CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP036299	Planctopirus ephydatiae strain spb1 chromosome, complete genome	3 crisprs	cas3,WYL,csa3,DinG,Cas9_archaeal,cas4,RT	1	2	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP036299_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP036299_1

2103013-2103227

Orphan

Consensus_repeat	Method
TACCAGACCTGCTATCGCGATGT	CRISPRCasFinder

4 spacers

The CRISPR arrays of NZ_CP036299_1

>merge|NZ_CP036299|1|2103013-2103227|CRISPRCasFinder
CGCGAGACCTGCTATCGTGAAGAGTGTTACACCGTGTGCAAGCCTGTTTATCAGACTTGCTACCGGGAAGTGACCTGCACGATCAAGAAGCCGGTTTACCAGACCTGCTACCGCGACGTGACCTGCACAATCAAGAAGCCGGTCTACCAGACCTGCTATCGCGATGTCTGCTACACCAAGTGCCGTCCTGTGTTCCAGACCTGCTATCGCGATGT

>NZ_CP036299|1|1|2103013-2103227|CRISPRCasFinder
CGCGAGACCTGCTATCGTGAAGA	GTGTTACACCGTGTGCAAGCCTGTT
TATCAGACTTGCTACCGGGAAGT	GACCTGCACGATCAAGAAGCCGGTT
TACCAGACCTGCTACCGCGACGT	GACCTGCACAATCAAGAAGCCGGTC
TACCAGACCTGCTATCGCGATGT	CTGCTACACCAAGTGCCGTCCTGTG
TTCCAGACCTGCTATCGCGATGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP036299.1\|WP_145298130.1\|2086050_2086428_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP036299.1\|WP_145298142.1\|2091212_2093819_-\|DUF1592-domain-containing-protein	unknown	unknown	gnl\|CDD\|377886
NZ_CP036299.1\|WP_145298136.1\|2088335_2088974_+\|histidine-phosphatase-family-protein	unknown	unknown	gnl\|CDD\|366010
NZ_CP036299.1\|WP_145298178.1\|2111350_2111572_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP036299.1\|WP_145298172.1\|2109414_2110482_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133030
NZ_CP036299.1\|WP_145304423.1\|2094103_2095120_+\|SUMF1/EgtB/PvdO-family-nonheme-iron-enzyme	unknown	unknown	gnl\|CDD\|335469
NZ_CP036299.1\|WP_145298168.1\|2108664_2109411_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|372616
NZ_CP036299.1\|WP_145298139.1\|2089206_2091126_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379080
NZ_CP036299.1\|WP_145298148.1\|2097234_2098314_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	unknown	unknown	gnl\|CDD\|176204
NZ_CP036299.1\|WP_145298187.1\|2114681_2114918_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP036299.1\|WP_145298190.1\|2115329_2116241_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP036299.1\|WP_145298165.1\|2106724_2108995_-\|phospholipid-carrier-dependent-glycosyltransferase	unknown	unknown	gnl\|CDD\|224720
NZ_CP036299.1\|WP_145298175.1\|2110442_2111039_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379312
NZ_CP036299.1\|WP_145298184.1\|2113309_2114485_-\|lipid-A-disaccharide-synthase	unknown	unknown	gnl\|CDD\|234580
NZ_CP036299.1\|WP_145298145.1\|2095116_2097081_+\|cadmium-translocating-P-type-ATPase	unknown	unknown	gnl\|CDD\|319844
NZ_CP036299.1\|WP_145298181.1\|2111769_2112147_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP036299.1\|WP_145298154.1\|2100783_2102265_-\|sulfatase-like-hydrolase/transferase	unknown	unknown	gnl\|CDD\|293763
NZ_CP036299.1\|WP_145298151.1\|2098404_2100444_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224055
NZ_CP036299.1\|WP_145298133.1\|2086322_2087729_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223533
NZ_CP036299.1\|WP_145298162.1\|2104519_2106262_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP036299.1\|WP_145298172.1\|2109414_2110482_-\|glycosyltransferase	gnl\|CDD\|133030	cd04187, DPM1_like_bac, Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.	5.08308e-80
NZ_CP036299.1\|WP_145298142.1\|2091212_2093819_-\|DUF1592-domain-containing-protein	gnl\|CDD\|377886	pfam07631, PSD4, Protein of unknown function (DUF1592). A region of similarity shared by several Rhodopirellula baltica cytochrome-like proteins that are predicted to be secreted. These proteins also match pfam07627, pfam07626, and pfam07624.	5.16497e-56
NZ_CP036299.1\|WP_145298136.1\|2088335_2088974_+\|histidine-phosphatase-family-protein	gnl\|CDD\|366010	pfam00300, His_Phos_1, Histidine phosphatase superfamily (branch 1). The histidine phosphatase superfamily is so named because catalysis centers on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a 'phosphate pocket' and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the 'phosphate pocket' and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members.	7.23323e-65
NZ_CP036299.1\|WP_145304423.1\|2094103_2095120_+\|SUMF1/EgtB/PvdO-family-nonheme-iron-enzyme	gnl\|CDD\|335469	pfam03781, FGE-sulfatase, Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.	4.05269e-85
NZ_CP036299.1\|WP_145298168.1\|2108664_2109411_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|372616	pfam13489, Methyltransf_23, Methyltransferase domain. This family appears to be a methyltransferase domain.	1.47856e-20
NZ_CP036299.1\|WP_145298139.1\|2089206_2091126_-\|hypothetical-protein	gnl\|CDD\|379080	pfam13231, PMT_2, Dolichyl-phosphate-mannose-protein mannosyltransferase. This family contains members that are not captured by pfam02366.	4.69548e-08
NZ_CP036299.1\|WP_145298148.1\|2097234_2098314_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	gnl\|CDD\|176204	cd08242, MDR_like, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.	7.27376e-121
NZ_CP036299.1\|WP_145298165.1\|2106724_2108995_-\|phospholipid-carrier-dependent-glycosyltransferase	gnl\|CDD\|224720	COG1807, ArnT, 4-amino-4-deoxy-L-arabinose transferase and related glycosyltransferases of PMT family [Cell envelope biogenesis, outer membrane].	8.79431e-08
NZ_CP036299.1\|WP_145298175.1\|2110442_2111039_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	1.26744e-23
NZ_CP036299.1\|WP_145298184.1\|2113309_2114485_-\|lipid-A-disaccharide-synthase	gnl\|CDD\|234580	PRK00025, lpxB, lipid-A-disaccharide synthase; Reviewed.	8.51429e-104
NZ_CP036299.1\|WP_145298145.1\|2095116_2097081_+\|cadmium-translocating-P-type-ATPase	gnl\|CDD\|319844	cd07544, P-type_ATPase_HM, P-type heavy metal-transporting ATPase; uncharacterized subfamily. Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.	0
NZ_CP036299.1\|WP_145298154.1\|2100783_2102265_-\|sulfatase-like-hydrolase/transferase	gnl\|CDD\|293763	cd16144, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	2.2322e-140
NZ_CP036299.1\|WP_145298151.1\|2098404_2100444_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	3.91388e-129
NZ_CP036299.1\|WP_145298133.1\|2086322_2087729_+\|hypothetical-protein	gnl\|CDD\|223533	COG0457, NrfG, FOG: TPR repeat [General function prediction only].	0.000115987

>NZ_CP036299.1|WP_145298154.1|2100783_2102265_-|sulfatase-like-hydrolase/transferase
MTEASPIRTIRKMLMSLGSHPAIALWLALVAFCSQTLSAAEDVNQTSQPGRPNILVIMADDLGYADLGVQGGCEIPTPHLDQLAASGIRCTNAYVSAPYCSPSRAGFLTGKYQTRFGHEFNPHVGEEAKLGLPLEEVTIASLLGKEGYRTALIGKWHQGFSKDHHPQSRGFDEFFGFLVGGHNYLLHKDVKPRFGSAHSHDMIYRGREVEPQEGYATDLFTNEALRWMSGPPDKPWFLYLSYNAVHTPLEIAPHLQKRIPESVKLPARRSYLSLLAGLDDSIGRIMQHLSQNGLRENTLIIFLSDNGGSGRAPILAYNSGLNHPLRGDKGQTLEGGIRVPFFVSWPRQLPAGTIYEQPIISLDILPTVCQLAAKDPAKPQPLPQGIDGVNLLPYWLAQRSGSPHESLFWRFGPQKAVRAGNWKLVDWRDFPASNSSGWELYDLSTDISEKNNLAEAHPETVARLKTSWEKWNQSNIEPLWRGSKMEDPTPMTK
>NZ_CP036299.1|WP_145298151.1|2098404_2100444_-|ATP-binding-cassette-domain-containing-protein
MESLNQLAPYLWRVRGYLIGSSIAALLVAIFWSAGLMLSYPLVKVLLQGQSLQAYLTEETQKAETETAQHQAEAARVQHQLDQLDPNVSSSEKISLLKSLDRAQRQLASSGWRLMFCTWLTKQLSTWLPEQAFPTLVLLLALLALVTLAKGLTVYLQENLVGIAVESTMVMLRQRMFQHVLRLDHVTLSLLGTPQLMARFTYDLQQLGTGLTLFGGRLVVEPLKILSVLICCFLVNWRLTTLSLIVVPLGALLFGRYGKKIKKASRKQMESMSRIFTQLEETLRSFRTILAFGLERQRRQSFHREQKVAFEKTMKILRMDALSSPTTEILATLGACMALLPGAYMVLRQKSEIFGIQLSEGPLDIAELALLYTLMGGLLDPARKLAAVYPKFKKSSAASDRVFGLLKTHTRLQQDRQWVPLPRHTDQIEFENITYTHPVAEDRNQARPPALDRVSLKIAFGETLAIVGGNGSGKSTLVNLLPRLYDPDFGILRIDGIDVRHTQLALLRKQIAVVPQETQLFNRTISENLRYGSWDAPADQVTRLAHDFAVDSFASRFPDGLETSVGERGQRLSGGQRQRIALVRALLRDPAILILDEATSAIDRESETQIYEALAHHKQNRTVLIVTHSLTDTLLKIVDRVVVMDHGQIIAHGEHTQLLKTCPIYRNLFAAQREQAHAA
>NZ_CP036299.1|WP_145298148.1|2097234_2098314_-|alcohol-dehydrogenase-catalytic-domain-containing-protein
MLAACLSSYWASMFSQPKARCFLSAKRMIRHPHERAPEQVMTKIVLSRGNIVIDSSVDEALLSPSSTTDETIIELRLAGICETDLQLISGYMGFEGVLGHEFVGTALNGPFAGKRVVGEINCPCGQCVYCQRGQNSHCPHRTVLGIYRRHGAFASRFSLPARNLHVVPESLSDDLAVLTEPLAAALRIPEQLDLAGKSVLVVGDGRLGSLCAAALFPLAGELAVVGKHPEKLQFANELGLTTYLKDKLPAQRKWEVVIETTGRKEGLEFALPLVEPEGVVVLKTTVAAPHQLSLTPVVIDEIQVIGSRCGPFAKALDWLIQQGSILQPLIEKTYYLHEGREALAHAQKPGTRKILLKPS
>NZ_CP036299.1|WP_145298145.1|2095116_2097081_+|cadmium-translocating-P-type-ATPase
MTAPRQKKSTAEPTTENSNRWLTEGQLQTSIAGLAIVAMLVWGIIAYALPSFTIYGSIQVADLSLLVALLLGGGYLVAGLLGNLFRGEFGSDLLAGISIVTSVLLGEYLAGTLVVLMLSGGEALEAYAVRRASSALDALAKRMPTVAHRLIDGHLTDVPLQEVQVGELLVVLPHEFCPTDGTVTAGQGTMDESFLTGEPYLLPKAVGASVLSGAINGEAALTIRVDQPASDSRHAKIMEVMRASEQQRPRLRRLGDQLGAWYTPLAVSIGIAAWVISGEAVRFLAVLVVATPCPLLIAIPVAIIGAVSLSARKGIVIKDPAVLETVTQCRVGIFDKTGTLTYGRPAMVELTPLSGFDRNNVLQLAATLEQYSRHPLAMPFLEAIQKTGLPLLEVSSVAELPGQGLTGLVQGHQIVVTGRAKLQKNQPALAEQLPPTQGGLECIILIDGQLAAVTSFRDRPRDDGKRFIDHLRERHHFQKVMIVSGDRESEVKYLADSVGISEIYFSQTPEQKVAIVRAETRKAKTVYVGDGINDAPALLEATVGLAFGRGSDVTAEAAGAVILDGNLKRVDEFLHISRRLRTIALQSAVGGIVLSLTGMSFAALGYLPPVFGAILQEVIDVIAVLNALRVGFPAGSLVDYDSSDSGGSSGNVQS
>NZ_CP036299.1|WP_145304423.1|2094103_2095120_+|SUMF1/EgtB/PvdO-family-nonheme-iron-enzyme
MLANPWIMANKVRGEKSGPPEGVMAPAGMVWIPGGEFRMGSNDPLAWDDERPTHPVSVEGFWLDKHEVTNREFAEFVKATGYVTTAEKAPTAEEILANSPPGTPAPDPAVLVPGSLVFTPPDHPVPLNDFSQWWVWTPGANWHHPEGPDSNIDERMDHPVVHVSWDDASAYAQWAGKRLPTEAEWERAARGGKEGLPFVWGTAPPSETSPQANLWNGKFPYENTAKDGFTRTAPVKSFPANDYGLYDMSGNVWEWCQDWYDRELYSRRPQLTVTKNPAGPEKSHDPTQPFQQLRSQRGGSFLCNDSYCSRYRPSARHGCSPDTGMSHVGFRCAKSVAP
>NZ_CP036299.1|WP_145298142.1|2091212_2093819_-|DUF1592-domain-containing-protein
MLKTYQFSITLCGLKGRNPFWLTLCSLFLFSMQPTVWAAEHGTTEFVPDQQGYQKLVAPFFKSYCSECHSGDKPEGEFSLDAAQLKNQLTDPVAKARWREVVNVLNSHEMPPEESRQPQAKEVAAVVDWVTAEAVRAEKFSREQTNVLRRLTRDEYRRTIRDLVGIDFDVSAFPEDPAAGGFDNNGSALTISPMHMELYLASARQILDRALVEGEQPPTIRWKFDPKVGPADRVRLRLDPKNNPLVNGGNNRQQGEWVAVHHASWDTNVGARDFRVPIAGTYRIRAQLAGTKPTRQEVIASATKILAKRRDEQIAKHPERTRQHQEQYQRDLQHFETSRIYDYGPVRAKLNVQLGSQPRTIAEFDIEGTRELPEIKTFLTRMTTETAGISFEYAYSIPRELENFWLQSSLEFARPELLVDWFEIEGPVVESWPPPSHQLIIGKENPSADNEVSAVTSILRNMMLRAYRRPPDEAEVQQRLAQFIAARKSRTFIEALKLPLISILTSPNFLYLVENPVQNPAQPLDDYQLATRLSFWLWSSMPDNELLQLAAEKRLSQPEVLKSQVARMLKDARSRAFVENFAGQWLGLRQVGANPPAKDLYPEYDRHLETSMIEESLAYFQEFLQHDLDVRQMIQSDFVVINERLARFYEIDGVRGDQFRRVQVSSDIPRGGIVTQASILCLTSNGTRTSPVKRGTWILKTLLGTDPGLPVANAGEIAPKVPGIDKATVRQRLEIHRELPQCARCHNKIDPLGFALENFNAAGDWRDREGFGYQGRIQANDPLIDASSRMPDGTNIVGVRGLQQALYQRHDLFVKALAERLLTYALGRELGLSDQPAIDRIVQAARDDNYRLSAMLESIATSETFCLK
>NZ_CP036299.1|WP_145298139.1|2089206_2091126_-|hypothetical-protein
MIATASQPNLTLSAIRHKIPVYSWLALFLAMGLLGYASFQIQATSSITFDETFYLNAGVRTVASGTLDPAICDCGVAPLPIIICYLPPLLLSRNEYRHEVWVGQNDDPQLIIWPRRLNTLLVGMPLLIVIWLWLGRKCGPAGASLGVLMTATSPTIQAHAALATTDLSFALFGLLGILALAHYLERPTWVRLGILAIAMAACLSAKYSGVFLFPVAGLMFLGRALRDQNVTKKKLTPTNETSTEKSVESASVSQLSQGWWPVVRQTFVTYTLLLLLVIPLWWAFHGFSFTGPLKNVPLEVTPPDSPWVEMLGRGPWADWIMDQAHRRWKRPAPIAGVLFQYLHNKSGHTAFLMGETSLTGWRTYFPCTIGFKSTPSELILIALLLFGTISLRLAGCISWSKLDFSRRCLWLSLAVLAALLLFARINIGHRYVLILYPLFIMLGIDTIFMIYRNYIDRFPNTNGTSKAHWPRIIFTLSTSLLLAMQFWSSWSIQPHALSYFNGLCGGPEQGGRLLLDSNIDWGQDLPTLQQLLSSEDSSKVALQYFGTALPTAYGIEADPTKALRQPLEDYELLAISVTHLGGLYVFGNDPYQKFRTWQPDARAGYSINLYRLDTPERKAAFAQAIQEHEKARTQSLLKQ
>NZ_CP036299.1|WP_145298136.1|2088335_2088974_+|histidine-phosphatase-family-protein
MRQAPPANVCRMLLCRHGATAANEMRPYILQGCEMNGPLTAIGEAQARSLAAALSGFLVAGVYASPLQRAHQTAEFIAKSHQLKVETDANLRECSVGRWEGLDWETIRTKDTEAHDHFFADPATNPHPGGESYSDVLNRAEPTLKQLAERHQGENIVVVAHNMLNRVILTPLLGLSLRMARQVKQANCCINVIEWTTDRAELITLNSVLHLD
>NZ_CP036299.1|WP_145298133.1|2086322_2087729_+|hypothetical-protein
MPATRPGAGGAVNRPGTGQGISNRPAQLPARLPGLGGGDVAQRLPNQGARVQDRMGDRPSVQDRQNNLSDRMANRGDWQENRQGLQDDRQDWRDQNREDWQNWGDNKLENYGDWYHDSWHPGSGWGYMWDNYPVAAAIGLTAWGINRIGYGWGYWNYANPYASSGGSYGYDYSQPLVSAESYAVASDPGASAEATQAASQQPTDEGLAAFEAAREAFRSGDYKGALAKLDITLKTMPNDTVVHEFRSLVLFALQKYPESAAAIYAVLAAGPGWDWTTMISLYPSTETYTEQLRVLEAFVKANPMSADGHFLLGYHYQTMKHDSAAAKQFSLASNLLPNDQLIKQLLGMTTPPEEATKSTVPSVPPVVPAEKVLQADQFIGNWKASQQGATFELDMTKSGVYTWTYAQGKRKQSVKGVFAVDQNNLALETDDGGETMLAEVQFISPTEFQFKMIGDSEKSPGLKFTKTQ
>NZ_CP036299.1|WP_145298130.1|2086050_2086428_+|hypothetical-protein
MAATLAREVAQQFNLVLDPTLVLAAVRSVHALHSCHQPGQRLALALGQESDRAQVLALAPVLALAPEVEPSEVEPSEGLDLVSCRVRGPLNCRRPGQVLVVLSTAPGQVRESAIVPLNCQPVCRG
>NZ_CP036299.1|WP_145298162.1|2104519_2106262_+|hypothetical-protein
MLQIQLGKWSTKCFSALALGASLLAATMVTRADEPRITFVQPGADRLREDLKYLVNLAPTPALKKEWENLDATLESFLAGVDGKTPIRVDLILGDKELIYQLNFPTTKLEGRDGFLDNVASFGYTVKKNAAGHYDLTEQGASKRKYFLRANGKYAMLSQRLQDIPANAPDPGKLAQNLLSGSQDIVADLKNDPATITQRQADFTKLRTELEAAVKFKRDEAKEVFELRKLGTNHQLSELERFIVQSEHLQATWTTDIEAGKGSGTLLLTALPGTELEKSIALLGTKPSAFSAIKLHDQPVISGKTCFELDDMRQKQLIEFYPVMNAAIGVNIENRPNLTAEGKAAAKEFSKTLFALLTDGVSLGVVDSYIDLHAVEGNVHNMTCGILAKETSTVPALLALMPKIRDDWKYEADVAEHNGVKIHKLTFPARRLEGFQSIFGKDQSDLYIGVGKEIVWGAAGKGGLDELKAAIDQQASGEKTVSPVVLSGTVKFGPTVQLLEIFRGNTPVSKTGKSKAELDRIKKIENLRKMAVDAFASGDDLLTFSLERKDREVVGQLNANQGILRYVGSVIANFSKEALR
>NZ_CP036299.1|WP_145298165.1|2106724_2108995_-|phospholipid-carrier-dependent-glycosyltransferase
MDRTRYDESASNAIHTCDAPGRPRRGTTGDRCIPLSLSLAGRREADNPRTGVRPGTRPVPAETALSVYKSTPGHPYHLGAAPRKRSGITLRKLFAHACASRRRHGKELKLRPGQRNASIASVAPQPLTRSHSIQMADWIYGSIAAIATGALLFALVPHQMYFHDEGQYAQGAERILLGELPHRDFHEMYTGGLAYLNALVFQVAGHRLDMLRYALVLLAIPVSVVSYHLLRGLKLSPWAACVLTVALFSTSLGTMHAPWANSYLMLFTLLAIAALLQDAKSPHLGWVLAAGICCGLAIAVKVTGLYTLAAIGLSLTYRGDPASPQVYPDLDFRPLSGAVWIERLWRGALALLMIALAVVLIRQHLSIHSFMYFVLPIAFAALTLVSSGGRLSWSMFGRYAVLGFGTAFPIALLLTPWLLEGAIQDFWHGVFELPRLRIGTTYYPPPPATGLLIAIPTVCCFLPIRHPWAPGVRITGLLILTSLMLYGLGDKSPSGFHTDGLLTAMSAWRWVLPIISAITCVVLTRSPQAPLSHRVGLYCLTICAACFSLNQYPFAQPIYFFFCVPLVILAAVALSLFDPSLPETTAAPGPRAMVHTGTGAVIVLAAFCLLRFGIDGTYGEFFESVGQRRQVYLSGIAVPAVYASGYNRLRELADEVLSEDQTVLAGPDCPHIYFLTGRRNPTPYMYDIFVTDPEYFSQLIELAHSDQVGMVIISRAPEFSPVWPQELVLKIAEAFSYAEEFERFIVLTKRAPASRP
>NZ_CP036299.1|WP_145298168.1|2108664_2109411_-|methyltransferase-domain-containing-protein
MDAGYVQVYRQLYNQHWWWRTRETAVLGAIREFHEPSPDDCVLDIGCGDGLFFDRLKDFGSVEGIEVDPLAVSETGPYRRQIHVGPFDDSFVTTRRYRLITMLDVLEHLDDPTAAAKLVRTLLTPDGLFVLTVPAFQTLWTGHDTMNQHRTRFTRATLRAVLDAAQLEIVASRYLFHWLAAAKLIIRGLECVRGPDQSPPKLPSPFINRLLGTLTTWELRRGKGLGLPFGSSLLMLARPAGAMGRNSN
>NZ_CP036299.1|WP_145298172.1|2109414_2110482_-|glycosyltransferase
MLANDVFQRTAALTSDEPHTAIGRTPPRVSVAIPVYNEEALIQELMRRVLAVLDGLPGGPHQLVLVDDGSRDRTFACICAAAQHDRRILPVALSRNFGHQIALTAALDYADGDLVVMMDGDLQDRPEVIPDMLTLWRDGADVVYAVRTRRKETWLLKTCYQAFYRVIERLAHLKLPRDSGDFCLVSREVADVMRTTREQHRYLRGLRAWAGFRQEPLLVERDARSAGDSKYGFRQLFQLAFDGIFSFSTVPIRVATWLGLTTVALTLFLGLFWVVAWSLNYAPQGFTALATSIAFFGGVQLVFLGLIGEYVGRIYEEVKNRPLYVVRKSSETGASAWPDDTPPAIQGLSAFTKRI
>NZ_CP036299.1|WP_145298175.1|2110442_2111039_-|methyltransferase-domain-containing-protein
MDLRSLLDHPMLYSAWQFPFVAQKVAPFLAVHDPMRTGRVLEIGCGPGTNASLFRQCDYVGVDLNPRYITTARKKHRGTFIQGDATSFVLEDSQPFDLVFCNSLFHHLDDAAVERTLARAASLLKPSGELHLLDLVLPDQPSVARFLARADRGDYPRSLSAWQALLSQHFVQDAFTPYPVKFLSITCWQMMYFRGRPL
>NZ_CP036299.1|WP_145298178.1|2111350_2111572_-|hypothetical-protein
MHDEITQNQGQSRIKAGSLAEEVVIGGRSRSQESTTDPWVNLAGYGNWTETNTSGWSESVSNYEFSLLTAGFE
>NZ_CP036299.1|WP_145298181.1|2111769_2112147_-|hypothetical-protein
MSSTMKMLVVFDPTKPDSQTTDFLIPWSRDGQRVFLGLKSGKESALGMMVFIGRSITENDLFAKLVDSGAVIPDVDETLALLRSYVERLQSLKIGNVARIRSIDQVNGSDVELELVANTPSALNA
>NZ_CP036299.1|WP_145298184.1|2113309_2114485_-|lipid-A-disaccharide-synthase
MHIFFSVGEPSGDQHAAHLIRALQHRDPGLKVSGLGGPAMEVAGCEVIYPLTNLAVMGIFRVLPLLTTFYKVFRQARAHLQKHRPDAVVLIDFPGFNWHIAKAAKSLGIPVYYFMPPQMWAWGGWRIHKLKRTVDHVISGLQFETEWYAQRNVPVTNVGHPFFDEIVHHPLDQSFVREWKPQAGRVVALLPGSRGHEVTHNWPRMLEAARMLHERFDDLTFYVANYKEKQRQWCSEEFVRTGGGLRMNFFVGRTPEIIDIADCALVVSGSVALELLARRTPYATFYSCSKLTHWIGRQIIHIPHFSLPNLMANRRIFPELLFVGEAPEAGRQMADAIAPWLADPQQMTMKLEELDALRRDVVQVGALTRTADLILRLTTDQAQTEQLSSAA
>NZ_CP036299.1|WP_145298187.1|2114681_2114918_-|hypothetical-protein
MEQTSAPMFVLSTDGELHGVDTEGNRELVRRIYACVQACEGISTDELEMGVIAEMKRLLGQVVPLLQNRSAAAEREAA
>NZ_CP036299.1|WP_145298190.1|2115329_2116241_+|hypothetical-protein
MALWIAIVTQENMHWLQEGQGRLPVCLWSFTTDAPLADLKLARETGEVVASDHSGGIYLIDIEGRVRALTRLGQVAREVAFADNGATIAAVSGPSSLSLMNRKLAFQWTRQLPDSILATALAPYGEHVAVSLTDGMNAIYTLGNKKQATFQTPRPLKHLAFLGTEAALIGAAEYGLISKIRLDGQILWSESLWSTVGGLAVTGNGESILLAGYMHGLQMFGNDGSAAGTLMLDGTASHVGQSFHQHRIYSATLEQHLACLSKAGDLVYLLGLPEPLHRLQVTAMGDAVIVGFPSGRIMKLAML

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Crispr_ID: NZ_CP036299_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP036299_2

2281065-2281135

TypeII

Consensus_repeat	Method
ACCATCTTGCAGGTGCGAACGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP036299_2

>merge|NZ_CP036299|2|2281065-2281135|CRISPRCasFinder
ACCATCTTGCAGGTGCGAACGGGAATCTTGCGGACACATTCTTCGCTCACCATCTTGCAGGTGCGAACTGG

>NZ_CP036299|2|2|2281065-2281135|CRISPRCasFinder
ACCATCTTGCAGGTGCGAACGGG	AATCTTGCGGACACATTCTTCGCTC
ACCATCTTGCAGGTGCGAACTGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP036299.1\|WP_145298464.1\|2272222_2272858_+\|universal-stress-protein	unknown	unknown	gnl\|CDD\|238182
NZ_CP036299.1\|WP_145298479.1\|2279685_2280633_+\|site-specific-tyrosine-recombinase-XerD	unknown	unknown	gnl\|CDD\|274043
NZ_CP036299.1\|WP_145298485.1\|2282869_2283682_+\|5'/3'-nucleotidase-SurE	unknown	unknown	gnl\|CDD\|234732
NZ_CP036299.1\|WP_145298458.1\|2270353_2270728_+\|(2Fe-2S)-binding-protein	unknown	unknown	gnl\|CDD\|377304
NZ_CP036299.1\|WP_145298488.1\|2283686_2284655_+\|cation-diffusion-facilitator-family-transporter	unknown	unknown	gnl\|CDD\|223131
NZ_CP036299.1\|WP_145298470.1\|2275923_2276412_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP036299.1\|WP_145298506.1\|2292695_2293490_-\|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379142
NZ_CP036299.1\|WP_145304441.1\|2288566_2289112_+\|acetolactate-synthase-small-subunit	unknown	unknown	gnl\|CDD\|183365
NZ_CP036299.1\|WP_145298509.1\|2293853_2294327_-\|DUF386-family-protein	unknown	unknown	gnl\|CDD\|377217
NZ_CP036299.1\|WP_145298476.1\|2278722_2279307_-\|DUF2892-domain-containing-protein	unknown	unknown	gnl\|CDD\|238089
NZ_CP036299.1\|WP_145298500.1\|2290532_2291024_-\|cell-division-protein-FtsH	unknown	unknown	gnl\|CDD\|273520
NZ_CP036299.1\|WP_145298503.1\|2291053_2292541_-\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	unknown	unknown	gnl\|CDD\|236486
NZ_CP036299.1\|WP_013109441.1\|2271255_2271813_-\|Hsp20/alpha-crystallin-family-protein	unknown	unknown	gnl\|CDD\|223149
NZ_CP036299.1\|WP_145298473.1\|2276515_2278636_+\|DUF255-domain-containing-protein	unknown	unknown	gnl\|CDD\|224250
NZ_CP036299.1\|WP_145298455.1\|2268514_2270275_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|284919
NZ_CP036299.1\|WP_145298461.1\|2270846_2271266_-\|Hsp20-family-protein	unknown	unknown	gnl\|CDD\|223149
NZ_CP036299.1\|WP_145298494.1\|2286040_2287411_-\|PTS-transporter-subunit-EIIA	unknown	unknown	gnl\|CDD\|224539
NZ_CP036299.1\|WP_145298467.1\|2273193_2275827_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379090
NZ_CP036299.1\|WP_145298497.1\|2289407_2290412_+\|ketol-acid-reductoisomerase	unknown	unknown	gnl\|CDD\|235491
NZ_CP036299.1\|WP_145298491.1\|2284692_2285988_-\|L-fuconate-dehydratase	unknown	unknown	gnl\|CDD\|239440

Protein	Function_ID	Function_description	E-value
NZ_CP036299.1\|WP_145298464.1\|2272222_2272858_+\|universal-stress-protein	gnl\|CDD\|238182	cd00293, USP_Like, Usp: Universal stress protein family. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, athough Usp lacks ATP-binding activity.	5.14959e-10
NZ_CP036299.1\|WP_145298479.1\|2279685_2280633_+\|site-specific-tyrosine-recombinase-XerD	gnl\|CDD\|274043	TIGR02225, Tyrosine_recombinase_XerD, tyrosine recombinase XerD. The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This model represents XerD, one of two closely related chromosomal proteins along with XerC (TIGR02224). XerC and XerD are site-specific recombinases which help resolve chromosome dimers to monomers for cell division after DNA replication. In species with a large chromosome and with homologs of XerD on other replicons, the chomosomal copy was preferred for building this model. This model does not detect all XerD, as some apparent XerD examples score below the trusted and noise cutoff scores. XerC and XerD interact with cell division protein FtsK. [DNA metabolism, DNA replication, recombination, and repair].	3.85014e-125
NZ_CP036299.1\|WP_145298485.1\|2282869_2283682_+\|5'/3'-nucleotidase-SurE	gnl\|CDD\|234732	PRK00346, surE, 5'(3')-nucleotidase/polyphosphatase; Provisional.	3.05706e-111
NZ_CP036299.1\|WP_145298458.1\|2270353_2270728_+\|(2Fe-2S)-binding-protein	gnl\|CDD\|377304	pfam04324, Fer2_BFD, BFD-like [2Fe-2S] binding domain. The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilisation functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).	1.09839e-05
NZ_CP036299.1\|WP_145298488.1\|2283686_2284655_+\|cation-diffusion-facilitator-family-transporter	gnl\|CDD\|223131	COG0053, MMT1, Predicted Co/Zn/Cd cation transporters [Inorganic ion transport and metabolism].	8.32419e-79
NZ_CP036299.1\|WP_145298500.1\|2290532_2291024_-\|cell-division-protein-FtsH	gnl\|CDD\|273520	TIGR01241, ATP-dependent_zinc_metalloprotease_FtsH, ATP-dependent metalloprotease FtsH. HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides].	1.06924e-09
NZ_CP036299.1\|WP_145298506.1\|2292695_2293490_-\|trypsin-like-peptidase-domain-containing-protein	gnl\|CDD\|379142	pfam13365, Trypsin_2, Trypsin-like peptidase domain. This family includes trypsin-like peptidase domains.	5.59666e-09
NZ_CP036299.1\|WP_145304441.1\|2288566_2289112_+\|acetolactate-synthase-small-subunit	gnl\|CDD\|183365	PRK11895, ilvH, acetolactate synthase 3 regulatory subunit; Reviewed.	1.32611e-73
NZ_CP036299.1\|WP_145298509.1\|2293853_2294327_-\|DUF386-family-protein	gnl\|CDD\|377217	pfam04074, DUF386, Domain of unknown function (DUF386). This family consists of conserved hypothetical proteins, typically about 150 amino acids in length, with no known function.	6.29645e-50
NZ_CP036299.1\|WP_145298476.1\|2278722_2279307_-\|DUF2892-domain-containing-protein	gnl\|CDD\|238089	cd00158, RHOD, Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.	4.63025e-26
NZ_CP036299.1\|WP_145298503.1\|2291053_2292541_-\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	gnl\|CDD\|236486	PRK09369, PRK09369, UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated.	0
NZ_CP036299.1\|WP_013109441.1\|2271255_2271813_-\|Hsp20/alpha-crystallin-family-protein	gnl\|CDD\|223149	COG0071, IbpA, Molecular chaperone (small heat shock protein) [Posttranslational modification, protein turnover, chaperones].	3.17148e-28
NZ_CP036299.1\|WP_145298473.1\|2276515_2278636_+\|DUF255-domain-containing-protein	gnl\|CDD\|224250	COG1331, COG1331, Highly conserved protein containing a thioredoxin domain [Posttranslational modification, protein turnover, chaperones].	0
NZ_CP036299.1\|WP_145298455.1\|2268514_2270275_+\|hypothetical-protein	gnl\|CDD\|284919	pfam07596, SBP_bac_10, Protein of unknown function (DUF1559). A large family of paralogous proteins apparently unique to planctomycetes.	0.000212707
NZ_CP036299.1\|WP_145298461.1\|2270846_2271266_-\|Hsp20-family-protein	gnl\|CDD\|223149	COG0071, IbpA, Molecular chaperone (small heat shock protein) [Posttranslational modification, protein turnover, chaperones].	3.27777e-24
NZ_CP036299.1\|WP_145298494.1\|2286040_2287411_-\|PTS-transporter-subunit-EIIA	gnl\|CDD\|224539	COG1624, COG1624, Uncharacterized conserved protein [Function unknown].	2.00076e-29
NZ_CP036299.1\|WP_145298467.1\|2273193_2275827_+\|hypothetical-protein	gnl\|CDD\|379090	pfam13248, zf-ribbon_3, zinc-ribbon domain. This family consists of a single zinc ribbon domain, ie half of a pair as in family DZR. pfam12773.	0.00223494
NZ_CP036299.1\|WP_145298497.1\|2289407_2290412_+\|ketol-acid-reductoisomerase	gnl\|CDD\|235491	PRK05479, PRK05479, ketol-acid reductoisomerase; Provisional.	0
NZ_CP036299.1\|WP_145298491.1\|2284692_2285988_-\|L-fuconate-dehydratase	gnl\|CDD\|239440	cd03324, rTSbeta_L-fuconate_dehydratase, Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, 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.	0

>NZ_CP036299.1|WP_145298479.1|2279685_2280633_+|site-specific-tyrosine-recombinase-XerD
MPPRFKPVQNSVASALPTALPSTHVEGFVAYLQGECGLARNTVISYERDIKRFSDWFHESAVARVTDITLQDLSGYLRYLHELKLATSTIARHLVSLKMFFRYLMLEGILKESVADLLNSPKLWEHLPKVLSEDAVNRLLDAPMHQDLNPYRDRALLAVLYATGCRASEVCSLKMRDLQLDEGFCRCVGKGNKERLVSLNPVAVAALKTYLARERPARAGTSLDSPVFTSRSGRSIDRIQVWKLVKRYASRIGLSDAVTPHTLRHSFATHMLANGAEIRALQELLGHASIRTTQIYTHVEHSRLKAIHKQCHPRG
>NZ_CP036299.1|WP_145298476.1|2278722_2279307_-|DUF2892-domain-containing-protein
MTIPTILPIELKTHIDAAEPVTIIDVRTPLEFQEVHAHGAVNIPLDELEAEKLSSFVNPESKTVYLICRSGGRGKKACEKLLAKGPWQPINIEGGTQGWEAAGLPVHRGKKIMSLERQVRIAAGSLVVLGCALGAFVTPYAFGLAAFVGAGLVFAGVTDTCAMGLLIARMPWNSTPRSNSSCSLNLTSPPATSH
>NZ_CP036299.1|WP_145298473.1|2276515_2278636_+|DUF255-domain-containing-protein
MNLVNRLAAETSLYLNQHAQNPVAWQPWDDEAWRLARELDRPVFLSIGYSACHWCHVMEHESFENPRIAELLNQWFVSIKVDREERPDLDQIYMAAVIAMTQQGGWPMSVFLTPQGHPFYGGTYFPPTSRYGRPGFAEVLAAIHDAWENRREVVTEQASQLTMSVHDQLSERQEPTTLQESLLEKAGRTLVRVCDRVNGGFGHAPKFPHAMDLRLALRLAHRFDTTETAEVAELGLTAMAKGGIHDHLGGGFARYSTDEVWLVPHFEKMLYDNALLLQAYLDGWQFYKTDFYRRTAQSIVHYVLREMQVPGAELPGGFCAAQDADSEGEEGRFFVWSQSEIRTVLSGSELGNDDSRLFERAYGVTSGGNWEGHNILNLPKTIAALGRELGMAETALEQKLSLLRAKLFEHRKSRIAPGRDEKLIVAWNGLMISALARSGLVLDDQEALQAAQRAARVILDMAESLPYGLPHSIQKGQPKHGAYLDDYGCFLEALIELFLADGDPSWLSRALPLIDRLVNEFHDEQGGFYFTSNKAEKLISRSRDFQDNVTPSGNAAVANALLKFGRITGDARSQELAHEVLQAASGLMQQSTMATAHSLAALDWWLGANYECVYVPAETTSTTDAEPLKQNAVERVAHELYLPNVLFLTGRAQWEGTLAAGLVNGRLAPASEPVLYVCQKGACQLPVVGEAAIIARLKGLAQSTDE
>NZ_CP036299.1|WP_145298470.1|2275923_2276412_+|hypothetical-protein
MPRFALLEHDWPENHGDFLLEVPGLKSRDGLGLCWTWRFPGDRKVWERLFLQGGSIEAERNTDHRAHYLDYQGAVTPAADGTPRGFVMIVFQGEFQWADPWELSPLEGPPVLPDFLQMVFQVHPGKQMMAGQMQLLESPEGWKFTILPETNSKALKTDKVHS
>NZ_CP036299.1|WP_145298467.1|2273193_2275827_+|hypothetical-protein
MAPLWCQVTTLKDSAMDFAVCPSCKQSVLDDDAVDCPFCGAPMKGGPRPGGAPAKPAASKAAQSPKSVSASAANTVSATNTVNRGAANKNAGKSSSADQSSGTDDLPFETETKAATTVAVATATKQRSFRIVCPMCETVGYISPKSAGTRVKCANPKCLVPVFDAPQLPPPEPEKPPEPPRKPNYILLGGGTAAICIIGGIVALFVASQPAASPVAVNRMTPEEAARLLAETAPAANNTSNQTKNSGTPDGSPQTTTETKPNPGDTKTAASSTVDLAKELPILIEKTVLIRGSQNRSLPFSRQMAAEAYALLGNIEKAQEQAVAFDRVGQNVPFYKISILTELGWAQLRAGTSDAAKASALAAYNLVNKLPGNGRSRLIFASRLGSLLIATGEADKATQLANDYATTWKPGLIDSNQVAERLERQDGQVAALLQAGLDDFAGSIAQVTATRPGVVWFEPQAAAMARSAAAQGFSEAAISWAISQPEVRQLETLGEIAALEGAIAAPDVTAEALKAKIEGWGANASVMKLPASKAYLFARAAAAVASVSKPAALGLIKEAQALLEPVELPAPMTWPNTQGLVNPQLPAIAPLERLFVAWAEVSIACQLAGDADGCDSALSKALATLQGVGPALNYVDQFLEQLNGPDVASIRDRLKDELGIRTEDAARQAFSSYRRGTLNYREHAAIRYDFELQALDRLAQAGGQAIVWKKLQEMATETNAVQKQLPSEISMKLVSSLATAFQLANEPTQAQAVTDWYSGITRIGAITPSAMLLSASRFGAKDGAGAVTVLKEADAPTRALMTSLLAGQLKDAGMVEPALVLVGQTSDLSVREEASIFAAHAAHHLGEAARIVTHLQTLPQATERLSWIRGLSMPIKK
>NZ_CP036299.1|WP_145298464.1|2272222_2272858_+|universal-stress-protein
MEASRGNIFKVIEMIRRRGLSHRLEKALMECRPWARVTFISNLQPEDDTVKLLLCVDASGSSDRAISRVTELGLGHSKSNSVTLFTVCESLPEHVFEISEKVGMHAKELASAWSLKSRSAGEQALAQAKAKLLESGLPESAIHIKLCVADATPESRQVAAAASLIEEMTSGNYDLVVIGRRGAKHLSENLIGSVADKVIRAASGRSVLLVD
>NZ_CP036299.1|WP_013109441.1|2271255_2271813_-|Hsp20/alpha-crystallin-family-protein
MAIFRWGNAWQAMENFEQEVDSLLAGVLQGLRVVRHYPAVNLYELPDQLLITAELPGIRLEELDISVNEGSLTLKGRHLGPEGVPDEAFRRQERPRGKWQRTLKLPDGIREEAVSAQFSNGVLLIRLPKVPPKPARQITVTAVAENPPPVESVPEAIPTPARRIATEPGQVSGLIEPKERESHES
>NZ_CP036299.1|WP_145298461.1|2270846_2271266_-|Hsp20-family-protein
MRAEQPEIPPGRASIRNPGDAAIEQPVEQQVVFTPPIDIFERPDGLILLADLPGVTLETLELQVQDNRLTLYGRVQTQWLEGVQTLHQEYPIGHFLRSFILNDEVDHEKITARLAHGVLEVFLPRATKAIPRKIEVKTD
>NZ_CP036299.1|WP_145298458.1|2270353_2270728_+|(2Fe-2S)-binding-protein
MELDDTICFCFHITKRKVMNFIRVHRPRVASQVSECGGAGTGCGWCRKYLKRYFDESQGRMPATSGGLDAHTEEAPEITLEEYATSRAAYIRAGHGKPAAGAIPLPGVTTEPTLQQPSDPESPE
>NZ_CP036299.1|WP_145298455.1|2268514_2270275_+|hypothetical-protein
MPFPACPKCLAPIRIRDRKFVGREIPCPSCAAHIVPLVTGHDEWQVILPEEYARQSAATSNSAKSNLEKQTTGVHASTGPAIVKPLGANTLRAGGRQLKAPSPFVMAWIGSGVITFCIVMVIVQSFSRRDHQARELVTQQPNESSQQQPVQPIENSDPGQTTGEKELVPQPLPASHEKLAGLGQWLSGELASQGAFPAATTGKSENPEEAWGWLNRYVAQTQPTIVPPPFEGSWRGPTHDRFVRRRMNSLLINEQEGLIGGDGYPATQLVGVAGVGIDGPHLPASSEYAGIFAYGRTTRQRDILDGLSQTAMVASVKEDLASWASGGKGGIRSLTAAPVIDGPDGFGIVGQSGQLLLMADGSVKELTNAADPVIMRRMFTMAEGIDLAEAASPDAPLFPARAASRQTMPMADPPGGSESVADSHSSAPTGISPEKDDPAAEKPNGKVEKSSTGEVVAPPAAQAPLPPAMVVQKQDLKINLGLSLQRFRTDEPVARRRLVKSAADLLGAPVITPEGPLPAELVEILDQKITIDLEKVSIENLLHEIFRDSQARWSLQDGQLLIQLSSEVVPGPPPATGGEPREVAVP
>NZ_CP036299.1|WP_145298485.1|2282869_2283682_+|5'/3'-nucleotidase-SurE
MHILLVNDDGIHAPGLNSLHAELVKFAQVTVVAPAVEQSGVGHSITYLHPLLAHREYRQDEFFGWKVEGSPADCVKLGIMELAQPRPDLVVSGINHGANVGINILYSGTVAAAIEGAFFGVTSFALSQWLGNSAPRFPQAARLGAQLIQQIMAQNPPAGSLWNINFPTWSTNDQSSAESWPRGVRLTSMGVSRQRETLEKRIDPRGRTYYWTGLEPIHGHELVEGSDVAALVDGYVTVTPLHFDLTNRSQLTQAETNWSPLVIPPQHDQE
>NZ_CP036299.1|WP_145298488.1|2283686_2284655_+|cation-diffusion-facilitator-family-transporter
MEQLPEVHLEASKVTSNNLRQLRYRDALFGAWLGLWINLALGITKLIAGIIGQSFALLADAFNSLSDCVTSSAVIFALNYSQRPANSNHPYGFSKAEALAGSHVALAILISCFLLGWEAIERLTVQHGLPPWWTLAVAAANAVIKESLYWYKLKIAKSTGSTALLAHAWDHRNDALCSVAVLIGLSVVRIGGEAWRSADEVASLVVVCVVGFSAASIFRQSLREMLDLQIDETEVDAMRATVQRVPGVQGIEKFRVRKTGIEQIAELHLRLPAEITVFAGHALAHQVKAELMQQHPMLRDVIIHVEPASEPASHSSPEESSR
>NZ_CP036299.1|WP_145298491.1|2284692_2285988_-|L-fuconate-dehydratase
MPKFSGIQAIDLRFPTSRLLDGSDAMNPDPDYSAAYVILKTDDAALPAGHGMTFTIGRGNELCVAAIESLGKLLIGRDLSEFTEAPGQFWRELTGDSQLRWLGPEKGVIHLATAALVNALWDLWAKIEQKPLWKLVTDFTPAQLVNCIDFRYLTDALTPAEAIERLERKVAGKSARVEQLLATGYPAYTTSAGWLGYSDEKLRQLCRSNLAQGWEVFKVKVGRNLDDDLRRLTIIREEIGPERRLMIDANQVWDVSTAIDWVRELAKFHPWFIEEPTSPDDILGHAAIAKAVHPIAVATGEHCANRVMFKQFLQAGAIGICQIDSCRLGGVNEVLAVMLLAEKFGIPVCPHAGGVGLCEYVQHLSMIDFIAISGSWENRFCEHADHLHEHFVHPISMKNGRYQAPLAPGYSIEMLPETIAAYRFPEGAIWA
>NZ_CP036299.1|WP_145298494.1|2286040_2287411_-|PTS-transporter-subunit-EIIA
MIIVDLADLVSGIRIVELTAKTRQGAIRALVQAANWDDDGINPENVLEAIEEREAAAQTLVANDFALPHAFIDWDGDFRIVLGRSKSRVDYGGPAGVNVQLIVLLVIGRRLQQTHVEVLAALAELLKSPDFRQNLIDAKDIKAIDLLLMTQAGIQPENRPVRGPSIPRLTVNMVKTAIQLTESLAAQALLLAVERVENVPWEALANYKGRLLLVTSQHSEEFDHKREDLHIFDVAHASLSRADRANLGLLLAASSGLLTEKNSVVCVTGPDGRRLDSINVTKPEVHFRAMLSEKNRRGADVVRPAVMLRVLTLAIEIAAEGREAHPIGALFVIGDSRQVLRHSQQLVLNPFHGYARQLRNVLDPSLAETMKEFALIDGAFIIQGDGTVLSAGTYLTPKSASGSVAHGLGARHQTAAAISAHTQAMAITVSQSTGTVTVFRNGSSVLSLERSGRTKW
>NZ_CP036299.1|WP_145304441.1|2288566_2289112_+|acetolactate-synthase-small-subunit
MKHVLSAMVMNQPGVLAHISGMLASRAFNIESLAVGETERPDFSRITFVVAGDNKVVDQVRKQLEKIVTVVKVMDYRDQDILERDLMLLKVSTVESGLSKVKELAEIFRAKIVDVGQSHVMIELSGPERKIDAFIDLMRPFGILELVRTGRIALAREVSLSVEDALKPPTPYDTSEVEIEV
>NZ_CP036299.1|WP_145298497.1|2289407_2290412_+|ketol-acid-reductoisomerase
MAAKVYYDDDADLSLLKGKTIAILGYGSQGHAQAQNLRDSGLNVVVGQRPGSKNYDLAVSHGFKPLSIAEAVKQADLVNILLPDEVQGDTYKSEILPNLKPNALLLCSHGFNLHFGQIVPPAGVDAALVAPKGPGHLVRSEYEKGGGVPSLIALWPGASDNSRKLALAYAKGIGGTRGGVIETTFAEETETDLFGEQVVLCGGVSALIKAAFEVLVEAGYQPEMAYFECMHEMKLIVDLFYQGGLNYMRYSVSNTAEYGDYTRGPRIITAETKQEMKKILGEIQSGQFARDWLLENRVNQASFKAVRRREREHQIEKVGRDLRKMMKWINAKEF
>NZ_CP036299.1|WP_145298500.1|2290532_2291024_-|cell-division-protein-FtsH
MDSAPLPQTELTATAYHEAGHAVVALFLGRPVHEVTIEPNSLRLGQCRLNKGNFKPSKDVLEGEILILLAGVAAEARYRGDYRWEGAVSDLRQVRHFSSMRATNIRQVERLEQRLLNKVEHILSQVGPWLAVEEIARELISRTTISGRSARHHFELAMERFAE
>NZ_CP036299.1|WP_145298503.1|2291053_2292541_-|UDP-N-acetylglucosamine-1-carboxyvinyltransferase
MDMLIIRGGIPLAGNVRLAGAKNASLPIMAASIAVSGLSQLRRVPQLADVSTLTQVLESLGAVVTRDLSTGELAITPPQATTGIADYDLVRRMRASVCVLGPLLARWGKAVVSLPGGCNIGHRPIDLHLKGLVALGARIRIERGYVHADATRLHGAEIYLGGPFGSTVTGTANIMTAASLARGMTRISAAACEPEIVDLGNFLNAAGARITGHGTPVIEIEGVDELHGVEHAVIPDRIEAGTMMIAAAATCGDVLIEDAQPRHLSAVIDILRQIGVSIEPSSTSDGRTGLHVSGAAHLNPADCTALPYPGVPTDLQAQLTALLCLVPGISIITDKVFPDRFMHVPELLRMGAQVRREGASAIIAGPAHLSGTNVMASDLRASAALVIAALAAEGESVIRRVYHLDRGYEKHDEKLRQLGAQIQRTTDHPEALPDSLRMTGESTIEQHKIQEIPGRFTQPFQNQPTKPHFLSDGYSIANPMVSQSDNFTAPAVDLP
>NZ_CP036299.1|WP_145298506.1|2292695_2293490_-|trypsin-like-peptidase-domain-containing-protein
MLVPELFLRVAKVETYGQGQLLTNASGFFFEWQSELYLITNRHVCVDEMAGHRPDTLKLQLHTVKDDLTKSGPLEIQLYKQGVPLWKAYPRPVNDIDVVAVPLPGKLLKQNYVISSFGASDILGPEETLPPGQQVLITGFPLGFHDTLNNLPLVRQAVVASDFSRPFKGNPYFVTDARTHRGTSGSPVVTKLLRPTPVAGQFEERWCLLGIHAATLDVSNRDPMYDDRLGLNVTWFASLIPQIIEGILPANPHPAPSSDSVCFN
>NZ_CP036299.1|WP_145298509.1|2293853_2294327_-|DUF386-family-protein
MIIDELANQHFYSHCHPAITRALQFLASPAAHELPTGKHRLDSDALIAIVEEYQTKQPTEAVWESHRKYVDVQYIVRGEEAFGLARTSDNLTIRTPYSDERDVVFYHPGTQRFVASAGMFLIFFPQDIHAPGLAVNEPSPVRKIVMKVRGDWVFNQD

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Crispr_ID: NZ_CP036299_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP036299_3

4233030-4233112

Orphan

Consensus_repeat	Method
CCATGCCCCGAAGAACCGTGCCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP036299_3

>merge|NZ_CP036299|3|4233030-4233112|CRISPRCasFinder
CCATGCCCCGAAGAACCGTGCCCAGAGGCTTCCTTTTTGGCTCCATGGCCGCTGGAAGAACCGTGGCCTGAAGAGCCATGCCC

>NZ_CP036299|3|3|4233030-4233112|CRISPRCasFinder
CCATGCCCCGAAGAACCGTGCCC	AGAGGCTTCCTTTTTGGCTCCATGGCCGCTGGAAGAA
CCGTGGCCTGAAGAGCCATGCCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP036299.1\|WP_145302241.1\|4225134_4226232_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|239946
NZ_CP036299.1\|WP_145302250.1\|4228350_4228809_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP036299.1\|WP_145302256.1\|4229722_4231384_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|276965
NZ_CP036299.1\|WP_145302271.1\|4236077_4237052_-\|RimK-family-alpha-L-glutamate-ligase	unknown	unknown	gnl\|CDD\|273261
NZ_CP036299.1\|WP_145302286.1\|4242312_4243392_-\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224169
NZ_CP036299.1\|WP_145302280.1\|4240880_4241783_+\|alpha/beta-hydrolase-fold-domain-containing-protein	unknown	unknown	gnl\|CDD\|223730
NZ_CP036299.1\|WP_145302267.1\|4235062_4236001_-\|inositol-monophosphatase	unknown	unknown	gnl\|CDD\|238815
NZ_CP036299.1\|WP_145304621.1\|4239299_4240271_+\|RluA-family-pseudouridine-synthase	unknown	unknown	gnl\|CDD\|223638
NZ_CP036299.1\|WP_145302264.1\|4233886_4234750_-\|flagellar-motor-stator-protein-MotA	unknown	unknown	gnl\|CDD\|274801
NZ_CP036299.1\|WP_145302277.1\|4238231_4238981_-\|Bax-inhibitor-1/YccA-family-protein	unknown	unknown	gnl\|CDD\|378959
NZ_CP036299.1\|WP_145302247.1\|4227281_4228157_+\|DUF1559-domain-containing-protein	unknown	unknown	gnl\|CDD\|284919
NZ_CP036299.1\|WP_145302234.1\|4223448_4224159_-\|carbonic-anhydrase	unknown	unknown	gnl\|CDD\|238449
NZ_CP036299.1\|WP_145302274.1\|4237048_4238008_-\|methenyltetrahydromethanopterin-cyclohydrolase	unknown	unknown	gnl\|CDD\|235020
NZ_CP036299.1\|WP_145302259.1\|4231669_4232635_+\|endonuclease/exonuclease/phosphatase-family-protein	unknown	unknown	gnl\|CDD\|377028
NZ_CP036299.1\|WP_145302231.1\|4223006_4223438_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP036299.1\|WP_145302238.1\|4224312_4224900_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|275319
NZ_CP036299.1\|WP_145302253.1\|4228874_4229678_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP036299.1\|WP_145302244.1\|4226123_4227041_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|234649
NZ_CP036299.1\|WP_145302289.1\|4243833_4244985_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|319972
NZ_CP036299.1\|WP_145302283.1\|4241810_4242449_+\|chemotaxis-protein-CheX	unknown	unknown	gnl\|CDD\|381734

Protein	Function_ID	Function_description	E-value
NZ_CP036299.1\|WP_145302241.1\|4225134_4226232_-\|hypothetical-protein	gnl\|CDD\|239946	cd04502, SGNH_hydrolase_like_7, Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.	4.08261e-62
NZ_CP036299.1\|WP_145302256.1\|4229722_4231384_+\|hypothetical-protein	gnl\|CDD\|276965	sd00038, Kelch, Kelch repeat. Kelch repeats are 44 to 56 amino acids in length and form a four-stranded beta-sheet corresponding to a single blade of five to seven bladed beta propellers. The Kelch superfamily is a large evolutionary conserved protein family whose members are present throughout the cell and extracellularly, and have diverse activities. Kelch repeats are often in combination with other domains, like BTB and BACK or F-box domains.	3.40365e-30
NZ_CP036299.1\|WP_145302271.1\|4236077_4237052_-\|RimK-family-alpha-L-glutamate-ligase	gnl\|CDD\|273261	TIGR00768, Tetrahydromethanopterin:alpha-L-glutamate_ligase, alpha-L-glutamate ligase, RimK family. This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).	9.24562e-59
NZ_CP036299.1\|WP_145302244.1\|4226123_4227041_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|234649	PRK00121, trmB, tRNA (guanine-N(7)-)-methyltransferase; Reviewed.	1.51848e-28
NZ_CP036299.1\|WP_145302280.1\|4240880_4241783_+\|alpha/beta-hydrolase-fold-domain-containing-protein	gnl\|CDD\|223730	COG0657, Aes, Esterase/lipase [Lipid metabolism].	4.84142e-31
NZ_CP036299.1\|WP_145302267.1\|4235062_4236001_-\|inositol-monophosphatase	gnl\|CDD\|238815	cd01637, IMPase_like, Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent metal ions such as Mg++, and many members are inhibited by Li+ (which is thought to displace a bivalent ion in the active site). Substrates include fructose-1,6-bisphosphate, inositol poly- and monophosphates, PAP and PAPS, sedoheptulose-1,7-bisphosphate and probably others.	1.40234e-10
NZ_CP036299.1\|WP_145304621.1\|4239299_4240271_+\|RluA-family-pseudouridine-synthase	gnl\|CDD\|223638	COG0564, RluA, Pseudouridylate synthases, 23S RNA-specific [Translation, ribosomal structure and biogenesis].	1.327e-91
NZ_CP036299.1\|WP_145302264.1\|4233886_4234750_-\|flagellar-motor-stator-protein-MotA	gnl\|CDD\|274801	TIGR03818, MotA1, flagellar motor stator protein MotA. The MotA protein, along with its partner MotB, comprise the stator complex of the bacterial flagellar motor. MotAB span the cytoplasmic membrane and undergo conformational changes powered by the translocation of protons. These conformational changes in turn are communicated to the rotor assembly, producing torque. This model represents one family of MotA proteins which are often not identified by the "transporter, MotA/TolQ/ExbB proton channel family" model, pfam01618.	3.74677e-116
NZ_CP036299.1\|WP_145302277.1\|4238231_4238981_-\|Bax-inhibitor-1/YccA-family-protein	gnl\|CDD\|378959	pfam12811, BaxI_1, Bax inhibitor 1 like. The Bax-inhibitor-1 region of the receptor molecules is conserved from bacteria to humans.	2.64027e-80
NZ_CP036299.1\|WP_145302247.1\|4227281_4228157_+\|DUF1559-domain-containing-protein	gnl\|CDD\|284919	pfam07596, SBP_bac_10, Protein of unknown function (DUF1559). A large family of paralogous proteins apparently unique to planctomycetes.	1.24618e-50
NZ_CP036299.1\|WP_145302234.1\|4223448_4224159_-\|carbonic-anhydrase	gnl\|CDD\|238449	cd00884, beta_CA_cladeB, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.	9.42399e-88
NZ_CP036299.1\|WP_145302274.1\|4237048_4238008_-\|methenyltetrahydromethanopterin-cyclohydrolase	gnl\|CDD\|235020	PRK02264, PRK02264, N(5),N(10)-methenyltetrahydromethanopterin cyclohydrolase; Provisional.	1.00634e-159
NZ_CP036299.1\|WP_145302259.1\|4231669_4232635_+\|endonuclease/exonuclease/phosphatase-family-protein	gnl\|CDD\|377028	pfam03372, Exo_endo_phos, Endonuclease/Exonuclease/phosphatase family. This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12, and Nocturnin.	3.59727e-15
NZ_CP036299.1\|WP_145302286.1\|4242312_4243392_-\|FAD-dependent-oxidoreductase	gnl\|CDD\|224169	COG1249, Lpd, Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase (E3) component, and related enzymes [Energy production and conversion].	1.03629e-16
NZ_CP036299.1\|WP_145302238.1\|4224312_4224900_-\|hypothetical-protein	gnl\|CDD\|275319	TIGR04526, predic_Ig_block, putative immunoglobulin-blocking virulence protein. Members of this family are putative virulence proteins of Mycoplasma and Ureaplasma species. Members share a region of sequence similarity (see TIGR04524) with protein M, a Mycoplasma genitalium protein that binds a conserved light chain region of IgG and blocks its protective function of antigen-specific binding. The seed alignment for this model includes an N-terminal signal-anchor domain and a proline-rich linker domain, and a C-terminal extension, in addition to the protein M-like domain recognized by TIGR04524. [Cellular processes, Pathogenesis].	0.00587471
NZ_CP036299.1\|WP_145302289.1\|4243833_4244985_+\|hypothetical-protein	gnl\|CDD\|319972	cd16344, LMWPAP, low molecular weight protein arginine phosphatase. Low molecular weight protein arginine phosphatases are part of the low molecular weight phosphatase (LMWP) family. They share a highly conserved active site motif (V/I)CXGNTCRS. It has been shown that the conserved threonine, which in many LMWPTPs is an isoleucine, confers specificity to phosphoarginine over phosphotyrosine.	1.6337e-54
NZ_CP036299.1\|WP_145302283.1\|4241810_4242449_+\|chemotaxis-protein-CheX	gnl\|CDD\|381734	cd17906, CheX, chemotaxis phosphatase CheX. This family contains CheX CheY-P phosphatase which is very closely related to CheC chemotaxis phosphatase; both dephosphorylate CheY, although CheC requires binding of CheD to achieve the level of activity of CheX. CheX has been shown to be the most powerful CheY-P phosphatase of the CheC-FliY-CheX (CXY) family. Structural and functional data of CheX and its CheY3 substrate in Borrelia burgdorferi (the causative agent of Lyme disease) bound to the phosphoryl analog BeF3(-) and Mg2+ reveal a unique mode of binding, but a catalytic mechanism which is virtually identical to that used by the structurally unrelated CheZ, providing a striking example of convergent evolution. Thus, CheX is quite divergent from the rest of the CXY family; it forms a dimer and some may function outside chemotaxis. The data also suggest a possible CheX regulatory mechanism through dissociation of the CheX homodimer.	5.62394e-17

>NZ_CP036299.1|WP_145302259.1|4231669_4232635_+|endonuclease/exonuclease/phosphatase-family-protein
MNGQWTRRVLKRSLLVAGFSWLLLSSTVTQAESPVVRVMSYNLWHGGDAGKQPLEQTARVIREARADLVGLQETRGYAASGQPRPDRAKEIAQILGWNYFDQGGGTAILSRYPIGKASPGKWGVEIEHPSGTKLYLFNAHLMYIPYQPYQLLNIPYGDYPFIKTEQEAIDFAKKARGEQVERLIADSKAAVPPDATVFVTGDFNEPSHWDWTAAAQKAGRCPIAVQWPSTSMMAETGFIDTYREAHPDPVTAPGITWTPITKITDPKDRHDRIDFVLMRQGGGKVLSSHVVGESKEAADVVIVPYPSDHRSVVSAVELTGK
>NZ_CP036299.1|WP_145302256.1|4229722_4231384_+|hypothetical-protein
MLSVRWVNLTSTLLLATCLMCAFSSTCQAHFLWVVDANQSADGKVHVYFSEEAAPDNPALLEKILGAKLWEANLHDDAVKVSPLKFEKGENSLEATFSPKSTNAGVFLDYGVMSKGGAEPYLLRYCGRSQTIANRKGGKVIGDAAVLPLEVVAERSGDGFLLRTFWQGQPAEGIEVTVDGGDLSARKEGVSNAQGELALGTLANGLYSIRVKKVLEEPGKLGDKEYKSIRIYSTTSLLIKPEAEVTQPAVSKALPELPRGITSFGGAVVGDVVYVYGGHTGGAHHYSKEDQSRELLALNVKQPSEWKVVGEGPERTGLSMVAVGTDLYRMGGFIADNGKEEKEVLKSTSDFARWDAASKQWIELPALPEPRSSLDAAVIGKTIYVVGGWNLNGGGKEAKWHETAWKCDVSANPPVWQPIANPPFLRRALSLAEHQGKLYVIGGMKNQGGPTTEVAIYDPATDSWSSGPALPGEGMEGFGNSAFAVNQNLFVSVMSGKVYKLSADGSKWDQVHQLEKPRFFHRMLPTSQHQLVFVGGASMEAGKAKTTEVLEVK
>NZ_CP036299.1|WP_145302253.1|4228874_4229678_+|hypothetical-protein
MKLCITIILLVIINLPTKFAQADPPLRFLRTEQGGVRLSLNTYTRVVMPDFHPPINTDSDSYSSGFVETAQESVTSASTILTNNAISHLQGDIVAEGDGDTTISAPAIVLGTHNISLDGSDPSDANLSASVGLDWDVEFVADNESELRENFGFYTVSVSVSYEAQALTSGIAHFNHGASGYIQVTVGEQIVTVYALDGVWVSDSNGIVTVTEPSSGIFSVSASSELFIEHDDVVDISGALWYNLTSATVDGGAVLGVSDMVIQVRVE
>NZ_CP036299.1|WP_145302250.1|4228350_4228809_+|hypothetical-protein
MFQKMTMLLLLFFGVFSFSGCGQNYIGRQPISGSILFDGTPMNEGTVRFIPDGQTKGPAAYGIIQDGFYEISHHEGVVPGTYRVEIEKKIELPFEIDDEAAYAKHLAEQKGRQFPRQPVPPKYNRNSELRVTIVPGRNASKLDFDLTTSENK
>NZ_CP036299.1|WP_145302247.1|4227281_4228157_+|DUF1559-domain-containing-protein
MRHLLPRRGFTLIELLVVIAIIAILIALLLPAVQQAREAARRTQCTNNLKQIGLAFHNYHDVHGAFCTTDGGTAATGSSAFAAILPQIDQGNLFLKYNFNLTNSDPANTAVTSQVIPAYLCPSAVLRRPVPMPGCTNTSTGRNIDDNRAPGTYAVNTGTTAGNGAIIPSSTGVTRLRDFTDGTSNTLLAGESAWNLPDYLFSSSASCAGQVRWGFTYWASPYNLSTAFVVQPPFNPKSGGSAVLSRFRSDHTGVVNMVFADGHVRFLSENIDSGLLSALATRSGGEVVGDF
>NZ_CP036299.1|WP_145302244.1|4226123_4227041_+|methyltransferase-domain-containing-protein
MTGSDESAQNPPSPRSPELSENRVEPLQDLSSQQPAFTEGTPKREKPEKSRRIEREFGIPIPGEILPPEQWVKTAIKALPSSGLLNWHEVFGQTLEQKQGIVLDLGCGNGRSTLWHAIVEPQYCYLGVDILPVVIRYATRRANQRGLGHLRFAVIGGKELLAQLVPAGSVSKICIYHPQPYYEEHLIGKRLVTPEFLAMAHQALVPGGELILQTDHPAYWQYMEQVVPAFFELRAIPGPWPDAPRGRTRREILATKRGLPVFRGVATRKEGLDRASAFEKASALPVPTFNADRRLLALDREEQSL
>NZ_CP036299.1|WP_145302241.1|4225134_4226232_-|hypothetical-protein
MQAADWRDPAKARLDFPKALVIWEMADSVLIRRILSSRPHPEEAFALLCKGIRNKFSSASLSLPPSTLILRWTSEDCSPARSTGTHAMKDLLYTLCPNRQSVSGCFWMPGRTCWLMLLGASAVLWHAVVFDQVEVIAAPPTVIDNPATTTAAPPQTAAVSQAERWNKELAAFDKENTMHPQRTGGLVFCGSSTIRLWKIKDSFPEYSPINRGFGGSRYDDLVRHAERILKPLQPAVLVIYSGDNDIAAKQSSEEVVQNFEKFHTWVRTELPETKIIVLGIKPSVKRWGMIESIRETNSQLAKICGKDPQATFIDTETVMLGADGQPIPELFVADGLHMSEEGYRRWAQLLRPYLEILHPVNHPTP
>NZ_CP036299.1|WP_145302238.1|4224312_4224900_-|hypothetical-protein
MASLHAIGETSLHSGLSQTGLFRQCFWRSWIFACGLLGIFGCDQINPPVPEVKPVAGFKRDDEDPPPPPQVTPPPAVVETVPEVKEPMPPPAPKLFTARLSSWRITPTQEKGVNGLLFQVEFEALENLNDVALLEISLLDNRSQEFRLLPMRDGNYIRVSKFVGNATAAGAPYSTVLWWKGVDGGNWKEAVRSRL
>NZ_CP036299.1|WP_145302234.1|4223448_4224159_-|carbonic-anhydrase
MRTLFAGLHQFHKEVYEKQRNLFEKLSSGQKPVALFIGCSDSRVVPDLIMMTNPGELFILRNAGNIVPPFGASTGGEAATIEFAVSALNVSDIIVCGHSQCGAIKALLNPASTEKLPMVRQWLLHAETTRRIMEENYPALAPAERYEVAIQEHVLVQLENLQTHPAVAVKLQRNQIALHGWVYQLETGQVHAFSTNTGIFEPLMGDKSMDSAALAQPVTSNVVNNANGSTPQSPPA
>NZ_CP036299.1|WP_145302231.1|4223006_4223438_-|hypothetical-protein
MNSAPQTAEISVTETNRLTPEKLQIRWKGFAPTVIIASGIALGGLYALGTRGGTQGLWMMLILGVTLGLTMTAAGMSWAGTIALAENAKKGLLFVLFPPYTLWRVIVRCDIFWQSMLVFVLGLIISFGCVWLASEGLKSQFAS
>NZ_CP036299.1|WP_145302264.1|4233886_4234750_-|flagellar-motor-stator-protein-MotA
MFVIIGFIVVTGCVLGGYTWAGGHVEALIHPSEVLTIGGASLGAMLVMGSPKILKDLIKSIIGALKGSPFNKKAYGDLFKLSYDLLKTARKDGLLALEPHLNDPHESKIFSKYPRLQKDHHFTTFLCDGLSSVVEASMSQEQLHDLLQKQIAVMDEEHHQAVGILAKSADAMPGFGIVAAVLGIVITMGAIDGPVEEIGHKVGAALVGTFLGILASYGFMAPLAARMDLLGKSEMDFYRTTAAIIEAAIGGAAPKQIIEQARRVVCSEARPERVELEKMLKEADAAA
>NZ_CP036299.1|WP_145302267.1|4235062_4236001_-|inositol-monophosphatase
MQSEFLINALSVHLPPILRWAGVIARRLRSHNISVATKTTGSALTDALTLADLTIQELLVAALRDVDPIFRHCRIEAEESTGDLDAFAQESEFVLALDPIDGTKQYRDHTGNGYAVMLHLRTASEMLYSLVYIPEKGVQGWWVEVTPERVVSGPDDWLRPATDVVRSLVVAEADRPTTSNKIYVIGFQHRDVMAASEITKCGYEGVAPDEMPGSIYELMASGEFAGSLIHSPNVYDFPVSMQIARYFGGNACWTDTGEPVHFRETWLDEKADMIRLPRVVACANDPQILAGLINLAKSWHPARYRPGDSLVE
>NZ_CP036299.1|WP_145302271.1|4236077_4237052_-|RimK-family-alpha-L-glutamate-ligase
MTAVLKMGVLSQPGNWSLEQIELAARERGHMVVPLEFSELAASCGSVTRSATWPIEITGQAFLKRSTEVMPRFELEELDALIVRSMPGGSLEQVVTRMNLLALAEQKGLPIINSPKSLECAIDKFLTTARLAHAGLPVPATFVCETAQAALEAFEKLGRNVVLKPLFGSEGRGIFRIEEPELLWRVAQTLVRTGAVLYLQEYIDHGGRDLRVLVLNGVPLGAIERMSQEDFRTNLSLGGQSMRTELDDEAASLAVAAAKTVGTVFAGVDLVRHPDGQWLLLEVNGVPGWKGFQAATGIPVAIRLIEYVEQLVELSQAGRSEPGG
>NZ_CP036299.1|WP_145302274.1|4237048_4238008_-|methenyltetrahydromethanopterin-cyclohydrolase
MNLELNELSLSIIEEVVESPDHFRIIAHESAGTGLLLDFGVEAEGSLEAGQVLSTVCMAGLATVNLQPQLLGKWQWPHVVVETDYPVAACLYSQYAGWQLSSGKFHAMGSGPMRAAAGVEPLFDKLWYKEEADHVVGILETAMLPPESIFEEISAKTGVEPADITLLIAPTSSVAGNYQVAARSVETAMHKLLELGFDVHRIRSGFGSAPLPPVAANDLQGIGRTNDAILYGSTVTLLMTGDDESIAEILPLVPSRSSSVFGKTFLEIFEAAGRDFYKIDKLLFSPAQVIVQNVDTGRVHVAGEPHVPLVLKSFGLVTE
>NZ_CP036299.1|WP_145302277.1|4238231_4238981_-|Bax-inhibitor-1/YccA-family-protein
MRTGNPVLNEGAFDRWAQEGGLSSSSVMTVSGAVNKSMVLIGLTASLGLLSFSYLQNNPQLLMPSLIGSAIGGLIASLCVCFWLRSAPVAAPIYALLEGVFLGGITTIFEARFPGIGVQAIAATVGVAAAMLLAYKVGLIRATATFRAGVIAATGGIGLVYLLAFVLSLFNIQAMSFVYDASLLGIGFTAFCVIIAALNLILDFDFIATAASQNLPKNYEWLAAHGLNVTLVWLYLEMLRLISKLQSRD
>NZ_CP036299.1|WP_145304621.1|4239299_4240271_+|RluA-family-pseudouridine-synthase
MAILSKTVTVEKYLAGVRVDSFLVKHFRSYTSWRILRMVAAGLVTIDGQVAATTQRVHPGQQVTIQLAEPPDLYIPPEPTPLEILFEDDSLLVINKPAGLIAHPTGEIPDGTLINAVQYYLDKQSTHPGLERPGIVHRLDRDTSGAMAICKEHLSHRLLSIQFQLGRISKSYLALVEGVLTEDKLVIDLPIGRAPGCSSALMSCRADALEAQASKTSLRVVERFPQHTLVEAKPRTGRMHQIRIHLATIGFPIVGDEFYLKEGEIRPLVWPESEREQVSPLINRQALHAACLSFAHPLTNEWQDFQAPLPDDLRQAIERARHG
>NZ_CP036299.1|WP_145302280.1|4240880_4241783_+|alpha/beta-hydrolase-fold-domain-containing-protein
MMHDDQRKPSRLIINQSLKLTRILGFLLIPLMAPVSLSAQFSYPPEFKEARVETYRKTGSTELKLWIFGESDPKTPKPAIVFFFGGGWNSGSPAQFENQARHFAKRGMIAIVADYRVKSRHNVQVVECVKDAKAAIAWVRENAKRLGVDPDKIAASGGSAGGHLAASTGTISGFGSDERPNAMILFNPACTLAPIAGWQPPGARAKLSTERFGVEATAISPAHHVGPQTPPTLILHGTKDTTVPYASVVAFEAEMKKAGRPCKLVGYEGAEHGFFNRGENYDKTLAEADRFLVELGWIKK
>NZ_CP036299.1|WP_145302283.1|4241810_4242449_+|chemotaxis-protein-CheX
MRFIGYPCTNTPLSRRTAFRLFESPSASMHFVIPNVSGFVVTEPYASPSAWIIPFCDAATEVFLCMLQATCQIQSIRPPDSAPPLESITIAIDLTGTAPGRVILSVAESVADQFVERLTGFGAEGDLGLLRDIVGEVANMVAGSGKGNLPQLGFLIGTPRQLTAEEFINLSANWPLRQTATLETSFGLCLLDVSWNFQFATPSADTPLPETV
>NZ_CP036299.1|WP_145302286.1|4242312_4243392_-|FAD-dependent-oxidoreductase
MYDCTIAGGTALAVEVATTAAQLGLRTALIEPASAWEISSESVGAQWSPEFLEMITQNEFAAAMSSQTLARRLLPYGRREQERQQRLLREARVDCFAGAAKVVGADGASIAVMAMSAANPSVKQPVVDGPLLMTHLLIVATGSVVAPVHHGVLPHTPHESMNSKSSLPSSLGELLLTRSVPQSMVVLGSNRWAQAVARIYSRLGSDVLLLGRRLPERQKSTEWQEFRAGIRGLRQRGDYCEVEICNGERVLVQTVVSCQTEVGVTVELDLGKVGIESDECGKLWCDAMGRTWHPQILAMGSVVGFPEELQQPRNIRQFLEEVYLLKESRTESSSSHPAGISRMKSPKWLSASKASLPTN
>NZ_CP036299.1|WP_145302289.1|4243833_4244985_+|hypothetical-protein
MTDIVEIRRSDDPRDVIHRVCQSLAQGELVGLPTETTYTVAASALSEVGIQRLKSLATELAVNHQAPQFELLLKAADEALDYLVEQSRYGRKLIRRCWPGPVTLRFPKSHCGWFFEQLPETSRHLLTAPENTVSFRVPAHTLPADILNLLPGPLIALSEAQPGQPPLRHARDADQRFGNNLALIVDDGPSRYGEPGTVVQIGNNDWNIAFPGVVSERTMGRLASEVILFACTGNTCRSPMAEVLFRKLLAEKLNCPEEELVDHGYVILSAGLAAAIGAPANPEAIALLADEGLDLRNHESQPLTERLLQQVDMIYTMTRGHRDAILAERPDLASRVRTLSPAGKDIADPIGGGRDVYRSCKQIIETHLQQIIQDLLSLRSHPS

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP036299_1	1.3\|2103132\|25\|NZ_CP036299\|CRISPRCasFinder	2103132-2103156	25	NZ_CP036299.1	2103228-2103252	2	0.92

1. spacer 1.3|2103132|25|NZ_CP036299|CRISPRCasFinder matches to position: 2103228-2103252, mismatch: 2, identity: 0.92

gacctgcacaatcaagaagccggtc	CRISPR spacer
gacctgcacagtcaagaagcctgtc	Protospacer
**********.********** ***

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP036299_1	1.2\|2103084\|25\|NZ_CP036299\|CRISPRCasFinder	2103084-2103108	25	NC_007974	Cupriavidus metallidurans CH34 megaplasmid, complete sequence	1734391-1734415	4	0.84
NZ_CP036299_1	1.2\|2103084\|25\|NZ_CP036299\|CRISPRCasFinder	2103084-2103108	25	NZ_CP046333	Cupriavidus metallidurans strain FDAARGOS_675 plasmid unnamed3	1892919-1892943	4	0.84
NZ_CP036299_1	1.4\|2103180\|25\|NZ_CP036299\|CRISPRCasFinder	2103180-2103204	25	NC_010811	Ralstonia phage RSL1, complete genome	144567-144591	5	0.8
NZ_CP036299_1	1.4\|2103180\|25\|NZ_CP036299\|CRISPRCasFinder	2103180-2103204	25	AB366653	Ralstonia phage RSL1 DNA, complete genome	144567-144591	5	0.8
NZ_CP036299_1	1.2\|2103084\|25\|NZ_CP036299\|CRISPRCasFinder	2103084-2103108	25	NC_008739	Marinobacter hydrocarbonoclasticus VT8 plasmid pMAQU02, complete sequence	71803-71827	6	0.76

1. spacer 1.2|2103084|25|NZ_CP036299|CRISPRCasFinder matches to NC_007974 (Cupriavidus metallidurans CH34 megaplasmid, complete sequence) position: , mismatch: 4, identity: 0.84

gacctgcacgatcaagaagccggtt	CRISPR spacer
gacctgcgcgatcatgaagccggag	Protospacer
*******.****** ********

2. spacer 1.2|2103084|25|NZ_CP036299|CRISPRCasFinder matches to NZ_CP046333 (Cupriavidus metallidurans strain FDAARGOS_675 plasmid unnamed3) position: , mismatch: 4, identity: 0.84

gacctgcacgatcaagaagccggtt	CRISPR spacer
gacctgcgcgatcatgaagccggag	Protospacer
*******.****** ********

3. spacer 1.4|2103180|25|NZ_CP036299|CRISPRCasFinder matches to NC_010811 (Ralstonia phage RSL1, complete genome) position: , mismatch: 5, identity: 0.8

ctgctacaccaagtgccgtcctgtg	CRISPR spacer
tcgctacaccaagcgccgtcctgac	Protospacer
..***********.*********

4. spacer 1.4|2103180|25|NZ_CP036299|CRISPRCasFinder matches to AB366653 (Ralstonia phage RSL1 DNA, complete genome) position: , mismatch: 5, identity: 0.8

ctgctacaccaagtgccgtcctgtg	CRISPR spacer
tcgctacaccaagcgccgtcctgac	Protospacer
..***********.*********

5. spacer 1.2|2103084|25|NZ_CP036299|CRISPRCasFinder matches to NC_008739 (Marinobacter hydrocarbonoclasticus VT8 plasmid pMAQU02, complete sequence) position: , mismatch: 6, identity: 0.76

gacctgcacgatcaagaagccggtt	CRISPR spacer
atcctgcacgatcaagaagcccacg	Protospacer
. ******************* ..

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

4792899 : 4837753

Paenibacillus_phage(50.0%)

transposase

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_145304682.1\|4792899_4793034_+\|transposase	transposase	NA	NA	NA	NA
WP_145303384.1\|4793502_4793721_+\|transposase	transposase	NA	NA	NA	NA
WP_145303403.1\|4793848_4794874_-	beta-ketoacyl-ACP synthase III	NA	NA	NA	NA
WP_145303408.1\|4796811_4803642_+	AMP-binding protein	D0R7J2	Paenibacillus_phage	6.7e-29	33.8
WP_145303412.1\|4803587_4804883_+	beta-ketoacyl-ACP synthase II	NA	NA	NA	NA
WP_145303415.1\|4804915_4805158_+	acyl carrier protein	NA	NA	NA	NA
WP_145303419.1\|4805154_4806183_+	hypothetical protein	NA	NA	NA	NA
WP_145303422.1\|4806302_4807451_+	StlD/DarB family beta-ketosynthase	NA	NA	NA	NA
WP_145303426.1\|4807522_4808743_+	beta-ketoacyl-[acyl-carrier-protein] synthase family protein	NA	NA	NA	NA
WP_145303429.1\|4808760_4809978_+	beta-ketoacyl-[acyl-carrier-protein] synthase family protein	NA	NA	NA	NA
WP_145303433.1\|4809974_4811231_+	hypothetical protein	NA	NA	NA	NA
WP_145303437.1\|4811264_4812164_-	hypothetical protein	NA	NA	NA	NA
WP_145303440.1\|4812309_4813110_+	hypothetical protein	NA	NA	NA	NA
WP_145303443.1\|4813184_4813940_-	ATP-binding cassette domain-containing protein	G9BWD6	Planktothrix_phage	2.8e-37	39.7
WP_145303446.1\|4814033_4814267_-	acyl carrier protein	NA	NA	NA	NA
WP_145303451.1\|4814512_4815754_-	FtsX-like permease family protein	NA	NA	NA	NA
WP_145303454.1\|4815809_4817054_-	efflux RND transporter periplasmic adaptor subunit	NA	NA	NA	NA
WP_145303457.1\|4817929_4820083_+	TolC family protein	NA	NA	NA	NA
WP_145303461.1\|4820668_4821436_-	alpha/beta fold hydrolase	NA	NA	NA	NA
WP_145303464.1\|4821509_4822022_-	dehydratase	NA	NA	NA	NA
WP_145303467.1\|4822071_4823064_-	sulfotransferase	NA	NA	NA	NA
WP_145303470.1\|4823185_4824403_-	hypothetical protein	NA	NA	NA	NA
WP_145303473.1\|4824519_4825128_-	sulfotransferase	NA	NA	NA	NA
WP_145303477.1\|4825633_4827094_-	hypothetical protein	NA	NA	NA	NA
WP_145303481.1\|4827228_4827948_-	SDR family oxidoreductase	NA	NA	NA	NA
WP_145303485.1\|4828438_4829260_-	methyltransferase domain-containing protein	NA	NA	NA	NA
WP_145303489.1\|4829352_4830846_-	hypothetical protein	NA	NA	NA	NA
WP_145303494.1\|4831121_4832162_-	zinc-binding dehydrogenase	E3SJ82	Synechococcus_phage	8.1e-11	26.0
WP_145303499.1\|4833136_4833682_+	hypothetical protein	NA	NA	NA	NA
WP_145303502.1\|4834020_4834329_-	hypothetical protein	NA	NA	NA	NA
WP_145303505.1\|4834985_4835810_-	hypothetical protein	NA	NA	NA	NA
WP_145303508.1\|4836292_4836502_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_145304685.1\|4836529_4836820_+	winged helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_145303511.1\|4836871_4837210_+\|transposase	transposase	A0A0N9SHJ4	Paenibacillus_phage	1.2e-08	33.0
WP_145303514.1\|4837251_4837428_+\|transposase	transposase	NA	NA	NA	NA
WP_145303518.1\|4837428_4837593_+\|transposase	transposase	NA	NA	NA	NA
WP_145303521.1\|4837606_4837753_-\|transposase	transposase family protein	NA	NA	NA	NA

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_CP036299

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