolysis, with optimal activity in low pH conditions. They are secreted into the periplasmic space, and their physiological role remains to be determined.	1.05029e-94
NZ_CP023677.1\|WP_011240089.1\|108978_110328_+\|replication-associated-recombination-protein-A	gnl\|CDD\|237355	PRK13342, PRK13342, recombination factor protein RarA; Reviewed.	0
NZ_CP023677.1\|WP_017466461.1\|121837_122560_+\|sel1-repeat-family-protein	gnl\|CDD\|276807	sd00010, SLR, Sel1-like repeat. Sel1-like repeats (SLRs) share similar alpha-helical conformations with Tetratricopeptide repeats (TPRs), but with different consensus sequence lengths and superhelical topologies. SLRs contain 36 to 44 amino acids and are present in bacteria and eukaryotes but not in archaea. SLR proteins are involved in a variety of functions, and many serve as adaptor proteins for the assembly of macromolecular complexes. The SLR family was named after the Caenorhabditis elegans Sel1 protein which is predicted to fold into 11 SLRs, a transmembrane domain, and an N-terminal signal sequence. The human Sel1L protein contains an additional fibronectin type-II domain and an N-terminal PEST sequence. Its downregulation is associated with the development of breast and pancreatic carcinomas.	6.08471e-43
NZ_CP023677.1\|WP_011240083.1\|102403_103015_+\|aminodeoxychorismate/anthranilate-synthase-component-II	gnl\|CDD\|235552	PRK05670, PRK05670, anthranilate synthase component II; Provisional.	1.6661e-98
NZ_CP023677.1\|WP_017466287.1\|124243_125068_+\|sel1-repeat-family-protein	gnl\|CDD\|276807	sd00010, SLR, Sel1-like repeat. Sel1-like repeats (SLRs) share similar alpha-helical conformations with Tetratricopeptide repeats (TPRs), but with different consensus sequence lengths and superhelical topologies. SLRs contain 36 to 44 amino acids and are present in bacteria and eukaryotes but not in archaea. SLR proteins are involved in a variety of functions, and many serve as adaptor proteins for the assembly of macromolecular complexes. The SLR family was named after the Caenorhabditis elegans Sel1 protein which is predicted to fold into 11 SLRs, a transmembrane domain, and an N-terminal signal sequence. The human Sel1L protein contains an additional fibronectin type-II domain and an N-terminal PEST sequence. Its downregulation is associated with the development of breast and pancreatic carcinomas.	1.13091e-44
NZ_CP023677.1\|WP_011240094.1\|115569_118062_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	1.31836e-38
NZ_CP023677.1\|WP_011240085.1\|104016_104454_+\|Rrf2-family-transcriptional-regulator	gnl\|CDD\|224870	COG1959, COG1959, Predicted transcriptional regulator [Transcription].	7.93449e-32
NZ_CP023677.1\|WP_011240093.1\|114592_115552_-\|S1/P1-Nuclease	gnl\|CDD\|367008	pfam02265, S1-P1_nuclease, S1/P1 Nuclease. This family contains both S1 and P1 nucleases (EC:3.1.30.1) which cleave RNA and single stranded DNA with no base specificity.	5.776e-93

>NZ_CP023677.1|WP_011240092.1|112712_113186_-|Cys-tRNA(Pro)-deacylase
MTKKTRGTAFLEKAGIAFTVHPYDYDPKAPAAGLQAAEALQQPAEIVYKTLMTEVDGKPVCVVVQVNHEVSMKKLAAAAGGKSANMIKPVDAERMTGYHVGGISPFGQKKRVPVIFDESAFQAEKIFINGGQRGVLVALAPEDARRAVDGKIASVAN
>NZ_CP023677.1|WP_012817485.1|111116_112700_-|ATP-binding-protein
MAINKERDEPFSYLWQILLFLTDLPLQKRTSLAQRCRMTVMIDMGKDPKGQVVPMDLEELLATRLLVQGNSGSGKSHLLRRMLEKSARFVQQIVIDPEGDFVTLAERFPHVAVEAAAYNESEIRVLAQRIREHRVSVVLNLEGLDVDNQMKCAAWFLATLFDAPRDHWYPAIVVVDEAQIFAPAQAGEVSDEARRLSLAAMTNLMCRGRKRGLAGVIATQRLAKLAKNVAAEASNFLMGRTFLDIDMARAADLLGMDRRQAESIRDLERGHFLALGPALCRRPIAVKIGEVETKSRTGGFKLMPLPDSKNSNPEDLLFSEPEEPALPLASPEPPPPPSSSQLMELLQKEKEEEAKIAEAEAAENPVDNSQKEALIDALLSSIVEEEENAYRQANLLYPEFTIGCRMHGLSTPPLDLTAFTKRLTIAKAGLSNDDLQDELWQPALKAASILEDDIQAVFLFLAKTAKENAPCPDDEMIARIYGTRSAGRARRLIGYMENQGIIAIRTDFGGRRSITLPALGWTTSTAA
>NZ_CP023677.1|WP_011240090.1|110562_110850_+|hypothetical-protein
MAAEIMDHMNYMVDDPDQLSVKPANALEHIFLYEDSGAVIAEIPVVFKGESGRVLYDISHNRLVHSDIKHDQLKEMVSSKMPDFKEELLEYFREN
>NZ_CP023677.1|WP_011240089.1|108978_110328_+|replication-associated-recombination-protein-A
MDDLFNSVEPLVFTENEKQPLPENRPLADILRPKHLSDVIGQAHVTGENGIIGRMVAAGRLSSLILWGPPGTGKTSIAQLLAESVGMRFEMVSAIFSGVADLKKIFLKAEHHRQQGRQTLLFIDEIHRFNKGQQDSFLPYIENGTFVLVGATTENPSFALNAALLSRAQVVTLNRLDEEALGLLLERAETVSGQLLPVDENARKALIASADGDGRFLLNQAEILLAMNLTKSLSVPELAQILQKRMAIYDKDRDGHYNLISALHKSVRGSDPQAALYYLSRMLVAGEDPLYLLRRLTRMANEEVGLADPRAMEQCIAAKETYQLLGSPEGELAIAQACVYVATAPKSNAIYKAYNQAMDLARESGSVLPPPNILNAPTEMMKQQGYGEGYHYDHDMPDAFSGDNYWPENLPPVTLYQPNIRGYEKHITERLAFWEHLRQERKKGKPSGK
>NZ_CP023677.1|WP_011240088.1|107643_108711_+|dihydroorotate-oxidase
MKTEIPYYNPELSYEDNYKEGPFGYFADIVEKPDPSFAVSVKKPVSFLGCSVDLPFGIPAGPLLNSRYIKAAFHAGFDLCVYKTVRTQEHKSHPLPNVLAIHPEGVLSADCEAVLADTRYNQPLSITNSFGVPSFNPDIWQPDMAEAVKAASDHQVMIGSFQGTRGKGKIEEDYALAARMVAETGAPVLEANLSCPNEGVNSLLCFDAPLVQKIVEAIKAAVPDRPLLIKTAYFKDNAKLADLVSRVGHLVSGFSTINTLSARPLDEKGQAALSPSRPEGGVCGDAIRWAGLEMVQRLAAFREEKSLDYAIVGVGGVNKPEHYKAYIEAGANAVMTATGSMWNPHLAEETKKFLA
>NZ_CP023677.1|WP_011240087.1|106316_107483_+|Na+/H+-antiporter-NhaA
MRFSIRRFFSAASGGAIILLLSALLGLLLSNSFLSESYFKVLHLKMPFSALDDAPNLAEFISIAPMSLFFFVVIAEIKEEIISGHLASFRRVILPLISALGGMMIPACLYGLITSGHLEVSRGWAIPIATDAAFTLPIILALGRHVSEGARVWLMALAIFDDLLGIVVIALFYASHLNGYALFAAGLITAVMIGLNKKSVQNLWVYASAGVVLWWALLVSGLHPTIAGVITGLALPSVADQPEKASPLERGKQIIAPWVTWLILPLFGFVSMGMSLSAMSFHVLLAPVPLGVALGLFLGKPIGVFGATIMATRLKIATLPKGTSLRMLFGLSLLCGIGFTISLFIAELAFSGSDFLVPAKYGILMGSLLSALAGWLWLRFLKFPAKGV
>NZ_CP023677.1|WP_011240086.1|104520_106158_+|hydroxylamine-reductase
MLCFQCEQTHSGTGCVIRGVCTKTPEVAAIQDLMIFASAGLSYVAKKLPDSCEAERKEAASLVIQALFSTVTNVNFDADVLTKALYHLVDFRDALKAKLPEDVELPLAATLDFSRDRETLVKQGESYGIASRQKTLGIDVTGLQELLTYGMKGMAAYAHHAAVLDYRDPDVDNFLLEGMAALTDHSLDIQALLAVVMRCGEASYKTLALLDKANTSSFGHPVPTNVKMGPSKGKAILVSGHDLLDMKELLEQTKDTGIKVYTHGEMLPAHGYPELNKYPHLAGHYGGAWMLQRQEFINFPGPIVMTTNCLMEPRKEYAGRVFTRDLVGWPGLTHLPDRDFSKVIEAALESEGFTEDQESRSHIAGFGHHTVLDSADAVVSAIKKGDIKHFMLVGGCDGIKSGRHYFTDIAEKAPKDWVILTLGCGKFRVTDLDLGKIGDLPRLLDMGQCNDSYSAIRVALALAEAFDTDVNSLPLSLVLSWYEQKAVCVLLALLHLGVKGIRLGPTLPAFITPNMLKILVDNFDIKPIGNSAEEDLQEILAAKAA
>NZ_CP023677.1|WP_011240085.1|104016_104454_+|Rrf2-family-transcriptional-regulator
MLSISQSTGYAVLALSAIHAESEKLTMARDIAEKANIPRPYLTKILGRLQEAGLITAKRGQNGGLRLNRPPETISLLEIVKAIDGKDWGCGCFLGLPGCSNEHPCPMHSFWLKTRPVIVKQLENMTLDKAKHFTEAGWKFRSEEG
>NZ_CP023677.1|WP_011240084.1|102980_103817_+|aminotransferase
MPIWLNGVLANNAVAEFNLNDKGLLLGYGVFDTALVIADKVAYREAHLEKLTKSCAALSLPVASSFLSEMMEKAAKDLPLGVIRITVTGGVGPRGMAFSPEAKPNVIVSASPIAATIFCPEIRLVLTPLRRNESSFTARIKTLNYLDAIMAVTEARQKSFDDALFLNTAGHVACSSTANLFMIRDGCLITPPVSDGILAGIMRANILRFAKSRDIPVEERSIGYEELLEADDIFLTNSLRLISQVTHLGEVALPRRSAALMALLESMVFDEINYSRSQ
>NZ_CP023677.1|WP_011240083.1|102403_103015_+|aminodeoxychorismate/anthranilate-synthase-component-II
MLLMIDNYDSFVVNLARYCERLGRKVSLFRHDKITLEEIEVMSPKAIILSPGPCSPEEAGISLDVLRQFSGKIPILGVCLGHQAIGVAFGGVIARASYPLHGRAVEISHVGKRLFKDIPNPFKAARYNSLIIQKTEEMEQHLTVDALSPEGEIMALSHKSHPTYGIQFHPESVLTEYGDALLSRFFDLEEAFYADMAERCISQ
>NZ_CP023677.1|WP_011240093.1|114592_115552_-|S1/P1-Nuclease
MTDNRVSKLFKKRLTKLAIVAAMLTLPQPLYAWGMEGHEAIAALAWKYMTPTTRKKVNAILAMDHDRLTEPDFMSRATWADKWRSAGHGETEPWHFVDIEIDNPNLVTACAAASNRSNPMKNGGAQPCVVSQLDRFERELSSKQTSDQDRVLALKYVLHFVGDLHQPLHAADHDDRGGNCVKVSINNARSLNLHSYWDTYVVKEIDPDPQHLADSLKKEISPEDKKSWVLGDSKQWAMESFQLGKRYAYSFNPPAGCDATRPPIPLSAGYDSAARKVAASQLKKAGVRLAYILNHRLRSIPLSYFLQAQKQDAAANNNG
>NZ_CP023677.1|WP_011240094.1|115569_118062_-|TonB-dependent-receptor
MKNLLSAKTKSFLSFKQSRLNWVILYSSLWVSGAMAQNTVPPQPATDDTSSQQHAVTDNSANHPAKNDGAIVVTGRSYADGVTRRAFGGGLMIKEDSPKSKSTLTRDYIEKQTPGLNPMQLIALLPGVNSSDSDPMGLTGGHTSVRGMNESSMGYILEGFPLNDVGSHAVYPQEIVDSENLSTIQVAQGSADLDSPTVSAAGGVVNMHMIDPAKKMGGRANFTYGSYNTFRGFARFDTGEIGNSGTRAYFSFSDTHEDLWRGPGTEKKLHGEMKVVKEWGKDNKASLLVIGNNLDNINMPSVNMASWQKYGKGIMGGPVSGIANTVYSSVYTGNTKANTTYYKLHPNPFTNIYVSAPVHLNLGHKMTLTETPYFLYSNGNGGGAYWQDMNKMSYGSQTMSGTVDGQNYGQTLLYEPSITKTYRSGSTTKWTWTSGINRLMIGYWFEYSSQRQTAPYSLLNDDGSPRDKWGGGSNVILANGEKAEYRDNLTRTFIHTPFIGDTISLLNDKLTIDGGVKISIINRQGRNYLPDTSTGKNINQTYREVLPSGSIRYKINDEHQVFFSVATNYRIPMNTSLFDSGSYVAGTGYSNQAVKDLKPETSISEEFGWRYHGKLINTSLTYFHYDFHNRLFSQTVIDPNNPTSYYSRSINGGNQTTNGVDFEIGTRAIYNIRPYVSAEYIDARNRSNLAASAAGVSAILPTKGKFAPQTPRYQVGFGLDYDNGHIFGNFSLKYVGSQYSTFMNDEQVPSYVRMNIGGGYRFKSWGGLKSPTIRFNLSNITNKHYLNYASGLQTNAQYAKALDGQMVKGSAPTYSIASPFSAMFSISSGF
>NZ_CP023677.1|WP_011240095.1|118384_119179_-|phosphatase-PAP2-family-protein
MIKVPRFICMIALTSGILASGLSQSVSAHTEKSEPSSTYHFHSDPLLYLAPPPTSGSPLQAHDDQTFNSTRQLKGSTRWALATQDADLHLASVLKDYACAAGMNLDIAQLPHLANLIKRALRTEYDDIGRAKNNWNRKRPFVDTDQPICTEKDREGLGKQGSYPSGHTTIGWSVALILAELIPDHAANILQRGQIFGTSRIVCGAHWFSDVQAGYIMASGEIAALHGDADFRRDMELARKELEKARTSAHTPDDLLCKIEQSAR
>NZ_CP023677.1|WP_011240096.1|119336_120281_-|metallophosphoesterase
MISFNRRRFLSLSAGATFAAATAPRLYAGVPNRPPLRSHQSFTFVFITDTHLQPELNGAEGCHEAFLKARQFPADFAIHGGDHVFDALGVNANRATMLADLYKRTADDLRLPVYNTMGNHDCFGIYKESGAQPTDPFYGKKYFQDNFGQTYYSFDHKGVHFVILDSIGITEDRSYEGRVDAEQFNWLSRDLAAQPVGTPIIVSTHIPIMNAIDYASVPLNKMKHHSLSVINAADILELFDHYNVIGVFQGHTHVVERVEWHGVPYITGGSVCGNWWHGTRYGTPEGFMVVKVEKGKVIPHYESYGFHTIDPRNT
>NZ_CP023677.1|WP_017466460.1|120788_121607_+|sel1-repeat-family-protein
MKKILLLWVVVFSFVASRTQMQIRKELESFQSKYAALIKKPVQEKSSGRRLVVEKDSIPPDPPLRYQILLHPQEAAKKGDAEAQMFLGKAYLTGRSDVPKNSKQAVFWFQKSANQGYAEGEVALADAYHNGTGVGRDEAKAAFWYQKAAAQNNIEAEARLGFIYHQGRGLPKDEKMSFFWFDKAAHQGSLLAQTMVGVAYYYGSGVPQDKGRAFMWYQKAAHQGDVMAQYLLGMAYLKGEGVARSKRDGVFWLQRAAAQGDYNAFKILQRLQ
>NZ_CP023677.1|WP_017466461.1|121837_122560_+|sel1-repeat-family-protein
MKRILVLTAALLPVFAQPAFARIGVGRVVKMTRDGLKSPLQKAAERGDAKAQYALGNAYSKGQDVSKSDEQAVSWYQKSASQGYAPAQAALGYAYSSGLGVTHDDQQAVSFFQKAANQGNASAQYNLGMAYSNGQGVPHSDEEAASWYQRAAHQGYAPAEFNLGAAYYHGEGVVQDYGQAVFWYQKAAEQGDAKAQTALGVAYITGRGVTKSRDNALIWIQKAADQGDVTAQKILPALKK
>NZ_CP023677.1|WP_160327976.1|122579_122729_+|hypothetical-protein
MRKGWGGLLWGCPAFIDIGDWGQASFPNDLFYHGWLSGGALSVVVIPFE
>NZ_CP023677.1|WP_014500662.1|122738_124106_+|sel1-repeat-family-protein
MKKILLLSVLLSSSVTPSMAAPEKPHVVESDQIPLKQAAEAGDIAAQSNLGLAYYVGAAVPKDAAMAAFWFEKAASKGFSAAQYNLAGLYATGEGVAQSDKQAAFWYEKAAEQGIDEAEYNLALAYEQGKGVEQNYERALFWLKKAADQNFFKAETHLGLAYQAGIMLPRDDKKAVALFMKADRQVYYAEAQMALGNAYRRGAGVKQDDQKAVSYYQKAADQGDGEALTALGVFYMTGRGVPQNYERGLDCFRKAADKDVSAAEDNLGNAYRHGYGVPKDDEKAVYWYQKAADKGDAEAEYNLGLAYRKGEGISQDDAKAAFWYKKAADQGHVKAQLNMGFAYYQARGVAQDYARGIFLYRKAAEQGDSKAEYNLAIAYYNGVGEPKDLAQSIYWFQRAASHGEMSAQYNLGAFYMRGEGVPKDRNEAIFWLEKAAAQGDVEAQSTLHNLDHYPL
>NZ_CP023677.1|WP_017466287.1|124243_125068_+|sel1-repeat-family-protein
MRKFLFFTAVFLPFVANPVQAQTAKSTKVVAGKTALSLEQKARAGNPKAQTDLGTAYYNGQGMAQDYKQAISWYQKAANQGYPLAQYYLGNACLQGIGLTQSDEQAVSWYQKAANQGLAEAQYSLAIAYYTGRGVTQNYEQASFWFQRSANQGFVPAQFYLGVMYRNGAGIPEDDDRALFWFHKAADKGYADAQYNLGLIYHEGKVVKKDEKQATFWYQQAANQGLVEAEFNLGIAYLKGQGVQKDKDKATFWLEKAADKGDSHAQDVLEMMNK
>NZ_CP023677.1|WP_011240099.1|125250_125751_+|sel1-repeat-family-protein
MKKRIILLGLLLSIGGQIVYSQVRKTPSIFSQKKLHELKLAADQGDAEAEAALGEAFDFGKITPQDYQKAFFWYQKAADQSVAEAQYNLGGLYYKGAGRPKDGEKAVYWYRKAADQGYIDAQRNLALLYAKGELVPQSDEQAVYWYQKAADQGDAEAQKLLAMLAR

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Crispr_ID: NZ_CP023677_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023677_2

1245355-1245866

Orphan

I-F

Consensus_repeat	Method
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	PILER-CR
GTTCACTGCCGCACAGGCAGCTTAGAAA	CRISPRCasFinder
GTTCACTGCCGCACAGGCAGCTTAGAAA	CRT

8 spacers

The CRISPR arrays of NZ_CP023677_2

>merge|NZ_CP023677|2|1245355-1245866|PILER-CR,CRISPRCasFinder,CRT
GTTCACTGCCGCACAGGCAGCTTAGAAATAGCAGTGCCAGTGCTATCAAGAAAGAAATCCGTTCACTGCCGCACAGGCAGCTTAGAAAAGATGGAACAAATGTGTGGTGGGAAAATACTTTGTTCACTGCCGCACAGGCAGCTTAGAAACCGTGCGTCATAGACACCGGAAGGTGCGCCGTGTTCACTGCCGCACAGGCAGCTTAGAAATTCTCAAAAAGGAAAAGAAATTGGAACAGATTGTTCACTGCCGCACAGGCAGCTTAGAAAGTCGAATAATTTTAAGCGTGAACCCGTATCAGGTTCACTGCCGCACAGGCAGCTTAGAAAATCGAACTGCGTGCCTGATAGCCGATACGCTGAGTTCACTGCCGCACAGGCAGCTTAGAAAGATCGCGGGCAACGGTTTATTCAGCTATCCGCGCGTTCACTGCCGCACAGGCAGCTTAGAAAATTTCGTCAGTGTCCGGAGAAACGCCCGTCAGGTTCACTGCCGCGCAGGCAGTTGCTTAG

>NZ_CP023677|2|2|1245355-1245806|PILER-CR
GTTCACTGCCGCACAGGCAGCTTAGAAA	TAGCAGTGCCAGTGCTATCAAGAAAGAAATCC
GTTCACTGCCGCACAGGCAGCTTAGAAA	AGATGGAACAAATGTGTGGTGGGAAAATACTTT
GTTCACTGCCGCACAGGCAGCTTAGAAA	CCGTGCGTCATAGACACCGGAAGGTGCGCCGT
GTTCACTGCCGCACAGGCAGCTTAGAAA	TTCTCAAAAAGGAAAAGAAATTGGAACAGATT
GTTCACTGCCGCACAGGCAGCTTAGAAA	GTCGAATAATTTTAAGCGTGAACCCGTATCAG
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATCGAACTGCGTGCCTGATAGCCGATACGCTGA
GTTCACTGCCGCACAGGCAGCTTAGAAA	GATCGCGGGCAACGGTTTATTCAGCTATCCGCGC
GTTCACTGCCGCACAGGCAGCTTAGAAA

>NZ_CP023677|2|1|1245355-1245866|CRISPRCasFinder
GTTCACTGCCGCACAGGCAGCTTAGAAA	TAGCAGTGCCAGTGCTATCAAGAAAGAAATCC
GTTCACTGCCGCACAGGCAGCTTAGAAA	AGATGGAACAAATGTGTGGTGGGAAAATACTTT
GTTCACTGCCGCACAGGCAGCTTAGAAA	CCGTGCGTCATAGACACCGGAAGGTGCGCCGT
GTTCACTGCCGCACAGGCAGCTTAGAAA	TTCTCAAAAAGGAAAAGAAATTGGAACAGATT
GTTCACTGCCGCACAGGCAGCTTAGAAA	GTCGAATAATTTTAAGCGTGAACCCGTATCAG
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATCGAACTGCGTGCCTGATAGCCGATACGCTGA
GTTCACTGCCGCACAGGCAGCTTAGAAA	GATCGCGGGCAACGGTTTATTCAGCTATCCGCGC
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATTTCGTCAGTGTCCGGAGAAACGCCCGTCAG
GTTCACTGCCGCGCAGGCAGTTGCTTAG

>NZ_CP023677|2|2|1245355-1245866|CRT
GTTCACTGCCGCACAGGCAGCTTAGAAA	TAGCAGTGCCAGTGCTATCAAGAAAGAAATCC
GTTCACTGCCGCACAGGCAGCTTAGAAA	AGATGGAACAAATGTGTGGTGGGAAAATACTTT
GTTCACTGCCGCACAGGCAGCTTAGAAA	CCGTGCGTCATAGACACCGGAAGGTGCGCCGT
GTTCACTGCCGCACAGGCAGCTTAGAAA	TTCTCAAAAAGGAAAAGAAATTGGAACAGATT
GTTCACTGCCGCACAGGCAGCTTAGAAA	GTCGAATAATTTTAAGCGTGAACCCGTATCAG
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATCGAACTGCGTGCCTGATAGCCGATACGCTGA
GTTCACTGCCGCACAGGCAGCTTAGAAA	GATCGCGGGCAACGGTTTATTCAGCTATCCGCGC
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATTTCGTCAGTGTCCGGAGAAACGCCCGTCAG
GTTCACTGCCGCGCAGGCAGTTGCTTAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023677.1\|WP_011241038.1\|1247285_1247549_-\|twin-arginine-translocase-TatA/TatE-family-subunit	unknown	unknown	gnl\|CDD\|234822
NZ_CP023677.1\|WP_011241045.1\|1252121_1253117_-\|dipeptide-epimerase	unknown	unknown	gnl\|CDD\|239435
NZ_CP023677.1\|WP_011241028.1\|1232277_1233267_+\|carbon-nitrogen-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|143588
NZ_CP023677.1\|WP_011241034.1\|1242404_1242617_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|375983
NZ_CP023677.1\|WP_011241035.1\|1242643_1244296_+\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226434
NZ_CP023677.1\|WP_011241043.1\|1251173_1251398_+\|30S-ribosomal-protein-S18	unknown	unknown	gnl\|CDD\|178997
NZ_CP023677.1\|WP_011241036.1\|1245957_1246746_-\|twin-arginine-translocase-subunit-TatC	unknown	unknown	gnl\|CDD\|376413
NZ_CP023677.1\|WP_011241037.1\|1246742_1247201_-\|twin-arginine-translocase-subunit-TatB	unknown	unknown	gnl\|CDD\|130477
NZ_CP023677.1\|WP_011241030.1\|1236622_1237969_-\|glutathione-disulfide-reductase	unknown	unknown	gnl\|CDD\|235701
NZ_CP023677.1\|WP_011241033.1\|1240539_1242060_+\|DEAD/DEAH-box-helicase	unknown	unknown	gnl\|CDD\|223587
NZ_CP023677.1\|WP_011241715.1\|1244663_1244798_+\|entericidin-A/B-family-lipoprotein	unknown	unknown	gnl\|CDD\|227797
NZ_CP023677.1\|WP_011241031.1\|1238131_1239655_-\|glucose-6-phosphate-isomerase	unknown	unknown	gnl\|CDD\|366041
NZ_CP023677.1\|WP_011241044.1\|1251412_1252042_+\|50S-ribosomal-protein-L9	unknown	unknown	gnl\|CDD\|234659
NZ_CP023677.1\|WP_011241029.1\|1234197_1236156_-\|potassium-transporter-Kup	unknown	unknown	gnl\|CDD\|225700
NZ_CP023677.1\|WP_011241039.1\|1247701_1248403_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023677.1\|WP_011241032.1\|1239986_1240412_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|227505
NZ_CP023677.1\|WP_011241041.1\|1249322_1250258_-\|ACP-S-malonyltransferase	unknown	unknown	gnl\|CDD\|223408
NZ_CP023677.1\|WP_011241040.1\|1248515_1249253_-\|3-oxoacyl-ACP-reductase-FabG	unknown	unknown	gnl\|CDD\|187594
NZ_CP023677.1\|WP_011241042.1\|1250778_1251153_+\|30S-ribosomal-protein-S6	unknown	unknown	gnl\|CDD\|179034
NZ_CP023677.1\|WP_011241027.1\|1231257_1232208_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176153

Protein	Function_ID	Function_description	E-value
NZ_CP023677.1\|WP_011241038.1\|1247285_1247549_-\|twin-arginine-translocase-TatA/TatE-family-subunit	gnl\|CDD\|234822	PRK00720, tatA, twin-arginine translocase TatA/TatE family subunit.	9.82533e-37
NZ_CP023677.1\|WP_011241045.1\|1252121_1253117_-\|dipeptide-epimerase	gnl\|CDD\|239435	cd03319, L-Ala-DL-Glu_epimerase, L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.	1.39911e-117
NZ_CP023677.1\|WP_011241028.1\|1232277_1233267_+\|carbon-nitrogen-hydrolase-family-protein	gnl\|CDD\|143588	cd07564, nitrilases_CHs, Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases). Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 1.	7.76992e-153
NZ_CP023677.1\|WP_011241034.1\|1242404_1242617_+\|hypothetical-protein	gnl\|CDD\|375983	pfam18557, NepR, Anti-sigma factor NepR. The general stress response sigma factor in alphaproteobacteria, sigma EcfG is inactivated by the anti-sigma factor NepR, which is itself regulated by the response regulator PhyR. NepR forms two helices that extend over the surface of the PhyR subdomains. Homology modeling and comparative analysis of NepR, PhyR and sigmaEcfG mutants indicate that NepR contacts both proteins with the same determinants, showing sigma factor mimicry at the atomic level. This entry represents NepR domains found in alphaproteobacteria.	1.35026e-06
NZ_CP023677.1\|WP_011241035.1\|1242643_1244296_+\|sensor-histidine-kinase	gnl\|CDD\|226434	COG3920, COG3920, Signal transduction histidine kinase [Signal transduction mechanisms].	3.23978e-20
NZ_CP023677.1\|WP_011241043.1\|1251173_1251398_+\|30S-ribosomal-protein-S18	gnl\|CDD\|178997	PRK00391, rpsR, 30S ribosomal protein S18; Reviewed.	2.27745e-35
NZ_CP023677.1\|WP_011241036.1\|1245957_1246746_-\|twin-arginine-translocase-subunit-TatC	gnl\|CDD\|376413	pfam00902, TatC, Sec-independent protein translocase protein (TatC). The bacterial Tat system has a remarkable ability to transport folded proteins even enzyme complexes across the cytoplasmic membrane. It is structurally and mechanistically similar to the Delta pH-driven thylakoidal protein import pathway. A functional Tat system or Delta pH-dependent pathway requires three integral membrane proteins: TatA/Tha4, TatB/Hcf106 and TatC/cpTatC. The TatC protein is essential for the function of both pathways. It might be involved in twin-arginine signal peptide recognition, protein translocation and proton translocation. Sequence analysis predicts that TatC contains six transmembrane helices (TMHs), and experimental data confirmed that N- and C-termini of TatC or cpTatC are exposed to the cytoplasmic or stromal face of the membrane. The cytoplasmic N-terminus and the first cytoplasmic loop region of the Escherichia coli TatC protein are essential for protein export. At least two TatC molecules co-exist within each Tat translocon.	3.94496e-76
NZ_CP023677.1\|WP_011241037.1\|1246742_1247201_-\|twin-arginine-translocase-subunit-TatB	gnl\|CDD\|130477	TIGR01410, Sec-independent_protein_translocase_protein_tatB., twin arginine-targeting protein translocase TatB. This model represents the TatB protein of a Sec-independent system for transporting folded proteins, often with a bound redox cofactor, across the bacterial inner membrane. TatC is the multiple membrane spanning component. TatB, like the related TatA/E proteins, appears to span the membrane one time. The tat system recognizes proteins with an elongated signal sequence containing a conserved R-R in a motif approximated by RRxFLK N-terminal to the transmembrane helix. TIGRFAMs model TIGR01409 describes this twin-Arg signal sequence. A similar system, termed Delta-pH-dependent transport, operates on chloroplast-encoded proteins. [Protein fate, Protein and peptide secretion and trafficking].	3.41204e-18
NZ_CP023677.1\|WP_011241030.1\|1236622_1237969_-\|glutathione-disulfide-reductase	gnl\|CDD\|235701	PRK06116, PRK06116, glutathione reductase; Validated.	0
NZ_CP023677.1\|WP_011241033.1\|1240539_1242060_+\|DEAD/DEAH-box-helicase	gnl\|CDD\|223587	COG0513, SrmB, Superfamily II DNA and RNA helicases [DNA replication, recombination, and repair / Transcription / Translation, ribosomal structure and biogenesis].	2.0881e-158
NZ_CP023677.1\|WP_011241715.1\|1244663_1244798_+\|entericidin-A/B-family-lipoprotein	gnl\|CDD\|227797	COG5510, COG5510, Predicted small secreted protein [Function unknown].	5.12008e-07
NZ_CP023677.1\|WP_011241031.1\|1238131_1239655_-\|glucose-6-phosphate-isomerase	gnl\|CDD\|366041	pfam00342, PGI, Phosphoglucose isomerase. Phosphoglucose isomerase catalyzes the interconversion of glucose-6-phosphate and fructose-6-phosphate.	0
NZ_CP023677.1\|WP_011241044.1\|1251412_1252042_+\|50S-ribosomal-protein-L9	gnl\|CDD\|234659	PRK00137, rplI, 50S ribosomal protein L9; Reviewed.	4.06061e-62
NZ_CP023677.1\|WP_011241029.1\|1234197_1236156_-\|potassium-transporter-Kup	gnl\|CDD\|225700	COG3158, Kup, K+ transporter [Inorganic ion transport and metabolism].	0
NZ_CP023677.1\|WP_011241041.1\|1249322_1250258_-\|ACP-S-malonyltransferase	gnl\|CDD\|223408	COG0331, FabD, (acyl-carrier-protein) S-malonyltransferase [Lipid metabolism].	1.07943e-120
NZ_CP023677.1\|WP_011241032.1\|1239986_1240412_+\|hypothetical-protein	gnl\|CDD\|227505	COG5178, PRP8, U5 snRNP spliceosome subunit [RNA processing and modification].	0.000693568
NZ_CP023677.1\|WP_011241040.1\|1248515_1249253_-\|3-oxoacyl-ACP-reductase-FabG	gnl\|CDD\|187594	cd05333, BKR_SDR_c, beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs. This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) 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 have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. 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 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. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. 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) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	4.93138e-124
NZ_CP023677.1\|WP_011241042.1\|1250778_1251153_+\|30S-ribosomal-protein-S6	gnl\|CDD\|179034	PRK00453, rpsF, 30S ribosomal protein S6; Reviewed.	6.50436e-48
NZ_CP023677.1\|WP_011241027.1\|1231257_1232208_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176153	cd08464, PBP2_DntR_like_2, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold. This CD includes an uncharacterized LysR-type transcriptional regulator similar to DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	3.05942e-78

>NZ_CP023677.1|WP_011241715.1|1244663_1244798_+|entericidin-A/B-family-lipoprotein
MRILIHFLMASAVLALAACNTVQGFGQDLSSAGQSMSNSAERNK
>NZ_CP023677.1|WP_011241035.1|1242643_1244296_+|sensor-histidine-kinase
MKAFFKNSPSKTFHKKQLLTRRLFLLFVSMPTWFRMLVVLSLAQLPPSFVALGAFIASSHQYRLNHQKEAQLIATESARTIDDSVDILAYDVRNIFDEEGSYDFADMGECSLLIQHMQSLGFVPVDYALMDTSGRLLCKSDNFKVNTAVLLPFKPLGANNFYNVDILENEGQLQFSFLGGHYPLSKYLVVGQIGRDSLLKIIERKVVPDGSALFLAQKSHLLPLISPKKPLLKQSHPVVIPTFDNSINLIYDNNLPPFRKVDLLFVLLPVLIWFMTASIGWVVVHYMLLRPLRRTQRAIVDYGKTGEIQKIKPASIGAAREIRQVSKAFYHVAVRLAAHERALRNALQHQKMLTREVHHRVKNNLQVVSSLLSIHSRRAETAKEKSAYATIQRRVNALAIVQRQYYNELDKGQGLDLSLLIKELVNGLQTSLQTFEKNFQIETEIDQVFVPLEKAMPIAFILVEIVDFSLAVDPLLPITIILHRHSAEFENTPDHAGLEIRAEALKQLSSRKGNEVIRRIISAFGRQLGGKSAEKEEDGYYYYDIDILPD
>NZ_CP023677.1|WP_011241034.1|1242404_1242617_+|hypothetical-protein
MNGSMTAHNHKRPVSQELPASSGNAAHADESAKQAEDRKNAIGFALRNVYQQTVEEAVPDDLLALLAKLN
>NZ_CP023677.1|WP_011241033.1|1240539_1242060_+|DEAD/DEAH-box-helicase
MSDKDYRLFLVRYFMSFADLGLSKELLQAVAELGYEEPTPVQAAAIPSVLMMRDLIAVAQTGTGKTASFVLPMIDILAHGRCRARMPRSLILEPTRELAAQVAENFEKYGKYHKLSMSLLIGGVPMAEQQAALEKGVDVLIATPGRLLDLFERGKILLSSCEMLVIDEADRMLDMGFIPDIETICTKLPTSRQTLLFSATMPPAIKKLADRFLSNPKQIEISRPATANTLIDQRLIEVSPRSKKKKLCDMLRAEKDHTAIIFCNRKTTVRQLATTLEQQGFSVGQIHGDMSQPERGSELERFKNGQISVLVASDIAARGLDVKGISHVFNFDVPTHPDDYIHRIGRTGRGGASGEALTFVTPADEEAITAIEKLMGVEIPRLGNRKKNTYPSKSEETVSPKQAKPAQEKSATPSPRKAPRKTETPKKLPEDRLDSVESDFPKNQAPRNTASRPVSKARTQERALRPENLRRVKPVALETAIDWNGPIPPFLNYSVPKTTARNVKKD
>NZ_CP023677.1|WP_011241032.1|1239986_1240412_+|hypothetical-protein
MPPRHFPHSGVMEIHLNVRNANGRNQRPLPPPPPPPDSPYNAPPPPPEAVWHEKKGPKCVSPEDIGAAAVSEKDSVDLMLKGGSRIRAHLEHCPALDFYSGFYVHAGRDGQICAKRDPVYARWGGECLINRFRVVEGVFKH
>NZ_CP023677.1|WP_011241031.1|1238131_1239655_-|glucose-6-phosphate-isomerase
MARIANKAAIDAAWKQVSACSEKTLKQLFEEDSNRLSGLVVETAKLRFDFSKNHLDSQKLTAFKKLLEACDFDARRKALFAGEKINITEDRAVEHMAERGQGAPASVARAKEYHARMRTLIEAIDAGAFGEVKHLLHIGIGGSALGPKLLIDALTRESGRYDVAVVSNVDGQALEEVFKKFNPHKTLIAVASKTFTTAETMLNAESAMEWMKKHGVEDPQGRMIALTANPAKASEMGIDDTRILPFAESIGGRYSLWSSIGFPAALALGWEGFQQLLEGGAAMDRHFLEAAPEKNAPILAAFADQYYSAVRGAQTHGIFAYDERLQLLPFYLQQLEMESNGKRVDLDGNLIDHPSAFITWGGVGTDAQHAVFQLLHQGTRLVPIEFIAAIKADDTLNPVHHKTLLTNAFAQGAALMSGRDNKDPARSYPGDRPSTTILMEELRPAQLGALIAFYEHRTFTNGVLLGINSFDQFGVELGKEMAHAIADHPENSDFDPSTKALIAAALK
>NZ_CP023677.1|WP_011241030.1|1236622_1237969_-|glutathione-disulfide-reductase
MTDYDFDLFVIGAGSGGVRASRIAASHGASVAIAEEYRIGGTCVIRGCVPKKMLYYAADFAADLKKAQRFGWTLPEKKFDWATLRDVVLSDVTRLEGLYTQTLDNNHITHYKEHAVIDSANQIRLASGKKITARYILVAVGAEPAKLDILGAEYAVTSNEMFLLPSLPKRALVVGGGYIANEFAGILNSFGVETTIATHGDRILRGYDEEIAARLVEIGQGHGIDYRFNADIARIDKDSSGRLTTHFKDGSQIESDLVLFAIGRVAKSRDLGLDKADVKTNDRGAILVDEENRTSCPSIYAVGDVTDRVQLTPVAIREGQAFADRVFGHKAASVDYDTIPTAVFSHPPLASAGLTEEEAKKRYKNIKIYKSNFRPMRNALIDSPDRALYKMVVDGDSDKVLGLHLIGQDSPEIIQLAAVAIKAGLTKQAFNDTVALHPSSAEELVLMR
>NZ_CP023677.1|WP_011241029.1|1234197_1236156_-|potassium-transporter-Kup
MSNDTSPGTSSVDSKSSDPSYGVPGHSHSDKDLLKLSLGAIGIVFGDIGTSPLYALKECFKGHHQLPVDDFHIYGLVSLIFWTMGLVVTVKYVMFIMKADNKGEGGSMSLLSLIIRGANPKLSRWLIVLGVFATALFYGDSMITPAMSVLSAVEGLTVIEPSFDSWVPPVSVVILIGLFCIQARGTESVGRLFGPIMLVYFATLAILGAFNIITRSPAILLALNPYYAIHFFASDPLQGFWALGSVVLSVTGAEALYADMGHFGRQPISLGWYWVVFPALTLNYLGQCALLSADHEAIANPFYFLAPDFLRVPLIILATFAAVIASQAVITGAFSVTQQAIQLGYIPRLRVNHTSASTVGQIYIPSVNWVLMFMVMVLIAMFKNSTNLANAYGIAVTGTMFITSCMMGVLVHRVWHWKAWQSIPLVSFFLLIDGAFFLSNVTKIPEGGWFPLLVGFVVFTMLMTWSRGRHLMAERMRQVAMPIQLFIRSAAASAVRIPGTAIFLTPEDDGVPHALLHNLKHNKILHERVILLTVKIEDVPYVDPHYRASMSSLEDGFYRLIVRYGFMEEPDVPLALNKIEQSGPMLRMDDTSFFISRQTLIPSTHTSMAIWREKLFAWMLRNSESATEFFKLPSNRVVELGSQIELVGSNGK
>NZ_CP023677.1|WP_011241028.1|1232277_1233267_+|carbon-nitrogen-hydrolase-family-protein
MSCHRVAVIQAGTSLFDTEKTLDRMEALCRQAAEQNVELAVFPEAYIGGYPKGLDFGARMGTRTEAGREDFLRYWKAAIDVPGKETARIGSFAAKMKAYLVVGVIERSEATLYCTALFFAPDGTLIGKHRKLMPTATERLVWGQGDGSTIEILDTAVGKLGAAICWENYMPVLRQVMYAGGVNIWCAPTVDQREIWQVSMRHIAYEGRLFVLSACQYMTRADAPADYDCIQGNDPETELIAGGSVIIDPMGNILAGPLYGQEGVLVADIDLSDTIKARYDLDVSGHYGRPDIFEIKVDRQSHQVITDQFSRDQATEKKPVSDSEISQLD
>NZ_CP023677.1|WP_011241027.1|1231257_1232208_-|LysR-family-transcriptional-regulator
MIRKINISDITRFDFNLVITFLALWHERSVTKAAARLSLSQSAVSASLSRLRQAAGDLLFIRTRQGMEPTQRAIDMVKSLSEGATLIYNAFISENEFDPARCNRHFSIGMSDDFQLALGSEISKQIQAIAPDASVVYRQTNRYTAQQMLENNDIDLAIVTTSLPRRGLWQQVIGEGGYACLCDAQSCGFSENPTLEAYLSLPHILVSYSGREGLVDEILSIMGRSRKIQTALTHFAALPPFLLGSKSIATIPSHAAISLAGYTGLTIFEAPLELTAYPIIATMRLSSQKDTALLWLFQIIKQAIRVQQNILPPPQS
>NZ_CP023677.1|WP_011241036.1|1245957_1246746_-|twin-arginine-translocase-subunit-TatC
MSETDDIHDEVDESAAPLLDHLLELRKRLLISLVALGIAFLLCLHFSRSIFAFLVQPLLRAGQGRLIYTDIFEAFFVDIKVAFFAAIMLAFPIVAMQIWRFIAPGLYSNEKRAFLPFLVMTPLLFLVGASMAYYVAMPIALHFLLGYQGNIGGVQQTALPAVGNYLNFVTKFIFGFGVAFLLPLVLLLLERAGFVTRQQLVAGRRYAIVASVAIAAVLTPPDIVSQLLLGVPLILLYEMALLAMLFGEKRRKKETDLVVAED
>NZ_CP023677.1|WP_011241037.1|1246742_1247201_-|twin-arginine-translocase-subunit-TatB
MFDVAPSELLLVAVVALVVIGPKDLPRAMRVVGRWLGKARKLSRHFRSGIDEMIRQSEMEDMEKRWAEENAKLLAENQGQGNQTASTSSPATPSPVSDDPAEQNIVFTSPADLEVNTADTSHLAANHTETTATTAASTPAKPKEADQQEKQS
>NZ_CP023677.1|WP_011241038.1|1247285_1247549_-|twin-arginine-translocase-TatA/TatE-family-subunit
MGGMSITHWIVVAVVVMIFFGKGRFSDMMGDVAKGIKSFKKGMSEDDTTPPAAPPAPAPRLENQPLPPENTTQNVAQNVPNDIKNNQ
>NZ_CP023677.1|WP_011241039.1|1247701_1248403_-|hypothetical-protein
MAFFFIPLFSGGHLSIFKSGFAPVITLSLASLLLGGCVVHHGQFDEMGSMTVRRSSCPAVAVPDYTGDVTLFNPSDQRTASAIDIEAVITKLRPKCDDTASGPVVTHLTFTVQARRRHVGGARDITLPYFVAVMRAGTRLLSKEMGTVRIHFEPGQMATDTEVTTSSAIDHDSATLPRDIIRQLNKVRQVTDVDASVDPTNDPKVRAAMKEASFEMLVGFQLTEPQLAYNATR
>NZ_CP023677.1|WP_011241040.1|1248515_1249253_-|3-oxoacyl-ACP-reductase-FabG
MFDLNGLTAVVTGASGGIGSAIAKALADQGAQVALSGTRESALKEVAAILPNDPIILPANLGQKEDVEQLVPRALEKLGKIDILVNNAGITRDGLMMRMKDEDWADVIALNLESVFRLSRAVIRPMMKTRFGRIINISSVVGQTGNAGQANYAAAKAGMIGMSKSLAREVASRGITVNCIAPGFIETKMTEILSEQQKEAAKSQIPAGRFGDIQDIAAAAVYLASKEAGYMTGQTLSVNGGMSML
>NZ_CP023677.1|WP_011241041.1|1249322_1250258_-|ACP-S-malonyltransferase
MRAFIFPGQGSQSVGMGQALADASLAARHVFEEVDEALKQNLFRLMSQGPEEELRLTENAQPAIMAHSMAVLAMLEKEGNIRLTDAASFVAGHSLGEYSALAAADAFNLPTTAHLLKKRGQAMQAAVPVGEGGMAAILGLDFETVESIAQEAAENDICQAANDNAPGQVVISGSLAAIERAVALAKGKGARRAVMLDVSAPFHCSLMQPAADVMAKALQENRPRQPIVPVFANVSATAETDPTKIMNLLVEQVTGRVRWRESIAAMAAAGVEEFVEFGGKVLAPMIKRIAPDCKATSLIAPADIENFAASL
>NZ_CP023677.1|WP_011241042.1|1250778_1251153_+|30S-ribosomal-protein-S6
MPLYEHVFLARQDLAQTQVDGLAATATSIIEEKSGKVVKTEIWGLRNLAYRIQKNRKAYYIMLEIDAPADAIQELERQMALNEDVIRYMTVRVDAHEQGPSAMMRRGDRDRSNRSDRRRDRDAA
>NZ_CP023677.1|WP_011241043.1|1251173_1251398_+|30S-ribosomal-protein-S18
MARPFFRRRKSCPFAAKDAPKIDYKDVRLLQGFVSERGKIVPSRITAVSAKKQRELARAIKRARHIGLLPFIVK
>NZ_CP023677.1|WP_011241044.1|1251412_1252042_+|50S-ribosomal-protein-L9
MDVILLERIEKLGHIGDVVAVKNGYARNFLLPRKKALRANEANRKIFEANRAQIEADNAARRTDAEKESEVVNGLTVTLIRQASNTGHLYGSVSARDLADAIVEAKPEAKVAKNQIVLDRPIKSIGISEVRVVLHPEVAVKIKVNVARSPEEAELQAEGVDVMNQMFERDGASFTEDYDPNAEPGLATEAEEAVADADDNAETNSEESL
>NZ_CP023677.1|WP_011241045.1|1252121_1253117_-|dipeptide-epimerase
MTATRSLSIMGESLPLKTPFRISRGVKNTIDTIVANISESGVTGRGEGIPYPRYGQTVESALIEANSVSHKITEHYGREALLTLLPPGPARNALDCALWDIEARISGQSVASMMGIAKLEPLATAVTISLDEPEVMAKAAAKLAYCPVIKVKVDEHNPEDCIKAVRDQAPKARLIVDPNESWSFDLLDKMQNFLADARVALLEQPLAAGADEALKGFSPAVPICADEVFHSADDLDHIADRYQVINIKLDKTGGLTAAIDIMKQARSLNLSIMVGCMVCSSLSLAPAFHLAAQADFVDLDGADWLVHDRNDGMLLDNGILHPPSATFWGGP

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Crispr_ID: NZ_CP023677_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023677_4

1606731-1606819

Orphan

I-F

Consensus_repeat	Method
GTTCACTGCCGCACAGGCAGCTTAGAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023677_4

>merge|NZ_CP023677|4|1606731-1606819|CRISPRCasFinder
GTTCACTGCCGCACAGGCAGCTTAGAAAATCCGCAATTTCTGGAACATGATCTTGCTGACTGTTCACTGCCGCATAGGCAGATTGTACT

>NZ_CP023677|4|3|1606731-1606819|CRISPRCasFinder
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATCCGCAATTTCTGGAACATGATCTTGCTGACT
GTTCACTGCCGCATAGGCAGATTGTACT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023677.1\|WP_011241329.1\|1614743_1615535_-\|pyruvate-formate-lyase-activating-protein	unknown	unknown	gnl\|CDD\|131546
NZ_CP023677.1\|WP_011241318.1\|1600007_1600973_+\|thiamine-phosphate-kinase	unknown	unknown	gnl\|CDD\|273589
NZ_CP023677.1\|WP_011241325.1\|1609610_1610177_-\|nicotinamide-mononucleotide-transporter	unknown	unknown	gnl\|CDD\|377432
NZ_CP023677.1\|WP_011241322.1\|1607139_1607844_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP023677.1\|WP_011241327.1\|1610976_1612149_-\|phosphotransferase	unknown	unknown	gnl\|CDD\|225213
NZ_CP023677.1\|WP_011241317.1\|1599515_1599989_+\|transcription-antitermination-factor-NusB	unknown	unknown	gnl\|CDD\|234686
NZ_CP023677.1\|WP_011241319.1\|1601281_1602052_+\|16S-rRNA-(uracil(1498)-N(3))-methyltransferase	unknown	unknown	gnl\|CDD\|236959
NZ_CP023677.1\|WP_011241324.1\|1608402_1609386_+\|DUF481-domain-containing-protein	unknown	unknown	gnl\|CDD\|377313
NZ_CP023677.1\|WP_011241315.1\|1597565_1598234_+\|ATP-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234971
NZ_CP023677.1\|WP_011241314.1\|1597171_1597477_+\|BolA-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|376601
NZ_CP023677.1\|WP_011241312.1\|1594047_1594614_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380063
NZ_CP023677.1\|WP_011241326.1\|1610646_1610970_+\|YnfA-family-protein	unknown	unknown	gnl\|CDD\|235016
NZ_CP023677.1\|WP_011241323.1\|1607910_1608378_+\|RNA-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|239643
NZ_CP023677.1\|WP_011241330.1\|1615518_1617834_-\|formate-C-acetyltransferase	unknown	unknown	gnl\|CDD\|153087
NZ_CP023677.1\|WP_011241313.1\|1594629_1596807_+\|squalene--hopene-cyclase	unknown	unknown	gnl\|CDD\|239222
NZ_CP023677.1\|WP_017466250.1\|1612161_1614585_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP023677.1\|WP_011241320.1\|1602357_1603746_+\|glutamate--cysteine-ligase	unknown	unknown	gnl\|CDD\|130503
NZ_CP023677.1\|WP_011241316.1\|1598223_1599516_+\|histidinol-dehydrogenase	unknown	unknown	gnl\|CDD\|234853
NZ_CP023677.1\|WP_011241321.1\|1604168_1605695_+\|amidophosphoribosyltransferase	unknown	unknown	gnl\|CDD\|236384
NZ_CP023677.1\|WP_011241331.1\|1618597_1620028_+\|cytochrome-ubiquinol-oxidase-subunit-I	unknown	unknown	gnl\|CDD\|376587

Protein	Function_ID	Function_description	E-value
NZ_CP023677.1\|WP_011241329.1\|1614743_1615535_-\|pyruvate-formate-lyase-activating-protein	gnl\|CDD\|131546	TIGR02493, PFLA, pyruvate formate-lyase 1-activating enzyme. An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair].	4.75927e-144
NZ_CP023677.1\|WP_011241318.1\|1600007_1600973_+\|thiamine-phosphate-kinase	gnl\|CDD\|273589	TIGR01379, Thiamine-monophosphate_kinase, thiamine-phosphate kinase. This model describes thiamine-monophosphate kinase, an enzyme that converts thiamine monophosphate into thiamine pyrophosphate (TPP, coenzyme B1), an enzyme cofactor. Thiamine monophosphate may be derived from de novo synthesis or from unphosphorylated thiamine, known as vitamin B1. Proteins scoring between the trusted and noise cutoff for this model include short forms from the Thermoplasmas (which lack the N-terminal region) and a highly derived form from Campylobacter jejuni. Eukaryotes lack this enzyme, and add pyrophosphate from ATP to unphosphorylated thiamine in a single step. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine].	3.56412e-120
NZ_CP023677.1\|WP_011241325.1\|1609610_1610177_-\|nicotinamide-mononucleotide-transporter	gnl\|CDD\|377432	pfam04973, NMN_transporter, Nicotinamide mononucleotide transporter. Members of this family are integral membrane proteins that are involved in transport of nicotinamide mononucleotide.	7.92226e-43
NZ_CP023677.1\|WP_011241322.1\|1607139_1607844_+\|SDR-family-oxidoreductase	gnl\|CDD\|212491	cd05233, SDR_c, classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	1.51834e-29
NZ_CP023677.1\|WP_011241327.1\|1610976_1612149_-\|phosphotransferase	gnl\|CDD\|225213	COG2334, COG2334, Putative homoserine kinase type II (protein kinase fold) [General function prediction only].	1.02009e-16
NZ_CP023677.1\|WP_011241317.1\|1599515_1599989_+\|transcription-antitermination-factor-NusB	gnl\|CDD\|234686	PRK00202, nusB, transcription antitermination factor NusB.	1.68678e-43
NZ_CP023677.1\|WP_011241319.1\|1601281_1602052_+\|16S-rRNA-(uracil(1498)-N(3))-methyltransferase	gnl\|CDD\|236959	PRK11713, PRK11713, 16S ribosomal RNA methyltransferase RsmE; Provisional.	1.99557e-75
NZ_CP023677.1\|WP_011241324.1\|1608402_1609386_+\|DUF481-domain-containing-protein	gnl\|CDD\|377313	pfam04338, DUF481, Protein of unknown function, DUF481. This family includes several proteins of uncharacterized function.	1.15385e-57
NZ_CP023677.1\|WP_011241315.1\|1597565_1598234_+\|ATP-phosphoribosyltransferase	gnl\|CDD\|234971	PRK01686, hisG, ATP phosphoribosyltransferase catalytic subunit; Reviewed.	1.37428e-112
NZ_CP023677.1\|WP_011241314.1\|1597171_1597477_+\|BolA-family-transcriptional-regulator	gnl\|CDD\|376601	pfam01722, BolA, BolA-like protein. This family consist of the morphoprotein BolA from E. coli and its various homologs. In E. coli over expression of this protein causes round morphology and may be involved in switching the cell between elongation and septation systems during cell division. The expression of BolA is growth rate regulated and is induced during the transition into the the stationary phase. BolA is also induced by stress during early stages of growth and may have a general role in stress response. It has also been suggested that BolA can induce the transcription of penicillin binding proteins 6 and 5.	3.78262e-28
NZ_CP023677.1\|WP_011241312.1\|1594047_1594614_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|380063	pfam17937, TetR_C_28, Tetracyclin repressor-like, C-terminal domain. TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain. This entry represents the C-terminal domain present in CgmR (C. glutamicum multidrug-responsive transcriptional repressor), previously called CGL2612 protein. CgmR (CGL2612) from Corynebacterium glutamicum is a multidrug-resistance-related transcription factor belonging to the TetR family. It regulates expression of the immediately upstream gene cgmA (cgl2611) by binding to the operator cgmO in the cgmA promoter. The cgmA gene encodes a permease belonging to the major facilitator superfamily, a protein family composed of bacterial multidrug exporters, and the pair of CgmR and CgmA confers multidrug resistance on C. glutamicum.	1.92303e-12
NZ_CP023677.1\|WP_011241326.1\|1610646_1610970_+\|YnfA-family-protein	gnl\|CDD\|235016	PRK02237, PRK02237, YnfA family protein.	2.17346e-38
NZ_CP023677.1\|WP_011241323.1\|1607910_1608378_+\|RNA-pyrophosphohydrolase	gnl\|CDD\|239643	cd03671, Ap4A_hydrolase_plant_like, Diadenosine tetraphosphate (Ap4A) hydrolase is a member of the Nudix hydrolase superfamily. Members of this family are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one group (represented by this subfamily) and fungi/animals/archaea enzymes fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for the inhibition of such invasive bacteria. Besides the signature nudix motif (G[X5]E[X7]REUXEEXGU where U is Ile, Leu, or Val), Ap4A hydrolase is structurally similar to the other members of the nudix superfamily with some degree of variations. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies.	7.05806e-74
NZ_CP023677.1\|WP_011241330.1\|1615518_1617834_-\|formate-C-acetyltransferase	gnl\|CDD\|153087	cd01678, PFL1, Pyruvate formate lyase 1. Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate in which two cysteines and one glycine form radicals that are required for catalysis. PFL has a ten-stranded alpha/beta barrel domain that is structurally similar to those of all three ribonucleotide reductase (RNR) classes as well as benzylsuccinate synthase and B12-independent glycerol dehydratase.	0
NZ_CP023677.1\|WP_011241313.1\|1594629_1596807_+\|squalene--hopene-cyclase	gnl\|CDD\|239222	cd02892, SQCY_1, Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. This group contains bacterial SQCY which catalyzes the convertion of squalene to hopene or diplopterol and eukaryotic OSQCY which transforms the 2,3-epoxide of squalene to compounds such as, lanosterol in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain.	0
NZ_CP023677.1\|WP_017466250.1\|1612161_1614585_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.35387e-37
NZ_CP023677.1\|WP_011241320.1\|1602357_1603746_+\|glutamate--cysteine-ligase	gnl\|CDD\|130503	TIGR01436, Glutamate--cysteine_ligase_chloroplastic, glutamate--cysteine ligase, plant type. This model represents one of two highly dissimilar forms of glutamate--cysteine ligase (gamma-glutamylcysteine synthetase), an enzyme of glutathione biosynthesis. The other type is modeled by TIGR01434. This type is found in plants (with a probable transit peptide), root nodule and other bacteria, but not E. coli and closely related species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs].	0
NZ_CP023677.1\|WP_011241316.1\|1598223_1599516_+\|histidinol-dehydrogenase	gnl\|CDD\|234853	PRK00877, hisD, bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed.	0
NZ_CP023677.1\|WP_011241321.1\|1604168_1605695_+\|amidophosphoribosyltransferase	gnl\|CDD\|236384	PRK09123, PRK09123, amidophosphoribosyltransferase; Provisional.	0
NZ_CP023677.1\|WP_011241331.1\|1618597_1620028_+\|cytochrome-ubiquinol-oxidase-subunit-I	gnl\|CDD\|376587	pfam01654, Cyt_bd_oxida_I, Cytochrome bd terminal oxidase subunit I. This family are the alternative oxidases found in many bacteria which oxidize ubiquinol and reduce oxygen as part of the electron transport chain. This family is the subunit I of the oxidase E. coli has two copies of the oxidase, bo and bd', both of which are represented here In some nitrogen fixing bacteria, e.g. Klebsiella pneumoniae this oxidase is responsible for removing oxygen in microaerobic conditions, making the oxidase required for nitrogen fixation. This subunit binds a single b-haem, through ligands at His186 and Met393 (using SW:P11026 numbering). In addition His19 is a ligand for the haem b found in subunit II.	0

>NZ_CP023677.1|WP_011241321.1|1604168_1605695_+|amidophosphoribosyltransferase
MSPSLSSELFSDSISTLTTTTESLDNGASDDTLHEECGVFGIWGADTAAAVVALGLHALQHRGQEAAGITSWDGKNFHSRRAVGHVAGNFDRDDAIRSLPGSCAIGHVRYATTGASTLCNVQPLYAELVSGGFAIAHNGNISNAETLRHQLVRHGSIFQSTSDTETIIHLVATSSYRSLLDRFIDALKQVEGAYSLVCLTPEGMIACRDPLGIRPLVLGKVGETFVVASETVALDIIGGTYIRQVEPGELIIISEKGLQSIHPFKKQKPRPCIFEHVYFSRPDSLIGSTSVYSVRKSIGIELARENPVDADMVIPVPDSGTPAAIGYAQQSSLPFELGIIRSHYVGRTFIQPGDQVRHLGVKLKHNANRALIKGKKLVLVDDSIVRGTTSVKIIRMLRDAGAKEIHLRIASPPTRHSCFYGVDTPERAKLLAAKMTVEQMAEYIGADSLAFISMDGLYRAVGEEARNDAQPQYCDACFTGAYPTPLTDLGELGASEQLVRLSEQVAIA
>NZ_CP023677.1|WP_011241320.1|1602357_1603746_+|glutamate--cysteine-ligase
MSTRQTSSSQNHPIESRDDLLRIFQAGEKPKAQWRVGTEHEKLVYKKQNHQAPSYEEKGGICDLLQGFTRFGWQPIYENDKIIGLSGDDGAISLEPAGQFELSGAPRSTIHESYDEICRHIQQTQEVGDELGLGFLGLGLWPDKKRSDLPLMPKGRYKIMTEYMPKVGKLGLDMMLRTCTIQSNIDYGSEADMVKKFRVSLALQPLATALFANSPFLEGHPNGFSSYRSHIWTDTDPHRTGILPFVFDDDFGYERYIDYMLSVPMYFVYRDGRYIDASGQDFRAFLRGELPALPNEKPILSDWVDHLSTAFPEVRLKSYLEMRGADGASAMMSPALSAFWISILYDSELLDTASDIIKSWSMDDYRNLRNEVPKKGLKTLIGGRQSLLDLGRQLWPLMNDALKRRAILNDKGQDESRYLAPIGEILESGQSLSDRLLARYHQTGNLDFIYQECDWAQPHILS
>NZ_CP023677.1|WP_011241319.1|1601281_1602052_+|16S-rRNA-(uracil(1498)-N(3))-methyltransferase
MVAEPAWPVNTLPRLYVEEKLSLEAVIIPDRAQAHYLLSVMRFKMGSQLVLFDNLTGEWLGEVIEAGRKHLQLKITHHLNEKESIPDLWLLTAPIKKGRIDWIYEKACELGVARITPVITQRTIVDRVNLERLQAHIVEAAEQCGRTSLSEVTEACSLKSLLAEWPEDRALFFADETGGEPMIEALSKRKMAAAILVGPEGGFTDQERDMINAVKQAVPVSLGPRILRADTAAIAATALWMAAAGDWQKQPRQANL
>NZ_CP023677.1|WP_011241318.1|1600007_1600973_+|thiamine-phosphate-kinase
MSGREQAFITALRQIAGDPAARNLSDDAAVLPRPSGDLVLSHDIIVENVHYFPSDPPETVAQKLVGVNLSDLAAKGAKPIGALMGYSLGPDYKWDQAFLKGLESVCHQYNLPLLGGDTVAVPRHTGHFSAMTVIGLAPSCGVPDRRAAKEGDELWVTSPIGDAGFGLNLLKQKKNINHSAQEKLVQAYRSPEPRLKEGIWLAPHVHAMADISDGLLIDAERIANASGLAVRIRLDRVPLSSEAISCFGDTKSTRLQAVTAGDDYQLIMACAANKRQELLKLSKEKQFDLYRVGQLTAGSGLSLFYGAEPIKQPDRLGYLHG
>NZ_CP023677.1|WP_011241317.1|1599515_1599989_+|transcription-antitermination-factor-NusB
MAQTQKRPHKNARSAARLAAVQALYQREMEKTPLNILLDEFHQYRLGATIEDATYTKAEPSFFDDIVRGVGTRCEEIDRVISENLSERWSLDRLDRPMRQILRAGTYELLARPDVPTATVISEYIDVANAFYDRQEKNFVNGLLDTVAKKLRSSNNA
>NZ_CP023677.1|WP_011241316.1|1598223_1599516_+|histidinol-dehydrogenase
MLLKLDSRKADFQADFTRLVDERRESEGDVSRDVSAIIADVKKRGDVAIAELTQKFDRHDLNKGGWQLTQEEIKKACDSLPSELMDALKLAATRIRYCHENQLPESSEMTDAAGVRMGVRWQAVEAAGLYVPGGRAAYCSSVLMNAVPAKVAGVKRLVMVTPTPDGFVNPAVIAAAVISEVDEIWKIGGAQAVAALALGTEKIKPVDVVVGPGNAWVAEAKRQLYGQVGIDMVAGPSEIVVVADKDNDPEWLAADLLSQAEHDPTSQSILISDSEDLIEKTIEAVGRRLEKLETQKVARESWDKHGATILVQSLDEAPALVDRLAPEHLELAVADPDALFANVHHSGSVFLGRYTPEAIGDYVGGPNHVLPTGRRARFSSGLSVIDFMKRTTYLNCSQEALSKIGPAAVTLAKAEGLPAHAESVISRLNK
>NZ_CP023677.1|WP_011241315.1|1597565_1598234_+|ATP-phosphoribosyltransferase
MTKPLVFAIPKGRILKEALPMLEAAGIIPEPAFLDKESRLLRFKTNRPDIEIIRVRAFDVATFVAHGAAQMGIVGSDVIEEFSYPELYAPVDLDIGHCRLSIAEPKRLAKDDDPREWSHVRVATKYPHLTHRHFEARGVQAECIKLNGAMEIAPALGLAGRIVDLVSSGRTLEENGLVEVEKIMPISARLIVNRAAFKMRAGDIAPLVENFRRLVGVADNVA
>NZ_CP023677.1|WP_011241314.1|1597171_1597477_+|BolA-family-transcriptional-regulator
MNMTSPSDTNEGPVTRLMRERLEAAFSPETLVIEDDSNKHAGHAGHPHRSESHFTVTLVSQAFENESRISRERMVHKALSDLLPDRIHALRLKLDTPLRQE
>NZ_CP023677.1|WP_011241313.1|1594629_1596807_+|squalene--hopene-cyclase
MGIDRMNSLSRLLMKKIFGAEKTSYKPASDTIIGTDTLKRPNRRPEPTAKVDKTIFKTMGNSLNNTLVSACDWLIGQQKPDGHWVGAVESNASMEAEWCLALWFLGLEDHPLRPRLGNALLEMQREDGSWGVYFGAGNGDINATVEAYAALRSLGYSADNPVLKKAAAWIAEKGGLKNIRVFTRYWLALIGEWPWEKTPNLPPEIIWFPDNFVFSIYNFAQWARATMVPIAILSARRPSRPLRPQDRLDELFPEGRARFDYELPKKEGIDLWSQFFRTTDRGLHWVQSNLLKRNSLREAAIRHVLEWIIRHQDADGGWGGIQPPWVYGLMALHGEGYQLYHPVMAKALSALDDPGWRHDRGESSWIQATNSPVWDTMLALMALKDAKAEDRFTPEMDKAADWLLARQVKVKGDWSIKLPDVEPGGWAFEYANDRYPDTDDTAVALIALSSYRDKEEWQKKGVEDAITRGVNWLIAMQSECGGWGAFDKDNNRSILSKIPFCDFGESIDPPSVDVTAHVLEAFGTLGLSRDMPVIQKAIDYVRSEQEAEGAWFGRWGVNYIYGTGAVLPALAAIGEDMTQPYITKACDWLVAHQQEDGGWGESCSSYMEIDSIGKGPTTPSQTAWALMGLIAANRPEDYEAIAKGCHYLIDRQEQDGSWKEEEFTGTGFPGYGVGQTIKLDDPALSKRLLQGAELSRAFMLRYDFYRQFFPIMALSRAERLIDLNN
>NZ_CP023677.1|WP_011241312.1|1594047_1594614_+|TetR/AcrR-family-transcriptional-regulator
MARPRTIDRERVLKSAEQLVQRAGATAMTLEAVAKEAGITKGGLQYCFGSKDDLITALIDRWFAAFDCEVKEYSQSDDSPAGEARAYVQASSQIDDATSARMVGMLVTLLQSPNHLKKIQAWYARWMEKNLGQSEEARHIRTMLFAAEGAFFLRSLGFIKMSESEWATVFDDIKKLVPSAQAGRASFK
>NZ_CP023677.1|WP_011241322.1|1607139_1607844_+|SDR-family-oxidoreductase
MTHRPLSDQIALVTGASRGIGAATAKALAEAGAHVILVARTATDLDKVEEQIYQKGGSATIAPLDITNSGSCHHLAAAISGRWPALDIMVFAAARYEAQPSIAAASPALQQMLAVNALATQDLLSRFDPLIQESRSAHIIGLTLPKSQAPYPYNGSYYASKMAMEAILLSYGAENAERDTIKVALAELEAVATEGRKRAFPDEKADLLRSPDEVAKAIVTMIVQDYANGWQGKL
>NZ_CP023677.1|WP_011241323.1|1607910_1608378_+|RNA-pyrophosphohydrolase
MDNLEYRSGVGIMLLNKDNLVFAACRNDMKEEAWQMPQGGLEAKETPEVGVLRELEEETGIPPRMVAIISHTKEWLTYDFPADLQASFFKNKYRGQRQLWFLARYLGRDEDININTDKPEFRAWKWVEPKQLPDLIVAFKKPLYEKILSEFSASL
>NZ_CP023677.1|WP_011241324.1|1608402_1609386_+|DUF481-domain-containing-protein
MQSRTISPWLLWRISQGAVLLSLVPVSEVWAEEPPKLIQEMVTKALALDDPKTVKSIVLIAKKTVPDSAAEIDAMVADYNTKVEAREAEKKRKELRRVADSGMFENWTGSVELGGAKMTGNTRQTAIYGAVALERNGINWTHTVKARTDFQRTYGTTSAERFTASYQPHYKFDERLYMYGLALYERDMFLGYRTRITGGSGIGYKVFDQPNLSLAVEGGPAYRHTIFIDSSRPNGRRIRDTAAMRGSFTTKWVVSPLLTVSEDSSIFFESKDITASSTTSLETKLIGNLSTKLSFSVYYEKDVSASKNPVDTTSRITFAYALGKKKK
>NZ_CP023677.1|WP_011241325.1|1609610_1610177_-|nicotinamide-mononucleotide-transporter
MSVLEWLAVLTSLLGIVFSTRQIRICWLFYGISSLLYGKIFFSIKLYADCLLQIFFFFSSIYGWFHWHHYQKADKMTVITASHKSLLRDIAMAAALSAIFGFYLKNYTDDAFPWVDAILSCYSIVAQFWAARLYKANWFLWIVIDFCYTALFCYRGLWLTAWLYSVFMVMAVIGLKKWQNKNPAVACD
>NZ_CP023677.1|WP_011241326.1|1610646_1610970_+|YnfA-family-protein
MLALLYIPAALAEITGCFSFWAWIRLHKSPLWLLPGIASLLLFAWLLTFSPAENAGKAYAVYGGIYIIMSLLWSWKVEATPPDHWDLIGAAFCLVGAAIILWMPRSL
>NZ_CP023677.1|WP_011241327.1|1610976_1612149_-|phosphotransferase
MAIKDDGMTEAAHKAVHQFGVSGYQTERDWPYLTILEINAVLASFSGQGKAIKILSHSRRPYSAAALFETDQKQTFFIKRHHHKIRNKTELLKEHLFARHLAQKSFPISTPMMADHNQTVIEKEPWIYEIHPQAQGVDIYQDVMSWEPFFNRDHAYEAGRMLALFHQAAQGFDESPRHHALLVSAGDTLLHDDFIKALSEWITAQPELLKQLEGKNWQQDITENILPFHHQLQPLTADITPLWGHGDWHSSNLMWTGRDPKAKVSCVLDLGMADYSSAMFDLATAIERNVIAWLDMDSRQDIVIYDQLFALLRGYHHIKPLSQMDKQLLSAFMPLLHVEYALSEIVYFGALLQDKTSADIAYYDYLLGHSRWFSGQEGQQLLQKIIHFEA
>NZ_CP023677.1|WP_017466250.1|1612161_1614585_-|TonB-dependent-receptor
MTYQDMTASEWRKYYQHFLVTSVFLAGISGVFPIHPAHAETQESPKSSDKTSSKNDAIIVTGRPLFKTANGFSVNDIGGGLIQKETETRSVSHISTDFIQKQAPTANAFDLVAMLPGANVTSSDPLGFSTQTNITIRGLSGDAIGYVLEGMPLNDVAYYTGYPTQFADSENYQQIGLAQGSADLDSPVLNAAGGVMNLNFRKPADKMGGYADFSYDSYNTNRQFLRFDMGEIGHSGVKGFVSYSHARTDNWRGAGYDEKQHVDFKFLKEWGQDSHVSLLGTWNKGITSYYPQVDKQSWKENGISGSNNLASRYNVNNDAAGSDYWRLYRAPEEIFYLAAPIDVRLASNLKLKVTPYGQWDRGNVPAGSTLNNSGLWNGTEAIAGTINLPNATDGTATVRSNYTQRSARAGVNASATWSLKNHDLTLGYWFDYSADKEQNSFTPVDSNGYASNIWADRHSTLIKMPDGSPLLGTNNRTHTYVNAVYLGDHMTFLQNRLTFDIGFKEVIMTRHGYNYLPGSQHKANFSTSEPLPRLGLRYQIDSKSHVFFSASTNFRTADETALYNSYDPTSGDIIVNGNKNLKNEYSVSEELGYRYSDALVTGSLTLFNYNFSNRQLQTVIVQNGSHIQSTINAGNQISRGVDFEIGLAPWHHISPYLSGEYLYTRQTSDLTVGDDLLPTKGKRAVRSPAFQGSLGVTYDDHHFFGMASVKYTGSQYGSFMNDEKIPAYVTGNISVGYRFTQEAFLKHPEIRLNFINIGNNHYLSGIASPTANAQDTVGRNGTVISGSAPQYYIGGGFAVLASLSSAF
>NZ_CP023677.1|WP_011241329.1|1614743_1615535_-|pyruvate-formate-lyase-activating-protein
MALIIKRPAVTSLVEEAGCDNTLKGRIHSTEIGGAVDGPGVRFVLFLAGCALRCQYCHNPDSWFLKNGRAVTLAEMMEEVASYADFLKRAGGGITISGGEPLVQPEFTGALLKAAKYLGLHTAIDTAGFLGAQADDALLSNTDLVLLDIKAFNDKRYKALTGVELQPTLAFAKRLAALKKPVWLRYVLVPGLTDNFNEIANLADFAATLGNIERVDVLPFHKMGEYKWKASGLAYKLGDTQPPSPALVEDVRGIFRDNGLNLS
>NZ_CP023677.1|WP_011241330.1|1615518_1617834_-|formate-C-acetyltransferase
MTISTLEKPDIAAGQASNAETQRMDSALDPWRGFKGRKWQREIDTRDFILSNVTSYTGNSDFLAGITPKTTKLWEKLQVSLEAERKTQGGVLDVDTSTVSNITAHAPGFIEKDLEVVVGLQTDAPLKRAIMPFGGYRMVKKGLEAYGFKEDESLSKIFPALRKTHNDGVFDVYTPEIMACRRSGIITGLPDAYGRGRIIGDYRRVALYGVDCLIEDKKEQGKRLERNPFDEETIKLREEVAEQIKALHELAAMAKSYGYDISQPAVTAQQAVQWTYFAYLAAVKEANGAAMSLGRVSTFLDIYIERDLKEGRITEAEAQELVDQFVMKLRIVRFLRTPEYDQLFSGDPTWVTESLGGMAIDGRTLVTKSSFRFLHTLENLGPAPEPNLTVLWSENLPKGFKDYCAKISIDTSSIQYENDDLMRSYWGDDYGIACCVSAMRIGKQMQFFGARANLAKTLLYAINGGRDEKSGVQVAPAFAPVTGDILDYEDVKSRMVQMMEWLSSVYINALNAIHFMHDKYMYERVEMALHDLEILRTMACGIAGLSVAADSLSAIKHAKVKIIRDERGLATDFKIEGDYPAYGNNDDRADEIAIWLVETFMNMLRKQTTYRRSVPTQSILTITSNVVYGKKTGNTPDGRRAGEPFAPGANPMHGRDLKGPVASMASVAKLPYAHAQDGISNTFTIVPNALGMNKEERIDNLIGLLSGYFGAGAHHMNVNVFDRNTLLDAVDHPEKYPQLTIRVSGYAVNFVKLTREQQMDVIHRTFHGLDN
>NZ_CP023677.1|WP_011241331.1|1618597_1620028_+|cytochrome-ubiquinol-oxidase-subunit-I
MVPDATALMLARIQFAFTVGFHIIFPAFSIGLAAYLAVLEGLWLKTGRNVYLHLFKYWIKIFALVFGMGVVSGLVMAYEFGTNWSLFSQKAGAITGPLLGYEVLTAFFLEAGFLGIMLFGLGRVGKGLHFLATCLVSIGTLISMTWILASNSWMQTPAGYSIDPKTGHFLPKSWFEVIFNPSFPYRLVHMGMAAFICVAFVVGATAAFHMLRDRKNGKPVTEPVRVMFSMALWMAAIAAPFQLLAGDMHGLNTLKYQPAKIAAMEGDWESEGPASEILFGIPNMKTERTDYAIKIPYAGSLILTHSLNGKVPGLKDYPRDQRPPSPILFFSFRIMVGLGGLMILLGLWSLFLRFRGQLYNNKALQWATLLMAPSGFIALLCGWVTTEVGRQPYTVYGLLRTSDSVSPVMLPSMIFSMTAFVIVYFFVFGAGMLILFRMLSHQPSSHEKGADPENPLQNSHAKGATQLAQDLSGKRS

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Crispr_ID: NZ_CP023677_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023677_3

1606170-1606561

Orphan

I-F

Consensus_repeat	Method
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	PILER-CR
GTTCACTGCCGCACAGGCAGCTTAGAAA	CRISPRCasFinder
GTTCACTGCCGCACAGGCAGCTTAGAAA	CRT

6 spacers

The CRISPR arrays of NZ_CP023677_3

>merge|NZ_CP023677|3|1606170-1606561|PILER-CR,CRISPRCasFinder,CRT
GTTCACTGCCGCACAGGCAGCTTAGAAAGCGCATCTTCTGATGCTTTTTTAGCTGCGGCCGTTCACTGCCGCACAGGCAGCTTAGAAATTGACGCTGTGAGCGTGACGATATGCTTTCACGTTCACTGCCGCACAGGCAGCTTAGAAAATCGGGGCATAAAATAGCGACTTGCTCACCGATGTTCACTGCCGCACAGGCAGCTTAGAAAGTCTGGCTGAAATGAGGTCCGACGATTTGCATGTTCACTGCCGCACAGGCAGCTTAGAAAACCCCTCTTGGTAGTCGTATCTGCAGACGCAATGTTCACTGCCGCACAGGCAGCTTAGAAAATATAGAAGATTTATCAGATACGTTGAGAATAAGTTCACTGCCGCACAGGCAGCTTAGAAAA

>NZ_CP023677|3|3|1606170-1606499|PILER-CR
GTTCACTGCCGCACAGGCAGCTTAGAAA	GCGCATCTTCTGATGCTTTTTTAGCTGCGGCC
GTTCACTGCCGCACAGGCAGCTTAGAAA	TTGACGCTGTGAGCGTGACGATATGCTTTCAC
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATCGGGGCATAAAATAGCGACTTGCTCACCGAT
GTTCACTGCCGCACAGGCAGCTTAGAAA	GTCTGGCTGAAATGAGGTCCGACGATTTGCAT
GTTCACTGCCGCACAGGCAGCTTAGAAA	ACCCCTCTTGGTAGTCGTATCTGCAGACGCAAT
GTTCACTGCCGCACAGGCAGCTTAGAAA

>NZ_CP023677|3|2|1606170-1606561|CRISPRCasFinder
GTTCACTGCCGCACAGGCAGCTTAGAAA	GCGCATCTTCTGATGCTTTTTTAGCTGCGGCC
GTTCACTGCCGCACAGGCAGCTTAGAAA	TTGACGCTGTGAGCGTGACGATATGCTTTCAC
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATCGGGGCATAAAATAGCGACTTGCTCACCGAT
GTTCACTGCCGCACAGGCAGCTTAGAAA	GTCTGGCTGAAATGAGGTCCGACGATTTGCAT
GTTCACTGCCGCACAGGCAGCTTAGAAA	ACCCCTCTTGGTAGTCGTATCTGCAGACGCAAT
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATATAGAAGATTTATCAGATACGTTGAGAATAA
GTTCACTGCCGCACAGGCAGCTTAGAAAA

>NZ_CP023677|3|3|1606170-1606560|CRT
GTTCACTGCCGCACAGGCAGCTTAGAAA	GCGCATCTTCTGATGCTTTTTTAGCTGCGGCC
GTTCACTGCCGCACAGGCAGCTTAGAAA	TTGACGCTGTGAGCGTGACGATATGCTTTCAC
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATCGGGGCATAAAATAGCGACTTGCTCACCGAT
GTTCACTGCCGCACAGGCAGCTTAGAAA	GTCTGGCTGAAATGAGGTCCGACGATTTGCAT
GTTCACTGCCGCACAGGCAGCTTAGAAA	ACCCCTCTTGGTAGTCGTATCTGCAGACGCAAT
GTTCACTGCCGCACAGGCAGCTTAGAAA	ATATAGAAGATTTATCAGATACGTTGAGAATAA
GTTCACTGCCGCACAGGCAGCTTAGAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023677.1\|WP_011241329.1\|1614743_1615535_-\|pyruvate-formate-lyase-activating-protein	unknown	unknown	gnl\|CDD\|131546
NZ_CP023677.1\|WP_011241318.1\|1600007_1600973_+\|thiamine-phosphate-kinase	unknown	unknown	gnl\|CDD\|273589
NZ_CP023677.1\|WP_011241325.1\|1609610_1610177_-\|nicotinamide-mononucleotide-transporter	unknown	unknown	gnl\|CDD\|377432
NZ_CP023677.1\|WP_011241322.1\|1607139_1607844_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP023677.1\|WP_011241327.1\|1610976_1612149_-\|phosphotransferase	unknown	unknown	gnl\|CDD\|225213
NZ_CP023677.1\|WP_011241317.1\|1599515_1599989_+\|transcription-antitermination-factor-NusB	unknown	unknown	gnl\|CDD\|234686
NZ_CP023677.1\|WP_011241319.1\|1601281_1602052_+\|16S-rRNA-(uracil(1498)-N(3))-methyltransferase	unknown	unknown	gnl\|CDD\|236959
NZ_CP023677.1\|WP_011241324.1\|1608402_1609386_+\|DUF481-domain-containing-protein	unknown	unknown	gnl\|CDD\|377313
NZ_CP023677.1\|WP_011241315.1\|1597565_1598234_+\|ATP-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234971
NZ_CP023677.1\|WP_011241314.1\|1597171_1597477_+\|BolA-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|376601
NZ_CP023677.1\|WP_011241312.1\|1594047_1594614_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380063
NZ_CP023677.1\|WP_011241326.1\|1610646_1610970_+\|YnfA-family-protein	unknown	unknown	gnl\|CDD\|235016
NZ_CP023677.1\|WP_011241323.1\|1607910_1608378_+\|RNA-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|239643
NZ_CP023677.1\|WP_011241330.1\|1615518_1617834_-\|formate-C-acetyltransferase	unknown	unknown	gnl\|CDD\|153087
NZ_CP023677.1\|WP_011241313.1\|1594629_1596807_+\|squalene--hopene-cyclase	unknown	unknown	gnl\|CDD\|239222
NZ_CP023677.1\|WP_017466250.1\|1612161_1614585_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP023677.1\|WP_011241320.1\|1602357_1603746_+\|glutamate--cysteine-ligase	unknown	unknown	gnl\|CDD\|130503
NZ_CP023677.1\|WP_011241316.1\|1598223_1599516_+\|histidinol-dehydrogenase	unknown	unknown	gnl\|CDD\|234853
NZ_CP023677.1\|WP_011241321.1\|1604168_1605695_+\|amidophosphoribosyltransferase	unknown	unknown	gnl\|CDD\|236384
NZ_CP023677.1\|WP_011241331.1\|1618597_1620028_+\|cytochrome-ubiquinol-oxidase-subunit-I	unknown	unknown	gnl\|CDD\|376587

Protein	Function_ID	Function_description	E-value
NZ_CP023677.1\|WP_011241329.1\|1614743_1615535_-\|pyruvate-formate-lyase-activating-protein	gnl\|CDD\|131546	TIGR02493, PFLA, pyruvate formate-lyase 1-activating enzyme. An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair].	4.75927e-144
NZ_CP023677.1\|WP_011241318.1\|1600007_1600973_+\|thiamine-phosphate-kinase	gnl\|CDD\|273589	TIGR01379, Thiamine-monophosphate_kinase, thiamine-phosphate kinase. This model describes thiamine-monophosphate kinase, an enzyme that converts thiamine monophosphate into thiamine pyrophosphate (TPP, coenzyme B1), an enzyme cofactor. Thiamine monophosphate may be derived from de novo synthesis or from unphosphorylated thiamine, known as vitamin B1. Proteins scoring between the trusted and noise cutoff for this model include short forms from the Thermoplasmas (which lack the N-terminal region) and a highly derived form from Campylobacter jejuni. Eukaryotes lack this enzyme, and add pyrophosphate from ATP to unphosphorylated thiamine in a single step. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine].	3.56412e-120
NZ_CP023677.1\|WP_011241325.1\|1609610_1610177_-\|nicotinamide-mononucleotide-transporter	gnl\|CDD\|377432	pfam04973, NMN_transporter, Nicotinamide mononucleotide transporter. Members of this family are integral membrane proteins that are involved in transport of nicotinamide mononucleotide.	7.92226e-43
NZ_CP023677.1\|WP_011241322.1\|1607139_1607844_+\|SDR-family-oxidoreductase	gnl\|CDD\|212491	cd05233, SDR_c, classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	1.51834e-29
NZ_CP023677.1\|WP_011241327.1\|1610976_1612149_-\|phosphotransferase	gnl\|CDD\|225213	COG2334, COG2334, Putative homoserine kinase type II (protein kinase fold) [General function prediction only].	1.02009e-16
NZ_CP023677.1\|WP_011241317.1\|1599515_1599989_+\|transcription-antitermination-factor-NusB	gnl\|CDD\|234686	PRK00202, nusB, transcription antitermination factor NusB.	1.68678e-43
NZ_CP023677.1\|WP_011241319.1\|1601281_1602052_+\|16S-rRNA-(uracil(1498)-N(3))-methyltransferase	gnl\|CDD\|236959	PRK11713, PRK11713, 16S ribosomal RNA methyltransferase RsmE; Provisional.	1.99557e-75
NZ_CP023677.1\|WP_011241324.1\|1608402_1609386_+\|DUF481-domain-containing-protein	gnl\|CDD\|377313	pfam04338, DUF481, Protein of unknown function, DUF481. This family includes several proteins of uncharacterized function.	1.15385e-57
NZ_CP023677.1\|WP_011241315.1\|1597565_1598234_+\|ATP-phosphoribosyltransferase	gnl\|CDD\|234971	PRK01686, hisG, ATP phosphoribosyltransferase catalytic subunit; Reviewed.	1.37428e-112
NZ_CP023677.1\|WP_011241314.1\|1597171_1597477_+\|BolA-family-transcriptional-regulator	gnl\|CDD\|376601	pfam01722, BolA, BolA-like protein. This family consist of the morphoprotein BolA from E. coli and its various homologs. In E. coli over expression of this protein causes round morphology and may be involved in switching the cell between elongation and septation systems during cell division. The expression of BolA is growth rate regulated and is induced during the transition into the the stationary phase. BolA is also induced by stress during early stages of growth and may have a general role in stress response. It has also been suggested that BolA can induce the transcription of penicillin binding proteins 6 and 5.	3.78262e-28
NZ_CP023677.1\|WP_011241312.1\|1594047_1594614_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|380063	pfam17937, TetR_C_28, Tetracyclin repressor-like, C-terminal domain. TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain. This entry represents the C-terminal domain present in CgmR (C. glutamicum multidrug-responsive transcriptional repressor), previously called CGL2612 protein. CgmR (CGL2612) from Corynebacterium glutamicum is a multidrug-resistance-related transcription factor belonging to the TetR family. It regulates expression of the immediately upstream gene cgmA (cgl2611) by binding to the operator cgmO in the cgmA promoter. The cgmA gene encodes a permease belonging to the major facilitator superfamily, a protein family composed of bacterial multidrug exporters, and the pair of CgmR and CgmA confers multidrug resistance on C. glutamicum.	1.92303e-12
NZ_CP023677.1\|WP_011241326.1\|1610646_1610970_+\|YnfA-family-protein	gnl\|CDD\|235016	PRK02237, PRK02237, YnfA family protein.	2.17346e-38
NZ_CP023677.1\|WP_011241323.1\|1607910_1608378_+\|RNA-pyrophosphohydrolase	gnl\|CDD\|239643	cd03671, Ap4A_hydrolase_plant_like, Diadenosine tetraphosphate (Ap4A) hydrolase is a member of the Nudix hydrolase superfamily. Members of this family are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one group (represented by this subfamily) and fungi/animals/archaea enzymes fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for the inhibition of such invasive bacteria. Besides the signature nudix motif (G[X5]E[X7]REUXEEXGU where U is Ile, Leu, or Val), Ap4A hydrolase is structurally similar to the other members of the nudix superfamily with some degree of variations. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies.	7.05806e-74
NZ_CP023677.1\|WP_011241330.1\|1615518_1617834_-\|formate-C-acetyltransferase	gnl\|CDD\|153087	cd01678, PFL1, Pyruvate formate lyase 1. Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate in which two cysteines and one glycine form radicals that are required for catalysis. PFL has a ten-stranded alpha/beta barrel domain that is structurally similar to those of all three ribonucleotide reductase (RNR) classes as well as benzylsuccinate synthase and B12-independent glycerol dehydratase.	0
NZ_CP023677.1\|WP_011241313.1\|1594629_1596807_+\|squalene--hopene-cyclase	gnl\|CDD\|239222	cd02892, SQCY_1, Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. This group contains bacterial SQCY which catalyzes the convertion of squalene to hopene or diplopterol and eukaryotic OSQCY which transforms the 2,3-epoxide of squalene to compounds such as, lanosterol in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain.	0
NZ_CP023677.1\|WP_017466250.1\|1612161_1614585_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.35387e-37
NZ_CP023677.1\|WP_011241320.1\|1602357_1603746_+\|glutamate--cysteine-ligase	gnl\|CDD\|130503	TIGR01436, Glutamate--cysteine_ligase_chloroplastic, glutamate--cysteine ligase, plant type. This model represents one of two highly dissimilar forms of glutamate--cysteine ligase (gamma-glutamylcysteine synthetase), an enzyme of glutathione biosynthesis. The other type is modeled by TIGR01434. This type is found in plants (with a probable transit peptide), root nodule and other bacteria, but not E. coli and closely related species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs].	0
NZ_CP023677.1\|WP_011241316.1\|1598223_1599516_+\|histidinol-dehydrogenase	gnl\|CDD\|234853	PRK00877, hisD, bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed.	0
NZ_CP023677.1\|WP_011241321.1\|1604168_1605695_+\|amidophosphoribosyltransferase	gnl\|CDD\|236384	PRK09123, PRK09123, amidophosphoribosyltransferase; Provisional.	0
NZ_CP023677.1\|WP_011241331.1\|1618597_1620028_+\|cytochrome-ubiquinol-oxidase-subunit-I	gnl\|CDD\|376587	pfam01654, Cyt_bd_oxida_I, Cytochrome bd terminal oxidase subunit I. This family are the alternative oxidases found in many bacteria which oxidize ubiquinol and reduce oxygen as part of the electron transport chain. This family is the subunit I of the oxidase E. coli has two copies of the oxidase, bo and bd', both of which are represented here In some nitrogen fixing bacteria, e.g. Klebsiella pneumoniae this oxidase is responsible for removing oxygen in microaerobic conditions, making the oxidase required for nitrogen fixation. This subunit binds a single b-haem, through ligands at His186 and Met393 (using SW:P11026 numbering). In addition His19 is a ligand for the haem b found in subunit II.	0

>NZ_CP023677.1|WP_011241321.1|1604168_1605695_+|amidophosphoribosyltransferase
MSPSLSSELFSDSISTLTTTTESLDNGASDDTLHEECGVFGIWGADTAAAVVALGLHALQHRGQEAAGITSWDGKNFHSRRAVGHVAGNFDRDDAIRSLPGSCAIGHVRYATTGASTLCNVQPLYAELVSGGFAIAHNGNISNAETLRHQLVRHGSIFQSTSDTETIIHLVATSSYRSLLDRFIDALKQVEGAYSLVCLTPEGMIACRDPLGIRPLVLGKVGETFVVASETVALDIIGGTYIRQVEPGELIIISEKGLQSIHPFKKQKPRPCIFEHVYFSRPDSLIGSTSVYSVRKSIGIELARENPVDADMVIPVPDSGTPAAIGYAQQSSLPFELGIIRSHYVGRTFIQPGDQVRHLGVKLKHNANRALIKGKKLVLVDDSIVRGTTSVKIIRMLRDAGAKEIHLRIASPPTRHSCFYGVDTPERAKLLAAKMTVEQMAEYIGADSLAFISMDGLYRAVGEEARNDAQPQYCDACFTGAYPTPLTDLGELGASEQLVRLSEQVAIA
>NZ_CP023677.1|WP_011241320.1|1602357_1603746_+|glutamate--cysteine-ligase
MSTRQTSSSQNHPIESRDDLLRIFQAGEKPKAQWRVGTEHEKLVYKKQNHQAPSYEEKGGICDLLQGFTRFGWQPIYENDKIIGLSGDDGAISLEPAGQFELSGAPRSTIHESYDEICRHIQQTQEVGDELGLGFLGLGLWPDKKRSDLPLMPKGRYKIMTEYMPKVGKLGLDMMLRTCTIQSNIDYGSEADMVKKFRVSLALQPLATALFANSPFLEGHPNGFSSYRSHIWTDTDPHRTGILPFVFDDDFGYERYIDYMLSVPMYFVYRDGRYIDASGQDFRAFLRGELPALPNEKPILSDWVDHLSTAFPEVRLKSYLEMRGADGASAMMSPALSAFWISILYDSELLDTASDIIKSWSMDDYRNLRNEVPKKGLKTLIGGRQSLLDLGRQLWPLMNDALKRRAILNDKGQDESRYLAPIGEILESGQSLSDRLLARYHQTGNLDFIYQECDWAQPHILS
>NZ_CP023677.1|WP_011241319.1|1601281_1602052_+|16S-rRNA-(uracil(1498)-N(3))-methyltransferase
MVAEPAWPVNTLPRLYVEEKLSLEAVIIPDRAQAHYLLSVMRFKMGSQLVLFDNLTGEWLGEVIEAGRKHLQLKITHHLNEKESIPDLWLLTAPIKKGRIDWIYEKACELGVARITPVITQRTIVDRVNLERLQAHIVEAAEQCGRTSLSEVTEACSLKSLLAEWPEDRALFFADETGGEPMIEALSKRKMAAAILVGPEGGFTDQERDMINAVKQAVPVSLGPRILRADTAAIAATALWMAAAGDWQKQPRQANL
>NZ_CP023677.1|WP_011241318.1|1600007_1600973_+|thiamine-phosphate-kinase
MSGREQAFITALRQIAGDPAARNLSDDAAVLPRPSGDLVLSHDIIVENVHYFPSDPPETVAQKLVGVNLSDLAAKGAKPIGALMGYSLGPDYKWDQAFLKGLESVCHQYNLPLLGGDTVAVPRHTGHFSAMTVIGLAPSCGVPDRRAAKEGDELWVTSPIGDAGFGLNLLKQKKNINHSAQEKLVQAYRSPEPRLKEGIWLAPHVHAMADISDGLLIDAERIANASGLAVRIRLDRVPLSSEAISCFGDTKSTRLQAVTAGDDYQLIMACAANKRQELLKLSKEKQFDLYRVGQLTAGSGLSLFYGAEPIKQPDRLGYLHG
>NZ_CP023677.1|WP_011241317.1|1599515_1599989_+|transcription-antitermination-factor-NusB
MAQTQKRPHKNARSAARLAAVQALYQREMEKTPLNILLDEFHQYRLGATIEDATYTKAEPSFFDDIVRGVGTRCEEIDRVISENLSERWSLDRLDRPMRQILRAGTYELLARPDVPTATVISEYIDVANAFYDRQEKNFVNGLLDTVAKKLRSSNNA
>NZ_CP023677.1|WP_011241316.1|1598223_1599516_+|histidinol-dehydrogenase
MLLKLDSRKADFQADFTRLVDERRESEGDVSRDVSAIIADVKKRGDVAIAELTQKFDRHDLNKGGWQLTQEEIKKACDSLPSELMDALKLAATRIRYCHENQLPESSEMTDAAGVRMGVRWQAVEAAGLYVPGGRAAYCSSVLMNAVPAKVAGVKRLVMVTPTPDGFVNPAVIAAAVISEVDEIWKIGGAQAVAALALGTEKIKPVDVVVGPGNAWVAEAKRQLYGQVGIDMVAGPSEIVVVADKDNDPEWLAADLLSQAEHDPTSQSILISDSEDLIEKTIEAVGRRLEKLETQKVARESWDKHGATILVQSLDEAPALVDRLAPEHLELAVADPDALFANVHHSGSVFLGRYTPEAIGDYVGGPNHVLPTGRRARFSSGLSVIDFMKRTTYLNCSQEALSKIGPAAVTLAKAEGLPAHAESVISRLNK
>NZ_CP023677.1|WP_011241315.1|1597565_1598234_+|ATP-phosphoribosyltransferase
MTKPLVFAIPKGRILKEALPMLEAAGIIPEPAFLDKESRLLRFKTNRPDIEIIRVRAFDVATFVAHGAAQMGIVGSDVIEEFSYPELYAPVDLDIGHCRLSIAEPKRLAKDDDPREWSHVRVATKYPHLTHRHFEARGVQAECIKLNGAMEIAPALGLAGRIVDLVSSGRTLEENGLVEVEKIMPISARLIVNRAAFKMRAGDIAPLVENFRRLVGVADNVA
>NZ_CP023677.1|WP_011241314.1|1597171_1597477_+|BolA-family-transcriptional-regulator
MNMTSPSDTNEGPVTRLMRERLEAAFSPETLVIEDDSNKHAGHAGHPHRSESHFTVTLVSQAFENESRISRERMVHKALSDLLPDRIHALRLKLDTPLRQE
>NZ_CP023677.1|WP_011241313.1|1594629_1596807_+|squalene--hopene-cyclase
MGIDRMNSLSRLLMKKIFGAEKTSYKPASDTIIGTDTLKRPNRRPEPTAKVDKTIFKTMGNSLNNTLVSACDWLIGQQKPDGHWVGAVESNASMEAEWCLALWFLGLEDHPLRPRLGNALLEMQREDGSWGVYFGAGNGDINATVEAYAALRSLGYSADNPVLKKAAAWIAEKGGLKNIRVFTRYWLALIGEWPWEKTPNLPPEIIWFPDNFVFSIYNFAQWARATMVPIAILSARRPSRPLRPQDRLDELFPEGRARFDYELPKKEGIDLWSQFFRTTDRGLHWVQSNLLKRNSLREAAIRHVLEWIIRHQDADGGWGGIQPPWVYGLMALHGEGYQLYHPVMAKALSALDDPGWRHDRGESSWIQATNSPVWDTMLALMALKDAKAEDRFTPEMDKAADWLLARQVKVKGDWSIKLPDVEPGGWAFEYANDRYPDTDDTAVALIALSSYRDKEEWQKKGVEDAITRGVNWLIAMQSECGGWGAFDKDNNRSILSKIPFCDFGESIDPPSVDVTAHVLEAFGTLGLSRDMPVIQKAIDYVRSEQEAEGAWFGRWGVNYIYGTGAVLPALAAIGEDMTQPYITKACDWLVAHQQEDGGWGESCSSYMEIDSIGKGPTTPSQTAWALMGLIAANRPEDYEAIAKGCHYLIDRQEQDGSWKEEEFTGTGFPGYGVGQTIKLDDPALSKRLLQGAELSRAFMLRYDFYRQFFPIMALSRAERLIDLNN
>NZ_CP023677.1|WP_011241312.1|1594047_1594614_+|TetR/AcrR-family-transcriptional-regulator
MARPRTIDRERVLKSAEQLVQRAGATAMTLEAVAKEAGITKGGLQYCFGSKDDLITALIDRWFAAFDCEVKEYSQSDDSPAGEARAYVQASSQIDDATSARMVGMLVTLLQSPNHLKKIQAWYARWMEKNLGQSEEARHIRTMLFAAEGAFFLRSLGFIKMSESEWATVFDDIKKLVPSAQAGRASFK
>NZ_CP023677.1|WP_011241322.1|1607139_1607844_+|SDR-family-oxidoreductase
MTHRPLSDQIALVTGASRGIGAATAKALAEAGAHVILVARTATDLDKVEEQIYQKGGSATIAPLDITNSGSCHHLAAAISGRWPALDIMVFAAARYEAQPSIAAASPALQQMLAVNALATQDLLSRFDPLIQESRSAHIIGLTLPKSQAPYPYNGSYYASKMAMEAILLSYGAENAERDTIKVALAELEAVATEGRKRAFPDEKADLLRSPDEVAKAIVTMIVQDYANGWQGKL
>NZ_CP023677.1|WP_011241323.1|1607910_1608378_+|RNA-pyrophosphohydrolase
MDNLEYRSGVGIMLLNKDNLVFAACRNDMKEEAWQMPQGGLEAKETPEVGVLRELEEETGIPPRMVAIISHTKEWLTYDFPADLQASFFKNKYRGQRQLWFLARYLGRDEDININTDKPEFRAWKWVEPKQLPDLIVAFKKPLYEKILSEFSASL
>NZ_CP023677.1|WP_011241324.1|1608402_1609386_+|DUF481-domain-containing-protein
MQSRTISPWLLWRISQGAVLLSLVPVSEVWAEEPPKLIQEMVTKALALDDPKTVKSIVLIAKKTVPDSAAEIDAMVADYNTKVEAREAEKKRKELRRVADSGMFENWTGSVELGGAKMTGNTRQTAIYGAVALERNGINWTHTVKARTDFQRTYGTTSAERFTASYQPHYKFDERLYMYGLALYERDMFLGYRTRITGGSGIGYKVFDQPNLSLAVEGGPAYRHTIFIDSSRPNGRRIRDTAAMRGSFTTKWVVSPLLTVSEDSSIFFESKDITASSTTSLETKLIGNLSTKLSFSVYYEKDVSASKNPVDTTSRITFAYALGKKKK
>NZ_CP023677.1|WP_011241325.1|1609610_1610177_-|nicotinamide-mononucleotide-transporter
MSVLEWLAVLTSLLGIVFSTRQIRICWLFYGISSLLYGKIFFSIKLYADCLLQIFFFFSSIYGWFHWHHYQKADKMTVITASHKSLLRDIAMAAALSAIFGFYLKNYTDDAFPWVDAILSCYSIVAQFWAARLYKANWFLWIVIDFCYTALFCYRGLWLTAWLYSVFMVMAVIGLKKWQNKNPAVACD
>NZ_CP023677.1|WP_011241326.1|1610646_1610970_+|YnfA-family-protein
MLALLYIPAALAEITGCFSFWAWIRLHKSPLWLLPGIASLLLFAWLLTFSPAENAGKAYAVYGGIYIIMSLLWSWKVEATPPDHWDLIGAAFCLVGAAIILWMPRSL
>NZ_CP023677.1|WP_011241327.1|1610976_1612149_-|phosphotransferase
MAIKDDGMTEAAHKAVHQFGVSGYQTERDWPYLTILEINAVLASFSGQGKAIKILSHSRRPYSAAALFETDQKQTFFIKRHHHKIRNKTELLKEHLFARHLAQKSFPISTPMMADHNQTVIEKEPWIYEIHPQAQGVDIYQDVMSWEPFFNRDHAYEAGRMLALFHQAAQGFDESPRHHALLVSAGDTLLHDDFIKALSEWITAQPELLKQLEGKNWQQDITENILPFHHQLQPLTADITPLWGHGDWHSSNLMWTGRDPKAKVSCVLDLGMADYSSAMFDLATAIERNVIAWLDMDSRQDIVIYDQLFALLRGYHHIKPLSQMDKQLLSAFMPLLHVEYALSEIVYFGALLQDKTSADIAYYDYLLGHSRWFSGQEGQQLLQKIIHFEA
>NZ_CP023677.1|WP_017466250.1|1612161_1614585_-|TonB-dependent-receptor
MTYQDMTASEWRKYYQHFLVTSVFLAGISGVFPIHPAHAETQESPKSSDKTSSKNDAIIVTGRPLFKTANGFSVNDIGGGLIQKETETRSVSHISTDFIQKQAPTANAFDLVAMLPGANVTSSDPLGFSTQTNITIRGLSGDAIGYVLEGMPLNDVAYYTGYPTQFADSENYQQIGLAQGSADLDSPVLNAAGGVMNLNFRKPADKMGGYADFSYDSYNTNRQFLRFDMGEIGHSGVKGFVSYSHARTDNWRGAGYDEKQHVDFKFLKEWGQDSHVSLLGTWNKGITSYYPQVDKQSWKENGISGSNNLASRYNVNNDAAGSDYWRLYRAPEEIFYLAAPIDVRLASNLKLKVTPYGQWDRGNVPAGSTLNNSGLWNGTEAIAGTINLPNATDGTATVRSNYTQRSARAGVNASATWSLKNHDLTLGYWFDYSADKEQNSFTPVDSNGYASNIWADRHSTLIKMPDGSPLLGTNNRTHTYVNAVYLGDHMTFLQNRLTFDIGFKEVIMTRHGYNYLPGSQHKANFSTSEPLPRLGLRYQIDSKSHVFFSASTNFRTADETALYNSYDPTSGDIIVNGNKNLKNEYSVSEELGYRYSDALVTGSLTLFNYNFSNRQLQTVIVQNGSHIQSTINAGNQISRGVDFEIGLAPWHHISPYLSGEYLYTRQTSDLTVGDDLLPTKGKRAVRSPAFQGSLGVTYDDHHFFGMASVKYTGSQYGSFMNDEKIPAYVTGNISVGYRFTQEAFLKHPEIRLNFINIGNNHYLSGIASPTANAQDTVGRNGTVISGSAPQYYIGGGFAVLASLSSAF
>NZ_CP023677.1|WP_011241329.1|1614743_1615535_-|pyruvate-formate-lyase-activating-protein
MALIIKRPAVTSLVEEAGCDNTLKGRIHSTEIGGAVDGPGVRFVLFLAGCALRCQYCHNPDSWFLKNGRAVTLAEMMEEVASYADFLKRAGGGITISGGEPLVQPEFTGALLKAAKYLGLHTAIDTAGFLGAQADDALLSNTDLVLLDIKAFNDKRYKALTGVELQPTLAFAKRLAALKKPVWLRYVLVPGLTDNFNEIANLADFAATLGNIERVDVLPFHKMGEYKWKASGLAYKLGDTQPPSPALVEDVRGIFRDNGLNLS
>NZ_CP023677.1|WP_011241330.1|1615518_1617834_-|formate-C-acetyltransferase
MTISTLEKPDIAAGQASNAETQRMDSALDPWRGFKGRKWQREIDTRDFILSNVTSYTGNSDFLAGITPKTTKLWEKLQVSLEAERKTQGGVLDVDTSTVSNITAHAPGFIEKDLEVVVGLQTDAPLKRAIMPFGGYRMVKKGLEAYGFKEDESLSKIFPALRKTHNDGVFDVYTPEIMACRRSGIITGLPDAYGRGRIIGDYRRVALYGVDCLIEDKKEQGKRLERNPFDEETIKLREEVAEQIKALHELAAMAKSYGYDISQPAVTAQQAVQWTYFAYLAAVKEANGAAMSLGRVSTFLDIYIERDLKEGRITEAEAQELVDQFVMKLRIVRFLRTPEYDQLFSGDPTWVTESLGGMAIDGRTLVTKSSFRFLHTLENLGPAPEPNLTVLWSENLPKGFKDYCAKISIDTSSIQYENDDLMRSYWGDDYGIACCVSAMRIGKQMQFFGARANLAKTLLYAINGGRDEKSGVQVAPAFAPVTGDILDYEDVKSRMVQMMEWLSSVYINALNAIHFMHDKYMYERVEMALHDLEILRTMACGIAGLSVAADSLSAIKHAKVKIIRDERGLATDFKIEGDYPAYGNNDDRADEIAIWLVETFMNMLRKQTTYRRSVPTQSILTITSNVVYGKKTGNTPDGRRAGEPFAPGANPMHGRDLKGPVASMASVAKLPYAHAQDGISNTFTIVPNALGMNKEERIDNLIGLLSGYFGAGAHHMNVNVFDRNTLLDAVDHPEKYPQLTIRVSGYAVNFVKLTREQQMDVIHRTFHGLDN
>NZ_CP023677.1|WP_011241331.1|1618597_1620028_+|cytochrome-ubiquinol-oxidase-subunit-I
MVPDATALMLARIQFAFTVGFHIIFPAFSIGLAAYLAVLEGLWLKTGRNVYLHLFKYWIKIFALVFGMGVVSGLVMAYEFGTNWSLFSQKAGAITGPLLGYEVLTAFFLEAGFLGIMLFGLGRVGKGLHFLATCLVSIGTLISMTWILASNSWMQTPAGYSIDPKTGHFLPKSWFEVIFNPSFPYRLVHMGMAAFICVAFVVGATAAFHMLRDRKNGKPVTEPVRVMFSMALWMAAIAAPFQLLAGDMHGLNTLKYQPAKIAAMEGDWESEGPASEILFGIPNMKTERTDYAIKIPYAGSLILTHSLNGKVPGLKDYPRDQRPPSPILFFSFRIMVGLGGLMILLGLWSLFLRFRGQLYNNKALQWATLLMAPSGFIALLCGWVTTEVGRQPYTVYGLLRTSDSVSPVMLPSMIFSMTAFVIVYFFVFGAGMLILFRMLSHQPSSHEKGADPENPLQNSHAKGATQLAQDLSGKRS

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP023677_2	2.6\|1245684\|33\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1245684-1245716	33	NZ_CP023677.1	293330-293362	1	0.97

1. spacer 2.6|1245684|33|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to position: 293330-293362, mismatch: 1, identity: 0.97

atcgaactgcgtgcctgatagccgatacgctga	CRISPR spacer
atcgaactacgtgcctgatagccgatacgctga	Protospacer
********.************************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP023677_3	3.2\|1606258\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606258-1606289	32	NZ_CP021792	Zymomonas mobilis subsp. mobilis strain NRRL B-1960 plasmid pZMO1960_1A, complete sequence	1418-1449	0	1.0
NZ_CP023677_3	3.2\|1606258\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606258-1606289	32	NC_019198	Zymomonas mobilis subsp. mobilis NCIMB 11163 plasmid pZMO1A, complete sequence	1479-1510	0	1.0
NZ_CP023677_3	3.2\|1606258\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606258-1606289	32	NC_019210	Zymomonas mobilis subsp. mobilis plasmid pZMO1B, complete sequence	1479-1510	0	1.0
NZ_CP023677_3	3.2\|1606258\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606258-1606289	32	NC_011363	Zymomonas mobilis subsp. mobilis ATCC 10988 plasmid pZMO1, complete sequence	1482-1513	1	0.969
NZ_CP023677_3	3.6\|1606500\|33\|NZ_CP023677\|CRISPRCasFinder,CRT	1606500-1606532	33	NC_001845	Zymomonas mobilis ATCC10988 plasmid pZMO1, complete sequence	653-685	1	0.97
NZ_CP023677_3	3.6\|1606500\|33\|NZ_CP023677\|CRISPRCasFinder,CRT	1606500-1606532	33	NC_009716	Escherichia sp. Sflu5 cryptic plasmid pAK51	3617-3649	1	0.97
NZ_CP023677_3	3.6\|1606500\|33\|NZ_CP023677\|CRISPRCasFinder,CRT	1606500-1606532	33	NC_005701	Zymomonas mobilis ATCC 10988 plasmid pZMO2, complete sequence	8-40	1	0.97
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	NC_013784	Zymomonas mobilis subsp. mobilis ZM4 plasmid pZZM401, complete sequence	12257-12288	2	0.938
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	NZ_CP003712	Zymomonas mobilis subsp. mobilis NRRL B-12526 plasmid pZM1252603, complete sequence	22552-22583	2	0.938
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	NZ_CP003718	Zymomonas mobilis subsp. mobilis str. CP4 = NRRL B-14023 plasmid pZM1402303, complete sequence	12257-12288	2	0.938
NZ_CP023677_3	3.2\|1606258\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606258-1606289	32	NC_019019	Zymomonas mobilis plasmid pZMN1-1, complete sequence	1475-1506	2	0.938
NZ_CP023677_3	3.2\|1606258\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606258-1606289	32	NC_009716	Escherichia sp. Sflu5 cryptic plasmid pAK51	4439-4470	4	0.875
NZ_CP023677_3	3.2\|1606258\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606258-1606289	32	NC_001845	Zymomonas mobilis ATCC10988 plasmid pZMO1, complete sequence	1513-1544	4	0.875
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	MK448979	Streptococcus phage Javan534, complete genome	13215-13246	7	0.781
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	MK448799	Streptococcus phage Javan535, complete genome	13215-13246	7	0.781
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	MK448800	Streptococcus phage Javan539, complete genome	13216-13247	7	0.781
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	MT939241	Enterococcus phage 9183, complete genome	69460-69491	7	0.781
NZ_CP023677_1	1.5\|114051\|32\|NZ_CP023677\|CRT,PILER-CR	114051-114082	32	NZ_CP018236	Rhizobium leguminosarum strain Vaf-108 plasmid unnamed8	109921-109952	8	0.75
NZ_CP023677_2	2.4\|1245564\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1245564-1245595	32	NZ_LR214998	Mycoplasma conjunctivae strain NCTC10147 plasmid 2	1218-1249	8	0.75
NZ_CP023677_2	2.4\|1245564\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1245564-1245595	32	NZ_CP049042	Pseudohalocynthiibacter aestuariivivens strain RR4-35 plasmid pRR4-35_5, complete sequence	37299-37330	8	0.75
NZ_CP023677_2	2.4\|1245564\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1245564-1245595	32	NZ_CP049700	Bradyrhizobium sp. 1S5 strain 323S2 plasmid pB323S2a, complete sequence	291573-291604	8	0.75
NZ_CP023677_3	3.2\|1606258\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606258-1606289	32	CP053324	Salmonella enterica subsp. salamae serovar 40:c:e,n,z15 strain 2013K-0524 plasmid unnamed, complete sequence	9447-9478	8	0.75
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	MT446411	UNVERIFIED: Escherichia virus TH40, complete genome	67504-67535	9	0.719
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	MT446421	UNVERIFIED: Escherichia virus TH55, complete genome	80840-80871	9	0.719
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	MT446396	UNVERIFIED: Escherichia virus TH22, complete genome	137515-137546	9	0.719
NZ_CP023677_2	2.4\|1245564\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1245564-1245595	32	MN692951	Marine virus AFVG_117M12, complete genome	19672-19703	10	0.688
NZ_CP023677_2	2.4\|1245564\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1245564-1245595	32	NC_019526	Enterobacteria phage vB_KleM-RaK2, complete genome	67317-67348	10	0.688
NZ_CP023677_2	2.4\|1245564\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1245564-1245595	32	MT708547	Klebsiella phage Muenster, complete genome	189204-189235	10	0.688
NZ_CP023677_2	2.4\|1245564\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1245564-1245595	32	AB897757	Klebsiella phage K64-1 DNA, complete genome	67288-67319	10	0.688
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	NC_020292	Clostridium saccharoperbutylacetonicum N1-4(HMT) plasmid Csp_135p, complete sequence	13543-13574	10	0.688
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	MN583270	Pseudomonas aeruginosa strain NK546 plasmid pNK546b, complete sequence	67159-67190	10	0.688
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	MF360958	Salicola phage SCTP-2, complete genome	175798-175829	10	0.688
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	JN231330	UNVERIFIED: Uncultured phage contig03 MexF-like gene, complete sequence	1910-1941	10	0.688
NZ_CP023677_2	2.4\|1245564\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1245564-1245595	32	KY549443	Enterococcus phage EFP01, complete genome	110490-110521	11	0.656
NZ_CP023677_3	3.1\|1606198\|32\|NZ_CP023677\|PILER-CR,CRISPRCasFinder,CRT	1606198-1606229	32	AP013403	Uncultured Mediterranean phage uvMED DNA, complete genome, group G15, isolate: uvMED-CGR-U-MedDCM-OCT-S41-C7	29040-29071	11	0.656

1. spacer 3.2|1606258|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP021792 (Zymomonas mobilis subsp. mobilis strain NRRL B-1960 plasmid pZMO1960_1A, complete sequence) position: , mismatch: 0, identity: 1.0

ttgacgctgtgagcgtgacgatatgctttcac	CRISPR spacer
ttgacgctgtgagcgtgacgatatgctttcac	Protospacer
********************************

2. spacer 3.2|1606258|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NC_019198 (Zymomonas mobilis subsp. mobilis NCIMB 11163 plasmid pZMO1A, complete sequence) position: , mismatch: 0, identity: 1.0

ttgacgctgtgagcgtgacgatatgctttcac	CRISPR spacer
ttgacgctgtgagcgtgacgatatgctttcac	Protospacer
********************************

3. spacer 3.2|1606258|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NC_019210 (Zymomonas mobilis subsp. mobilis plasmid pZMO1B, complete sequence) position: , mismatch: 0, identity: 1.0

ttgacgctgtgagcgtgacgatatgctttcac	CRISPR spacer
ttgacgctgtgagcgtgacgatatgctttcac	Protospacer
********************************

4. spacer 3.2|1606258|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NC_011363 (Zymomonas mobilis subsp. mobilis ATCC 10988 plasmid pZMO1, complete sequence) position: , mismatch: 1, identity: 0.969

ttgacgctgtgagcgtgacgatatgctttcac	CRISPR spacer
ttgacgctgtgagcgtgacgatatgctttcgc	Protospacer
******************************.*

5. spacer 3.6|1606500|33|NZ_CP023677|CRISPRCasFinder,CRT matches to NC_001845 (Zymomonas mobilis ATCC10988 plasmid pZMO1, complete sequence) position: , mismatch: 1, identity: 0.97

atatagaagatttatcagatacgttgagaataa	CRISPR spacer
atatagaagatttgtcagatacgttgagaataa	Protospacer
*************.*******************

6. spacer 3.6|1606500|33|NZ_CP023677|CRISPRCasFinder,CRT matches to NC_009716 (Escherichia sp. Sflu5 cryptic plasmid pAK51) position: , mismatch: 1, identity: 0.97

atatagaagatttatcagatacgttgagaataa	CRISPR spacer
atatagaagatttgtcagatacgttgagaataa	Protospacer
*************.*******************

7. spacer 3.6|1606500|33|NZ_CP023677|CRISPRCasFinder,CRT matches to NC_005701 (Zymomonas mobilis ATCC 10988 plasmid pZMO2, complete sequence) position: , mismatch: 1, identity: 0.97

atatagaagatttatcagatacgttgagaataa	CRISPR spacer
atatagaagatttgtcagatacgttgagaataa	Protospacer
*************.*******************

8. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NC_013784 (Zymomonas mobilis subsp. mobilis ZM4 plasmid pZZM401, complete sequence) position: , mismatch: 2, identity: 0.938

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
gcgcttcttctgctgcttttttagctgcggcc	Protospacer
**** ******* *******************

9. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP003712 (Zymomonas mobilis subsp. mobilis NRRL B-12526 plasmid pZM1252603, complete sequence) position: , mismatch: 2, identity: 0.938

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
gcgcttcttctgctgcttttttagctgcggcc	Protospacer
**** ******* *******************

10. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP003718 (Zymomonas mobilis subsp. mobilis str. CP4 = NRRL B-14023 plasmid pZM1402303, complete sequence) position: , mismatch: 2, identity: 0.938

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
gcgcttcttctgctgcttttttagctgcggcc	Protospacer
**** ******* *******************

11. spacer 3.2|1606258|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NC_019019 (Zymomonas mobilis plasmid pZMN1-1, complete sequence) position: , mismatch: 2, identity: 0.938

ttgacgctgtgagcgtgacgatatgctttcac	CRISPR spacer
ttgacgctgtgaccgtgacgatatcctttcac	Protospacer
************ *********** *******

12. spacer 3.2|1606258|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NC_009716 (Escherichia sp. Sflu5 cryptic plasmid pAK51) position: , mismatch: 4, identity: 0.875

ttgacgctgtgagcgtgacgatatgctttcac	CRISPR spacer
ttgacgctgtgagcgtgacgatatgcttatcg	Protospacer
**************************** .

13. spacer 3.2|1606258|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NC_001845 (Zymomonas mobilis ATCC10988 plasmid pZMO1, complete sequence) position: , mismatch: 4, identity: 0.875

ttgacgctgtgagcgtgacgatatgctttcac	CRISPR spacer
ttgacgctgtgagcgtgacgatatgcttatcg	Protospacer
**************************** .

14. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MK448979 (Streptococcus phage Javan534, complete genome) position: , mismatch: 7, identity: 0.781

gcgcatcttctgatgcttttttagctg--cggcc	CRISPR spacer
acccatcttctgatggttttttcgctgactgg--	Protospacer
.* ************ ****** ****  .**

15. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MK448799 (Streptococcus phage Javan535, complete genome) position: , mismatch: 7, identity: 0.781

gcgcatcttctgatgcttttttagctg--cggcc	CRISPR spacer
acccatcttctgatggttttttcgctgactgg--	Protospacer
.* ************ ****** ****  .**

16. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MK448800 (Streptococcus phage Javan539, complete genome) position: , mismatch: 7, identity: 0.781

gcgcatcttctgatgcttttttagctg--cggcc	CRISPR spacer
acccatcttctgatggttttttcgctgactgg--	Protospacer
.* ************ ****** ****  .**

17. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MT939241 (Enterococcus phage 9183, complete genome) position: , mismatch: 7, identity: 0.781

gcgc-atcttctgatgcttttttagctgcggcc	CRISPR spacer
-cgctgtcttctgatgctttcttagccgcacca	Protospacer
 *** .**************.*****.**. *

18. spacer 1.5|114051|32|NZ_CP023677|CRT,PILER-CR matches to NZ_CP018236 (Rhizobium leguminosarum strain Vaf-108 plasmid unnamed8) position: , mismatch: 8, identity: 0.75

acagctaaaacccttttacctttactgtcggc	CRISPR spacer
tgacatcgaaccattttacctttcctgtcggc	Protospacer
  *  * .**** ********** ********

19. spacer 2.4|1245564|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NZ_LR214998 (Mycoplasma conjunctivae strain NCTC10147 plasmid 2) position: , mismatch: 8, identity: 0.75

ttctcaaaaaggaaaagaaattggaacagatt	CRISPR spacer
ccaacaaaaaggaaaataaaatggaacaaaat	Protospacer
..  ************ *** *******.* *

20. spacer 2.4|1245564|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP049042 (Pseudohalocynthiibacter aestuariivivens strain RR4-35 plasmid pRR4-35_5, complete sequence) position: , mismatch: 8, identity: 0.75

---ttctcaaaaaggaaaagaaattggaacagatt	CRISPR spacer
aggtcttc---aaggaaaagatattggaagagatg	Protospacer
   *..**   ********** ******* ****

21. spacer 2.4|1245564|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP049700 (Bradyrhizobium sp. 1S5 strain 323S2 plasmid pB323S2a, complete sequence) position: , mismatch: 8, identity: 0.75

ttctcaaaaaggaaaagaaattggaacagatt--	CRISPR spacer
gactcaaacaggaaaagaaactgga--cgatcgg	Protospacer
  ****** ***********.****   ***.

22. spacer 3.2|1606258|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to CP053324 (Salmonella enterica subsp. salamae serovar 40:c:e,n,z15 strain 2013K-0524 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.75

ttgacgctgtgagcgtgacgatatgctttcac	CRISPR spacer
gtcacgctgtgaacgtaacgatatgcgtaaat	Protospacer
 * *********.***.********* *  *.

23. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MT446411 (UNVERIFIED: Escherichia virus TH40, complete genome) position: , mismatch: 9, identity: 0.719

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
tcgcatcttctgtttcttttttagacgccatg	Protospacer
 *********** * ********* .** ..

24. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MT446421 (UNVERIFIED: Escherichia virus TH55, complete genome) position: , mismatch: 9, identity: 0.719

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
tcgcatcttctgtttcttttttagacgccatg	Protospacer
 *********** * ********* .** ..

25. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MT446396 (UNVERIFIED: Escherichia virus TH22, complete genome) position: , mismatch: 9, identity: 0.719

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
tcgcatcttctgtttcttttttagacgccatg	Protospacer
 *********** * ********* .** ..

26. spacer 2.4|1245564|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MN692951 (Marine virus AFVG_117M12, complete genome) position: , mismatch: 10, identity: 0.688

ttctcaaaaaggaaaagaaattggaacagatt	CRISPR spacer
ggacgcaacaggaaaagaaattggaaaagaaa	Protospacer
   .  ** ***************** ***

27. spacer 2.4|1245564|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NC_019526 (Enterobacteria phage vB_KleM-RaK2, complete genome) position: , mismatch: 10, identity: 0.688

ttctcaaaaaggaaaagaaattggaacagatt	CRISPR spacer
agtacaaaaaggacaagaaattggtactgcaa	Protospacer
  . ********* ********** ** *

28. spacer 2.4|1245564|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MT708547 (Klebsiella phage Muenster, complete genome) position: , mismatch: 10, identity: 0.688

ttctcaaaaaggaaaagaaattggaacagatt	CRISPR spacer
agtacaaaaaggacaagaaattggtactgcaa	Protospacer
  . ********* ********** ** *

29. spacer 2.4|1245564|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to AB897757 (Klebsiella phage K64-1 DNA, complete genome) position: , mismatch: 10, identity: 0.688

ttctcaaaaaggaaaagaaattggaacagatt	CRISPR spacer
agtacaaaaaggacaagaaattggtactgcaa	Protospacer
  . ********* ********** ** *

30. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to NC_020292 (Clostridium saccharoperbutylacetonicum N1-4(HMT) plasmid Csp_135p, complete sequence) position: , mismatch: 10, identity: 0.688

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
tattatcatctgatgcttctttagctgaattc	Protospacer
   .*** **********.******** . .*

31. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MN583270 (Pseudomonas aeruginosa strain NK546 plasmid pNK546b, complete sequence) position: , mismatch: 10, identity: 0.688

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
agtgaaggacttatgcttttttagctgaggcc	Protospacer
.   *    ** *************** ****

32. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to MF360958 (Salicola phage SCTP-2, complete genome) position: , mismatch: 10, identity: 0.688

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
catcatcttctggtgcttttttacctaagaaa	Protospacer
   *********.********** **. *.

33. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to JN231330 (UNVERIFIED: Uncultured phage contig03 MexF-like gene, complete sequence) position: , mismatch: 10, identity: 0.688

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
ccccaacttcagatgcttttttagctaatcta	Protospacer
 * ** **** ***************.   .

34. spacer 2.4|1245564|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to KY549443 (Enterococcus phage EFP01, complete genome) position: , mismatch: 11, identity: 0.656

ttctcaaaaaggaaaagaaattggaacagatt	CRISPR spacer
cgtccaaaatggaaaagaaattgaaacgtgaa	Protospacer
. ..***** *************.***. .

35. spacer 3.1|1606198|32|NZ_CP023677|PILER-CR,CRISPRCasFinder,CRT matches to AP013403 (Uncultured Mediterranean phage uvMED DNA, complete genome, group G15, isolate: uvMED-CGR-U-MedDCM-OCT-S41-C7) position: , mismatch: 11, identity: 0.656

gcgcatcttctgatgcttttttagctgcggcc	CRISPR spacer
cggcaacttctgatgcttttgtagcaattaat	Protospacer
  *** ************** **** .. . .

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

383000 : 393484

Sinorhizobium_phage(33.33%)

terminase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_011240296.1\|383000_385427_-	endopeptidase La	A0A0R6PGP8	Moraxella_phage	1.1e-204	48.0
WP_011240297.1\|385622_386243_+	DNA-3-methyladenine glycosylase 2 family protein	NA	NA	NA	NA
WP_011240298.1\|386326_386833_+	helix-turn-helix domain-containing protein	Q8W6H9	Sinorhizobium_phage	1.8e-27	53.3
WP_011240299.1\|386832_388119_+\|terminase	PBSX family phage terminase large subunit	F8TUR5	EBPR_podovirus	5.4e-174	69.9
WP_011240300.1\|388161_390351_+	hypothetical protein	A0A1B1IQR4	uncultured_Mediterranean_phage	4.4e-75	32.5
WP_011240301.1\|390350_390650_+	hypothetical protein	NA	NA	NA	NA
WP_011240302.1\|390772_391624_+	hypothetical protein	NA	NA	NA	NA
WP_011240303.1\|391649_391757_+	hypothetical protein	NA	NA	NA	NA
WP_011240305.1\|392089_393004_+	DUF5309 domain-containing protein	A0A1Y0T0F4	Sinorhizobium_phage	2.3e-65	48.1
WP_011240306.1\|393157_393484_+	hypothetical protein	A0A218MLW6	uncultured_virus	5.1e-12	41.9

DBSCAN-SWA_2

1209064 : 1222272

Pseudomonas_phage(12.5%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_011241009.1\|1209064_1211005_+	lytic transglycosylase domain-containing protein	K4NWI2	Pseudomonas_phage	1.8e-08	35.5
WP_011241010.1\|1211016_1211829_-	bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase	G3MA33	Bacillus_virus	1.4e-29	32.4
WP_011241011.1\|1212138_1212867_+	bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE	NA	NA	NA	NA
WP_011241012.1\|1212870_1214409_+	2-polyprenylphenol 6-hydroxylase	A0A167R6U4	Powai_lake_megavirus	1.8e-06	26.0
WP_011241013.1\|1214435_1215689_+	bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase CoaBC	Q9HH70	Methanothermobacter_phage	8.7e-44	31.5
WP_011241014.1\|1215720_1216161_+	dUTP diphosphatase	A0A2L1IVN2	Streptomyces_phage	5.4e-33	51.7
WP_011241015.1\|1216157_1216916_+	HesA/MoeB/ThiF family protein	A0A1V0SAV8	Catovirus	5.9e-11	27.3
WP_011241016.1\|1217324_1220963_-	type I DNA topoisomerase	A0A1V0SCS0	Indivirus	2.8e-98	37.1
WP_011241017.1\|1221114_1222272_-	DNA-protecting protein DprA	S6BFL3	Thermus_phage	1.3e-28	38.1

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP023680

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NZ_CP023677

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection