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_CP053419	Cellulosimicrobium sp. 72-3 chromosome, complete genome	3 crisprs	csa3,WYL,DEDDh,DinG,cas3,PD-DExK	0	4	0	0

Cas Category Instructions

Results visualization

1. NZ_CP053419

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP053419_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053419_1

486312-486403

Orphan

Consensus_repeat	Method
AGGCTGCTGGCGTGGTCGACCTCCGCCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053419_1

>merge|NZ_CP053419|1|486312-486403|CRISPRCasFinder
AGGCTGCTGGCGTGGTCGACCTCCGCCTGTGGAGGACCACGACCGCTGCGCCGCCGGGTTCGTTAGGCTGCTGGCGTGATCGACCTCCGCCT

>NZ_CP053419|1|1|486312-486403|CRISPRCasFinder
AGGCTGCTGGCGTGGTCGACCTCCGCCT	GTGGAGGACCACGACCGCTGCGCCGCCGGGTTCGTT
AGGCTGCTGGCGTGATCGACCTCCGCCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053419.1\|WP_171467355.1\|497280_498258_-\|NAD(P)H-quinone-oxidoreductase	unknown	unknown	gnl\|CDD\|176180
NZ_CP053419.1\|WP_171467350.1\|480302_485003_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053419.1\|WP_076403734.1\|479350_480298_+\|choloylglycine-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|238303
NZ_CP053419.1\|WP_021483010.1\|494598_495549_+\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_CP053419.1\|WP_171467347.1\|474216_474642_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053419.1\|WP_043655287.1\|492034_493441_+\|carbohydrate-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|224567
NZ_CP053419.1\|WP_171467349.1\|477332_478475_-\|mandelate-racemase/muconate-lactonizing-enzyme-family-protein	unknown	unknown	gnl\|CDD\|239432
NZ_CP053419.1\|WP_171467353.1\|489771_490563_-\|type-I-methionyl-aminopeptidase	unknown	unknown	gnl\|CDD\|238519
NZ_CP053419.1\|WP_034652574.1\|493618_494602_+\|sugar-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224096
NZ_CP053419.1\|WP_171467348.1\|474660_476103_-\|sugar-porter-family-MFS-transporter	unknown	unknown	gnl\|CDD\|340917
NZ_CP053419.1\|WP_171468647.1\|487555_488497_+\|HAD-family-hydrolase	unknown	unknown	gnl\|CDD\|369792
NZ_CP053419.1\|WP_086149329.1\|476562_477336_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|235546
NZ_CP053419.1\|WP_043655291.1\|490751_491762_+\|LacI-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224525
NZ_CP053419.1\|WP_171467354.1\|496593_497226_-\|bacterial-proteasome-activator-family-protein	unknown	unknown	gnl\|CDD\|378489
NZ_CP053419.1\|WP_076403726.1\|495659_496580_+\|EamA-family-transporter	unknown	unknown	gnl\|CDD\|227339
NZ_CP053419.1\|WP_076403736.1\|476143_476566_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377776
NZ_CP053419.1\|WP_171467352.1\|488541_489471_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053419.1\|WP_021482493.1\|478586_479228_+\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224715
NZ_CP053419.1\|WP_171467351.1\|485115_486249_-\|diacylglycerol-kinase	unknown	unknown	gnl\|CDD\|224513
NZ_CP053419.1\|WP_021482310.1\|473878_474220_-\|transcriptional-regulator	unknown	unknown	gnl\|CDD\|316153

Protein	Function_ID	Function_description	E-value
NZ_CP053419.1\|WP_086149329.1\|476562_477336_-\|SDR-family-oxidoreductase	gnl\|CDD\|235546	PRK05653, fabG, 3-oxoacyl-ACP reductase FabG.	9.98943e-64
NZ_CP053419.1\|WP_021483010.1\|494598_495549_+\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	4.88509e-84
NZ_CP053419.1\|WP_171467349.1\|477332_478475_-\|mandelate-racemase/muconate-lactonizing-enzyme-family-protein	gnl\|CDD\|239432	cd03316, MR_like, Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).	1.22289e-116
NZ_CP053419.1\|WP_043655287.1\|492034_493441_+\|carbohydrate-ABC-transporter-substrate-binding-protein	gnl\|CDD\|224567	COG1653, UgpB, ABC-type sugar transport system, periplasmic component [Carbohydrate transport and metabolism].	3.28898e-24
NZ_CP053419.1\|WP_171467354.1\|496593_497226_-\|bacterial-proteasome-activator-family-protein	gnl\|CDD\|378489	pfam10759, DUF2587, Protein of unknown function (DUF2587). This is a bacterial family of proteins with no known function.	8.6035e-87
NZ_CP053419.1\|WP_171467353.1\|489771_490563_-\|type-I-methionyl-aminopeptidase	gnl\|CDD\|238519	cd01086, MetAP1, Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.	4.69708e-114
NZ_CP053419.1\|WP_034652574.1\|493618_494602_+\|sugar-ABC-transporter-permease	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	8.07263e-65
NZ_CP053419.1\|WP_171467348.1\|474660_476103_-\|sugar-porter-family-MFS-transporter	gnl\|CDD\|340917	cd17359, MFS_XylE_like, D-xylose-proton symporter and similar transporters of the Major Facilitator Superfamily. This subfamily includes bacterial transporters such as D-xylose-proton symporter (XylE or XylT), arabinose-proton symporter (AraE), galactose-proton symporter (GalP), major myo-inositol transporter IolT, glucose transport protein, putative metabolite transport proteins YfiG, YncC, and YwtG, and similar proteins. The symporters XylE, AraE, and GalP facilitate the uptake of D-xylose, arabinose, and galactose, respectively, across the boundary membrane with the concomitant transport of protons into the cell. IolT is involved in polyol metabolism and myo-inositol degradation into acetyl-CoA. The XylE-like subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	6.60902e-125
NZ_CP053419.1\|WP_076403736.1\|476143_476566_-\|hypothetical-protein	gnl\|CDD\|377776	pfam07100, ASRT, Anabaena sensory rhodopsin transducer. The family of bacterial Anabaena sensory rhodopsin transducers are likely to bind sugars or related metabolites. The entire protein is comprised of a single globular domain with an eight-stranded beta-sandwich fold. There are a few characteristics which define this beta-sandwich fold as being distinct from other so-named folds, and these are: 1) a well conserved tryptophan, usually following a polar residue, present at the start of the first strand; this tryptophan appears to be central to a hydrophobic interaction required to hold the two beta-sheets of the sandwich together, and 2) a nearly absolutely conserved asparagine located at the end of the second beta-strand, that hydrogen bonds with the backbone carbonyls of the residues 2 and 4 positions downstream from it, thereby stabilizing the characteristic tight turn between strands 2 and 3 of the structure.	1.40328e-60
NZ_CP053419.1\|WP_043655291.1\|490751_491762_+\|LacI-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	5.03817e-99
NZ_CP053419.1\|WP_076403734.1\|479350_480298_+\|choloylglycine-hydrolase-family-protein	gnl\|CDD\|238303	cd00542, Ntn_PVA, Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer.	1.45275e-126
NZ_CP053419.1\|WP_076403726.1\|495659_496580_+\|EamA-family-transporter	gnl\|CDD\|227339	COG5006, rhtA, Threonine/homoserine efflux transporter [Amino acid transport and metabolism].	7.15625e-60
NZ_CP053419.1\|WP_171468647.1\|487555_488497_+\|HAD-family-hydrolase	gnl\|CDD\|369792	pfam08282, Hydrolase_3, haloacid dehalogenase-like hydrolase. This family contains haloacid dehalogenase-like hydrolase enzymes.	4.2713e-53
NZ_CP053419.1\|WP_171467355.1\|497280_498258_-\|NAD(P)H-quinone-oxidoreductase	gnl\|CDD\|176180	cd05276, p53_inducible_oxidoreductase, PIG3 p53-inducible quinone oxidoreductase. PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	4.43015e-167
NZ_CP053419.1\|WP_021482493.1\|478586_479228_+\|GntR-family-transcriptional-regulator	gnl\|CDD\|224715	COG1802, GntR, Transcriptional regulators [Transcription].	7.34202e-39
NZ_CP053419.1\|WP_171467351.1\|485115_486249_-\|diacylglycerol-kinase	gnl\|CDD\|224513	COG1597, LCB5, Sphingosine kinase and enzymes related to eukaryotic diacylglycerol kinase [Lipid metabolism / General function prediction only].	8.85612e-36
NZ_CP053419.1\|WP_021482310.1\|473878_474220_-\|transcriptional-regulator	gnl\|CDD\|316153	pfam13601, HTH_34, Winged helix DNA-binding domain.	1.00397e-22

>NZ_CP053419.1|WP_171467351.1|485115_486249_-|diacylglycerol-kinase
MAWTLWVAIAALAVAVVALVVALGLRAQQSRLRRAHGADLPVEETPPDDDPRELVAFVANPSKPDVVGLEAVVRRAFADAALPDPLWFETTIADPGVGQTRAALAQGADVVVAVGGDGTVRAVAEGMVGSGRTMGLVPVGTGNLLARNLDLPVGDARAALAVVIAGSDRPIDVGWVTVLRYADPAGPGDVEGTALDPARAPGKEHIFLVIAGLGFDAAMVADADDELKAKVGWVAYFVAGIRHLHGRRMRARIQLDDSPPVDARLRSLMIGNCGRLPGGITLLPDAVIDDGVLDVAAVDTRGGVVGWAQLFGEVVMQGLGVRNDLPAKIGRIDHARARRVRVRVEEGEQAQVDGDVLGLAVEIETRVDPGALVVRTA
>NZ_CP053419.1|WP_171467350.1|480302_485003_-|hypothetical-protein
MTFPAAALPPARTQPARRDRGLGPRTAALATAVALLLTLLATAGPAAATTAAGSAAATTAGPSAATTTAAAPTVTQGGPATTGATVASGSLAAAPAHDPRPVVLVAVAGLYWSDVSPTATPTLWSMIRTGSVASLNLGRTACTTDAWLTLSAGRMVSAQAEEAPVEPLPADAEEPASGCLPLPVPAVATTGTTTPDARPADVPGWAVLTTPATEETPAQAARHDPGTAAARLVETGVCTTAVGPGAAVMLADAVGHVERYAPSLAALPDGGLDACDVTVVDQGEIVDSATGRGESLDELDEALARVMDEVDRGTRVVVAGVSAGPVSEAGLQVVVDWRKGQPTSRWLHSPSTQQDGIVQLADLTATVVESAGGSTEGLEGAALEQGEVRRMDVARTVENRQYLNVLTSTIPTLYPVLVGLLVATLVLALGGVLWARRAAVRRGREPGPGPRGLRVLSAVLMVAAAAPVAASLASLSRWWVWSAPAPALTLALAVSAVVVALVAWVVSRLLPRRPWALPSALAGVTWLVLTVDGATGTTLQQASLLGTSAVVGFTRFYGFNNVTFAVYAVAGLVLAGGLASAATARGRRRLAAWSVVAVGVVTVVIDGWPAFGADFGGILALVPAFAVLALLVGRIRITWLRALVVALATVLVVVVVAVVDWLLPGGRSHLGGFVQTVVDGAALDVIGRKALGAWATLANPLGAVAAVLVVLVAVAVLRPERFRLPEVARAYENWPVLRPLVVALVVVAGVGSVLNDSGVIIAVMVVVVATAMIVPGFLARPAPRQTTGAVPEPGIRRMPTMLATVGGGLLLVVLLAATVLASTGLRPAASAAPAGGEASVTRSDAIATDRPVVVVGTTGVTWSDVTSSATPTLHALLTDGAGAGGVSQPTGAASRCTVGGWLALSAGQLAEVTTERAPDGAWACPTAQPAPDGADGAQVEGWDDLVALQRGSGYQARLGVLGDALAAAGADGAVCATAVGPGAAVALADSAGQVARYRDLADTTAPGSDAFACPVTVVDAGDATPPVVDPDLPADERATLRSTLRADRLTAVDATVGAVLDAAPSGTTVLVVDVAGAPGTRPALGTTLVRPSSDGPDQSRYLTSAATRTDGVARVLDVPATVLDAAGAATPARIQDTPLAWGSPRPADATSTADALADLTTRDHVRRAVYTAFVDVPLYAGLVIAGLCLLLAPRAARATGDRARARWARAAHWARGAALVVAAVPTAAFLVSLTGWWRFGNQTLAIVVSTVLATAAVAGLGALAPRRPVWLGPGIVAGITFAVLTLDALVGTPLNRASPLGSAPTFGARFYGFGNPTFSVYAVAALVVAAALAQWLVARGHRYAAAATVGVIGLVTMVVDVWPTLGADLGGGLVVVPAFAVLGLAASGARVTWRRFLLVATAGVALVAAIGVLDWLRPADERSHLGRFVGQVVDGSAWETLLRKAGYAARSVLGGVPVWLTIAVLVAAALLLFWPRRFTPRWFARTEAAWPLVRPTLLALWIVAVAGSLVNDFGVRIALIALIPAVPLLTVAALHAADAGDRDGEREDPDERAGAGSASRVESATS
>NZ_CP053419.1|WP_076403734.1|479350_480298_+|choloylglycine-hydrolase-family-protein
MCTGIRFSDDQGSVYLARNLDWTSGYGQQVVVTPTGYAPRSPFGAVRSIEHAVIGMGIVEEDTPLYFDCGNDAGLAVAGLNFPGYAAYAPGPVDGAVNVAAFELPLWVCAQFASVDEVEAALADVVVVDRPINEKYPSSLLHWIVADAQRAIVLEHTADGLHVFQDDVDVLTNQPGFDWHHENLRNYLNVSPDFPEDTVVGRAHLAPFGSGSHMRGVPGDYYSPSRFVRAAYVNSHYPTKGTEEENVSRAFHTLQQVAMVDGCAAMGSGEFEITVYTGLFSSRTSTYYWNTYEDPAIRSVALGDHATGGTELVLV
>NZ_CP053419.1|WP_021482493.1|478586_479228_+|GntR-family-transcriptional-regulator
MPVLPASPPESRRDWVLRHLRERIASGDLAAGDRLVERDLSAAYGISRGPVREAIMVLEQEGLVVSHPYRGAVVVDISQEEIAEILVPVRTVIEKVAFRSAARAQDPALLDALDRTVAAMERAADPLDARRLADLDLEFHEAVIAAASHTQSLQIWRLIQPRVRAYFVRDAPHHEDPHAVVEQHRDLLAALRSADPDRAERAVEEHIAVYLQP
>NZ_CP053419.1|WP_171467349.1|477332_478475_-|mandelate-racemase/muconate-lactonizing-enzyme-family-protein
MRITAITAAGLRGATPEGGWQEELRQDDVVHTLVAVHTDEGLVGVGSVFTTEDLVRGALDVLRSLLLGANALEPERTSERLHRTTFWMGRGGSITHAISGVDTALWDLLGQATGQPVGRLLGGRYRDRVRPYASLLMDEPDALRDHLTALRAEGWTAFKIGWGPFGRVDERLDERIVAAARDAVGPDAMLMVDAGGSDSAWSQGYKWALRTARMLDAYGVAWFEEPLPPDAIEDYTHLRRRSPVPISGGEVLTRRQAFQPWIEGGALDIVQPDVTKVGGTSELRRIAWSAHDHGVKLVPHGWNTAVGLATDLQLASALPDTDLVEYVTGSPYIDDLTTDRWTLDADGMLPIPDGPGLGITLDRDRLARYCDVDALLRSAS
>NZ_CP053419.1|WP_086149329.1|476562_477336_-|SDR-family-oxidoreductase
MSPRSLVVTGAASGIGRAVAVGAARDGWFVHVLDLDPDGAAATVDLARQAGGDGRAHVLDVTDAAAVAAAVGTVAESGPPLRGLFAGAGIDVGGAAHELDPATWRRVLDVNVTGTFLVVREVLRAMIDGDGGSVVLCGSPAATVGFAAGGATAYGASKGAVSSMVRTLAVDYARHGVRVNAIVPGPTETPLMWANVPADEVAATRAQIEHEVPLGRLARPEEIAEPVLWLLSDRSSYTTGSLVGCDGGVLAKSSISV
>NZ_CP053419.1|WP_076403736.1|476143_476566_-|hypothetical-protein
MSAPDAPARRPRVGATCWAIGDGWIPPYGTGDDPTLASHESLCLLNAGPDDARVEIRLYFADRPPAGPYVVVVPAERVRHVTLNDLDDPEPVPRGTDYSAVVVASAPVVVQHTRLDSRQAANALFSTIAHPVDTLREDLR
>NZ_CP053419.1|WP_171467348.1|474660_476103_-|sugar-porter-family-MFS-transporter
MNAATGRLGHGALTPLVVASTVGAALGGFMFGFDTAVVNGAVDALKAELGVGSALVGVIVASALLGAAVGAFAAGTIADRFGRRRLMMVAGTLFVTTSMLCAVAHDGPTLALWRFLGGVGVGMASVVAPLYIAEIAPARLRGRLATAQQMSIVLGIFAALVSNASLVRAAGGAEAELALGLPAWRWMFLVAVVPSLAYVVAAVLLPESPRYLVMRGDRDGAARTLRRLHRVPEGDALLGVATIEGTLHEARPAWSHLFSGPGRLKPIVWLGIALAALQALVGIDVIFYYSTSLWAQVGFGEQQAFWLSALTSLVNVAATVVAIFLVDRVGRRRLLLVGSVGMTVALAVMATGFAQAQQTADGVAFVDAWGVVTLVAANVFVVAFAVSWGPVVWILVGEMFPNLLRARAASLAAAANWAAGIAVNLTFPSLRDLSLPGSYALYAVFAAASFVLVLRALPETANRPLEEMREDTASGGQQSL
>NZ_CP053419.1|WP_171467347.1|474216_474642_-|hypothetical-protein
MIPNSITPEQARRQLGQAEEVAAQAHRATRWYPWLSVGHAVAALAYTIAIDALDAPWWPATTVLVVVLALLWSAVARHHRTAPRHWVRDMGIALITWAVLYFVMLDPALQLVGATSPAWWVVAGVVAASPFAACAFASARR
>NZ_CP053419.1|WP_021482310.1|473878_474220_-|transcriptional-regulator
MSHPRKGLDALIHSPVRFSILAALANVESADFRFLADLVELSDSSLSQALTALSDAGLVEIRKEAAGRRTRTWVRISDRGLDAFRQHVRTLEQIARTGAIEPQPDPTPRGTAP
>NZ_CP053419.1|WP_171468647.1|487555_488497_+|HAD-family-hydrolase
MDRRDPREPPAARRVGPRARRAAAVPRRPRGPRAGGGVTDARETTDAAEPLLVALDIDGTLMSYDQELSEDVRDAVADLRAAGHHVVLASGRSLIAMTPVAEILGIDRGWVVASNGAVTARLDPDEPDGYVLEDVVTFDPGPALRLLREHLPDARYAVEDVGVGFRMNELFPDGELDGVHRVVEFDELWSGEVTRVVVRAPGSTSEQFHELVERLGLDDVTYAVGWTAWMDLAPLGVTKATGLELVRRTLHVQPHRTVAVGDGRNDVEMLRWAARGVAMGHADDVVQAAADEVTGTIEDDGAARVLQSLLPAR
>NZ_CP053419.1|WP_171467352.1|488541_489471_-|hypothetical-protein
MTLGGGEPLPASPAVSPSPSCAPGAVDTDTTESVAVVEDFFASLEAGRASDAAALTTIDLDEDLVDDDFYRASVARPTDARVVASSGSSAGASVTVEFTLDGVDGPVSLEVRTTRDGDRTTISDLGTADTIGAGQPVSGTLTVNGQVEYPAAELTPVTLLPGAYAVEYTDPTGLLEGLRRGSSFTAFAPDVVREDGVVAEGFAFTPTLRPDVEPGVEEAVEGLRAACEDEGLAGPSCPSELVENARETSRTEWFAEPGPEIRYVDGAYEATAEYTVLLWDDGDLPVEVRASYTGTVARDAAGKITFTRP
>NZ_CP053419.1|WP_171467353.1|489771_490563_-|type-I-methionyl-aminopeptidase
MIELRTPREIEQMRPAGRFVADVLTTVRAATKVGTNLLELDEIAHRMIRDRGAESCYIDYHPSFGASPFGKVICTSVNDAVLHGLPHDYALRDGDLLSIDFAASVDGWVADSALSFVVGTPRAGALGEADARLIQTTERALEAGIAAAQPGKKVGDISAAIADVAHAAGYSVNTDFGGHGVGRTMHGEPHIPNDGRRKRGFPLKPGLVIAIEPWFLETTDEIYTDPDGWTLRSADGSRGAHSEHTVAITEDGPVVLTAREPRD
>NZ_CP053419.1|WP_043655291.1|490751_491762_+|LacI-family-DNA-binding-transcriptional-regulator
MAGIDDVAQAAGVSTATVSRALRGLPNVSEATRLRVLAEAARLGYVPTPSASSLATGRTRTIGVLTPWVNRWFFANVIEGAERALRDLGYDVLLYTFDVRRTSSRRRVDPSVLRHRVDGTLVVGLPLDDDEVRSLVGLARPLAFVGSGPAEQVTVRLDDVATGRAATRHLLDLGHRVIGHVTGVPDLVSSWSPPVERARGYVRALEEAGVVVQPDLEVNGDFDVAGGRESTAELLRRRPDVTAVFAASDEMAMGAILAARDLGLRVPEDLSVVGVDGHDLGELVGLTTIAQDAYQQGFDAALLLLDMINGAPVPESLTYPTELVRRGSTAPLAPGA
>NZ_CP053419.1|WP_043655287.1|492034_493441_+|carbohydrate-ABC-transporter-substrate-binding-protein
MTRTTRTSAARRRTLAVAAGGASLALVLGACSSGGGGGGDDESPSAEVDCADFEQYGDLSGKTVSVYSTIVDTEAEQQQASYEPFEECTGATIEYEGSKEFEAQLPVRIQSGSAPDIAYLPQPGLLRRIVADFPDAIQPVGDQAAANVDQYYTESWKDYGTVDGTLYATPLGANVKSFVWYSPSMFEEAGYEVPTTWDELMELSDQIVADNPEGDVKPWCAGIASGEATGWPATDWMEDVVLRTAGPDVYDQWVNHEIPFNDPQIATALAAVGDVLKNEDYVNGGLGDVSSIATTEFTEGGYPIIDGLCYMHRQATFYQANWTTLDPDLEVAEDGDVWAFYLPGESADDKPLLGGGEFVAAFNDRPEVQAFHAYLSSPEWSNAKASVTPQGWISANNGLDPELLQSPMDQQAYELLTDESYTFRFDGSDMMPAAVGAGSFWSEMTEWIASDKSDQAVLDAIEASWPTS
>NZ_CP053419.1|WP_034652574.1|493618_494602_+|sugar-ABC-transporter-permease
MDWLLEPSGTGGKLAVMVVAILLFVVVMGLILFLVDRPKRVPGWVVAIAFAGPAVVMLAFGLLYPGLRTIRDSFYNRTGSAFVGLDNYVTAFTRDEFQIVLRNTAIWVIVVPLVSTFLGLVYAVVVDRSRFEKLAKTLIFLPMAISMVGAGIIWKFMYEYKPASQPQIGLFNQVLVWLGLEPQQFLLSAPANTFFLILVMIWIQAGFAMTILAAAIRAIPDDIVEAARLDGVGGMRMFRYITVPSIRPALVVVLTTIAIGTLKVFDIVRTMTGGRFETSVVANEFYTQALRQGEQGLGAALAVILFVLVIPIIVYNVRQLKQAEEIR
>NZ_CP053419.1|WP_021483010.1|494598_495549_+|carbohydrate-ABC-transporter-permease
MSTPLSASVPDAPLVDETVEEGSGKGVVAGLDARADKVRRKVSSRPASIIAIVLAVLWTIPTFGLLVTSFRPPREIRRSGWWEAFANPEFTVDNYTDALFGGSTSFATYFVNSLVITLPAVIIPITLASLAAYAFAWVNFKGRNLLFVAVFALQIVPIQVTLVPLLTQYVDWGIDGSFWPVWLSHSIFALPLAIFLLHNFMKDIPRELVEAARVDGAGHVKIFFQVLMPLLVPAIAAFGIFQFLWVWNDLLVALTFASGQDTAPITVRLAELSGSRGASWHLLPAGAFISMVVPVVVFLALQRYFVRGLLAGSVKG
>NZ_CP053419.1|WP_076403726.1|495659_496580_+|EamA-family-transporter
MPTRTAALDRVPAPALFVVSGLTQYLGAAIAVGLFAVAGAVEVGWLRIAASALLLLAWRRPWRRRWTRHDLAWAAVFGVALAAMNLAFYVAIDHLPLGTAVAIEFLGPVAVAAVTGSGWRERGAIAVAAAGVVLLAGVTVGSDLPHDDAVLGLAAIAVAAACWAAYIVLGRRVAVGGSGVTSLAVGMAVGALAFAPFLAPDAVPVLGDWRHALAVAGIALFSSVVPYALEQVILRRVSAATFSVLLALLPATAAVVGAVVLRQVPSPLELVGLVLVSGAIAMTAARPGASGRGEPDGVLPTDPPPA
>NZ_CP053419.1|WP_171467354.1|496593_497226_-|bacterial-proteasome-activator-family-protein
MADEPRDPRPDEPTAPDPAANAQGDDEPGRSTVVMPDGTGVSVVESDDSTDPDRNPATVIEEPAKVMRIGGMIKKLLDEVRDAPLDEAARSRLAEIHERSLTELEEGLSPDLVDELHRITLPFSDDSVPTDAELRVAQAQLVGWLEGLFHGIQTALVAQQMAAQAQLSQMRRALPPGSLPPMGHGAPGGMPGQQPRPDEHDGRPSPGQYL
>NZ_CP053419.1|WP_171467355.1|497280_498258_-|NAD(P)H-quinone-oxidoreductase
MRGVTISGSGGPEKLTVSTLPDQTPGPDELVVDVASAGVNRADLLQRAGSYPPPPGAPDWPGLEVSGTVARVGDAVSGWSVGDGVVALLDGGGYAEQVRVRATQVLPVPDGVDLVDAAALPEAVCTVWSNVVDVGRLAPGEWLLVHGGSGGVGTVGVQLGAALGAHVAVTAGGRDRADRCLALGASLAVDHREEDFVAAVRDASGGHGADVVLDVVGAAYLPRNLEVLATGGRLVVIGMQKGRRAELDLGLLLARRATVAGTTLRARPPQEKARIVHEVLTHVWPLVEDGRVRPVVHARLPLDEAARAHELLDSGEVFGKVLLVP

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Crispr_ID: NZ_CP053419_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053419_2

553116-553291

Orphan

Consensus_repeat	Method
TGCTGGCCGGGCTGGCCGGGGTA	CRT

3 spacers

The CRISPR arrays of NZ_CP053419_2

>merge|NZ_CP053419|2|553116-553291|CRT
TGCGCGCCGGGCTGGCCGTACTGACCCGGGTACTGGCCCTGCTGGCCCTGACCGGGGTACTGGCCGGGCTGGCCGGGGTAGGGCTGCTGGCCGGGGTACTGGCCCTGCTGGCCGGGCTGGCCCGGGTACTGCCCCGGGGCGCCGTAGACGCCCTGCTGGCCGGGCTGGCCGGGGTA

>NZ_CP053419|2|1|553116-553291|CRT
TGCGCGCCGGGCTGGCCGTACTG	ACCCGGGTACTGGCCCTGCTGGCCCTGACCGGGG
TACTGGCCGGGCTGGCCGGGGTA	GGGCTGCTGGCCGGGGTACTGGCCC
TGCTGGCCGGGCTGGCCCGGGTA	CTGCCCCGGGGCGCCGTAGACGCCC
TGCTGGCCGGGCTGGCCGGGGTA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053419.1\|WP_171467381.1\|560322_561630_-\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|226951
NZ_CP053419.1\|WP_034652741.1\|550177_551155_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|225176
NZ_CP053419.1\|WP_021482449.1\|543491_544091_+\|Na+/H+-antiporter-subunit-E	unknown	unknown	gnl\|CDD\|181598
NZ_CP053419.1\|WP_086149279.1\|564572_565244_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|366102
NZ_CP053419.1\|WP_171468650.1\|546579_547221_+\|CAP-domain-containing-protein	unknown	unknown	gnl\|CDD\|349398
NZ_CP053419.1\|WP_171467371.1\|541881_543495_+\|Na+/H+-antiporter-subunit-D	unknown	unknown	gnl\|CDD\|237165
NZ_CP053419.1\|WP_085386649.1\|562668_563382_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213235
NZ_CP053419.1\|WP_171467373.1\|545125_546118_+\|cation-diffusion-facilitator-family-transporter	unknown	unknown	gnl\|CDD\|223131
NZ_CP053419.1\|WP_085386648.1\|563674_564484_+\|peptidoglycan-binding-protein	unknown	unknown	gnl\|CDD\|366659
NZ_CP053419.1\|WP_171468651.1\|558936_559665_+\|DUF2071-domain-containing-protein	unknown	unknown	gnl\|CDD\|378271
NZ_CP053419.1\|WP_171467379.1\|558106_558862_+\|UdgX-family-uracil-DNA-binding-protein	unknown	unknown	gnl\|CDD\|274850
NZ_CP053419.1\|WP_076403690.1\|544087_544495_+\|pH-regulation-protein-F	unknown	unknown	gnl\|CDD\|181179
NZ_CP053419.1\|WP_171467372.1\|544494_544998_+\|monovalent-cation/H(+)-antiporter-subunit-G	unknown	unknown	gnl\|CDD\|237169
NZ_CP053419.1\|WP_171467382.1\|561775_562669_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053419.1\|WP_171467378.1\|557060_558044_+\|diacylglycerol-kinase	unknown	unknown	gnl\|CDD\|224513
NZ_CP053419.1\|WP_171467374.1\|547356_547905_+\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|225168
NZ_CP053419.1\|WP_171467377.1\|554315_556937_+\|ATP-dependent-chaperone-ClpB	unknown	unknown	gnl\|CDD\|274529
NZ_CP053419.1\|WP_171467380.1\|559666_560326_-\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225107
NZ_CP053419.1\|WP_171467375.1\|547932_548511_-\|methylated-DNA--[protein]-cysteine-S-methyltransferase	unknown	unknown	gnl\|CDD\|223427
NZ_CP053419.1\|WP_171467376.1\|548507_550112_-\|DNA-3-methyladenine-glycosylase-2-family-protein	unknown	unknown	gnl\|CDD\|225080

Protein	Function_ID	Function_description	E-value
NZ_CP053419.1\|WP_171467381.1\|560322_561630_-\|sensor-histidine-kinase	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.23283e-38
NZ_CP053419.1\|WP_034652741.1\|550177_551155_-\|alpha/beta-hydrolase	gnl\|CDD\|225176	COG2267, PldB, Lysophospholipase [Lipid metabolism].	2.58265e-30
NZ_CP053419.1\|WP_021482449.1\|543491_544091_+\|Na+/H+-antiporter-subunit-E	gnl\|CDD\|181598	PRK08965, PRK08965, putative monovalent cation/H+ antiporter subunit E; Reviewed.	2.85813e-38
NZ_CP053419.1\|WP_086149279.1\|564572_565244_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|366102	pfam00440, TetR_N, Bacterial regulatory proteins, tetR family.	4.38439e-12
NZ_CP053419.1\|WP_171468650.1\|546579_547221_+\|CAP-domain-containing-protein	gnl\|CDD\|349398	cd05379, CAP_bacterial, Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins. Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown.	6.22587e-43
NZ_CP053419.1\|WP_171467371.1\|541881_543495_+\|Na+/H+-antiporter-subunit-D	gnl\|CDD\|237165	PRK12665, PRK12665, putative monovalent cation/H+ antiporter subunit D; Reviewed.	0
NZ_CP053419.1\|WP_085386649.1\|562668_563382_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213235	cd03268, ABC_BcrA_bacitracin_resist, ATP-binding cassette domain of the bacitracin-resistance transporter. The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.	1.43618e-90
NZ_CP053419.1\|WP_171467373.1\|545125_546118_+\|cation-diffusion-facilitator-family-transporter	gnl\|CDD\|223131	COG0053, MMT1, Predicted Co/Zn/Cd cation transporters [Inorganic ion transport and metabolism].	7.01427e-32
NZ_CP053419.1\|WP_171468651.1\|558936_559665_+\|DUF2071-domain-containing-protein	gnl\|CDD\|378271	pfam09844, DUF2071, Uncharacterized conserved protein (COG2071). This conserved protein (similar to YgjF), found in various prokaryotes, has no known function.	1.35357e-51
NZ_CP053419.1\|WP_171467379.1\|558106_558862_+\|UdgX-family-uracil-DNA-binding-protein	gnl\|CDD\|274850	TIGR03914, SPO1_DNA_polymerase-related_protein, uracil-DNA glycosylase family domain. This model represents a clade within the uracil-DNA glycosylase superfamily. Among characterized proteins, it most closely resembles the Thermus thermophilus uracil-DNA glycosylase TTUDGA, which acts uracil (deamidated cytosine) in both single-stranded DNA and U/G pairs of double-stranded DNA. This domain may occur either as a stand-alone protein or as the C-terminal domain of a fusion with another domain that always pairs with a particular radical-SAM family protein.	4.33451e-71
NZ_CP053419.1\|WP_076403690.1\|544087_544495_+\|pH-regulation-protein-F	gnl\|CDD\|181179	PRK07948, PRK07948, putative monovalent cation/H+ antiporter subunit F; Reviewed.	5.70124e-14
NZ_CP053419.1\|WP_171467372.1\|544494_544998_+\|monovalent-cation/H(+)-antiporter-subunit-G	gnl\|CDD\|237169	PRK12674, PRK12674, putative monovalent cation/H+ antiporter subunit G; Reviewed.	1.46904e-33
NZ_CP053419.1\|WP_085386648.1\|563674_564484_+\|peptidoglycan-binding-protein	gnl\|CDD\|366659	pfam01471, PG_binding_1, Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.	2.91455e-11
NZ_CP053419.1\|WP_171467378.1\|557060_558044_+\|diacylglycerol-kinase	gnl\|CDD\|224513	COG1597, LCB5, Sphingosine kinase and enzymes related to eukaryotic diacylglycerol kinase [Lipid metabolism / General function prediction only].	1.42163e-49
NZ_CP053419.1\|WP_171467374.1\|547356_547905_+\|DoxX-family-protein	gnl\|CDD\|225168	COG2259, COG2259, Predicted membrane protein [Function unknown].	0.00695709
NZ_CP053419.1\|WP_171467377.1\|554315_556937_+\|ATP-dependent-chaperone-ClpB	gnl\|CDD\|274529	TIGR03346, chaperone_ClpB, ATP-dependent chaperone ClpB. Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization].	0
NZ_CP053419.1\|WP_171467380.1\|559666_560326_-\|response-regulator-transcription-factor	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	9.79021e-67
NZ_CP053419.1\|WP_171467375.1\|547932_548511_-\|methylated-DNA--[protein]-cysteine-S-methyltransferase	gnl\|CDD\|223427	COG0350, Ada, Methylated DNA-protein cysteine methyltransferase [DNA replication, recombination, and repair].	6.38845e-32
NZ_CP053419.1\|WP_171467376.1\|548507_550112_-\|DNA-3-methyladenine-glycosylase-2-family-protein	gnl\|CDD\|225080	COG2169, Ada, Adenosine deaminase [Nucleotide transport and metabolism].	2.87132e-51

>NZ_CP053419.1|WP_034652741.1|550177_551155_-|alpha/beta-hydrolase
MDEATRTDGTWRPDVLGGDWVARDLDLPDGAVATLVRRDAAAPAGDRPAVLYVHGFIDYFFQTHVAEAVEARGYRFYAVDLRGYGRSIGRGTGAPSRPDDDPNFVTDLAVYAQDLDAAARAVRAEGHDRLVVLGHSTGGLLASLWADARPGRLAALVLNSPWFDLNKPWVFRGPVTWVVDVVGRVAPRLVVGALDPHWAKALHASTGGEWDFDLAWKPIEGFPVRAGFLRAVRRGHARVARGLHVDCPVLVLASARSGPASGWHDALLTTDSVLDVGHITSRAERLGDDVTVVTVEGGAHDLALSPEPARSTYLREVLDWLDARV
>NZ_CP053419.1|WP_171467376.1|548507_550112_-|DNA-3-methyladenine-glycosylase-2-family-protein
MTTTLATPPATTDPVFAERYRAIASRDRRFDGQFITAVSSTGIYCRPSCPARTPKPENVTFYLTSAAAHEAGYRACKRCLPEAVPGTPSWDLGHDLSARAMRLVADGVVDREGVDGLAARLGYSARHVHRVLVAELGAGPVALARALRAQTARALLTGTDLRLADVAFAAGFGSVRQFNDTITEVFDTTPGELRRRARPDRAPSTGDPRRPPAAAPAGSTADDGGATAALDLTLPLREPFDARGVFAFLAARAVDGVEVVDLDGPLLSYARTLALPHGPGAFRATYGPPPGSRRRAPRFHVELELTSVADLPAAIARVRRLFDLDADPAAVDAALAADPALAASVRAVPGIRVPGAVDPAEILVRALVGQQISVAAARTHLSRLAVALGTAFASRFGPTRLFPTPAQLAAEGADHLRGPARRTAAVLGVAHALADGSLALSPADDPAAQCAALEAMPGVGPWTSGYVATRVLHDPDVLLDGDLALRAGAAALGLPDDRRALAARAERWAPWRSYAAMHLWRAAAPTPTPAKETP
>NZ_CP053419.1|WP_171467375.1|547932_548511_-|methylated-DNA--[protein]-cysteine-S-methyltransferase
MTTAPAPTTTTTAGTSPAVTTTLTTPDGPFTVVVDAGGAVLASGWTDEPADLVALVHPGLRPATVSSVPDDDPAVATAVAAVRAYYAGDVRAIDAVPVRQASGPYRAHAWDVLRTVEPGDPVTYTRYAELSGRPAAVRAAAGACAMNAAALFVPCHRVLRTDGSLGGFRYGLDVKRSLLDREARATVTAPAR
>NZ_CP053419.1|WP_171467374.1|547356_547905_+|DoxX-family-protein
MAPTGPAAPTPSTPVPAAEGPRRAAARRLREGLCERLAAWSVPALRVALGLVFLVFGVLKFFPGASPAEQIVRRTVDALTFGLVDGTAAVVLTAVVETAVGLALLTGRALRAGLVVLAVTLAGVLSPVALFPGDLFGDGMTLMGQYVLKDVVLVAAAGVVAAATLGARFTLAAAEPARAPAA
>NZ_CP053419.1|WP_171468650.1|546579_547221_+|CAP-domain-containing-protein
MAPGAPGADDGPPAATAPAPAATEEPPADPVPTPAPEDVPPAEGAADPAGPDGATATGPTPGTGTADGAAPAAGTASAAGAAAPGGAGPGKITAEGAAVVELTNAERAAAGCEPLAVDDRLTAAAQLHSEDMDAQGYMDHTSLDGRSPWDRAHAQGYPNPGAENVAKGYRTAQDVVRGWMDSPGHRANILDCGLREIGVGHANGAWTQVFGWG
>NZ_CP053419.1|WP_171467373.1|545125_546118_+|cation-diffusion-facilitator-family-transporter
MPDAPTPAPPQPESRNPRIARPEGGGDSTVTVIVAFLANALIAGAKTVAATVTGSASMLAEAVHSWADTGNEIFLLVADRRSRRPADTEHPLGFGREAYVWSMFAAIGLFAVGAGVSITHGIQELVHPQPADDFVVAYAVLALAFVLEGVSFLRARRQARAEARAADRDTLHHVLVTSDPTLRAVYAEDAAALIGLVVAFGGVLAHQLTGSPVPDAVGSIVVGLVLAVVSVVLIDRNRRFLVGEAAMPATRAAVLAGIRDLPEVERVTYLRLEYVGPRALYLVASVDLRGDESETSVARRLDELERRVTSVPLIAGAVFTVSAPEEPSIV
>NZ_CP053419.1|WP_171467372.1|544494_544998_+|monovalent-cation/H(+)-antiporter-subunit-G
MDPTTGLWDTIADVVSAVFLLCGAFLAFAAGVGVVRFPDLLARMHAATKPQVLGLILVLAGLSLRLRSWGAVATLFLVVVFQLLTSPVAAHMVGRAGYRTGKVRTDLLVVDELTRDQEAAEREDTGEHDDADRHGEPGATGGVELADTSDPGPDDAGRPADAEGPAR
>NZ_CP053419.1|WP_076403690.1|544087_544495_+|pH-regulation-protein-F
MSDTVYLVIVVVSAVLLAAGASLAVARAERGPSMLDRTIALDVFTTTLVGAIALEAAFSRRTDTIPILVVLSLVGFVGSVTIARFASVEPEDEGRIRTAEEIAAEDAARREAEESDRDSAVDAEHHGGAPEGEVR
>NZ_CP053419.1|WP_021482449.1|543491_544091_+|Na+/H+-antiporter-subunit-E
MSLHRRRRALASGWFARVTTQWRTVLWLTIVWVMLWGDLSVGNVLAGVLIGFAVITFFPLPSIAARGKFRPWPFLVLVGRFVSDLVVASFQVSLLALNPRHTPRGAVVGVRLRNPSDIYLTITAELSSLVPGSIVVEAHRLTGMLYLHVLDVETAGGVEKVREDTLALEARVLHAFASNDELRAAGLYDVPSAREVAEA
>NZ_CP053419.1|WP_171467371.1|541881_543495_+|Na+/H+-antiporter-subunit-D
MSLTAAALVPLPVVLPLVAAGLALALWRHPRAQRIITVAALALVLAASVGLLVAADSGPIVVDVGGWAAPVGIDLVADRLSSLMLVVSSFVMLCVLLYSLAQGVADGDEEAPVAIYHPTFMVLAAGVFNAFLSGDLFNLYVGFEIFLAASYVLLTLGGTGERIRAGSIYVVVALLSSIVFLVAIALTYAATGTVNLAQLSERYAEIDPGTALAIQLLLLLAFGIKAAIFPLSAWLPDSYPTAPAPVTAVFAGLLTKVGVYAIIRTQTLLFPEDSVVDDVLMWLALLTMVVGILGAVAQNDIKRLLSFTLVSHIGYMIFGIALASEPGMAAAIFYVVHHITVQTTLFLVVGLVERRGGSTSLDRLGGLAKLAPGLAILFFIPAMNLAGIPPLSGFLGKVGLLEEGVAQGTPLTWALVVGSVVTSLLTLYAIVKAWNKAFWQTAPVEIPADARLPRGMVGPATALVAFGLALTVVAGPLYSYTERAAATLLDGHTYVDAVFPGDSDRGQGESNEVATGESDGTEPAGTEPAGMDGGADG
>NZ_CP053419.1|WP_171467377.1|554315_556937_+|ATP-dependent-chaperone-ClpB
METKFTTMSQQAIGEAIQTASAAGNPQLEPTHLLAALLTQEGGVAVGLLDAVGADKQAVGQKVRAALVALPTASGSAVAQPTPSRATSAALDAAAKEAQALGDEYVSTEHLLLGIAAGSSQAATILQQAGATAEALRSALPAVRGSARVTSPNPEGTYKALEQYGTDLTARAAEGKLDPVIGRDSEIRRVVQVLSRRTKNNPVLIGEPGVGKTAVVEGLAQRIVAGDVPTSLQGKRLVSLDLASMVAGAKYRGEFEERLKAVLEEIKSSDGEVVTFIDELHTVVGAGAGGEGAMDAGNMLKPMLARGELRLVGATTLDEYREYIEKDPALERRFQQVFVGEPSVEDTVAILRGLKERYEAHHKVTIADSALVAAASLSDRYITGRQLPDKAIDLVDEAASRLRMELDSSPIEIDELQRAVTRLEMEEVVLSESTDPASLERLEKLRADLADRREELAALTARWEAEKAGHNRVGDLRAKLDELRVQVERAIREGDLETAGRLQYGEIPHVQRELDEAEAAEQADDAFAASGPEAAPMIADKVGADEIAEVVSAWTGIPAGRMLQGESEKLLHMEEVIGERLIGQQAAVRSVSDAVRRSRAGVADPDRPTGSFLFLGPTGVGKTELAKSLADFLFDDERAMVRIDMSEYSEKHSVARLVGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEVEKAHPEVFDILLQVLDDGRLTDGQGRTVDFRNVILVLTSNLGSQFLVDPMLDDAEKREAVMSTVRASFKPEFLNRLDDVIVFEPLTIEELGRIVDIQVAALGRRLADRRITLDVTTAAREWLALEGFDPAYGARPLRRLVQREIGDRLARMLLSGDVADGDVVRVDRDPEGDGLALGTEILTA
>NZ_CP053419.1|WP_171467378.1|557060_558044_+|diacylglycerol-kinase
MPTDETTSSATTSAQRRPDDVPRRSAVIVNPNRVEGLDALRELIVARLTDAGWPEPAWLETTAEDPGTGQARQAVEDGAEVVFVSGGDGTVRAVVEGLAGTDAALAILPGGTGNLLAANLGVPSDAEEGIRLVLRGGRRTIDVGVADGQTFAIMAGMGLDAAMMQDAPTALKARAGSIAYVLSALKHLADDEMHVEVTVDGRTRRRRARTVVIGNVGRLQAGTNLLPDAEPDNGQLEVAIIAPRNLQHWVQLLWGVVRGKSRVPSREVVRGREVSVVSDRPQPRQLDGDVIDPDERLDVSVRPDALHVCVYHPEESEDLTRGAPGNR
>NZ_CP053419.1|WP_171467379.1|558106_558862_+|UdgX-family-uracil-DNA-binding-protein
MSPRPPERPGAQEWLPRGRAVHDVEALDRAARDCHGCELWADATQVVFSRGPHDARLALVGEQPGDHEDREGEPFVGPAGRLLDDALDAAGLAADDVYLTNAVKHFRFEQRGGRRLHKSPDVAHVRACLRWLTAEVAAVGPRVVVAMGATAGRAVLGRPVRVTAERGRVLDLGDAEPASPFSPGGPGGGGRPEPSDGARPPRPTDAPRVVLTTHPSALLRVRDRAERQAAFAALVDDLRLAADAADAAGTR
>NZ_CP053419.1|WP_171468651.1|558936_559665_+|DUF2071-domain-containing-protein
MVVNAQRWEALTFLHWPVDPAVVQGWLPPGLTVQQAGGTTWLGVVPFSMAGVRVPPLPPLGAWSAFPELNVRVYVRDRAGTEGVWFLGLWATSRAFVAATRAAGVPYHPARAAVHARGDRDGAPSAVRYRFRSDGRGPLRVPHEHPGLRDLSLHAEVRAHEEVDASSGLVRWLTARWSAYGARAGRLWRFPVVHEPWSLRRGTLDVLDTDLLDRLGLPSADPPLVHVAAPVHARFAVPRPVR
>NZ_CP053419.1|WP_171467380.1|559666_560326_-|response-regulator-transcription-factor
MTRVVLVDDQAVVRAGFTVILESEGLEVVGEASNGADAVRVARRERPDVVCMDVRMPGGDGITATRALAGPDVADPVPVLVVSTFDLDDYVFGALEAGASGFLLKDAEPEVLVDAVRRVASGDGLVDQSLTRRVLGEFARRRAPVARDDDAAALLTPRELDIVTLLCRGSSNAEIATALFLEPSTVKSHLSRAMTKTGARDRVQLVVWAFRHGIVDPAA
>NZ_CP053419.1|WP_171467381.1|560322_561630_-|sensor-histidine-kinase
MTETLRRALDRVGVLTDTGRDAVLAGVVALATVALFLGIERVLATEVGATFGAGPGESVIGPGVRAAVLALVVGQAAALVLRRRAPLLCLALTVVAQVAITALLPPYVGFQAPATLVAAYSAGAYAPRRARLGAPALAALAQVLLVFALGGLGNPAGAGPAQHALQVGGALLSAVLTFVGAALVGSYVATRRELVAELRDRVVRAEREREALAAQAVLEERARMARELHDVAAHHLSGIVVQASAAERLVDADPERAKESVRWIRSQGRETLDDLRLVVGILRGRDDEGDEREAPQPTLADLPALLETARAAGTTVTVETEGEPWEPAPTAQIAVYRVLQEALANARRHAPGRPVAVRLAWSPADVVVTVRNPAGRAAPPQDARPGHGLVGMRERAAVLGGTLDARRTPDGAWLVRLTVPRAPARDPRTPAQEAS
>NZ_CP053419.1|WP_171467382.1|561775_562669_-|hypothetical-protein
MYRAEMLKLRTTRATWVVAAVAVAGMLVVQAFTLLLPTILRSADAAGSGTTVGLQAPPEMVAELAPDLGALADVSQPAFQRSMLDLLGTGLGGSGSVGVATVCMLLLGVLAVTTDFRTGGIVPTALVQPSRLRILGAKAGATATVALGVGVVLALLGALGLLIAIVTTPGAGLALGPGDVLGVWARGLAVLVLLAWLGLGIGTLVRGQVAGVVTVAALALAEPIVRGAVTLLSGGDSAAAEWLPLGLGALASTGGSAATLLGGAAPLGALAALAGLAAWAALLLGGGAVSLRRRDLV
>NZ_CP053419.1|WP_085386649.1|562668_563382_-|ATP-binding-cassette-domain-containing-protein
MTTIHVSGLRKAYGAFDAVHDVTFTAAPGRVVGLLGPNGAGKTTTLHVLLGLAAPTAGTATFDGRAFADLAHPARTVGALLDAGGLHPGRTGRDHLRVLASAGRIPARRVDEVLALVGMTPAADRRVRTYSLGMRQRVGIAAALLGDPEVLVLDEPANGLDPAGMRWLRDLVRAFADDGGTVLLASHVLSEVRQVADDLVVVGQGRVVAEGPLDELLHGESLEDFYLDLTATTEGVR
>NZ_CP053419.1|WP_085386648.1|563674_564484_+|peptidoglycan-binding-protein
MRRRHDRSGPAERDRTAPLQRPARRTATPWVTVAAGAGAVTLVVAVAGMVGAATGGGEAVVVGGVSAEGGANGEDTVPAVTPRPDTPRPEVTRIPPPDAADGTSDDARPAPSPRPSASGQGEQAAPGAPSPTTEPAPAPTASEPTPAPTEPAPTSSPTTDPGTGSVSWVQERLRVHGADVAVTGTMDDATRTALRSFQKAHGLTPDGTVTAATAEALRAAPPDVEDPTGPGPTPPAEPAPTPSTDRPSVAVPGPSSSADEPAPTLAPAP
>NZ_CP053419.1|WP_086149279.1|564572_565244_+|TetR/AcrR-family-transcriptional-regulator
MTSAAIGAGQDRTGSRRAAAPDPARGYAKGRAKREEILQAAVVLFGEVGFHAASLRELASRVGMSHPGLLHHFPTKAALLEAVLDHRETVDRADLEEDLARGTDFFDALVRLVERNALRRPIVELFTALAAEATSPDHPAHAYFVERYESTVARIGEQLSRRARAGGLRDGVEPDVAARQLVALMDGLQVQWLLSLDRPRPERVDMAADLRAYLRLVLSDAER

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Crispr_ID: NZ_CP053419_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053419_3

1008135-1008260

Orphan

Consensus_repeat	Method
GGACGAGCGGTGGGGTCGGACCGTGCGCGAAGGACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053419_3

>merge|NZ_CP053419|3|1008135-1008260|CRISPRCasFinder
GGACGAGCGGTGGGGTCGGACCGTGCGCGAAGGACGCCGGGGCGCACTTCTTCGACCTCTGCCCGGAGGACCAGCGCGACGGCCAGGACGGGACGAGCGGTGGGGTCGGACCGTGCGCGAAGGACG

>NZ_CP053419|3|2|1008135-1008260|CRISPRCasFinder
GGACGAGCGGTGGGGTCGGACCGTGCGCGAAGGACG	CCGGGGCGCACTTCTTCGACCTCTGCCCGGAGGACCAGCGCGACGGCCAGGACG
GGACGAGCGGTGGGGTCGGACCGTGCGCGAAGGACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053419.1\|WP_081600078.1\|1013400_1013661_+\|glutaredoxin-family-protein	unknown	unknown	gnl\|CDD\|368604
NZ_CP053419.1\|WP_171467524.1\|983158_987040_+\|carbohydrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|226064
NZ_CP053419.1\|WP_171467529.1\|1002350_1004927_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350097
NZ_CP053419.1\|WP_171467527.1\|994646_997061_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350117
NZ_CP053419.1\|WP_081600076.1\|1012448_1013321_-\|HAD-IB-family-hydrolase	unknown	unknown	gnl\|CDD\|273654
NZ_CP053419.1\|WP_081600037.1\|981832_982894_+\|sugar-ABC-transporter-permease-YjfF	unknown	unknown	gnl\|CDD\|183235
NZ_CP053419.1\|WP_171467531.1\|1005949_1007275_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863
NZ_CP053419.1\|WP_061269154.1\|1008382_1009087_-\|TrkA-family-potassium-uptake-protein	unknown	unknown	gnl\|CDD\|223643
NZ_CP053419.1\|WP_021483424.1\|1009255_1010632_-\|potassium-transporter-Trk	unknown	unknown	gnl\|CDD\|273349
NZ_CP053419.1\|WP_081600075.1\|1013657_1014392_+\|redox-sensing-transcriptional-repressor-Rex	unknown	unknown	gnl\|CDD\|235486
NZ_CP053419.1\|WP_171467533.1\|1010843_1012070_+\|acetoin-utilization-protein-AcuC	unknown	unknown	gnl\|CDD\|212520
NZ_CP053419.1\|WP_009862579.1\|1014512_1015064_-\|YceI-family-protein	unknown	unknown	gnl\|CDD\|377274
NZ_CP053419.1\|WP_171467525.1\|987308_991442_+\|glycoside-hydrolase-family-127-protein	unknown	unknown	gnl\|CDD\|369609
NZ_CP053419.1\|WP_171467534.1\|1015227_1015755_+\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP053419.1\|WP_171467530.1\|1005208_1005904_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377558
NZ_CP053419.1\|WP_171467528.1\|997290_1002228_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350149
NZ_CP053419.1\|WP_171467526.1\|991597_994495_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350115
NZ_CP053419.1\|WP_003792170.1\|1012255_1012354_+\|AURKAIP1/COX24-domain-containing-protein	unknown	unknown	unknown
NZ_CP053419.1\|WP_043655743.1\|1015826_1016498_+\|histidine-phosphatase-family-protein	unknown	unknown	gnl\|CDD\|366010
NZ_CP053419.1\|WP_171467532.1\|1007352_1007955_+\|winged-helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238042

Protein	Function_ID	Function_description	E-value
NZ_CP053419.1\|WP_081600078.1\|1013400_1013661_+\|glutaredoxin-family-protein	gnl\|CDD\|368604	pfam05768, DUF836, Glutaredoxin-like domain (DUF836). These proteins are related to the pfam00462 family.	6.39627e-15
NZ_CP053419.1\|WP_171467524.1\|983158_987040_+\|carbohydrate-binding-domain-containing-protein	gnl\|CDD\|226064	COG3534, AbfA, Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].	8.36126e-34
NZ_CP053419.1\|WP_171467529.1\|1002350_1004927_+\|family-43-glycosylhydrolase	gnl\|CDD\|350097	cd08983, GH43_Bt3655-like, Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655. This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	1.72838e-108
NZ_CP053419.1\|WP_171467527.1\|994646_997061_+\|family-43-glycosylhydrolase	gnl\|CDD\|350117	cd09003, GH43_XynD-like, Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized Bacillus subtilis arabinoxylan arabinofuranohydrolase (AXH), Caldicellulosiruptor sp. Tok7B.1 beta-1,4-xylanase (EC 3.2.1.8) / alpha-L-arabinosidase (EC 3.2.1.55) XynA, Caldicellulosiruptor sp. Rt69B.1 xylanase C (EC 3.2.1.8) XynC, and Caldicellulosiruptor saccharolyticus beta-xylosidase (EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) XynF. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. It belongs to the GH43_AXH-like subgroup which includes enzymes that have been annotated as having beta-xylosidase, alpha-L-arabinofuranosidase and arabinoxylan alpha-L-1,3-arabinofuranohydrolase, xylanase (endo-alpha-L-arabinanase) as well as AXH activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Bacillus subtilis AXH (BsAXH-m2,3) has been shown to cleave arabinose units from O-2- or O-3-mono-substituted xylose residues and superposition of its structure with known structures of the GH43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	7.44327e-156
NZ_CP053419.1\|WP_081600076.1\|1012448_1013321_-\|HAD-IB-family-hydrolase	gnl\|CDD\|273654	TIGR01490, Uncharacterized_protein_Rv3661/MT3761, HAD-superfamily subfamily IB hydrolase, TIGR01490. This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI\|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI\|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity].	1.13657e-55
NZ_CP053419.1\|WP_081600037.1\|981832_982894_+\|sugar-ABC-transporter-permease-YjfF	gnl\|CDD\|183235	PRK11618, PRK11618, inner membrane ABC transporter permease protein YjfF; Provisional.	1.59938e-130
NZ_CP053419.1\|WP_171467531.1\|1005949_1007275_-\|MFS-transporter	gnl\|CDD\|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	8.51501e-58
NZ_CP053419.1\|WP_061269154.1\|1008382_1009087_-\|TrkA-family-potassium-uptake-protein	gnl\|CDD\|223643	COG0569, TrkA, K+ transport systems, NAD-binding component [Inorganic ion transport and metabolism].	4.77336e-42
NZ_CP053419.1\|WP_021483424.1\|1009255_1010632_-\|potassium-transporter-Trk	gnl\|CDD\|273349	TIGR00933, Trk_system_potassium_uptake_protein_trkH., potassium uptake protein, TrkH family. The proteins of the Trk family are derived from Gram-negative and Gram-positive bacteria, yeast and wheat. The proteins of E. coli K12 TrkH and TrkG as well as several yeast proteins have been functionally characterized.The E. coli TrkH and TrkG proteins are complexed to two peripheral membrane proteins, TrkA, an NAD-binding protein, and TrkE, an ATP-binding protein. This complex forms the potassium uptake system. [Transport and binding proteins, Cations and iron carrying compounds].	2.80485e-82
NZ_CP053419.1\|WP_081600075.1\|1013657_1014392_+\|redox-sensing-transcriptional-repressor-Rex	gnl\|CDD\|235486	PRK05472, PRK05472, redox-sensing transcriptional repressor Rex; Provisional.	1.3525e-100
NZ_CP053419.1\|WP_171467533.1\|1010843_1012070_+\|acetoin-utilization-protein-AcuC	gnl\|CDD\|212520	cd09994, HDAC_AcuC_like, Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes. AcuC (Acetoin utilization protein) is a class I deacetylase found only in bacteria and is involved in post-translational control of the acetyl-coenzyme A synthetase (AcsA). Deacetylase AcuC works in coordination with deacetylase SrtN (class III), possibly to maintain AcsA in active (deacetylated) form and let the cell grow under low concentration of acetate. B. subtilis AcuC is a member of operon acuABC; this operon is repressed by the presence of glucose and does not show induction by acetoin; acetoin is a bacterial fermentation product that can be converted to acetate via the butanediol cycle in absence of other carbon sources. Inactivation of AcuC leads to slower growth and lower cell yield under low-acetate conditions in Bacillus subtilis. In general, Class I histone deacetylases (HDACs) are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.	9.74391e-155
NZ_CP053419.1\|WP_009862579.1\|1014512_1015064_-\|YceI-family-protein	gnl\|CDD\|377274	pfam04264, YceI, YceI-like domain. E. coli YceI is a base-induced periplasmic protein. The recent structure of a member of this family shows that it binds to poly-isoprenoid. The structure consists of an extended, eight-stranded, antiparallel beta-barrel that resembles the lipocalin fold.	6.19429e-52
NZ_CP053419.1\|WP_171467525.1\|987308_991442_+\|glycoside-hydrolase-family-127-protein	gnl\|CDD\|369609	pfam07944, Glyco_hydro_127, Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.	7.94485e-118
NZ_CP053419.1\|WP_171467534.1\|1015227_1015755_+\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	6.3119e-10
NZ_CP053419.1\|WP_171467530.1\|1005208_1005904_+\|hypothetical-protein	gnl\|CDD\|377558	pfam05818, TraT, Enterobacterial TraT complement resistance protein. The traT gene is one of the F factor transfer genes and encodes an outer membrane protein which is involved in interactions between an Escherichia coli and its surroundings.	0.000265161
NZ_CP053419.1\|WP_171467528.1\|997290_1002228_+\|family-43-glycosylhydrolase	gnl\|CDD\|350149	cd18828, GH43_BT3675-like, Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675). This glycosyl hydrolase family 43 (GH43) subgroup includes the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the GH43_bXyl subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl subgroup also includes enzymes annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	4.34181e-156
NZ_CP053419.1\|WP_171467526.1\|991597_994495_+\|family-43-glycosylhydrolase	gnl\|CDD\|350115	cd09001, GH43_FsAxh1-like, Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase. This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	5.00991e-111
NZ_CP053419.1\|WP_043655743.1\|1015826_1016498_+\|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.	5.93263e-37
NZ_CP053419.1\|WP_171467532.1\|1007352_1007955_+\|winged-helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238042	cd00090, HTH_ARSR, Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.	1.33786e-11

>NZ_CP053419.1|WP_171467532.1|1007352_1007955_+|winged-helix-turn-helix-transcriptional-regulator
MTPEPTPESTLESIPDPTAGPAPRPGAPGVPGRRPPTALEAKALAHPLRQRIVRQCGTREMTNKELADHLGVPPGTALHHVRLLVRAGLLEPAEVRTGTGGALERPYRATGATWWLDDPLRDAAPGARFGPVAAALDDALAAGPDAVTTSAAFYLHLSDDDVAELDRRILAVLDEYVATDADRHDRPLHRGLFVLHRPPS
>NZ_CP053419.1|WP_171467531.1|1005949_1007275_-|MFS-transporter
MASRPGRRRPAAAPLGAPFRRLWAASTVSNLADGVLKVALPLVAVRYTDSPALVAGLTFALTLPWLLFALPAGALADRLDRRLAMVGANVARAVLVVALAAVALVPDAGSIAVLYFVAFAVGATETLYDTSAQSILPQVVPRTALPRANGRLYAAELTANQFVGPPLGGLLVAAGAAVAFGVPGALWALAVVLLLGLPGTYRTVRATRTTLRADVAEGLRFLWHDRILRTLAMMVGGINFASNAAFAVFVLYAVGPDSPLGLSEPAYGVLLTATAVGAFAGSFVAERVVGTIGRARSLALTILGTVALVGVPAVTTNAWVIGAVSAVGGAGIAVWNVVTLSLRQRITPDALLGRLNACYRLLAWGTLPLGAAVGGLLGELFGLRTVFVVMAAVSGATLLGMLVVDDRAMDAAEAAADARDTDARLADAARPGAEAEPQPES
>NZ_CP053419.1|WP_171467530.1|1005208_1005904_+|hypothetical-protein
MTTTTRRLLAALVLTGSLVVPAGTAGAATPTTIPAAAAAPAGTPVAISVTDPADGVRVSVEIAERAVPTAPRVAVVGSGPFVVGGRLELRGTGLAPHAVHEVWLESDPVLLGTGTTDADGAFLFVATIPAGTTPGEHHVRLVPTAGGADVVSEPFLVLAAPGEPHEPGTTPSAGSGGAGGSGGAAAGGGPGSSRPGLATTGAGLGLVAALAGAAVLAGAALRRQAGRGGAA
>NZ_CP053419.1|WP_171467529.1|1002350_1004927_+|family-43-glycosylhydrolase
MISIHRARSALAAGLVGALAVSTLAAAVAAPAAADVGGPTDDGLVAWYPLDAASTTGGTTANRAEGSTFGPATVVGGTATANGTTLDGTDDYVDLPDHLLAGLTDATVSLDVLVSQDQGTPYFVYGLGNTSGSNGNGYLFTTGNAYRTSIATGSWTTEQTVTKGANLQRGVWKTLTYTLSGTTATLYEDGVQVKQATNVTTDPGQIGGGQTTANYVGRSLYSGDRYLKGQVRDFRLYDRALSPAEAAELAARTSTAAADADLAALDLGDTSAVTADLVLPTTGAQGSIVTWTSSDAGVVGATGKVTRPAAGEDDATVTLTALVTRGAVARTAQFDVTVLAHLAPAEAVAWDASHVVVPHLDDVRGNLTLPAEGANGSALTWESSDPATVSATGEVTRPAHGEPAAVVRLTVTATKDGATATHTYDATVRPLPAAADYEGYFFPYFEGESTADGESVYFSASNGNDPLDWVELNDGEPVLTSTLGEKGLRDPFIIRSPEGDRFFLLATDLRIYGGNNFGNAQERGSRALMIWESTDLVHWSDQRMVTVSSAYAGNTWAPEAFWDAQRGEYIVYWASALYPTTSTDGRRIADSYQRMMYATTRDFVTFSEPQVWIDEKRGNGLGMIDSSIVEHEGTYYRFTKDEAYMIPRLEKSTDLRSTDWDLVAEKIGYGQPNPWGGTLTAGEGPTVFKSNTEEKWYLFVDQPSYHGGQGYLPLESTDLDSGVWTSVDAHLPSSPRHGTVLPITAAEHAALLAAYGEQPPAPELDLAVEVTPRCLAGKAYVAVRATNGEDVPVTLTLTTPYGEKTVADVAPGKNAYQSFAARTTAVPAGTVTVTGVATLDGREVTATREAAVDALDCA
>NZ_CP053419.1|WP_171467528.1|997290_1002228_+|family-43-glycosylhydrolase
MTSRHEPPPTPAEPRARRRRRSLAALLGLALVAPLAPVGAAAAGPMPAAPAPVPAAAEPTTDGLRLWLPLDETEGAVAHDASGHGLDAALVGSGGGWRAGQGLTFGGANHVDLPDDLLAGYDAVTVSADVWVDTSLSGNYFFYTLGNPAVGTPQSGNGYLFSTGNANYRATISDLAWGREQNTAKTPAGALQRGVWKTVTYTLAGGTARLYEDGTQVGQNTAVTITPGAIGGGTTTANALGKSAYAADNLFKGRMKDFRLYDRALTAQEVADLASDAAQDAVAADAAALDLGDTSAVATDLALPAKGVGGSAVAWSSSDAGVVSASGAVTRPAGDESATATLTATVTLRGATATRTFDVTVLPGDGDQAKADAAAAALEVTNLDDVRGNLTLPTTGLHGASVTWESSSDTIAPTGEVTRPAHGEDAETVTLTATVAVGAATATRELAAHVPPLPEQEDLAGYLFSYFVGEGTATGEQVYFGLSQGNDPLRYQNLNDNQPVLTSELGEKGLRDPFIIRSPEGDKFYQIATDLKIYGNGNWDASQRTGSKSIMVWESTDLVNWTDQRLVQVSPDTAGNTWAPEAYYDETIGAYVVFWASKLYAEDDPGHTGNTYNRMMYATTRDFVTFSEAQVWVDPGYSVIDSTVTQHDGQYYRFTKDERNNTSSTPCSKFILAEKAAELRSTDYDFITDCIGKANSLGGGINQGEGPTIFKSNTEEKWYLFIDEFGGRGYVPFESTSLDAAEWTMSTDYEMPSRPRHGTVLPVTQAEYDRLLRTYQPDAFVESVDDVAVTVQTGSAPVLPATVTARFADGSTGSADVTWDAVDPASYAQAGSFEVLGTLGGGVSVRARAVVTVTDDVVPVEGLSVTPESLEVGVGGTRQLTATVTPANATARAITWASGDADVATVSADGVVTGVGEGHALVTATTADGSRTAYVAVEVTADVPGLVVRYAFDETSGTAAANTAPGSSFGPATLTNGAAFSGTGEGVRLDGTDDYVDLPDHLLAGLTDVTVALDVKVATDQATPYFVYGLGNTSGTAGNGYLFTTGNAYRTSIATGNWTTEQTVTKNANLQRGVWKHLTYALSGTTAVLYEDGVEVGRQTGVTIDPKDIGNGSTLANYIGRSLYSGDRYLKGSVRDFRIYDRALTADEVYQVGADHTAVTGAELDALKVPAIVDGASSTVTLAVEPGTDVSALAPVLTVSPRATVTPGNGSVQDLTQPVEYTVSGPDGSSRTWTVHAKQMGSPVLPGTYADPNIAQFGDTFYLYATTDGTPGWGGKDFYVWKSTDLVTWERSEQPFLTLDGANGNVPWATGNAWAPTIIERDGKYWFYFSGHNPTYDRKTIGVAVADSPEGPFTAQPTAMITNGEAVTSGQAIDPAAFRDPETGKHWLLWGNGGPSNGPVMAELGDDMTSIKQDTLRRIPGLTDFREGLFLNYRDGVYHLTYSIDDTGSESYRVGYATSDSIDGPWTYRGVILEKDASQGILGTGHSSILNVEGTDDWYIAYHRFAIPGGDGTHRETTIDRLTFGEDGLIQKVVPTLESVDPVDVAPAPRVELTVEATPRCLAGKVYVAVRATNAGDVPADVTLTTPYGTRTFAGVTPGANAYQSFATRATSVPAGTVTVTGTAVLDGTPVTTPYDVAYDAHPCG
>NZ_CP053419.1|WP_171467527.1|994646_997061_+|family-43-glycosylhydrolase
MDTHHRRRRRLRGAVAGAALVTLLSASLAALPSYAADEELVVNGGFEDGTTGWFVNNGNATDKAVLSTTDQAFAGEAAALTTERATTGSGPMQDLSGKVRAGETYELTAKIRYDAAAAPATKQFFATMHYGGGSYTNLVSVTATKGQWATLDGRFTIPADQNVGTARLFFETPWTSNPSADPATHLMDFVLDDVSVVGAAPPGPPSKTIEVLGKLPGEHNPLISHKFGADGFGFVEDGRVYMYMTNDTQGYAPDPVTGVSPQINYGSINQITLISSEDLVNWTDHGEIQVAGPQGVAPFTNNSWAPGMAKKTVDGVDKYFLYYANGGGSSNVITGASPLGPWTSERDSTLIDGRTPGAEAVAWKFDPAPLVTDDGAYLYFGGGPASTSMPAAERFNNPKNIRVIELGDDMVSTQGTAAVVDAPVAFEAAQVFERDGKYYLSYSSHFGGNDFGGNQATLPGYPGGGQIGYMISDDPMSFPKETYAGVMFPNQSQFFGAGTGGNNHQSVFELDGKYYFTYHAPTLNKRINGSTTQGYRSPHIQELTFNADGTVQQVVGDYAGVDQVKDLDPFQVLEAETFAWQQGLTTAKVDGGSAQFGDQAPNLVVRDVDAGDWSALSSVDFGDGAASVTARVKPLVEGATVEVRLDDREGAVVGTLGLDTPVGEWADVTAALEGVSGVHDVYFTFAGPAGVDLVEVDTWEFAADAAGPAVELDVTASARCLAGKAYVAVRATNLADVAADVELVTPFGTRVVRDVAPGANAYQSFATRSASLAAGVATATGTAVLDGATVETAHEAAYGDLSCG
>NZ_CP053419.1|WP_171467526.1|991597_994495_+|family-43-glycosylhydrolase
MSRHRRRRAAATIVAGVLALGAGLPAAHATATADDEPPAATALTGLTTTDRGDGTYDVPLLRSDVPDISVTRVPAAENDEGRDLYYMISTTMHLAPGAPIMKSYDLVSWEIVGYVYDRLGVGDVSSLRNGKNGYGNGQWASSLRYRDGTFYVVFNTNDLGGSYLFRTDDVEHGAWERTALGRGFHDPSLFFDEADGGTPYIFYGSGATSAVRLNDDLTAIEADFPNIFRAADYAGEPFVGGLFEGAQVHYIDGEYYVAIITWPSGQNRQEVLFRSPHLLGRYETADGSNPYEARSALNSDGFAQGGLVEVPDGAGGYEWWGMFFRDTYPLGRIPALIPATWEDGWPTFGDDGVVRVGDTFAKPIVLDPATERRERLKSIVASDDFANDAEHRAFSDTVWEVPDAPTYDESLLGVELVANPGFEDAGTAPWAAQFGATLSRETSGAASGTGALRVAGRTLNGSGPNQQLGGKIQAGVTYEVSARVRYASGPAQVRFNLVGDWGAGVTTLAWANATPGEWTTVRGTYTVPQDADVRTFKLAVETPWGNPQPPSSSVEYLLDDVSVVGRAPAVETPTLEEVSYNGSDLDLAWQWNHAPDNRYWSLTEREGWLRLTNGHVVTGEAEYTKAPGRDLTYLEEARNTLGQRTFGPTASAETRVDVSGMLDGDVAGLAVYGRSFAYAGVQQVDGERTLGLVTRLQPFTDTIDREAVESFVPGSQVPLGERTDVHLKADADFASPNGQLWVQYSYSLDGRTWQPLGPRQGPLVMDWSLSHFMGYRFGLFSYAKERTGGHVDFDHFLLSDVLDADGGADRTALDAVVAEAEGLDPEDHTAESWAAVEQALAWARSTTAPSTQNQADAPARALALAVASLEPTTSPDVAFAAEAGLRALAGTDYVAVRVVNEEDVPVDVVVTTPYGSRTFADVRPGASAYQAFPTRRSQAPAGEATVTVTRSTDAATTTRTVPFGR
>NZ_CP053419.1|WP_171467525.1|987308_991442_+|glycoside-hydrolase-family-127-protein
MARLAAVAAAAALAVTAWAPSAVAADALPAPVLDLAFDGDVADASPLAHPVALRGHTGSAPTGFSYVDGVDGAGQALRLSGSTYLDLGSSTALQPEDLTLSFWVEPSGKLSGEHVITWNKRAYNSDGWYLSSESDTVPLALSVGPASGQPYKVRVASSDRAAFFPADEWTHVVVTYDHATKAVAFYRNGEQVPSTVASAVAGDATGVLGSDPALPKTIGFNGPQYNGAYLKAALDDYRLYDAVADLGDVVGLYEESGRTVDRDAIAQDDADALSLPERATVALVLPATGSRGSTVTWRSSHPEVVATDGTVVRPAIGEDDAHVTLTATVRYLDGEPVTRDLEVVVPAIVDETPLEETALPSVLLSDDFLQNAAAKEHEYLLSLDSETFLYEFYKVGGLTPTTAAGYGGWERSNAVNFRGHAFGHYLSALAMSWSSTQDEATKDALFTEIEEGVGGLARVQDAYAAAHPGSAGYVSAFRESILDQVQGTGTSDENVIVPWYNLHKVLAGLLDVAEHVDGPVGDQALAVATDFGLYVQGRVAKLPSTDVMLRTEYGGMNEALYELFDLTGDVRIKEAAEAFDEVTFFRQLAAGQDVLPGKHANTQIPKLLGALKRYQVFTQNPAYYDLLTPAEKDELPMYLAAAENFFDIVVRDHTYVTGANSQAEHFHAPGSLHERADEQGTARNAETAETCNEYNMLKLARELFTLSKDVRYADYYENAFINTILASQNPETGTTTYFNPMASGYHRVYNLPFTEFWCCTGTGMESFSKLGDSIYFTGQGSVWVNMFFSSTVEHAEQNLRLTQEANLPNEDTVTFRVDALDGGAVAEDATLRLRVPSWIAGEPAVEVNGAAVEPHVSRGYVVLPVAAGDVVRYTMPMAASVVDTPDNPYFVAFRYGPVVLSANLGEVPEPAWQGTGILVRSSTRDADAQTTITAANMGADEWKERIAENLVRVEDDAEGRVQLELRNTADGGDLVFTPHHTNWDVTYGLHLHLDEPDSAASQDRILRAKQELRDADRTVDSLTSFDDNNFENAKNLQQSGSSVGTFSGRQFRHANGTGWFSYDLMVDPASASNHLGVTLYSGDQGRVFDVYVNDEKLKTITTVANAPTKDEQGFYVDTTQLPAKYLEIGEGTRWKVDSAGEYVLDEDGERIPVVTVRFQATGGWAGGVFGVRVDRAASYDATPGLAALAFDTGSLAPAFDPAVTDYTLTVPAGTTGVVLDADPHVPSGLVRVDGVLIDDTQGRVVPLPADGSARTVEVVGVAQDHETATTYRVEIVPGATAVVPLDVEVSSRCLAGRAYVAVRATNTGATPVDVTLATPYGERSSTGVAPGANAYQSFASRATAVPAGTATVTATAVLDGAPVTTTHDVDIEPRTCG
>NZ_CP053419.1|WP_171467524.1|983158_987040_+|carbohydrate-binding-domain-containing-protein
METSVHPSLPASRRRPARRPSVAVALVAGMVGTVALATSLPAAAAEPDLPDGAWVDTFDGAALGPDWTVVNPVPEALSVGGGKLTLTSQPGDTYQDANSAKNVVLLDVPAGDFTVVTRLEAPVASVYQGAGLVAWQDMDNYVRSGLTFVGDLSPSGRAIENDVETGGVFSAAAFTDRPGSTGETLRMQRTGDTIATSFWDGTAWQPAGSVTVDFPTTHVGLYALAAQSGAAHTAAFDYVAVQAAEGADQVPDGTFTLAGPGDARYLVATDDGLALDDERPATTVALAATAVDGAEGTSPVTLAVGDRPVVVSGASRLSLGPAGADATALRLTDAGGGTVWLRSAADPERYAGVRASDGALVLGPRDAATKLTITPATSADHEITVDLAGERTQMSDELYGIFYEDINYAADGGLYAELVRNRSFEFSNQDNGSFTGLTAWSAANRGGATATTQVVNDAGRLNATNRNYLNLTTTGAGAGVRNAGYNTGLFVEEGESYDFSVWARSATAQNVTVRVEDAAGTTAYATGQVAVDGSNAWKRYDVTLTATGTTNAGRLALLSGAAGTLALDQVSLFPQDTWVGPVNGKSVLRKDLAEKIDALDPQFLRFPGGCVTNVGTFRTYEESGFTDRRRTYQWKETIGPVEERATNWNFWGYNQSYGIGYLEYFLLAEDLGATPLPVVSVGANGCGSTIPEMTDPAQIQRWVDDTVDLIEFANGDVTTEWGAVRAELGHPEPFGLKYVGLGNEENTKTFEANFPAFRDAIAAAYPDVQIISNSGPDDTGQRFDELWEFNREQDVDLVDEHYYNDPQWFLENDERYDSYDREGPHVFLGEYASRGNTFANALSEAAFMTGLERNSDVVRLASYAPLLANESYVQWSPDAIWFDNDESWGSVNYYVQQLFSANAGDEVVPSTHSGPAPADATLDGGVFLSTWNTAAQYDNVRVTDNASGDVLFADDFESGASQWEPQSGTWAAQDGAYVQSATNVTDARSIVAGAYAKDWSSYTLELDARKTSGAEGFLVGFAAGGPNDYYWWNLGGWNNTRQALQRASGGSANEVQAVENHSIEAGQPYHVKVVVEGSTIELYLDGELQMSYEQPSTKSLYQVVTRDDETGDVVVKVVNPTATAARTQVHVEGSEGIADQATVTEMVGAPSDTNTKADPERVVPVERTLTGVGEEFSYEFPAHSITFVRLHASDTEPELDLAVEVTPRCLAGKAYVAVRATNGEDVPVALTLATPFGQKAFADVAPGKNAYQSFAARATSAPAGTATVTGTATLDGEQVTSTVDVAYDALDCG
>NZ_CP053419.1|WP_081600037.1|981832_982894_+|sugar-ABC-transporter-permease-YjfF
MSAVQTPAPTSPPDPRGAETAAPGGRPTMTERLTSRVRLDRRYLPVLGTFAVLALMLVVGGSRYENFLSARVVSNLFINNSFLIVLAVGMTFVILTGGIDLSVGAVVALSGITTASLLQSGWPVAVVLVIAVLIGTVLGLAVGLMVHVFDIQPFIATLAAMFLARGLCYVISLQSIPITNESFVALAGWSQEIGDGWRLTTAVIIALVVVAIAFYVLHYTQFGRTVYAIGGGEQSAMLMGLPVARTKVLVYVVSGTCAGIGGLLFAMFSRSGYSLTGVGMELDAIAAVVIGGTLLTGGTGFVLGSVLGVLVLGLIQTIITFEGTLSSWWTKIVIGVLLLVFVILQRVLVVRRR
>NZ_CP053419.1|WP_061269154.1|1008382_1009087_-|TrkA-family-potassium-uptake-protein
MVERGRAERARRDEAKAPRKDAGVLVIGLGRFGTAIAATLDRLGQDVLAVERDPDLVAQWSGQLPLVEADASNPVALEQLGARDFPVAVVGVGTSLEASVLITGNLVDMGTPQIWAKAISAEHGRILQRIGAHHVVFPEADAGSRVAHLVSGKLLDYIEVEDGFTIVKMRPPREVQGFTLAQSKVRERYGVTVIGVKSPGEEFLYATPETRISANDLLIVSGHADLLERFAARP
>NZ_CP053419.1|WP_021483424.1|1009255_1010632_-|potassium-transporter-Trk
MPTSMTGRLFRGREIVDRLARQSPARLAVTVFAAVIAVFTALLMAPWATASGRSAPFVDAFFTATSAVCVTGLVVVPTGTYWSGYGQVVILLGIKIGGLGVMTLASILGMAVSRRIGLTQKLLTASETKTTRLGEVGSLVRVVIITSTSLELLIALLLLPRFVVLEETFGEAAWHGIFYGISAFNNAGFIPTEHGLAPYVGDWMLCLPIILGVFIGSLGFPVILNVMRNRRRASKWSLHTKLTLTTSAALVVVGTVLFAAVEWGNQRTLGPLDLGEKLLASLFAGVMPRSGGFSTVDTGGMHEASWLITDALMFVGGGSASTAGGIKVTTLAVMLIAIVSEARGDRDMEAFGRRIPRDTLRLAVAVSFVGATAVLLSSLLLLEITGETLDVILFETISAFATVGLSTGITPDLPDAGKYVLIALMFVGRTGTMTFAAALALRDRRRIVRYPEERPIIG
>NZ_CP053419.1|WP_171467533.1|1010843_1012070_+|acetoin-utilization-protein-AcuC
MPTTDPTSSPAPTGAAAAPGACVVWSPELLGYDFGPGHPMAPARLDLTMGLVRALGLLDDDADLRVVRPEPAPDDVLELVHEPAYVAAVRAASEHGTPDPARGLGTEDDPVFRGMHEAAARIVAGSYEAAGEIAAGRTQHAVNVAGGMHHAKAGAASGFCVYNDAAVAIRRLLDDGVERVAYVDLDAHHGDGVEEAFWGDPRVLTVSVHQSGATLFPGTGHPTDLGGPGAEGTAVNVALPRRTDGARWLRAVDAVVPPVLRAFRPEVLVTQHGCDAHGEDPLSDLDVSVDAQRTAATWMHGLAHELTDGRWLALGGGGYAIARVVPLVWSAVVGEVVHRPVTAGVPLPAEWRERVAEVAGFDAPLAFGPEVEVRRWSSGYDPDDDVDRAVAATRRAVFPLLGLDAHFD
>NZ_CP053419.1|WP_003792170.1|1012255_1012354_+|AURKAIP1/COX24-domain-containing-protein
MGSVIKKRRKRMAKKKHRKLLRKTRHQRRNKK
>NZ_CP053419.1|WP_081600076.1|1012448_1013321_-|HAD-IB-family-hydrolase
MATSPGPGPDPTSRPTLPEEAPARAPGPPHRTAAFFDVDNTIIRGASSFHLARALYQREFFSTLDIVRFAVHQARYLAFGENKQQIDRIRSRALALIAGRSVAEVTAIGEEVYDTVLSLRIYPGTRRLLDEHLAAGHQVWLVSATPVEIGELIARRLGTTGALGTVAEHEDGFYTGRLVGDMMHGRAKAAGVRALAEREGIDLEASYAYGDSLNDVTMMEAVGHPCPINPDARLRRHAQDVGWPIREFRGRRRRVARSSVRTASWAGAAWAAALVLRSVRRAVDRRIARL
>NZ_CP053419.1|WP_081600078.1|1013400_1013661_+|glutaredoxin-family-protein
MLFGRAGCHLCDDARTVVEDVCAEAGVAWAEVDLDAPGTDPALREQYGEYVPVVTVGGVQQGFWRVDARRLARAVARISAPRADLG
>NZ_CP053419.1|WP_081600075.1|1013657_1014392_+|redox-sensing-transcriptional-repressor-Rex
MIPPVERDRRRGRSLDDGVTVAEQVVGEVTAPGIPSATVARLPSYLRALRDLVARGVGTTSSVELAELSGVGPAQLRKDLSFLGSFGTRGVGYDVDSLAQYITEALGLVDEHRIAIVGIGNLGHALANYSGYEQRGFHVAALLDASPDVVGTRAAGLVVEHVDALEEVVEREKVSIVVLATPAAHAQAVADRVVAAGVREILNFAPRALQVPADVDVRGVDVGSELQILAFHSQARALAASQER
>NZ_CP053419.1|WP_009862579.1|1014512_1015064_-|YceI-family-protein
MASSLPAGLTAGTYALDASHSQASFTVRHAGISKVRGTLAITDGTITVGDDLESTSVTAQLDAASVSTGDENRDNHLRSADFWDAENKPTWTFTSTRITGDGDDYVVAGDLTINGVTKPVELETEFAGTATDPFGNPRAGFEATTEISRKEFGLTWNAALETGGVLVGDKIKIALDVSAIKQA
>NZ_CP053419.1|WP_171467534.1|1015227_1015755_+|MarR-family-transcriptional-regulator
MTRNDVDTPTASTVRTPAVPAVEPRWLDAEQQRLWRAYLDGTVRFIEALGRDHEERSEVSLNEYELLVRLSESPDHTLRMSALADGLARSRSRVTHTVARMEARGLVRRSASSGDRRGVNCAMTSEGYRVLVASAPAHVAAVRRYLVDVLTPEQFRALGEAMAAVAEACKADRDA
>NZ_CP053419.1|WP_043655743.1|1015826_1016498_+|histidine-phosphatase-family-protein
MVSTIVHLLRHGEVHNPDGVLYGRIPGYHLSERGHEMARRVAAHLAGEPGPDGTSRPRADLTVVVASPLQRAQETATPAAEAFGLELGTDERLIEAANHFEGKTFGVGDGSLRHPQHWPYLWNPFRPSWGEPYVEQVARMRAAVADARDKAAGHEALLVSHQLPVWLTRLSFENRRLWHDPRKRECSLASLTSLHFEDDRLVGLHYTEPVADLLPGAATVSGA

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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_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NZ_CP015867	Streptomyces parvulus strain 2297 plasmid pSPA1, complete sequence	230324-230348	2	0.92
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NZ_CP017451	Klebsiella sp. LTGPAF-6F plasmid unnamed1, complete sequence	185221-185245	3	0.88
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NZ_CP013071	Sphingobium indicum B90A plasmid pSRL1, complete sequence	84572-84596	3	0.88
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NZ_CP029357	Azospirillum sp. CFH 70021 plasmid unnamed2	114237-114261	3	0.88
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NC_016624	Azospirillum lipoferum 4B plasmid AZO_p5, complete sequence	57646-57670	4	0.84
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NZ_LR134465	Tsukamurella tyrosinosolvens strain NCTC13231 plasmid 23, complete sequence	366946-366970	4	0.84
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NC_007765	Rhizobium etli CFN 42 plasmid p42e, complete sequence	60997-61021	4	0.84
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NZ_CP020909	Rhizobium etli strain NXC12 plasmid pRetNXC12c, complete sequence	60830-60854	4	0.84
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NC_021908	Rhizobium etli bv. mimosae str. Mim1 plasmid pRetMIM1d, complete sequence	60816-60840	4	0.84
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NZ_AP020327	Mycobacterium avium subsp. hominissuis strain JP-H-1 plasmid p1-JPH1	23370-23394	4	0.84
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NC_008010	Deinococcus geothermalis DSM 11300 plasmid pDGEO01, complete sequence	267397-267421	4	0.84
NZ_CP053419_2	2.2\|553196\|25\|NZ_CP053419\|CRT	553196-553220	25	NC_006824	Aromatoleum aromaticum EbN1 plasmid 2, complete sequence	14195-14219	5	0.8
NZ_CP053419_2	2.3\|553244\|25\|NZ_CP053419\|CRT	553244-553268	25	NZ_CP030772	Streptomyces sp. YIM 121038 plasmid pSSP121038, complete sequence	414303-414327	5	0.8
NZ_CP053419_2	2.1\|553139\|34\|NZ_CP053419\|CRT	553139-553172	34	NZ_CP023071	Sinorhizobium fredii CCBAU 83666 plasmid pSF83666b, complete sequence	124263-124296	7	0.794
NZ_CP053419_2	2.1\|553139\|34\|NZ_CP053419\|CRT	553139-553172	34	NZ_CP043441	Cupriavidus campinensis strain MJ1 plasmid unnamed1, complete sequence	2233458-2233491	8	0.765
NZ_CP053419_2	2.1\|553139\|34\|NZ_CP053419\|CRT	553139-553172	34	NZ_CP032347	Azospirillum brasilense strain MTCC4039 plasmid p2, complete sequence	766539-766572	8	0.765
NZ_CP053419_2	2.1\|553139\|34\|NZ_CP053419\|CRT	553139-553172	34	NZ_CP024310	Sinorhizobium fredii strain NXT3 plasmid pSfreNXT3c, complete sequence	1635288-1635321	8	0.765
NZ_CP053419_2	2.1\|553139\|34\|NZ_CP053419\|CRT	553139-553172	34	NZ_CP007795	Azospirillum brasilense strain Az39 plasmid AbAZ39_p2, complete sequence	4255-4288	9	0.735
NZ_CP053419_1	1.1\|486340\|36\|NZ_CP053419\|CRISPRCasFinder	486340-486375	36	NZ_CP016080	Mesorhizobium loti NZP2037 plasmid pML2037, complete sequence	44772-44807	10	0.722

1. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NZ_CP015867 (Streptomyces parvulus strain 2297 plasmid pSPA1, complete sequence) position: , mismatch: 2, identity: 0.92

gggctgctggccggggtactggccc	CRISPR spacer
gggctgctggccggcgtactcgccc	Protospacer
************** ***** ****

2. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NZ_CP017451 (Klebsiella sp. LTGPAF-6F plasmid unnamed1, complete sequence) position: , mismatch: 3, identity: 0.88

gggctgctggccggggtactggccc	CRISPR spacer
gggctgctggcccgggtactgggct	Protospacer
************ ********* *.

3. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NZ_CP013071 (Sphingobium indicum B90A plasmid pSRL1, complete sequence) position: , mismatch: 3, identity: 0.88

gggctgctggccggggtactggccc	CRISPR spacer
gcgctgctggccggggtgctggcgc	Protospacer
* ***************.***** *

4. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NZ_CP029357 (Azospirillum sp. CFH 70021 plasmid unnamed2) position: , mismatch: 3, identity: 0.88

gggctgctggccggggtactggccc	CRISPR spacer
gtgctgctggccggcgtgctggccc	Protospacer
* ************ **.*******

5. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NC_016624 (Azospirillum lipoferum 4B plasmid AZO_p5, complete sequence) position: , mismatch: 4, identity: 0.84

gggctgctggccggggtactggccc	CRISPR spacer
ctgctgctggccggggttctggccg	Protospacer
  *************** ******

6. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NZ_LR134465 (Tsukamurella tyrosinosolvens strain NCTC13231 plasmid 23, complete sequence) position: , mismatch: 4, identity: 0.84

gggctgctggccggggtactggccc	CRISPR spacer
ctgcggctggccggggtactgcccc	Protospacer
  ** **************** ***

7. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NC_007765 (Rhizobium etli CFN 42 plasmid p42e, complete sequence) position: , mismatch: 4, identity: 0.84

gggctgctggccggggtactggccc	CRISPR spacer
cagctgatggccggggtactcgccc	Protospacer
 .**** ************* ****

8. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NZ_CP020909 (Rhizobium etli strain NXC12 plasmid pRetNXC12c, complete sequence) position: , mismatch: 4, identity: 0.84

gggctgctggccggggtactggccc	CRISPR spacer
cagctgatggccggggtactcgccc	Protospacer
 .**** ************* ****

9. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NC_021908 (Rhizobium etli bv. mimosae str. Mim1 plasmid pRetMIM1d, complete sequence) position: , mismatch: 4, identity: 0.84

gggctgctggccggggtactggccc	CRISPR spacer
cagctgatggccggggtactcgccc	Protospacer
 .**** ************* ****

10. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NZ_AP020327 (Mycobacterium avium subsp. hominissuis strain JP-H-1 plasmid p1-JPH1) position: , mismatch: 4, identity: 0.84

gggctgctggccggggtactggccc	CRISPR spacer
gggctgctggccgggggactgccgg	Protospacer
**************** **** *

11. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NC_008010 (Deinococcus geothermalis DSM 11300 plasmid pDGEO01, complete sequence) position: , mismatch: 4, identity: 0.84

gggctgctggccggggtactggccc	CRISPR spacer
tggctgctggccgggctgctggccg	Protospacer
 ************** *.******

12. spacer 2.2|553196|25|NZ_CP053419|CRT matches to NC_006824 (Aromatoleum aromaticum EbN1 plasmid 2, complete sequence) position: , mismatch: 5, identity: 0.8

gggctgctggccggggtactggccc	CRISPR spacer
gggctgctggccggggcactgattt	Protospacer
****************.****....

13. spacer 2.3|553244|25|NZ_CP053419|CRT matches to NZ_CP030772 (Streptomyces sp. YIM 121038 plasmid pSSP121038, complete sequence) position: , mismatch: 5, identity: 0.8

ctgccccggggcgccgtagacgccc	CRISPR spacer
gatccccggggcaccgtagacgcca	Protospacer
   *********.***********

14. spacer 2.1|553139|34|NZ_CP053419|CRT matches to NZ_CP023071 (Sinorhizobium fredii CCBAU 83666 plasmid pSF83666b, complete sequence) position: , mismatch: 7, identity: 0.794

---acccgggtactggccctgctggccctgaccgggg	CRISPR spacer
ctcgcccg---actggccctgctggccctggccggtt	Protospacer
   .****   *******************.****

15. spacer 2.1|553139|34|NZ_CP053419|CRT matches to NZ_CP043441 (Cupriavidus campinensis strain MJ1 plasmid unnamed1, complete sequence) position: , mismatch: 8, identity: 0.765

acccgggtactggccctgctggccctgaccgggg	CRISPR spacer
tcgcccgtgctggccctgctggccctgagcgcgc	Protospacer
 * *  **.******************* ** *

16. spacer 2.1|553139|34|NZ_CP053419|CRT matches to NZ_CP032347 (Azospirillum brasilense strain MTCC4039 plasmid p2, complete sequence) position: , mismatch: 8, identity: 0.765

acccgggtactggccctgctggccctgaccgggg	CRISPR spacer
ctgctggcgctggccctgctggccctgacggtgg	Protospacer
 . * **..******************** * **

17. spacer 2.1|553139|34|NZ_CP053419|CRT matches to NZ_CP024310 (Sinorhizobium fredii strain NXT3 plasmid pSfreNXT3c, complete sequence) position: , mismatch: 8, identity: 0.765

---acccgggtactggccctgctggccctgaccgggg	CRISPR spacer
ctcgcccg---actggccctgctggccctcgccggtc	Protospacer
   .****   ****************** .****

18. spacer 2.1|553139|34|NZ_CP053419|CRT matches to NZ_CP007795 (Azospirillum brasilense strain Az39 plasmid AbAZ39_p2, complete sequence) position: , mismatch: 9, identity: 0.735

acccgggtactggccctgctggccctgaccgggg	CRISPR spacer
ctgctggcggtggccctgctggccctgacggtgg	Protospacer
 . * **.. ******************* * **

19. spacer 1.1|486340|36|NZ_CP053419|CRISPRCasFinder matches to NZ_CP016080 (Mesorhizobium loti NZP2037 plasmid pML2037, complete sequence) position: , mismatch: 10, identity: 0.722

gtggaggaccacgaccgctgcgccgccgggttcgtt	CRISPR spacer
ccggaggactacgaccgctgggccgccgacggctgt	Protospacer
 .*******.********** *******.   *  *

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site	Prophage annotation

Anti-CRISPR protein detection

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