CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Target MGE spacer number	Prophage number
NZ_CP003713	Zymomonas mobilis subsp. mobilis NRRL B-12526 plasmid pZM1252604, complete sequence	0 crisprs	NA	0	0
NZ_CP003709	Zymomonas mobilis subsp. mobilis NRRL B-12526, complete genome	3 crisprs	cas6f,cas7f,cas5f,cas8f,cas3f,cas1,DEDDh,csa3	7	1
NZ_CP003714	Zymomonas mobilis subsp. mobilis NRRL B-12526 plasmid pZM1252605, complete sequence	0 crisprs	NA	0	0
NZ_CP003712	Zymomonas mobilis subsp. mobilis NRRL B-12526 plasmid pZM1252603, complete sequence	0 crisprs	NA	0	1
NZ_CP003710	Zymomonas mobilis subsp. mobilis NRRL B-12526 plasmid pZM1252601, complete sequence	0 crisprs	NA	0	0
NZ_CP003711	Zymomonas mobilis subsp. mobilis NRRL B-12526 plasmid pZM1252602, complete sequence	0 crisprs	NA	0	0

Results visualization

Click the left colored region to show detailed information

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

14775 : 37017

Burkholderia_phage(35.0%)

tail,plate,portal,head,terminase,capsid

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_012954678.1\|14775_15768_-	late control D family protein	A0A0F7LDZ2	Escherichia_phage	1.4e-41	29.0
WP_012954679.1\|15764_16310_-\|tail	phage tail protein	Q9ZXJ9	Pseudomonas_virus	1.9e-19	32.0
WP_023593782.1\|16309_18940_-\|tail	phage tail tape measure protein	A0A088FV68	Escherichia_phage	5.6e-24	27.8
WP_012954681.1\|18917_19052_-\|tail	GpE family phage tail protein	A0A2H4JFK5	uncultured_Caudovirales_phage	2.4e-08	61.5
WP_012954682.1\|19060_19441_-\|tail	phage tail assembly protein	R4JJY8	Burkholderia_phage	3.5e-12	45.3
WP_012954683.1\|19525_20038_-\|tail	phage major tail tube protein	R4JEU1	Burkholderia_phage	1.8e-24	37.6
WP_012954684.1\|20057_21215_-\|tail	tail sheath protein	S4TRX2	Salmonella_phage	2.2e-86	46.1
WP_012954685.1\|21214_21556_-	GPW/gp25 family protein	A0A077K8R5	Ralstonia_phage	8.5e-18	43.4
WP_023593784.1\|21640_22177_-\|plate	phage baseplate assembly protein V	NA	NA	NA	NA
WP_012954687.1\|22402_22849_-	hypothetical protein	NA	NA	NA	NA
WP_012954688.1\|22872_25182_-	hypothetical protein	V9IQX0	Stenotrophomonas_phage	8.6e-37	50.3
WP_012954689.1\|25181_25733_-\|tail	phage tail protein I	V9IQK7	Stenotrophomonas_phage	4.5e-37	40.9
WP_012954690.1\|25729_26647_-\|plate	baseplate assembly protein J	R4JDM0	Burkholderia_phage	9.2e-67	46.8
WP_012954691.1\|26736_27495_-	phage virion morphogenesis protein	NA	NA	NA	NA
WP_012954692.1\|27476_27980_-	hypothetical protein	NA	NA	NA	NA
WP_043940410.1\|27976_28240_-	hypothetical protein	NA	NA	NA	NA
WP_012954694.1\|28199_28625_-	hypothetical protein	NA	NA	NA	NA
WP_012954695.1\|28618_29062_-	N-acetylmuramyl-L-alanine amidase negative regulator of AmpC AmpD	A0A218MLJ9	uncultured_virus	1.6e-21	44.0
WP_012954696.1\|29058_29397_-	hypothetical protein	NA	NA	NA	NA
WP_012954697.1\|29400_29613_-\|tail	tail X family protein	A0A077K8R0	Ralstonia_phage	1.6e-06	42.2
WP_012954698.1\|29609_30095_-\|head	head completion/stabilization protein	E5E3S2	Burkholderia_phage	8.6e-24	43.2
WP_012954699.1\|30091_30883_-\|terminase	small terminase subunit	E5E3W7	Burkholderia_phage	1.4e-31	45.5
WP_012954700.1\|30885_32013_-\|capsid	phage major capsid protein, P2 family	Q9ZXM3	Pseudomonas_virus	4.1e-77	46.1
WP_012954701.1\|32054_32864_-\|capsid	phage capsid scaffolding protein	Q9ZXM4	Pseudomonas_virus	3.4e-25	49.3
WP_012954702.1\|32996_34772_+	DUF264 domain-containing protein	E5FFI8	Burkholderia_phage	6.3e-165	50.6
WP_012954703.1\|34771_35791_+\|portal	phage portal protein	E5FFI9	Burkholderia_phage	3.2e-84	48.2
WP_012954704.1\|36146_36374_-	hypothetical protein	NA	NA	NA	NA
WP_012954705.1\|36366_37017_-	AAA family ATPase	K7R2R7	Vibrio_phage	2.7e-36	40.7

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_CP003709

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP003709_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP003709_1

131560-132020

Orphan

I-F

Consensus_repeat	Method
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CRISPRCasFinder
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CRT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	PILER-CR

7 spacers

The CRISPR arrays of NZ_CP003709_1

>merge|NZ_CP003709|1|131560-132020|CRISPRCasFinder,CRT,PILER-CR
CTAAGCAACTGCCTGTGCGGCAGTGAACTTCATCCGCATTTCGGCCAACATTGCCTGAATTTGCTCTAGCATTTCTAAGCTGCCTGTGCGGCAGTGAACGTATGCTGATGATTGCCCCATGCCCACAATCCTTTCTAAGCTGCCTGTGCGGCAGTGAACCATCGTCTATTAGCTTATGGGATATGGTTACTTTTCTAAGCTGCCTGTGCGGCAGTGAACCCAATCGATTAAAGCATCGACAAAAGCACGCTTTTCTAAGCTGCCTGTGCGGCAGTGAACCTGATATGCGGTGATCTGGCTGATCTGTTGTTTTTTCTAAGCTGCCTGTGCGGCAGTGAACATATGGGCAGCGGTCATATGATGCGGCAGGGATTTCTAAGCTGCCTGTGCGGCAGTGAACAGCGTTATTAGATTCTTTAACAATTTCAAATTATTTCTAAGCTGCCTGTGCGGCAGTGAAC

>NZ_CP003709|1|1|131560-132020|CRISPRCasFinder
CTAAGCAACTGCCTGTGCGGCAGTGAAC	TTCATCCGCATTTCGGCCAACATTGCCTGAATTTGCTCTAGCA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	GTATGCTGATGATTGCCCCATGCCCACAATCC
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CATCGTCTATTAGCTTATGGGATATGGTTACT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CCAATCGATTAAAGCATCGACAAAAGCACGCT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CTGATATGCGGTGATCTGGCTGATCTGTTGTTT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	ATATGGGCAGCGGTCATATGATGCGGCAGGGA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	AGCGTTATTAGATTCTTTAACAATTTCAAATTA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC

>NZ_CP003709|1|1|131560-132020|CRT
CTAAGCAACTGCCTGTGCGGCAGTGAAC	TTCATCCGCATTTCGGCCAACATTGCCTGAATTTGCTCTAGCA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	GTATGCTGATGATTGCCCCATGCCCACAATCC
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CATCGTCTATTAGCTTATGGGATATGGTTACT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CCAATCGATTAAAGCATCGACAAAAGCACGCT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CTGATATGCGGTGATCTGGCTGATCTGTTGTTT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	ATATGGGCAGCGGTCATATGATGCGGCAGGGA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	AGCGTTATTAGATTCTTTAACAATTTCAAATTA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC

>NZ_CP003709|1|1|131631-132020|PILER-CR
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	GTATGCTGATGATTGCCCCATGCCCACAATCC
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CATCGTCTATTAGCTTATGGGATATGGTTACT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CCAATCGATTAAAGCATCGACAAAAGCACGCT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CTGATATGCGGTGATCTGGCTGATCTGTTGTTT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	ATATGGGCAGCGGTCATATGATGCGGCAGGGA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	AGCGTTATTAGATTCTTTAACAATTTCAAATTA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP003709.1\|WP_023593047.1\|130224_130683_+\|twin-arginine-translocase-subunit-TatB	unknown	unknown	gnl\|CDD\|130477
NZ_CP003709.1\|WP_023593052.1\|144105_145095_-\|carbon-nitrogen-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|143588
NZ_CP003709.1\|WP_025420117.1\|143432_143759_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP003709.1\|WP_023593051.1\|139404_140751_+\|glutathione-disulfide-reductase	unknown	unknown	gnl\|CDD\|235701
NZ_CP003709.1\|WP_011241042.1\|126272_126647_-\|30S-ribosomal-protein-S6	unknown	unknown	gnl\|CDD\|179034
NZ_CP003709.1\|WP_011241031.1\|137718_139242_+\|glucose-6-phosphate-isomerase	unknown	unknown	gnl\|CDD\|366041
NZ_CP003709.1\|WP_011241029.1\|141217_143176_+\|potassium-transporter-Kup	unknown	unknown	gnl\|CDD\|225700
NZ_CP003709.1\|WP_023593050.1\|135313_136834_-\|DEAD/DEAH-box-helicase	unknown	unknown	gnl\|CDD\|223587
NZ_CP003709.1\|WP_011241044.1\|125383_126013_-\|50S-ribosomal-protein-L9	unknown	unknown	gnl\|CDD\|234659
NZ_CP003709.1\|WP_011241032.1\|136961_137387_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|227505
NZ_CP003709.1\|WP_011241045.1\|124308_125304_+\|dipeptide-epimerase	unknown	unknown	gnl\|CDD\|239435
NZ_CP003709.1\|WP_011241038.1\|129876_130140_+\|twin-arginine-translocase-TatA/TatE-family-subunit	unknown	unknown	gnl\|CDD\|234822
NZ_CP003709.1\|WP_011241034.1\|134756_134969_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|375983
NZ_CP003709.1\|WP_011241040.1\|128173_128911_+\|3-oxoacyl-ACP-reductase-FabG	unknown	unknown	gnl\|CDD\|187594
NZ_CP003709.1\|WP_023593046.1\|127168_128104_+\|ACP-S-malonyltransferase	unknown	unknown	gnl\|CDD\|223408
NZ_CP003709.1\|WP_011241715.1\|132575_132710_-\|entericidin-A/B-family-lipoprotein	unknown	unknown	gnl\|CDD\|227797
NZ_CP003709.1\|WP_012816906.1\|133077_134730_-\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226434
NZ_CP003709.1\|WP_012816903.1\|129061_129724_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP003709.1\|WP_011241043.1\|126027_126252_-\|30S-ribosomal-protein-S18	unknown	unknown	gnl\|CDD\|178997
NZ_CP003709.1\|WP_023593048.1\|130679_131468_+\|twin-arginine-translocase-subunit-TatC	unknown	unknown	gnl\|CDD\|376413

Protein	Function_ID	Function_description	E-value
NZ_CP003709.1\|WP_023593047.1\|130224_130683_+\|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].	3.34195e-18
NZ_CP003709.1\|WP_023593052.1\|144105_145095_-\|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.	1.65304e-151
NZ_CP003709.1\|WP_011241031.1\|137718_139242_+\|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_CP003709.1\|WP_011241042.1\|126272_126647_-\|30S-ribosomal-protein-S6	gnl\|CDD\|179034	PRK00453, rpsF, 30S ribosomal protein S6; Reviewed.	6.50436e-48
NZ_CP003709.1\|WP_011241715.1\|132575_132710_-\|entericidin-A/B-family-lipoprotein	gnl\|CDD\|227797	COG5510, COG5510, Predicted small secreted protein [Function unknown].	5.12008e-07
NZ_CP003709.1\|WP_011241029.1\|141217_143176_+\|potassium-transporter-Kup	gnl\|CDD\|225700	COG3158, Kup, K+ transporter [Inorganic ion transport and metabolism].	0
NZ_CP003709.1\|WP_023593050.1\|135313_136834_-\|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].	1.77926e-158
NZ_CP003709.1\|WP_011241044.1\|125383_126013_-\|50S-ribosomal-protein-L9	gnl\|CDD\|234659	PRK00137, rplI, 50S ribosomal protein L9; Reviewed.	4.06061e-62
NZ_CP003709.1\|WP_011241032.1\|136961_137387_-\|hypothetical-protein	gnl\|CDD\|227505	COG5178, PRP8, U5 snRNP spliceosome subunit [RNA processing and modification].	0.000693568
NZ_CP003709.1\|WP_011241045.1\|124308_125304_+\|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_CP003709.1\|WP_011241038.1\|129876_130140_+\|twin-arginine-translocase-TatA/TatE-family-subunit	gnl\|CDD\|234822	PRK00720, tatA, twin-arginine translocase TatA/TatE family subunit.	9.82533e-37
NZ_CP003709.1\|WP_011241034.1\|134756_134969_-\|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_CP003709.1\|WP_023593051.1\|139404_140751_+\|glutathione-disulfide-reductase	gnl\|CDD\|235701	PRK06116, PRK06116, glutathione reductase; Validated.	0
NZ_CP003709.1\|WP_023593046.1\|127168_128104_+\|ACP-S-malonyltransferase	gnl\|CDD\|223408	COG0331, FabD, (acyl-carrier-protein) S-malonyltransferase [Lipid metabolism].	3.31802e-123
NZ_CP003709.1\|WP_011241040.1\|128173_128911_+\|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_CP003709.1\|WP_023593048.1\|130679_131468_+\|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.	1.31e-75
NZ_CP003709.1\|WP_011241043.1\|126027_126252_-\|30S-ribosomal-protein-S18	gnl\|CDD\|178997	PRK00391, rpsR, 30S ribosomal protein S18; Reviewed.	2.27745e-35
NZ_CP003709.1\|WP_012816906.1\|133077_134730_-\|sensor-histidine-kinase	gnl\|CDD\|226434	COG3920, COG3920, Signal transduction histidine kinase [Signal transduction mechanisms].	3.27983e-20

>NZ_CP003709.1|WP_023593048.1|130679_131468_+|twin-arginine-translocase-subunit-TatC
MSETDDIHDEVDESAAPLLDHLLELRKRLLISLVALGIAFLLCLHFSRSIFAFLVQPLLRAGQGRLIYTDIFEAFFVDIKVAFFAAIMLAFPIVAMQIWRFIAPGLYSNEKRAFLPFLVMTPLLFLVGASMAYYVAMPIALHFLLGYQGNIGGVQQMALPAVGNYLNFVTKFIFGFGVAFLLPLVLLLLERAGFVTRQQLVAGRRYAIVASVAIAAVLTPPDIVSQLLLGVPLILLYEMALLAMLFGEKRRKKETDLVVAED
>NZ_CP003709.1|WP_023593047.1|130224_130683_+|twin-arginine-translocase-subunit-TatB
MFDVAPSELLLVAVVALVVIGPKDLPRAMRVVGRWLGKARKLSRHFRSGIDEMIRQSEMEDMEKRWAEENAKLLAENQGQGNQTASTSSPATPSPVSDDPAEQNIVFASPADLEVNTADTSHLAANHTETAATTSASTPATPKEADQQEKQS
>NZ_CP003709.1|WP_011241038.1|129876_130140_+|twin-arginine-translocase-TatA/TatE-family-subunit
MGGMSITHWIVVAVVVMIFFGKGRFSDMMGDVAKGIKSFKKGMSEDDTTPPAAPPAPAPRLENQPLPPENTTQNVAQNVPNDIKNNQ
>NZ_CP003709.1|WP_012816903.1|129061_129724_+|hypothetical-protein
MSIFKSGFAPVITLSLASLLLGGCVVHHGQFDEMGSMTVRRSSCPAVAVPDYTGDVTLFNPSDQRTASAIDIEAVITKLRPKCDDTASGPVVTHLTFTVQARRRHVGGARDITLPYFVAVMRAGTRLLSKEMGTVRIHFEPGQMATDTEVTTSSAIDHDSATLPRDIIRQLNKVRQVTDVDASVDPTNDPKVRAAMKEASFEMLVGFQLTEPQLAYNATR
>NZ_CP003709.1|WP_011241040.1|128173_128911_+|3-oxoacyl-ACP-reductase-FabG
MFDLNGLTAVVTGASGGIGSAIAKALADQGAQVALSGTRESALKEVAAILPNDPIILPANLGQKEDVEQLVPRALEKLGKIDILVNNAGITRDGLMMRMKDEDWADVIALNLESVFRLSRAVIRPMMKTRFGRIINISSVVGQTGNAGQANYAAAKAGMIGMSKSLAREVASRGITVNCIAPGFIETKMTEILSEQQKEAAKSQIPAGRFGDIQDIAAAAVYLASKEAGYMTGQTLSVNGGMSML
>NZ_CP003709.1|WP_023593046.1|127168_128104_+|ACP-S-malonyltransferase
MRAFIFPGQGSQSVGMGQALADASLAARHVFEEVDEALKQNLFRLMSQGPEEELRLTENAQPAIMAHSMAVLAMLEKEGNIRLTDAASFVAGHSLGEYSALAAADAFDLPTTARLLKKRGQAMQAAVPVGEGGMAAILGLDFETVESIAQEAAENDICQAANDNAPGQVVISGSLAAIERAVALAKEKGARRAVMLDVSAPFHCSLMQPAADVMAKALQENRPRQPIVPVFANVSATAETDPTKIMNLLVEQVTGRVRWRESIAAMAAAGVEEFVEFGGKVLAPMIKRIAPDCKATSLIAPADIENFAASL
>NZ_CP003709.1|WP_011241042.1|126272_126647_-|30S-ribosomal-protein-S6
MPLYEHVFLARQDLAQTQVDGLAATATSIIEEKSGKVVKTEIWGLRNLAYRIQKNRKAYYIMLEIDAPADAIQELERQMALNEDVIRYMTVRVDAHEQGPSAMMRRGDRDRSNRSDRRRDRDAA
>NZ_CP003709.1|WP_011241043.1|126027_126252_-|30S-ribosomal-protein-S18
MARPFFRRRKSCPFAAKDAPKIDYKDVRLLQGFVSERGKIVPSRITAVSAKKQRELARAIKRARHIGLLPFIVK
>NZ_CP003709.1|WP_011241044.1|125383_126013_-|50S-ribosomal-protein-L9
MDVILLERIEKLGHIGDVVAVKNGYARNFLLPRKKALRANEANRKIFEANRAQIEADNAARRTDAEKESEVVNGLTVTLIRQASNTGHLYGSVSARDLADAIVEAKPEAKVAKNQIVLDRPIKSIGISEVRVVLHPEVAVKIKVNVARSPEEAELQAEGVDVMNQMFERDGASFTEDYDPNAEPGLATEAEEAVADADDNAETNSEESL
>NZ_CP003709.1|WP_011241045.1|124308_125304_+|dipeptide-epimerase
MTATRSLSIMGESLPLKTPFRISRGVKNTIDTIVANISESGVTGRGEGIPYPRYGQTVESALIEANSVSHKITEHYGREALLTLLPPGPARNALDCALWDIEARISGQSVASMMGIAKLEPLATAVTISLDEPEVMAKAAAKLAYCPVIKVKVDEHNPEDCIKAVRDQAPKARLIVDPNESWSFDLLDKMQNFLADARVALLEQPLAAGADEALKGFSPAVPICADEVFHSADDLDHIADRYQVINIKLDKTGGLTAAIDIMKQARSLNLSIMVGCMVCSSLSLAPAFHLAAQADFVDLDGADWLVHDRNDGMLLDNGILHPPSATFWGGP
>NZ_CP003709.1|WP_011241715.1|132575_132710_-|entericidin-A/B-family-lipoprotein
MRILIHFLMASAVLALAACNTVQGFGQDLSSAGQSMSNSAERNK
>NZ_CP003709.1|WP_012816906.1|133077_134730_-|sensor-histidine-kinase
MKAFFKNSPSKTFHKKQLLTRRLFLLFVSMPTWFRMLVVLSLAQLPPSFVALGAFIASSHQYRLNHQKEAQLIATESARTIDDSVDILAYDVRNIFDEEGSYDFADMGECSLLIQHMQSLGFVPVDYALMDTSGRLLCKSDNFKVNTAVLLPFKPLGANNFYNVDILENEGQLQFSFLGGHYPLSKYLVVGQIGRDSLLKIIERKVVPDGSALFLAQKSHLLPLISPKKPLLKQSHPVVIPTFDNSINLIYDNNLPPFRKVDLLFVLLPVLIWFMTASIGWVVVHYMLLRPLRRTQRAIVDYGKTGEIQKIKPASIGAAREIRQVSKAFYHVAVRLAAHERALRNALQHQKMLTREVHHRVKNNLQVVSSLLSIHSRRAETAKEKSAYATIQRRVNALAIVQRQYYNELDKGQGLDLSLLIKELVNGLQTSLQTFEKNFQIETEIDQVFVPLEKAMPIAFILVEIVDFSLAVDPLLPITIILHRHSAEFENTPDHAGLEIRAEALKQLSSRKGNEVIRRIISAFGRQLGGKSVEKEEDGYYYYDIDILPD
>NZ_CP003709.1|WP_011241034.1|134756_134969_-|hypothetical-protein
MNGSMTAHNHKRPVSQELPASSGNAAHADESAKQAEDRKNAIGFALRNVYQQTVEEAVPDDLLALLAKLN
>NZ_CP003709.1|WP_023593050.1|135313_136834_-|DEAD/DEAH-box-helicase
MSDKDYRLFLVRYFMSFADLGLSKELLQAVAELGYEEPTPVQAAAIPSVLMMRDLIAVAQTGTGKTASFVLPMIDILAHGRCRARMPRSLILEPTRELAAQVAENFEKYGKYHKLSMSLLIGGVPMAEQQAALEKGVDVLIATPGRLLDLFERGKILLSSCEMLVIDEADRMLDMGFIPDIETICTKLPTSRQTLLFSATMPPAIKKLADRFLSNPKQIEISRPATANTLIDQRLIEVSPRSKKKKLCDMLRAEKDHTAIIFCNRKTTVRQLATTLEQQGFSVGQIHGDMSQPERGSELERFKNGQISVLVASDIAARGLDVKGISHVFNFDVPTHPDDYIHRIGRTGRGGASGEALTFVTPADEEAITAIEKLMGVEIPRLGNRKKNAYPSKSEETVSPKQAKPAQEKSATPSPRKAPRKAEIPKKLPEDRLDSVESDFPKNQAPRNTASRPVSKARTQERALRPENLRRVKPVALETAIDWNGPIPPFLNYSVPKTTARNAKKD
>NZ_CP003709.1|WP_011241032.1|136961_137387_-|hypothetical-protein
MPPRHFPHSGVMEIHLNVRNANGRNQRPLPPPPPPPDSPYNAPPPPPEAVWHEKKGPKCVSPEDIGAAAVSEKDSVDLMLKGGSRIRAHLEHCPALDFYSGFYVHAGRDGQICAKRDPVYARWGGECLINRFRVVEGVFKH
>NZ_CP003709.1|WP_011241031.1|137718_139242_+|glucose-6-phosphate-isomerase
MARIANKAAIDAAWKQVSACSEKTLKQLFEEDSNRLSGLVVETAKLRFDFSKNHLDSQKLTAFKKLLEACDFDARRKALFAGEKINITEDRAVEHMAERGQGAPASVARAKEYHARMRTLIEAIDAGAFGEVKHLLHIGIGGSALGPKLLIDALTRESGRYDVAVVSNVDGQALEEVFKKFNPHKTLIAVASKTFTTAETMLNAESAMEWMKKHGVEDPQGRMIALTANPAKASEMGIDDTRILPFAESIGGRYSLWSSIGFPAALALGWEGFQQLLEGGAAMDRHFLEAAPEKNAPILAAFADQYYSAVRGAQTHGIFAYDERLQLLPFYLQQLEMESNGKRVDLDGNLIDHPSAFITWGGVGTDAQHAVFQLLHQGTRLVPIEFIAAIKADDTLNPVHHKTLLTNAFAQGAALMSGRDNKDPARSYPGDRPSTTILMEELRPAQLGALIAFYEHRTFTNGVLLGINSFDQFGVELGKEMAHAIADHPENSDFDPSTKALIAAALK
>NZ_CP003709.1|WP_023593051.1|139404_140751_+|glutathione-disulfide-reductase
MTDYDFDLFVIGAGSGGVRASRIAASHGASVAIAEEYRIGGTCVIRGCVPKKMLYYAADFAADLKKAQRFGWTLPEKKFDWSTLRDVVLSDVTRLEGLYTQTLDNNHIAHYKEHAVIEGANQIRLASGKKITARYILVAVGAEPAKLDIPGAEYAVTSNEMFLLPSLPKRALVVGGGYIANEFAGILNSFGVETTIATHGDRILRGYDEEIAARLVEIGQGHGIDYRFNADIARIDKGSSGHLTTHFKDGSQIESDLVLFAIGRVAKSRDLGLDKADVKTNDRGAILVDEENRTSCPSIYAVGDVTDRVQLTPVAIREGQAFADRVFGHKAASVDYDTIPTAVFSHPPLASAGLTEEEAKKRYKNIKIYKSNFRPMRNALIDSPDRALYKMVVEGDSDKVLGLHLIGQDSPEIIQLAAVAIKAGLTKQAFNDTVALHPSSAEELVLMR
>NZ_CP003709.1|WP_011241029.1|141217_143176_+|potassium-transporter-Kup
MSNDTSPGTSSVDSKSSDPSYGVPGHSHSDKDLLKLSLGAIGIVFGDIGTSPLYALKECFKGHHQLPVDDFHIYGLVSLIFWTMGLVVTVKYVMFIMKADNKGEGGSMSLLSLIIRGANPKLSRWLIVLGVFATALFYGDSMITPAMSVLSAVEGLTVIEPSFDSWVPPVSVVILIGLFCIQARGTESVGRLFGPIMLVYFATLAILGAFNIITRSPAILLALNPYYAIHFFASDPLQGFWALGSVVLSVTGAEALYADMGHFGRQPISLGWYWVVFPALTLNYLGQCALLSADHEAIANPFYFLAPDFLRVPLIILATFAAVIASQAVITGAFSVTQQAIQLGYIPRLRVNHTSASTVGQIYIPSVNWVLMFMVMVLIAMFKNSTNLANAYGIAVTGTMFITSCMMGVLVHRVWHWKAWQSIPLVSFFLLIDGAFFLSNVTKIPEGGWFPLLVGFVVFTMLMTWSRGRHLMAERMRQVAMPIQLFIRSAAASAVRIPGTAIFLTPEDDGVPHALLHNLKHNKILHERVILLTVKIEDVPYVDPHYRASMSSLEDGFYRLIVRYGFMEEPDVPLALNKIEQSGPMLRMDDTSFFISRQTLIPSTHTSMAIWREKLFAWMLRNSESATEFFKLPSNRVVELGSQIELVGSNGK
>NZ_CP003709.1|WP_025420117.1|143432_143759_+|hypothetical-protein
MQLKFIHLAASGKRPIPLETNLRAKIHGFFSGQGNQNPYRNHQIVAIISLSGIFGLVFTLVCLKRLSLKADQKILGFSSLIAQNSFFIQKLDKAGLHSRAKNPKLDFS
>NZ_CP003709.1|WP_023593052.1|144105_145095_-|carbon-nitrogen-hydrolase-family-protein
MSCHRVAVIQAGTSLFDTEKTLDRMEALCCQAAEQNVELAVFPEAYIGGYPKGLDFGARMGTRTEAGREDFLRYWKAAIDVPGKETARIGSFAAKMKAYLVVGVIERSEATLYCTALFFAPDGTLIGKHRKLMPTATERLVWGQGDGSTIEILDTAVGKLGAAICWENYMPALRQVMYAGGVNIWCAPTVDQREIWQVSMRHIAYEGRLFVLSACQYMTRADAPADYDCIQGNDPETELIAGGSVIIDPMGNILAGPLYGQEGVLVADIDLSDTIKARYDLDVSGHYGRPDIFEIKVDRQSHQVITDQFSRDQATEKKSVSDSEISQLD

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Crispr_ID: NZ_CP003709_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP003709_2

1254477-1254746

Orphan

I-F

Consensus_repeat	Method
TTTCTAAGCTGCCTGTGCGGCAGTGAACT	PILER-CR
AGTTCACTGCCGCACAGGCAGCTTAGAAA	CRT
GTTCACTGCCGCACAGGCAGCTTAGAAA	CRISPRCasFinder

4 spacers

The CRISPR arrays of NZ_CP003709_2

>merge|NZ_CP003709|2|1254477-1254746|PILER-CR,CRT,CRISPRCasFinder
AGTTCACTGCCGCACAGGCAGCTTAGAAAGAACAGAAGGATTTTTGCCCGGGACAAAATTTTGTTCACTGCCGCACAGGCAGCTTAGAAATACCCCAGCTTTGCGCTTTAGCGTTGCGGTAAGTTCACTGCCGCACAGGCAGCTTAGAAAAGAAACTCCAAGAAGAGATCGCAACCGAGCGAGTTCACTGCCGCACAGGCAGCTTAGAAAGATTAAAAAGACACGATATGCGATGTGGCCTAGTTCACTGCCGCACAGGCAGCATCAAAT

>NZ_CP003709|2|2|1254477-1254686|PILER-CR
AGTTCACTGCCGCACAGGCAGCTTAGAAA	GAACAGAAGGATTTTTGCCCGGGACAAAATTT
TGTTCACTGCCGCACAGGCAGCTTAGAAA	TACCCCAGCTTTGCGCTTTAGCGTTGCGGTA
AGTTCACTGCCGCACAGGCAGCTTAGAAA	AGAAACTCCAAGAAGAGATCGCAACCGAGCG
AGTTCACTGCCGCACAGGCAGCTTAGAAA

>NZ_CP003709|2|2|1254477-1254746|CRT
AGTTCACTGCCGCACAGGCAGCTTAGAAA	GAACAGAAGGATTTTTGCCCGGGACAAAATTT
TGTTCACTGCCGCACAGGCAGCTTAGAAA	TACCCCAGCTTTGCGCTTTAGCGTTGCGGTA
AGTTCACTGCCGCACAGGCAGCTTAGAAA	AGAAACTCCAAGAAGAGATCGCAACCGAGCG
AGTTCACTGCCGCACAGGCAGCTTAGAAA	GATTAAAAAGACACGATATGCGATGTGGCCT
AGTTCACTGCCGCACAGGCAGCATCAAAT

>NZ_CP003709|2|2|1254478-1254746|CRISPRCasFinder
GTTCACTGCCGCACAGGCAGCTTAGAAA	GAACAGAAGGATTTTTGCCCGGGACAAAATTTT
GTTCACTGCCGCACAGGCAGCTTAGAAA	TACCCCAGCTTTGCGCTTTAGCGTTGCGGTAA
GTTCACTGCCGCACAGGCAGCTTAGAAA	AGAAACTCCAAGAAGAGATCGCAACCGAGCGA
GTTCACTGCCGCACAGGCAGCTTAGAAA	GATTAAAAAGACACGATATGCGATGTGGCCTA
GTTCACTGCCGCACAGGCAGCATCAAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP003709.1\|WP_011240090.1\|1257678_1257966_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP003709.1\|WP_023593481.1\|1260610_1261525_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176161
NZ_CP003709.1\|WP_011240085.1\|1266074_1266512_-\|Rrf2-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224870
NZ_CP003709.1\|WP_023593476.1\|1244567_1245935_-\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP003709.1\|WP_023593475.1\|1243605_1244430_-\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP003709.1\|WP_011240086.1\|1264370_1266008_-\|hydroxylamine-reductase	unknown	unknown	gnl\|CDD\|235391
NZ_CP003709.1\|WP_012817482.1\|1249494_1250289_+\|phosphatase-PAP2-family-protein	unknown	unknown	gnl\|CDD\|239491
NZ_CP003709.1\|WP_023593480.1\|1259704_1260478_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|183716
NZ_CP003709.1\|WP_014500669.1\|1255342_1255816_+\|Cys-tRNA(Pro)-deacylase	unknown	unknown	gnl\|CDD\|237976
NZ_CP003709.1\|WP_012817481.1\|1247066_1247885_-\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP003709.1\|WP_011240093.1\|1253121_1254081_+\|S1/P1-Nuclease	unknown	unknown	gnl\|CDD\|367008
NZ_CP003709.1\|WP_023593478.1\|1255828_1257412_+\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|223510
NZ_CP003709.1\|WP_023593479.1\|1258199_1259549_-\|replication-associated-recombination-protein-A	unknown	unknown	gnl\|CDD\|237355
NZ_CP003709.1\|WP_023593483.1\|1263043_1264210_-\|Na+/H+-antiporter-NhaA	unknown	unknown	gnl\|CDD\|377746
NZ_CP003709.1\|WP_025420184.1\|1246113_1246836_-\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP003709.1\|WP_023593474.1\|1242814_1243423_-\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_CP003709.1\|WP_011240096.1\|1248392_1249337_+\|metallophosphoesterase	unknown	unknown	gnl\|CDD\|277347
NZ_CP003709.1\|WP_023593477.1\|1250611_1253104_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP003709.1\|WP_023593482.1\|1261815_1262883_-\|dihydroorotate-dehydrogenase	unknown	unknown	gnl\|CDD\|239204
NZ_CP003709.1\|WP_023593473.1\|1242005_1242707_-\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807

Protein	Function_ID	Function_description	E-value
NZ_CP003709.1\|WP_023593481.1\|1260610_1261525_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176161	cd08472, PBP2_CrgA_like_3, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 3. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of 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.	5.91817e-100
NZ_CP003709.1\|WP_011240085.1\|1266074_1266512_-\|Rrf2-family-transcriptional-regulator	gnl\|CDD\|224870	COG1959, COG1959, Predicted transcriptional regulator [Transcription].	7.93449e-32
NZ_CP003709.1\|WP_023593476.1\|1244567_1245935_-\|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.	7.00107e-41
NZ_CP003709.1\|WP_023593475.1\|1243605_1244430_-\|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.	8.58577e-44
NZ_CP003709.1\|WP_011240086.1\|1264370_1266008_-\|hydroxylamine-reductase	gnl\|CDD\|235391	PRK05290, PRK05290, hybrid cluster protein; Provisional.	0
NZ_CP003709.1\|WP_012817482.1\|1249494_1250289_+\|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.	1.57004e-94
NZ_CP003709.1\|WP_023593480.1\|1259704_1260478_-\|SDR-family-oxidoreductase	gnl\|CDD\|183716	PRK12744, PRK12744, SDR family oxidoreductase.	4.79536e-167
NZ_CP003709.1\|WP_014500669.1\|1255342_1255816_+\|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.	1.70667e-68
NZ_CP003709.1\|WP_012817481.1\|1247066_1247885_-\|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.	2.43204e-39
NZ_CP003709.1\|WP_011240093.1\|1253121_1254081_+\|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_CP003709.1\|WP_023593478.1\|1255828_1257412_+\|ATP-binding-protein	gnl\|CDD\|223510	COG0433, COG0433, HerA helicase [Replication, recombination, and repair].	1.85395e-14
NZ_CP003709.1\|WP_023593479.1\|1258199_1259549_-\|replication-associated-recombination-protein-A	gnl\|CDD\|237355	PRK13342, PRK13342, recombination factor protein RarA; Reviewed.	0
NZ_CP003709.1\|WP_023593483.1\|1263043_1264210_-\|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.	8.34741e-138
NZ_CP003709.1\|WP_025420184.1\|1246113_1246836_-\|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.	2.48589e-43
NZ_CP003709.1\|WP_023593474.1\|1242814_1243423_-\|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.	1.82196e-40
NZ_CP003709.1\|WP_011240096.1\|1248392_1249337_+\|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_CP003709.1\|WP_023593477.1\|1250611_1253104_+\|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.	3.49713e-39
NZ_CP003709.1\|WP_023593482.1\|1261815_1262883_-\|dihydroorotate-dehydrogenase	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.	2.13495e-101
NZ_CP003709.1\|WP_023593473.1\|1242005_1242707_-\|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.	6.54334e-43

>NZ_CP003709.1|WP_011240093.1|1253121_1254081_+|S1/P1-Nuclease
MTDNRVSKLFKKRLTKLAIVAAMLTLPQPLYAWGMEGHEAIAALAWKYMTPTTRKKVNAILAMDHDRLTEPDFMSRATWADKWRSAGHGETEPWHFVDIEIDNPNLVTACAAASNRSNPMKNGGAQPCVVSQLDRFERELSSKQTSDQDRVLALKYVLHFVGDLHQPLHAADHDDRGGNCVKVSINNARSLNLHSYWDTYVVKEIDPDPQHLADSLKKEISPEDKKSWVLGDSKQWAMESFQLGKRYAYSFNPPAGCDATRPPIPLSAGYDSAARKVAASQLKKAGVRLAYILNHRLRSIPLSYFLQAQKQDAAANNNG
>NZ_CP003709.1|WP_023593477.1|1250611_1253104_+|TonB-dependent-receptor
MKNLLSAKTKSFLSFKQSRLNWVILYSSLWVSGAMAQNTVPPQPATDDTSSQQHAVTDNSANHPAKNDGAIVVTGRSYADGVTRRAFGGGLMIKEDSPKSKSTLTRDYIEKQTPGLNPMQLIALLPGVNSSDSDPMGLTGGHTSVRGMNESSMGYILEGFPLNDVGSHAVYPQEIVDSENLSTIQVAQGSADLDSPTVSAAGGVVNMHMIDPAKKMGGRANFTYGSYNTFRGFARFDTGEIGNSGTRAYFSFSDTHEDLWRGPGTEKKLHGEMKVVKEWGKDNKASLLVIGNNLDNINMPSVNMASWQKYGKGIMGGPVSGIANTVYSSVYTGNTKANTTYYKLHPNPFTNIYVSAPVHLNLGHKMTLTETPYFLYSNGNGGGAYWQDMNKMSYGSQTMSGTVDGQNYGQTLLYEPSITKTYRSGSTTKWTWTSGINRLMIGYWFEYSSQRQTAPYSLLNDDGSPRDKWGGGSNVILANGEKAEYRDNSTRTFIHTPFIGDTISLLNDKLTIDGGVKISIINRQGRNYLPDTSTGKNINQTYREVLPSGSIRYKINDEHQVFFSVATNYRIPMNTSLFDSGSYVAGTGYSNQAVKDLKPETSISEEFGWRYHGKLINTSLTYFHYDFHNRLFSQTVIDPNNPTSYYSRSINGGNQTTNGVDFEIGTRAIYNIRPYVSAEYIDARNRSNLAASAAGVSAILPTKGKFAPQTPRYQVGFGLDYDNGHIFGNFSLKYVGSQYSTFMNDEQVPSYVRMNIGGGYRFKSWGGLKSPTIRFNLSNITNKHYLNYASGLQTNAQYAKALDGQMVKGSAPTYSIASPFSAMFSISSGF
>NZ_CP003709.1|WP_012817482.1|1249494_1250289_+|phosphatase-PAP2-family-protein
MIKVPRFICMIALTSGVLASGLSQSVSAHTEKSEPSSTYHFHSDPLLYLAPPPTSGSPLQAHDDQTFNSTRQLKGSTRWALATQDADLHLASVLKDYACAAGMNLDIAQLPHLANLIKRALRTEYDDIGRAKNNWNRKRPFVDTDQPICTEKDREGLGKQGSYPSGHTTIGWSVALILAELIPDHAANILQRGQIFGTSRIVCGAHWFSDVQAGYIMASGEIAALHGDADFRRDMELARKELEKARTSAHTPDDLLCKIEQSAR
>NZ_CP003709.1|WP_011240096.1|1248392_1249337_+|metallophosphoesterase
MISFNRRRFLSLSAGATFAAATAPRLYAGVPNRPPLRSHQSFTFVFITDTHLQPELNGAEGCHEAFLKARQFPADFAIHGGDHVFDALGVNANRATMLADLYKRTADDLRLPVYNTMGNHDCFGIYKESGAQPTDPFYGKKYFQDNFGQTYYSFDHKGVHFVILDSIGITEDRSYEGRVDAEQFNWLSRDLAAQPVGTPIIVSTHIPIMNAIDYASVPLNKMKHHSLSVINAADILELFDHYNVIGVFQGHTHVVERVEWHGVPYITGGSVCGNWWHGTRYGTPEGFMVVKVEKGKVIPHYESYGFHTIDPRNT
>NZ_CP003709.1|WP_012817481.1|1247066_1247885_-|sel1-repeat-family-protein
MKKILLLWVVVFSFVASRTQMQIRKELESFQSKYAALIKKPVQEKSSGRRLVVEKDSIPPDPPLRYQILLHPQEAAKKGDAEAQMFLGKSYLAGRSDVPKNSKQAVFWFQKSANQGYAEGEVELADAYHNGTGVGRDEAKAAFWYQKAAAQNNIEAEARLGFVYHQGRGLSKDEKMSFFWFDKAAHQGSLLAQTMVGVAYYYGSGVPQDKGRAFMWYQKAAHQGDVMAQYLLGMAYLKGEGVARSKRDGVFWLQRAAAQGDYNAFKILQRLQ
>NZ_CP003709.1|WP_025420184.1|1246113_1246836_-|sel1-repeat-family-protein
MKRILVLTAALLPVFAQPAFARIGVGRVVKMTRDGLKSPLQKAAERGDAKAQYALGNAYSKGQDVSKSDEQAVSWYQKSASQGYAPAQAALGYAYSSGLGVPHDDQQAVSFFQKAANQGNASAQYNLGMAYSNGQGVPHSDEEAASWYQRAAHQGYAPAEFNLGAAYYHGEGVVQDYGQAVFWYQKAAEQGDAKAQTALGVAYITGRGVTKSRDNALIWIQKAADQGDVTAQKILPALKK
>NZ_CP003709.1|WP_023593476.1|1244567_1245935_-|sel1-repeat-family-protein
MKKILLFSVLLSSSVTPSMAAPEKPHVVESDQIPLKQAAEAGDIAAQSNLGLAYYVGAAVPKDAAMAAFWFEKAASKGFSAAQYNLAGLYATGEGVAQSDKQAAFWYEKAAEQGIDEAEYNLALAYEQGKGVEQNYERALFWLKKAADQNFFKAETHLGLAYQAGIMLPRDDKKAVALFMKADRQAYYAEAQMALGNAYRRGAGVKQDDQKAVSYYQKAADQGDGEALTALGVFYMTGRGVPQNYERGLDCFRKAADKDVSAAEDNLGNAYRHGYGVPKDDEKAVYWYQKAADKGDAEAEYNLGLAYRKGEGISQDDAKAAFWYKKAADQGHVKAQLNMGFAYYQARGVAQDYARGIFLYRKAAEQGDSKAEYNLAIAYYNGVGEPKDLAQSIYWFQRAASHGEMSAQYNLGAFYMRGEGVPKDRNEAIFWLEKAAAQGDVEAQSTLHNLDHYPL
>NZ_CP003709.1|WP_023593475.1|1243605_1244430_-|sel1-repeat-family-protein
MRKFLFFTAVFLPFVANPVQAQTAKSTKVVAGKTALSLEQKARAGNPKAQTDLGTAYYNGQGMAQDYKQAISWYQKAANQGYPLAQYYLGNACLQGIGLTQSDEQAVSWYQKAANQGLAEAQYSLAIAYYTGRGVTQNYGQASFWFQRSANQGFVPAQFYLGVMYRNGAGIPEDDDRALFWFHKAADKGYADAQYNLGLIYHEGKVVKKDEKQATFWYQQAANQGLVEAEFNLGIAYLKGQGVQKDKDKATFWLEKAADKGDSHAQDVLEMMNK
>NZ_CP003709.1|WP_023593474.1|1242814_1243423_-|sel1-repeat-family-protein
MKKRIILLGLLLSVGGQIVYSQVRKMPSIFSQKKLYELKQAADQGDAEAEAALGEAFDFGKITPQDYQKAFFWYQKAADQAVAEAQYNLGGLYYKGAGRPKDGEKAVYWYRKAADQGYIDAQRNLALLYAKGELVPQSDEQAVYWYQKAADQGNAEAQRALGSAYALGKGVPRNKEKALFWIGKAADQGDAEAQKLLAMLAR
>NZ_CP003709.1|WP_023593473.1|1242005_1242707_-|sel1-repeat-family-protein
MFFVPLVVLSLSVSPLTMQADKERYDREMISSLEVRAKAGNSLAEEVLGEAYAHGRGRPQDDEKAVYWYQKAADKGMKESQYNLGDAYLHGRGVGVDYEKAAFWYRKAADQNFIQAQYNLGLLYVKGQGLPKSDEHAAFWWQKAAEQGEAKAKFNLGVFYHNGRAVPKNDARAIFWMEQAAHQGLVEAQMLLAMAYASGQGAPKDKEKAVFWYRKAAEQGNAAAQKALQALSY
>NZ_CP003709.1|WP_014500669.1|1255342_1255816_+|Cys-tRNA(Pro)-deacylase
MTKKTRGTAFLEKAGIAFTVHPYDYDPKASAAGLQAAEALQQPAEIVYKTLMTEVDGKPVCVVVQVNHEVSMKKLAAAAGGKSANMIKPVDAERMTGYHVGGISPFGQKKRVPVIFDESAFQAEKIFINGGQRGVLVALAPEDARRAVDGKIASVAN
>NZ_CP003709.1|WP_023593478.1|1255828_1257412_+|ATP-binding-protein
MAINKERDEPFSYLWQILLFLTDLPLQKRTSLAQRCRMTVMIDMGKDPKGQVVPMDLEELLATRLLVQGNSGSGKSHLLRRMLEKSARFVQQIVIDPEGDFVTLAERFPHVAVEAAAYNESEIRVLAQRIREHRVSVVLNLEGLDVDNQMKCAAWFLATLFDAPRDHWYPAIVVVDEAQIFAPAQAGEVSDEARRLSLAAMTNLMCRGRKRGLAGVIATQRLAKLAKNVAAEASNFLMGRTFLDIDMARAADLLGMDRRQAESIRDLERGHFLALGPALCRRPVAVKIGEVETKSRTGGFKLMPLPDSKNSNPEDLLFSEPEEPALPLASPEPPPPPSSSQLMELLQKEKEEEAKIAEAEAAENPVDNSQKEALIDALLSSIVEEEENAYRQANLLYPEFTIGCRMHGLSTPPLDLTAFTKRLTIAKAGLSNDDLQDELWQPALKAASILEDDIQAVFLFLAKTAKENAPCPDDEMIARIYGTRSAGRARRLIGYMENQGIIAIRTDFGGRRSITLPALGWTTSTAA
>NZ_CP003709.1|WP_011240090.1|1257678_1257966_-|hypothetical-protein
MAAEIMDHMNYMVDDPDQLSVKPANALEHIFLYEDSGAVIAEIPVVFKGESGRVLYDISHNRLVHSDIKHDQLKEMVSSKMPDFKEELLEYFREN
>NZ_CP003709.1|WP_023593479.1|1258199_1259549_-|replication-associated-recombination-protein-A
MDDLFNSVEPLVFTENEKQPLPENRPLADILRPKHLSDVIGQVHVTGENGIIGRMVAAGRLSSLILWGPPGTGKTSIAQLLAESVGMRFEMVSAIFSGVADLKKIFLKAEHHRQQGRQTLLFIDEIHRFNKGQQDSFLPYIENGTFVLVGATTENPSFALNAALLSRAQVVTLNRLDEEALGLLLERAETVSGQLLPVDEDARKALIASADGDGRFLLNQAEILLAMNLTKSLSVPELAQILQKRMAIYDKDRDGHYNLISALHKSVRGSDPQAALYYLSRMLVAGEDPLYLLRRLTRMANEEVGLADPRAMEQCIAAKETYQLLGSPEGELAIAQACVYVATAPKSNAIYKAYNQAMALARESGSVLPPPNILNAPTEMMKQQGYGEGYHYDHDMPDAFSGDNYWPENLPPVTLYQPNIRGYEKHITERLAFWEHLRQERKKGKPSGK
>NZ_CP003709.1|WP_023593480.1|1259704_1260478_-|SDR-family-oxidoreductase
MTTHNITGKKILIAGGSKNLGGLLARDLAKHGAKAIAIHYNKPSSLPETEKTMAAVKQAGADVYVFQGDLTTAGAVEKLFTDAKMAMGGIDIAVNTVGKVLKKPIVDISEEEYDSMSAVNAKSAFFFIKEAGKNLNDNGKIVTLVTSLLGAFTPFYASYAGLKAPVEHFTRAAAKEFGDRGISVNAIGPGPMDTDFFYGQESEEAQAYHKTAAALSKFSKTGLTDIEDIVPYIRFLVSEGWWMTGQTILVNGGYTTK
>NZ_CP003709.1|WP_023593481.1|1260610_1261525_+|LysR-family-transcriptional-regulator
MDRIDLFRVFVRVVETASFTQAAASLGMPRSSVSAAIAELEDHVGTRLLHRTTRKVSSTLDGTAFYERCLHLIDEIEETESLFRPKDAKPKGKLRIDLPGRIARRIVAPALPDFLQKYPDIDIEMGVSDRVVDLVESGTDCALRIGKLQDSTLIARPMGQLSLINVASPAYLEKYGIPLTPDDLCCHWVVNYASPTTARIAPWEWVEKGQIKTIFPKSRITVNNAESYIACSLAGLGLIQIPAYDVRNDIQQQKLVEIMDHYQAEAMLMALVYPHRQHLSRRIQVFAYWLESLLKNTMTVKREG
>NZ_CP003709.1|WP_023593482.1|1261815_1262883_-|dihydroorotate-dehydrogenase
MKTEIPYYNPELSYEDNYKEGPFGYFADIVEKPDPSFAVSVKKPVSFLGCSVDLPFGIPAGPLLNSRYIKAAFHAGFDLCVYKTVRTQEHKSHPLPNVLAIHPEGVLSADCEAVLADTRYNQPLSITNSFGVPSFNPDIWQPDMAEAVKAASDHQVMIGSFQGTRGKGKIEEDYALAARMVAETGAPVLEANLSCPNEGVNSLLCFDAPLVQKIVEAIKVAVPDRPLLIKTAYFKDNAKLDDLVSRVGHLVSGFSTINTLSARPLDEKGQAALSPSRPEGGVCGDAIRWAGLEMVQRLAAFREEKSLDYAIVGVGGVNKPEHYKAYIEAGANAVMTATGSMWNPHLAEETKKFLA
>NZ_CP003709.1|WP_023593483.1|1263043_1264210_-|Na+/H+-antiporter-NhaA
MRFSIRRFFSAASGGAIILLLSALLGLLLSNSFLSESYFKVLHLKMPFSALDDAPNLAEFISIAPMSLFFFVVIAEIKEEIISGHLASFRRVILPLISALGGMMIPACLYGLITSGHLEVSRGWAIPIATDAAFTLPIILALGRHVSEGARVWLMALAIFDDLLGIVVIALFYASHLNGYALFAAGLITAVMIGLNKKSVQNLWVYASAGVVLWWALLVSGLHPTIAGVITGLALPSVADQPEKASPLERGKQIIAPWVIWLILPLFGFVSMGMSLSAMSFHVLLAPVPLGVALGLFLGKPIGVFGATIMATRLKIATLPKGTSLQMLFGLSLLCGIGFTISLFIAELAFSGSDFLVPAKYGILMGSLLSALAGWLWLRFLKFPAKGV
>NZ_CP003709.1|WP_011240086.1|1264370_1266008_-|hydroxylamine-reductase
MLCFQCEQTHSGTGCVIRGVCTKTPEVAAIQDLMIFASAGLSYVAKKLPDSCEAERKEAASLVIQALFSTVTNVNFDADVLTKALYHLVDFRDALKAKLPEDVELPLAATLDFSRDRETLVKQGESYGIASRQKTLGIDVTGLQELLTYGMKGMAAYAHHAAVLDYRDPDVDNFLLEGMAALTDHSLDIQALLAVVMRCGEASYKTLALLDKANTSSFGHPVPTNVKMGPSKGKAILVSGHDLLDMKELLEQTKDTGIKVYTHGEMLPAHGYPELNKYPHLAGHYGGAWMLQRQEFINFPGPIVMTTNCLMEPRKEYAGRVFTRDLVGWPGLTHLPDRDFSKVIEAALESEGFTEDQESRSHIAGFGHHTVLDSADAVVSAIKKGDIKHFMLVGGCDGIKSGRHYFTDIAEKAPKDWVILTLGCGKFRVTDLDLGKIGDLPRLLDMGQCNDSYSAIRVALALAEAFDTDVNSLPLSLVLSWYEQKAVCVLLALLHLGVKGIRLGPTLPAFITPNMLKILVDNFDIKPIGNSAEEDLQEILAAKAA
>NZ_CP003709.1|WP_011240085.1|1266074_1266512_-|Rrf2-family-transcriptional-regulator
MLSISQSTGYAVLALSAIHAESEKLTMARDIAEKANIPRPYLTKILGRLQEAGLITAKRGQNGGLRLNRPPETISLLEIVKAIDGKDWGCGCFLGLPGCSNEHPCPMHSFWLKTRPVIVKQLENMTLDKAKHFTEAGWKFRSEEG

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Crispr_ID: NZ_CP003709_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP003709_3

1807530-1807858

Orphan

I-F

Consensus_repeat	Method
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CRISPRCasFinder
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CRT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	PILER-CR

5 spacers

The CRISPR arrays of NZ_CP003709_3

>merge|NZ_CP003709|3|1807530-1807858|CRISPRCasFinder,CRT,PILER-CR
AGTACAATCTACCTATGCGGCAGTGAACGCGTGTCTTCGATAATAACTCTGCGACGATCATTTCTAAGCTGCCTGTGCGGCAGTGAACCGACAGTCGGGCCGGATACCATGATCCGAGTATTTCTAAGCTGCCTGTGCGGCAGTGAACAAGGTAATATTATCGTCACTGACAAGCAAGGTTTTCTAAGCTGCCTGTGCGGCAGTGAACTCTTGTGACATTGCTGGCTTTGCTTGAGCATTTTTCTAAGCTGCCTGTGCGGCAGTGAACGCCAATTTTTCAGCATAACGTCGCAGCTCAACATTTCTAAGCTGCCTGTGCGGCAGTGAAC

>NZ_CP003709|3|3|1807530-1807858|CRISPRCasFinder
AGTACAATCTACCTATGCGGCAGTGAAC	GCGTGTCTTCGATAATAACTCTGCGACGATCA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CGACAGTCGGGCCGGATACCATGATCCGAGTA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	AAGGTAATATTATCGTCACTGACAAGCAAGGT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	TCTTGTGACATTGCTGGCTTTGCTTGAGCATT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	GCCAATTTTTCAGCATAACGTCGCAGCTCAACA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC

>NZ_CP003709|3|3|1807530-1807858|CRT
AGTACAATCTACCTATGCGGCAGTGAAC	GCGTGTCTTCGATAATAACTCTGCGACGATCA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CGACAGTCGGGCCGGATACCATGATCCGAGTA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	AAGGTAATATTATCGTCACTGACAAGCAAGGT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	TCTTGTGACATTGCTGGCTTTGCTTGAGCATT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	GCCAATTTTTCAGCATAACGTCGCAGCTCAACA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC

>NZ_CP003709|3|3|1807590-1807858|PILER-CR
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	CGACAGTCGGGCCGGATACCATGATCCGAGTA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	AAGGTAATATTATCGTCACTGACAAGCAAGGT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	TCTTGTGACATTGCTGGCTTTGCTTGAGCATT
TTTCTAAGCTGCCTGTGCGGCAGTGAAC	GCCAATTTTTCAGCATAACGTCGCAGCTCAACA
TTTCTAAGCTGCCTGTGCGGCAGTGAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP003709.1\|WP_011241316.1\|1814511_1815804_-\|histidinol-dehydrogenase	unknown	unknown	gnl\|CDD\|234853
NZ_CP003709.1\|WP_023593704.1\|1806504_1807209_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP003709.1\|WP_023593702.1\|1803378_1803702_-\|YnfA-family-protein	unknown	unknown	gnl\|CDD\|235016
NZ_CP003709.1\|WP_023593700.1\|1799763_1802187_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP003709.1\|WP_023593701.1\|1802199_1803372_+\|phosphotransferase	unknown	unknown	gnl\|CDD\|225213
NZ_CP003709.1\|WP_011241317.1\|1814038_1814512_-\|transcription-antitermination-factor-NusB	unknown	unknown	gnl\|CDD\|234686
NZ_CP003709.1\|WP_023593707.1\|1816550_1816856_-\|BolA-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|376601
NZ_CP003709.1\|WP_011241315.1\|1815793_1816462_-\|ATP-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234971
NZ_CP003709.1\|WP_014501138.1\|1796514_1798830_+\|formate-C-acetyltransferase	unknown	unknown	gnl\|CDD\|153087
NZ_CP003709.1\|WP_011241312.1\|1819410_1819977_-\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380063
NZ_CP003709.1\|WP_011241324.1\|1804962_1805946_-\|DUF481-domain-containing-protein	unknown	unknown	gnl\|CDD\|377313
NZ_CP003709.1\|WP_011241318.1\|1813054_1814020_-\|thiamine-phosphate-kinase	unknown	unknown	gnl\|CDD\|273589
NZ_CP003709.1\|WP_023593708.1\|1817217_1819395_-\|squalene--hopene-cyclase	unknown	unknown	gnl\|CDD\|239222
NZ_CP003709.1\|WP_023593705.1\|1810281_1811670_-\|glutamate--cysteine-ligase	unknown	unknown	gnl\|CDD\|130503
NZ_CP003709.1\|WP_011241331.1\|1794320_1795751_-\|cytochrome-ubiquinol-oxidase-subunit-I	unknown	unknown	gnl\|CDD\|376587
NZ_CP003709.1\|WP_023593703.1\|1804171_1804738_+\|nicotinamide-mononucleotide-transporter	unknown	unknown	gnl\|CDD\|377432
NZ_CP003709.1\|WP_011241323.1\|1805970_1806438_-\|RNA-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|239643
NZ_CP003709.1\|WP_011241329.1\|1798813_1799605_+\|pyruvate-formate-lyase-activating-protein	unknown	unknown	gnl\|CDD\|131546
NZ_CP003709.1\|WP_023593706.1\|1811976_1812747_-\|16S-rRNA-(uracil(1498)-N(3))-methyltransferase	unknown	unknown	gnl\|CDD\|236959
NZ_CP003709.1\|WP_014501143.1\|1808332_1809859_-\|amidophosphoribosyltransferase	unknown	unknown	gnl\|CDD\|236384

Protein	Function_ID	Function_description	E-value
NZ_CP003709.1\|WP_011241316.1\|1814511_1815804_-\|histidinol-dehydrogenase	gnl\|CDD\|234853	PRK00877, hisD, bifunctional histidinal dehydrogenase/ histidinol dehydrogenase; Reviewed.	0
NZ_CP003709.1\|WP_023593704.1\|1806504_1807209_-\|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.	1.09676e-28
NZ_CP003709.1\|WP_023593702.1\|1803378_1803702_-\|YnfA-family-protein	gnl\|CDD\|235016	PRK02237, PRK02237, YnfA family protein.	1.55802e-38
NZ_CP003709.1\|WP_023593700.1\|1799763_1802187_+\|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.	8.21011e-37
NZ_CP003709.1\|WP_023593701.1\|1802199_1803372_+\|phosphotransferase	gnl\|CDD\|225213	COG2334, COG2334, Putative homoserine kinase type II (protein kinase fold) [General function prediction only].	5.2285e-17
NZ_CP003709.1\|WP_011241317.1\|1814038_1814512_-\|transcription-antitermination-factor-NusB	gnl\|CDD\|234686	PRK00202, nusB, transcription antitermination factor NusB.	1.68678e-43
NZ_CP003709.1\|WP_023593707.1\|1816550_1816856_-\|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.	3.25339e-28
NZ_CP003709.1\|WP_011241315.1\|1815793_1816462_-\|ATP-phosphoribosyltransferase	gnl\|CDD\|234971	PRK01686, hisG, ATP phosphoribosyltransferase catalytic subunit; Reviewed.	1.37428e-112
NZ_CP003709.1\|WP_014501138.1\|1796514_1798830_+\|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_CP003709.1\|WP_011241312.1\|1819410_1819977_-\|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_CP003709.1\|WP_011241324.1\|1804962_1805946_-\|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_CP003709.1\|WP_011241318.1\|1813054_1814020_-\|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_CP003709.1\|WP_023593708.1\|1817217_1819395_-\|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_CP003709.1\|WP_023593705.1\|1810281_1811670_-\|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_CP003709.1\|WP_011241331.1\|1794320_1795751_-\|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_CP003709.1\|WP_023593703.1\|1804171_1804738_+\|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.	1.57318e-43
NZ_CP003709.1\|WP_011241323.1\|1805970_1806438_-\|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_CP003709.1\|WP_011241329.1\|1798813_1799605_+\|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_CP003709.1\|WP_023593706.1\|1811976_1812747_-\|16S-rRNA-(uracil(1498)-N(3))-methyltransferase	gnl\|CDD\|236959	PRK11713, PRK11713, 16S ribosomal RNA methyltransferase RsmE; Provisional.	6.89003e-76
NZ_CP003709.1\|WP_014501143.1\|1808332_1809859_-\|amidophosphoribosyltransferase	gnl\|CDD\|236384	PRK09123, PRK09123, amidophosphoribosyltransferase; Provisional.	0

>NZ_CP003709.1|WP_023593704.1|1806504_1807209_-|SDR-family-oxidoreductase
MTHRPLSDQIALVTGASRGIGAATAKALAEAGAHVILVARTATDLDKVEEQIYQKGGSATIAPLDITNSGSCHHLAAAISGRWPALDIMVFAAARYEAQPSIAAASPALQQMLAVNALATQDLLSRFDPLIQESRSAHIIGLTLPKSQAPYPYNGSYYASKMAMEAILLSYGAENVERDTIKVALAELEAVATEGRKRAFPDEKADLLRSPDEVAKAIVTMIVQDYANGWQGKL
>NZ_CP003709.1|WP_011241323.1|1805970_1806438_-|RNA-pyrophosphohydrolase
MDNLEYRSGVGIMLLNKDNLVFAACRNDMKEEAWQMPQGGLEAKETPEVGVLRELEEETGIPPRMVAIISHTKEWLTYDFPADLQASFFKNKYRGQRQLWFLARYLGRDEDININTDKPEFRAWKWVEPKQLPDLIVAFKKPLYEKILSEFSASL
>NZ_CP003709.1|WP_011241324.1|1804962_1805946_-|DUF481-domain-containing-protein
MQSRTISPWLLWRISQGAVLLSLVPVSEVWAEEPPKLIQEMVTKALALDDPKTVKSIVLIAKKTVPDSAAEIDAMVADYNTKVEAREAEKKRKELRRVADSGMFENWTGSVELGGAKMTGNTRQTAIYGAVALERNGINWTHTVKARTDFQRTYGTTSAERFTASYQPHYKFDERLYMYGLALYERDMFLGYRTRITGGSGIGYKVFDQPNLSLAVEGGPAYRHTIFIDSSRPNGRRIRDTAAMRGSFTTKWVVSPLLTVSEDSSIFFESKDITASSTTSLETKLIGNLSTKLSFSVYYEKDVSASKNPVDTTSRITFAYALGKKKK
>NZ_CP003709.1|WP_023593703.1|1804171_1804738_+|nicotinamide-mononucleotide-transporter
MSVLEWLAVLTSLFGIVFSTRQIRICWLFYGISSLLYGKIFFSIKLYADCLLQIFFFFSSIYGWFHWHHYQKADKMTVITASHKSLLRDIAMAAALSAIFGFYLKNYTDDAFPWLDAILSCYSIVAQFWAARLYKANWFLWIVIDFCYTALFCYRGLWLTAGLYSVFMVMAVIGLKKWQNKNPAVACD
>NZ_CP003709.1|WP_023593702.1|1803378_1803702_-|YnfA-family-protein
MLALLYIPAALAEITGCFSFWAWIRLHKSPLWLLPGIASLLLFAWLLTFSPAENAGKAYAVYGGIYIIMSLLWSWKVEATPPDHWDLIGAAFCLVGASIILWMPRSL
>NZ_CP003709.1|WP_023593701.1|1802199_1803372_+|phosphotransferase
MAIKDDGMTEAAHKAVHQFGVSGYQTERDWPYLTILEINAVLASFSGQGKAIKILSHSRRPYSAAALFETDQKQTFFIKRHHHKIRNKTELLKEHLFARHLAQKSFPISTPMMADHNQTVIEKEPWIYEIHPQAQGVDLYQDVMSWEPFFNRDHAYEAGRMLALFHQAAQGFDESPRHHALLVSAGDTLLHDDFIKALSEWITAQPELLKQLEGKNWQQDITENILPFHHQLQPLIADITPLWGHGDWHSSNLMWTGSNPKAKVSCVLDLGMADYSSAMFDLATAIERNVIAWLDMDSRQDIVIYDQLFALLRGYHHIKPLSQTDKQLLSAFMPLLHVEYALSEIVYFGALLQDKTSADIAYYDYLLGHSRWFSGQEGQQLLRKIIHFEA
>NZ_CP003709.1|WP_023593700.1|1799763_1802187_+|TonB-dependent-receptor
MTYQDMTASEWRKYYQHFLVTSVFLAGISGVFPLHPAHAETQESPKSSDKTSSKNDAIIVTGRPVFKTANGFSVNDIGGGLIQKETETRSVSHISTDFIQKQAPTANAFDLVAMLPGANVTSSDPLGFSTQTNITIRGLSGDAIGYVLEGMPLNDVAYYTGYPTQFADSENYQQIGLAQGSADLDSPVLNAAGGVMNLNFRKPADKMGGYADFSYGSYNTNRQFLRFDMGEIGHSGVKGFVSYSHARTDNWRGAGYDEKQHVDFKFLKEWGQDSHVSLLGTWNKGITSYYPQVDKQSWKENGISGSNNLASHYNVNNDAAGSDYWRLYRAPEEIFYLAAPIDVRLASNLKLKVTPYGQWDRGNVPAGSTLNNSGLWNGTEAIAGTINLPNATDGTATVRSNYTQRSARAGVNASATWSLKNHDLTLGYWFDYSADKEQNSFTSVDSNGYASNLWADRHSTLIKMPDGSPLLGTNNRTHTYVNAVYLGDHMTFLQNRLTFDIGFKEVIMTRHGYNYLPGSQHKANFSTSEPLPRLGLRYQIDSKSHVFFSASTNFRTADETALYNSYDPTSGDIIVNGNKNLKNEYSVSEELGYRYSDALVTGSLTLFNYNFSNRQLQTVIVQNGSHIQSTINTGNQISRGVDFEIGLAPWHHISPYLSGEYLYTRQTSDLTVGDDLLPTKGKRAVRSPAFQGSLGVTYDDHHFFGMASVKYTGSQYGSFMNDEKIPAYVTGNISVGYRFTQEAFLKHPEIRLNFINIGNNHYLSGIASPTANAQDTVGRNGTVISGSAPQYYIGGGFAVLASLSSAF
>NZ_CP003709.1|WP_011241329.1|1798813_1799605_+|pyruvate-formate-lyase-activating-protein
MALIIKRPAVTSLVEEAGCDNTLKGRIHSTEIGGAVDGPGVRFVLFLAGCALRCQYCHNPDSWFLKNGRAVTLAEMMEEVASYADFLKRAGGGITISGGEPLVQPEFTGALLKAAKYLGLHTAIDTAGFLGAQADDALLSNTDLVLLDIKAFNDKRYKALTGVELQPTLAFAKRLAALKKPVWLRYVLVPGLTDNFNEIANLADFAATLGNIERVDVLPFHKMGEYKWKASGLAYKLGDTQPPSPALVEDVRGIFRDNGLNLS
>NZ_CP003709.1|WP_014501138.1|1796514_1798830_+|formate-C-acetyltransferase
MTISTLEKPDIAAGQASNAETQRMDSALDPWRGFKGRKWQREIDTRDFILSNVTSYTGNSDFLAGITPKTTKLWEKLQVSLEAERKTQGGVLDVDTSTVSDITAHAPGFIEKDLEVVVGLQTDAPLKRAIMPFGGYRMIKKGLEAYGFKEDESLSKIFPALRKTHNDGVFDVYTPEIMACRRSGIITGLPDAYGRGRIIGDYRRVALYGVDCLIEDKKEQGKRLERNPFDEETIKLREEVAEQIKALHELAAMAKSYGYDISQPAVTAQQAVQWTYFAYLAAVKEANGAAMSLGRVSTFLDIYIERDLKEGRITEAEAQELVDQFVMKLRIVRFLRTPEYDQLFSGDPTWVTESLGGMAIDGRTLVTKSSFRFLHTLENLGPAPEPNLTVLWSENLPKGFKDYCAKISIDTSSIQYENDDLMRSYWGDDYGIACCVSAMRIGKQMQFFGARANLAKTLLYAINGGRDEKSGVQVAPAFAPVTGDILDYEDVKSRMVQMMEWLASVYINALNAIHFMHDKYMYERVEMALHDLEILRTMACGIAGLSVAADSLSAIKHAKVKIIRDERGLATDFEIEGDYPAYGNNDDRADEIAIWLVETFMNMLRKQTTYRRSVPTQSILTITSNVVYGKKTGNTPDGRRAGEPFAPGANPMHGRDLKGPVASMASVAKLPYAHAQDGISNTFTIVPNALGMNKEERIDNLIGLLSGYFGAGAHHMNVNVFDRNTLLDAVDHPEKYPQLTIRVSGYAVNFVKLTREQQMDVIHRTFHGLDN
>NZ_CP003709.1|WP_011241331.1|1794320_1795751_-|cytochrome-ubiquinol-oxidase-subunit-I
MVPDATALMLARIQFAFTVGFHIIFPAFSIGLAAYLAVLEGLWLKTGRNVYLHLFKYWIKIFALVFGMGVVSGLVMAYEFGTNWSLFSQKAGAITGPLLGYEVLTAFFLEAGFLGIMLFGLGRVGKGLHFLATCLVSIGTLISMTWILASNSWMQTPAGYSIDPKTGHFLPKSWFEVIFNPSFPYRLVHMGMAAFICVAFVVGATAAFHMLRDRKNGKPVTEPVRVMFSMALWMAAIAAPFQLLAGDMHGLNTLKYQPAKIAAMEGDWESEGPASEILFGIPNMKTERTDYAIKIPYAGSLILTHSLNGKVPGLKDYPRDQRPPSPILFFSFRIMVGLGGLMILLGLWSLFLRFRGQLYNNKALQWATLLMAPSGFIALLCGWVTTEVGRQPYTVYGLLRTSDSVSPVMLPSMIFSMTAFVIVYFFVFGAGMLILFRMLSHQPSSHEKGADPENPLQNSHAKGATQLAQDLSGKRS
>NZ_CP003709.1|WP_014501143.1|1808332_1809859_-|amidophosphoribosyltransferase
MSPSLSSELFSDSISTLTTTTESLDNGASDDTLHEECGVFGIWGADTAAAVVALGLHALQHRGQEAAGITSWDGKNFHSRRAVGHVAGNFDRDDAIRSLPGSCAIGHVRYATTGASTLCNVQPLYAELVSGGFAIAHNGNISNAETLRHQLVRHGSIFQSTSDTETIIHLVATSSYRSLLDRFIDALKQVEGAYSLVCLTPEGMIACRDPLGIRPLVLGKVGETFVVASETVALDIIGGTYIRQVEPGELIIISEKGLQSIHPFKKQKPRPCIFEHVYFSRPDSLIGSTSVYSVRKSIGIELARENPVDADMVIPVPDSGTPAAIGYAQQSSLPFELGIIRSHYVGRTFIQPGDQVRHLGVKLKHNANRALIKGKKLVLVDDSIVRGTTSVKIIRMLRDAGAKEIHLRIASPPTRHSCFYGVDTPERAKLLAAKMTVEQMAEYIGADSLAFISMDGLYRAVGEEGRNDAQPQYCDACFTGAYPTPLTDLGELGASEQLVRLSEQVAIA
>NZ_CP003709.1|WP_023593705.1|1810281_1811670_-|glutamate--cysteine-ligase
MSTRQTSSSQNHPIESRDDLLRIFQAGEKPKAQWRVGTEHEKLVYKKQNHQAPSYEEKGGICDLLQGFTRFGWQPIYENDKIIGLSGDDGAISLEPAGQFELSGAPRSTIHESYDEICRHIQQTQEVGDELGLGFLGLGLWPDKKRSDLPLMPKGRYKIMTEYMPKVGKLGLDMMLRTCTIQSNIDYGSEADMVKKFRVSLALQPLATALFANSPFLEGRPNGFSSYRSHIWTDTDPHRTGILPFVFDDDFGYERYIDYMLSVPMYFVYRDGRYIDASGQDFRAFLRGELPALPNEKPILSDWVDHLSTAFPEVRLKSYLEMRGADGASAMMSPALSAFWISILYDSELLDTASDIIKSWSMDDYRNLRNEVPKKGLKTLIGGRQSLLDLGRQLWPLMNDALKRRAILNDKGQDESRYLAPIGKILESGQSLSDRLLARYHQTGNLDFIYQECDWAQPHILS
>NZ_CP003709.1|WP_023593706.1|1811976_1812747_-|16S-rRNA-(uracil(1498)-N(3))-methyltransferase
MVAEPAWPVNTLPRLYVEEKLSLEAVITPDRAQAHYLLSVMRFKIGSQLVLFDNLTGEWLGEVIEAGRKHLQLKITHHLNEKESIPDLWLLTAPIKKGRIDWIYEKACELGVARITPVITQRTIVDRVNLERLQAHIVEAAEQCGRTSLSEVTEACSLKSLLAEWPEDRALFFADETGGEPMIEAISKRRMAAAILVGPEGGFTDQERDMINAVKQAVPVSLGPRILRADTAAIAATALWMAAAGDWQKQPRQANL
>NZ_CP003709.1|WP_011241318.1|1813054_1814020_-|thiamine-phosphate-kinase
MSGREQAFITALRQIAGDPAARNLSDDAAVLPRPSGDLVLSHDIIVENVHYFPSDPPETVAQKLVGVNLSDLAAKGAKPIGALMGYSLGPDYKWDQAFLKGLESVCHQYNLPLLGGDTVAVPRHTGHFSAMTVIGLAPSCGVPDRRAAKEGDELWVTSPIGDAGFGLNLLKQKKNINHSAQEKLVQAYRSPEPRLKEGIWLAPHVHAMADISDGLLIDAERIANASGLAVRIRLDRVPLSSEAISCFGDTKSTRLQAVTAGDDYQLIMACAANKRQELLKLSKEKQFDLYRVGQLTAGSGLSLFYGAEPIKQPDRLGYLHG
>NZ_CP003709.1|WP_011241317.1|1814038_1814512_-|transcription-antitermination-factor-NusB
MAQTQKRPHKNARSAARLAAVQALYQREMEKTPLNILLDEFHQYRLGATIEDATYTKAEPSFFDDIVRGVGTRCEEIDRVISENLSERWSLDRLDRPMRQILRAGTYELLARPDVPTATVISEYIDVANAFYDRQEKNFVNGLLDTVAKKLRSSNNA
>NZ_CP003709.1|WP_011241316.1|1814511_1815804_-|histidinol-dehydrogenase
MLLKLDSRKADFQADFTRLVDERRESEGDVSRDVSAIIADVKKRGDVAIAELTQKFDRHDLNKGGWQLTQEEIKKACDSLPSELMDALKLAATRIRYCHENQLPESSEMTDAAGVRMGVRWQAVEAAGLYVPGGRAAYCSSVLMNAVPAKVAGVKRLVMVTPTPDGFVNPAVIAAAVISEVDEIWKIGGAQAVAALALGTEKIKPVDVVVGPGNAWVAEAKRQLYGQVGIDMVAGPSEIVVVADKDNDPEWLAADLLSQAEHDPTSQSILISDSEDLIEKTIEAVGRRLEKLETQKVARESWDKHGATILVQSLDEAPALVDRLAPEHLELAVADPDALFANVHHSGSVFLGRYTPEAIGDYVGGPNHVLPTGRRARFSSGLSVIDFMKRTTYLNCSQEALSKIGPAAVTLAKAEGLPAHAESVISRLNK
>NZ_CP003709.1|WP_011241315.1|1815793_1816462_-|ATP-phosphoribosyltransferase
MTKPLVFAIPKGRILKEALPMLEAAGIIPEPAFLDKESRLLRFKTNRPDIEIIRVRAFDVATFVAHGAAQMGIVGSDVIEEFSYPELYAPVDLDIGHCRLSIAEPKRLAKDDDPREWSHVRVATKYPHLTHRHFEARGVQAECIKLNGAMEIAPALGLAGRIVDLVSSGRTLEENGLVEVEKIMPISARLIVNRAAFKMRAGDIAPLVENFRRLVGVADNVA
>NZ_CP003709.1|WP_023593707.1|1816550_1816856_-|BolA-family-transcriptional-regulator
MNMTSPSDNNEGPVTRLMRERLEAAFSPETLVIEDDSNKHAGHAGHPHRSESHFTVTLVSQAFENESRISRERMVHKALSDLLPDRIHALRLKLDTPLRQE
>NZ_CP003709.1|WP_023593708.1|1817217_1819395_-|squalene--hopene-cyclase
MGIDRMNSLSRLLMKKIFGAEKTSYKPASDTIIGTDTLRRPNRRPEPTAKVDKTIFKTMGNSLNNTLVSACDWLIGQQKPDGHWVGAVESNASMEAEWCLALWFLGLEDHPLRPRLGNALLEMQREDGSWGVYFGAGNGDINATVEAYAALRSLGYSADNPVLKKAAAWIAEKGGLKNIRVFTRYWLALIGEWPWEKTPNLPPEIIWFPDNFVFSIYNFAQWARATMVPIAILSARRPSRPLRPQDRLDELFPEGRARFDYELPKKEGINLWSQFFRTTDRGLHWVQSNLLKRNSLREAAIRHVLEWIIRHQDADGGWGGIQPPWVYGLMALHGEGYQLYHPVMAKALSALDDPGWRHDRGESSWIQATNSPVWDTMLALMALKDAKAEDRFTPEMDKAADWLLARQVKVKGDWSIKLPDVEPGGWAFEYANDRYPDTDDTAVALIALSSYRDKEEWQKKGVEDAITRGVNWLIAMQSECGGWGAFDKDNNRSILSKIPFCDFGESIDPPSVDVTAHVLEAFGTLGLSRDMPVIQKAIDYVRSEQEAEGAWFGRWGVNYIYGTGAVLPALAAIGEDMTQPYITKACDWLVAHQQEDGGWGESCSSYMEIDSIGKGPTTPSQTAWALMGLIAANRPEDYEAIAKGCHYLIDRQEQDGSWKEEEFTGTGFPGYGVGQTIKLDDPALSKRLLQGAELSRAFMLRYDFYRQFFPIMALSRAERLIDLNN
>NZ_CP003709.1|WP_011241312.1|1819410_1819977_-|TetR/AcrR-family-transcriptional-regulator
MARPRTIDRERVLKSAEQLVQRAGATAMTLEAVAKEAGITKGGLQYCFGSKDDLITALIDRWFAAFDCEVKEYSQSDDSPAGEARAYVQASSQIDDATSARMVGMLVTLLQSPNHLKKIQAWYARWMEKNLGQSEEARHIRTMLFAAEGAFFLRSLGFIKMSESEWATVFDDIKKLVPSAQAGRASFK

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP003709_1	1.2\|131659\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131659-131690	32	NC_013784	Zymomonas mobilis subsp. mobilis ZM4 plasmid pZZM401, complete sequence	18200-18231	4	0.875
NZ_CP003709_1	1.2\|131659\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131659-131690	32	NZ_CP023686	Zymomonas mobilis subsp. mobilis strain ZM4 substr. 8b plasmid pZM41, complete sequence	817-848	4	0.875
NZ_CP003709_1	1.2\|131659\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131659-131690	32	NZ_CP023680	Zymomonas mobilis subsp. mobilis strain ZM4 substr. 2032 plasmid pZM36, complete sequence	817-848	4	0.875
NZ_CP003709_1	1.2\|131659\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131659-131690	32	NZ_CP003712	Zymomonas mobilis subsp. mobilis NRRL B-12526 plasmid pZM1252603, complete sequence	28495-28526	4	0.875
NZ_CP003709_1	1.2\|131659\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131659-131690	32	NZ_CP003718	Zymomonas mobilis subsp. mobilis str. CP4 = NRRL B-14023 plasmid pZM1402303, complete sequence	18200-18231	4	0.875
NZ_CP003709_1	1.2\|131659\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131659-131690	32	CP036464	Zymomonas mobilis strain ZM4* plasmid pZM36o, complete sequence	817-848	4	0.875
NZ_CP003709_1	1.2\|131659\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131659-131690	32	CP036460	Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821 strain ZM4 plasmid pER79ap36, complete sequence	817-848	4	0.875
NZ_CP003709_3	3.3\|1807678\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	1807678-1807709	32	HQ317387	Sulfitobacter phage phiCB2047-B genomic sequence	46059-46090	6	0.812
NZ_CP003709_1	1.7\|131960\|33\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131960-131992	33	MK415408	CrAssphage GF1-2_000079F, complete genome	42652-42684	7	0.788
NZ_CP003709_1	1.7\|131960\|33\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131960-131992	33	MW067001	CrAssphage sp. C0521BW15, complete genome	36380-36412	7	0.788
NZ_CP003709_1	1.7\|131960\|33\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131960-131992	33	MW067000	CrAssphage sp. C0521BD4, complete genome	36380-36412	7	0.788
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	AP018278	Calothrix sp. NIES-4101 plasmid plasmid5 DNA, complete genome	31242-31272	7	0.774
NZ_CP003709_3	3.4\|1807738\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	1807738-1807769	32	NZ_CP049808	Acinetobacter pittii strain A1254 plasmid pA1254_2, complete sequence	31674-31705	7	0.781
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_AP018205	Leptolyngbya boryana NIES-2135 plasmid plasmid2 DNA, complete genome	56641-56671	8	0.742
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_AP014640	Leptolyngbya boryana IAM M-101 plasmid pLBX	448755-448785	8	0.742
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	AP018278	Calothrix sp. NIES-4101 plasmid plasmid5 DNA, complete genome	31241-31272	8	0.75
NZ_CP003709_3	3.4\|1807738\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	1807738-1807769	32	NZ_CP040856	Lactobacillus johnsonii strain G2A plasmid unnamed2, complete sequence	54491-54522	8	0.75
NZ_CP003709_1	1.7\|131960\|33\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131960-131992	33	MK800154	Enterococcus phage Entf1, complete genome	37521-37553	9	0.727
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NC_004041	Rhizobium etli CFN 42 plasmid p42d, complete sequence	208348-208378	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013633	Rhizobium sp. N324 plasmid pRspN324c, complete sequence	281867-281897	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013555	Rhizobium phaseoli strain N931 plasmid pRphaN931c, complete sequence	298599-298629	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP020950	Rhizobium sp. CIAT894 plasmid pRheCIAT894c, complete sequence	311621-311651	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013587	Rhizobium phaseoli strain N161 plasmid pRphaN161b, complete sequence	242082-242112	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013550	Rhizobium phaseoli strain R611 plasmid pRetR611c, complete sequence	275430-275460	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013530	Rhizobium phaseoli strain R723 plasmid pRphaR723c, complete sequence	267827-267857	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013535	Rhizobium phaseoli strain R650 plasmid pRphaR650c, complete sequence	275430-275460	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013540	Rhizobium phaseoli strain R630 plasmid pRphaR630c, complete sequence	287326-287356	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013566	Rhizobium phaseoli strain N831 plasmid pRphaN831c, complete sequence	298312-298342	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013583	Rhizobium phaseoli strain N261 plasmid pRphaN261c, complete sequence	267827-267857	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP021125	Rhizobium sp. Kim5 plasmid pRetKim5a, complete sequence	274743-274773	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP054022	Rhizobium sp. JKLM12A2 plasmid pPR12A201, complete sequence	1010981-1011011	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NC_010996	Rhizobium etli CIAT 652 plasmid pB, complete sequence	274731-274761	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	CP006880	Rhizobium gallicum bv. gallicum R602 plasmid pRgalR602c, complete sequence	1221098-1221128	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP017243	Rhizobium etli 8C-3 plasmid pRsp8C3b, complete sequence	279494-279524	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP020898	Rhizobium phaseoli Brasil 5 strain Bra5 plasmid pRetBra5b, complete sequence	268735-268765	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	NZ_CP013635	Rhizobium sp. N324 plasmid pRspN324e, complete sequence	165420-165450	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	CP047389	Agrobacterium sp. CGMCC 11546 plasmid pA	113488-113518	9	0.71
NZ_CP003709_2	2.3\|1254627\|31\|NZ_CP003709\|PILER-CR,CRT	1254627-1254657	31	CP047390	Agrobacterium sp. CGMCC 11546 plasmid pB	155821-155851	9	0.71
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NC_004041	Rhizobium etli CFN 42 plasmid p42d, complete sequence	208347-208378	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP020898	Rhizobium phaseoli Brasil 5 strain Bra5 plasmid pRetBra5b, complete sequence	268735-268766	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013633	Rhizobium sp. N324 plasmid pRspN324c, complete sequence	281866-281897	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013635	Rhizobium sp. N324 plasmid pRspN324e, complete sequence	165420-165451	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013555	Rhizobium phaseoli strain N931 plasmid pRphaN931c, complete sequence	298598-298629	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP020950	Rhizobium sp. CIAT894 plasmid pRheCIAT894c, complete sequence	311620-311651	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	CP047389	Agrobacterium sp. CGMCC 11546 plasmid pA	113488-113519	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	CP047390	Agrobacterium sp. CGMCC 11546 plasmid pB	155821-155852	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013587	Rhizobium phaseoli strain N161 plasmid pRphaN161b, complete sequence	242081-242112	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013550	Rhizobium phaseoli strain R611 plasmid pRetR611c, complete sequence	275429-275460	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013530	Rhizobium phaseoli strain R723 plasmid pRphaR723c, complete sequence	267826-267857	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013535	Rhizobium phaseoli strain R650 plasmid pRphaR650c, complete sequence	275429-275460	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013540	Rhizobium phaseoli strain R630 plasmid pRphaR630c, complete sequence	287325-287356	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013566	Rhizobium phaseoli strain N831 plasmid pRphaN831c, complete sequence	298311-298342	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP013583	Rhizobium phaseoli strain N261 plasmid pRphaN261c, complete sequence	267826-267857	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP021125	Rhizobium sp. Kim5 plasmid pRetKim5a, complete sequence	274742-274773	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP054022	Rhizobium sp. JKLM12A2 plasmid pPR12A201, complete sequence	1010980-1011011	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NC_010996	Rhizobium etli CIAT 652 plasmid pB, complete sequence	274730-274761	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	CP006880	Rhizobium gallicum bv. gallicum R602 plasmid pRgalR602c, complete sequence	1221097-1221128	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_CP017243	Rhizobium etli 8C-3 plasmid pRsp8C3b, complete sequence	279493-279524	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_AP014640	Leptolyngbya boryana IAM M-101 plasmid pLBX	448755-448786	9	0.719
NZ_CP003709_2	2.7\|1254627\|32\|NZ_CP003709\|CRISPRCasFinder	1254627-1254658	32	NZ_AP018205	Leptolyngbya boryana NIES-2135 plasmid plasmid2 DNA, complete genome	56640-56671	9	0.719
NZ_CP003709_1	1.4\|131779\|32\|NZ_CP003709\|CRISPRCasFinder,CRT,PILER-CR	131779-131810	32	KC595511	Bacillus phage Basilisk, complete genome	4616-4647	11	0.656

1. spacer 1.2|131659|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to NC_013784 (Zymomonas mobilis subsp. mobilis ZM4 plasmid pZZM401, complete sequence) position: , mismatch: 4, identity: 0.875

gtatgctgatgattgccccatgcccacaatcc	CRISPR spacer
gtatgctgatgattgccccatacccaagaacc	Protospacer
*********************.**** .* **

2. spacer 1.2|131659|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP023686 (Zymomonas mobilis subsp. mobilis strain ZM4 substr. 8b plasmid pZM41, complete sequence) position: , mismatch: 4, identity: 0.875

gtatgctgatgattgccccatgcccacaatcc	CRISPR spacer
gtatgctgatgattgccccatacccaagaacc	Protospacer
*********************.**** .* **

3. spacer 1.2|131659|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP023680 (Zymomonas mobilis subsp. mobilis strain ZM4 substr. 2032 plasmid pZM36, complete sequence) position: , mismatch: 4, identity: 0.875

gtatgctgatgattgccccatgcccacaatcc	CRISPR spacer
gtatgctgatgattgccccatacccaagaacc	Protospacer
*********************.**** .* **

4. spacer 1.2|131659|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP003712 (Zymomonas mobilis subsp. mobilis NRRL B-12526 plasmid pZM1252603, complete sequence) position: , mismatch: 4, identity: 0.875

gtatgctgatgattgccccatgcccacaatcc	CRISPR spacer
gtatgctgatgattgccccatacccaagaacc	Protospacer
*********************.**** .* **

5. spacer 1.2|131659|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP003718 (Zymomonas mobilis subsp. mobilis str. CP4 = NRRL B-14023 plasmid pZM1402303, complete sequence) position: , mismatch: 4, identity: 0.875

gtatgctgatgattgccccatgcccacaatcc	CRISPR spacer
gtatgctgatgattgccccatacccaagaacc	Protospacer
*********************.**** .* **

6. spacer 1.2|131659|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to CP036464 (Zymomonas mobilis strain ZM4* plasmid pZM36o, complete sequence) position: , mismatch: 4, identity: 0.875

gtatgctgatgattgccccatgcccacaatcc	CRISPR spacer
gtatgctgatgattgccccatacccaagaacc	Protospacer
*********************.**** .* **

7. spacer 1.2|131659|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to CP036460 (Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821 strain ZM4 plasmid pER79ap36, complete sequence) position: , mismatch: 4, identity: 0.875

gtatgctgatgattgccccatgcccacaatcc	CRISPR spacer
gtatgctgatgattgccccatacccaagaacc	Protospacer
*********************.**** .* **

8. spacer 3.3|1807678|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to HQ317387 (Sulfitobacter phage phiCB2047-B genomic sequence) position: , mismatch: 6, identity: 0.812

aaggtaatattatcgtcactgacaagcaaggt	CRISPR spacer
agggtaattttatcctcactgacaagcataga	Protospacer
*.****** ***** ************* .*

9. spacer 1.7|131960|33|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to MK415408 (CrAssphage GF1-2_000079F, complete genome) position: , mismatch: 7, identity: 0.788

agcgttattagattctttaacaatttcaaatta	CRISPR spacer
agtttcattagcttctttaacattttcaaagtt	Protospacer
**. *.***** ********** ******* *

10. spacer 1.7|131960|33|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to MW067001 (CrAssphage sp. C0521BW15, complete genome) position: , mismatch: 7, identity: 0.788

agcgttattagattctttaacaatttcaaatta	CRISPR spacer
agtttcattagcttctttaacattttcaaagtt	Protospacer
**. *.***** ********** ******* *

11. spacer 1.7|131960|33|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to MW067000 (CrAssphage sp. C0521BD4, complete genome) position: , mismatch: 7, identity: 0.788

agcgttattagattctttaacaatttcaaatta	CRISPR spacer
agtttcattagcttctttaacattttcaaagtt	Protospacer
**. *.***** ********** ******* *

12. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to AP018278 (Calothrix sp. NIES-4101 plasmid plasmid5 DNA, complete genome) position: , mismatch: 7, identity: 0.774

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
ctaaactgcaagaagcgatcgcaactgcacg	Protospacer
  ***** ******* *********.* .**

13. spacer 3.4|1807738|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP049808 (Acinetobacter pittii strain A1254 plasmid pA1254_2, complete sequence) position: , mismatch: 7, identity: 0.781

-tcttgtgacattgctggctttgcttgagcatt	CRISPR spacer
aatttataa-attgctggcattgctttagcatt	Protospacer
  .**.*.* ********* ****** ******

14. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_AP018205 (Leptolyngbya boryana NIES-2135 plasmid plasmid2 DNA, complete genome) position: , mismatch: 8, identity: 0.742

agaaactccaagaagagatcgcaa---ccgagcg	CRISPR spacer
ggaaactccaagaacagaacgcaaaatctaa---	Protospacer
.************* *** *****   *..*

15. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_AP014640 (Leptolyngbya boryana IAM M-101 plasmid pLBX) position: , mismatch: 8, identity: 0.742

agaaactccaagaagagatcgcaa---ccgagcg	CRISPR spacer
ggaaactccaagaacagaacgcaaaatctaa---	Protospacer
.************* *** *****   *..*

16. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to AP018278 (Calothrix sp. NIES-4101 plasmid plasmid5 DNA, complete genome) position: , mismatch: 8, identity: 0.75

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
ctaaactgcaagaagcgatcgcaactgcacgt	Protospacer
  ***** ******* *********.* .**

17. spacer 3.4|1807738|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to NZ_CP040856 (Lactobacillus johnsonii strain G2A plasmid unnamed2, complete sequence) position: , mismatch: 8, identity: 0.75

tcttgtgacattgctggctttgcttgagcatt	CRISPR spacer
attggtgaaattgctgcctttgcttgatctgt	Protospacer
 .* **** ******* ********** *  *

18. spacer 1.7|131960|33|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to MK800154 (Enterococcus phage Entf1, complete genome) position: , mismatch: 9, identity: 0.727

agcgttattagattctttaacaatttcaaatta	CRISPR spacer
ttctttattggattctttagcaatttcaacaac	Protospacer
  * *****.*********.*********

19. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NC_004041 (Rhizobium etli CFN 42 plasmid p42d, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

20. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013633 (Rhizobium sp. N324 plasmid pRspN324c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

21. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013555 (Rhizobium phaseoli strain N931 plasmid pRphaN931c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

22. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP020950 (Rhizobium sp. CIAT894 plasmid pRheCIAT894c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

23. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013587 (Rhizobium phaseoli strain N161 plasmid pRphaN161b, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

24. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013550 (Rhizobium phaseoli strain R611 plasmid pRetR611c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

25. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013530 (Rhizobium phaseoli strain R723 plasmid pRphaR723c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

26. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013535 (Rhizobium phaseoli strain R650 plasmid pRphaR650c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

27. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013540 (Rhizobium phaseoli strain R630 plasmid pRphaR630c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

28. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013566 (Rhizobium phaseoli strain N831 plasmid pRphaN831c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

29. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013583 (Rhizobium phaseoli strain N261 plasmid pRphaN261c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

30. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP021125 (Rhizobium sp. Kim5 plasmid pRetKim5a, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

31. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP054022 (Rhizobium sp. JKLM12A2 plasmid pPR12A201, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
ctcgtttccaagaagcgatcgcagccgagca	Protospacer
   . .********* *******.******.

32. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NC_010996 (Rhizobium etli CIAT 652 plasmid pB, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

33. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to CP006880 (Rhizobium gallicum bv. gallicum R602 plasmid pRgalR602c, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcacaaccgagca	Protospacer
   . .********* ****.*********.

34. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP017243 (Rhizobium etli 8C-3 plasmid pRsp8C3b, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

35. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP020898 (Rhizobium phaseoli Brasil 5 strain Bra5 plasmid pRetBra5b, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

36. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to NZ_CP013635 (Rhizobium sp. N324 plasmid pRspN324e, complete sequence) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

37. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to CP047389 (Agrobacterium sp. CGMCC 11546 plasmid pA) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

38. spacer 2.3|1254627|31|NZ_CP003709|PILER-CR,CRT matches to CP047390 (Agrobacterium sp. CGMCC 11546 plasmid pB) position: , mismatch: 9, identity: 0.71

agaaactccaagaagagatcgcaaccgagcg	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagca	Protospacer
   . .********* ******.*******.

39. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NC_004041 (Rhizobium etli CFN 42 plasmid p42d, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

40. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP020898 (Rhizobium phaseoli Brasil 5 strain Bra5 plasmid pRetBra5b, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

41. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013633 (Rhizobium sp. N324 plasmid pRspN324c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

42. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013635 (Rhizobium sp. N324 plasmid pRspN324e, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

43. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013555 (Rhizobium phaseoli strain N931 plasmid pRphaN931c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

44. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP020950 (Rhizobium sp. CIAT894 plasmid pRheCIAT894c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

45. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to CP047389 (Agrobacterium sp. CGMCC 11546 plasmid pA) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

46. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to CP047390 (Agrobacterium sp. CGMCC 11546 plasmid pB) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

47. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013587 (Rhizobium phaseoli strain N161 plasmid pRphaN161b, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

48. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013550 (Rhizobium phaseoli strain R611 plasmid pRetR611c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

49. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013530 (Rhizobium phaseoli strain R723 plasmid pRphaR723c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

50. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013535 (Rhizobium phaseoli strain R650 plasmid pRphaR650c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

51. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013540 (Rhizobium phaseoli strain R630 plasmid pRphaR630c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

52. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013566 (Rhizobium phaseoli strain N831 plasmid pRphaN831c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

53. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP013583 (Rhizobium phaseoli strain N261 plasmid pRphaN261c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

54. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP021125 (Rhizobium sp. Kim5 plasmid pRetKim5a, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

55. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP054022 (Rhizobium sp. JKLM12A2 plasmid pPR12A201, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
ctcgtttccaagaagcgatcgcagccgagcaa	Protospacer
   . .********* *******.******.*

56. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NC_010996 (Rhizobium etli CIAT 652 plasmid pB, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

57. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to CP006880 (Rhizobium gallicum bv. gallicum R602 plasmid pRgalR602c, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcacaaccgagcaa	Protospacer
   . .********* ****.*********.*

58. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_CP017243 (Rhizobium etli 8C-3 plasmid pRsp8C3b, complete sequence) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgcaaccgagcga	CRISPR spacer
cttgtttccaagaagcgatcgcgaccgagcaa	Protospacer
   . .********* ******.*******.*

59. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_AP014640 (Leptolyngbya boryana IAM M-101 plasmid pLBX) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgc--aaccgagcga	CRISPR spacer
ggaaactccaagaacagaacgcaaaatctaat--	Protospacer
.************* *** ***  **.* *..

60. spacer 2.7|1254627|32|NZ_CP003709|CRISPRCasFinder matches to NZ_AP018205 (Leptolyngbya boryana NIES-2135 plasmid plasmid2 DNA, complete genome) position: , mismatch: 9, identity: 0.719

agaaactccaagaagagatcgc--aaccgagcga	CRISPR spacer
ggaaactccaagaacagaacgcaaaatctaat--	Protospacer
.************* *** ***  **.* *..

61. spacer 1.4|131779|32|NZ_CP003709|CRISPRCasFinder,CRT,PILER-CR matches to KC595511 (Bacillus phage Basilisk, complete genome) position: , mismatch: 11, identity: 0.656

ccaatcgattaaagcatcgacaaaagcacgct	CRISPR spacer
gtaatcgattaaatcatctacaaaactttctg	Protospacer
 .*********** **** ****** . . .

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

155100 : 168323

Thermus_phage(12.5%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_011241017.1\|155100_156258_+	DNA-protecting protein DprA	S6BFL3	Thermus_phage	1.3e-28	38.1
WP_023593058.1\|156409_160063_+	type I DNA topoisomerase	A0A1V0SCS0	Indivirus	6.2e-98	36.9
WP_023593059.1\|160471_161230_-	HesA/MoeB/ThiF family protein	A0A1V0SAV8	Catovirus	5.9e-11	27.8
WP_023593060.1\|161226_161667_-	dUTP diphosphatase	A0A2L1IVN2	Streptomyces_phage	2.7e-32	51.0
WP_023593061.1\|161698_162952_-	bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase CoaBC	Q9HH70	Methanothermobacter_phage	3.0e-44	31.8
WP_023593062.1\|162978_164517_-	2-polyprenylphenol 6-hydroxylase	A0A167R6U4	Powai_lake_megavirus	8.0e-07	26.0
WP_023593063.1\|164520_165249_-	ubiquinone/menaquinone biosynthesis methyltransferase	NA	NA	NA	NA
WP_011241010.1\|165558_166371_+	bifunctional DNA-formamidopyrimidine glycosylase/DNA-(apurinic or apyrimidinic site) lyase	G3MA33	Bacillus_virus	1.4e-29	32.4
WP_023593064.1\|166382_168323_-	lytic transglycosylase domain-containing protein	K4NWI2	Pseudomonas_phage	1.7e-09	28.6

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP003712

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_CP003709

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

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection