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_CP048642	Streptomyces aureoverticillatus strain HN6 plasmid unnamed, complete sequence	0 crisprs	NA	0	0	0	0
NZ_CP048641	Streptomyces aureoverticillatus strain HN6 chromosome, complete genome	10 crisprs	csa3,DEDDh,DinG,WYL,cas3,Cas9_archaeal,Cas14u_CAS-V,cas4,casR	0	3	0	0

Cas Category Instructions

Results visualization

1. NZ_CP048641

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP048641_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_1

1630575-1630675

Orphan

Consensus_repeat	Method
GCGTGCCGCCCTCCTGCCCGCCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP048641_1

>merge|NZ_CP048641|1|1630575-1630675|CRISPRCasFinder
CCGCGCCGCCGTCCTGCCCGCCGCCGGTCTGCGTGCCGCCCTCCTGCCCGCCGGTCGTCCGCCCGCCATCGGTCTGCGTGCCGCCGCCGTCCTGCGCGCTG

>NZ_CP048641|1|1|1630575-1630675|CRISPRCasFinder
CCGCGCCGCCGTCCTGCCCGCCG	CCGGTCTGCGTGCCGCCCTCCTGCCCGCCGGTCGTCCGCCCGCCATCGGTCTGCG
TGCCGCCGCCGTCCTGCGCGCTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164318626.1\|1633871_1635509_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164318628.1\|1635525_1636911_-\|amino-acid-permease	unknown	unknown	gnl\|CDD\|182613
NZ_CP048641.1\|WP_164318630.1\|1639346_1639772_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238206
NZ_CP048641.1\|WP_164328042.1\|1636995_1639122_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377198
NZ_CP048641.1\|WP_164318635.1\|1643950_1644826_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164328041.1\|1629750_1630521_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|375319
NZ_CP048641.1\|WP_164318620.1\|1627940_1628279_-\|4a-hydroxytetrahydrobiopterin-dehydratase	unknown	unknown	gnl\|CDD\|234845
NZ_CP048641.1\|WP_164318616.1\|1625953_1626997_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|369778
NZ_CP048641.1\|WP_164318614.1\|1625216_1625927_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319937
NZ_CP048641.1\|WP_164318622.1\|1628406_1629597_-\|ADP-ribosylglycohydrolase-family-protein	unknown	unknown	gnl\|CDD\|377122
NZ_CP048641.1\|WP_164318632.1\|1639874_1640654_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|225130
NZ_CP048641.1\|WP_164328044.1\|1642575_1643823_-\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|223513
NZ_CP048641.1\|WP_164328043.1\|1641400_1642426_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|293841
NZ_CP048641.1\|WP_164318612.1\|1622940_1624674_-\|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379142
NZ_CP048641.1\|WP_164318634.1\|1640650_1641301_+\|DedA-family-protein	unknown	unknown	gnl\|CDD\|223659
NZ_CP048641.1\|WP_164318610.1\|1617422_1621850_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|366375
NZ_CP048641.1\|WP_164318624.1\|1632796_1633222_-\|OsmC-family-protein	unknown	unknown	gnl\|CDD\|274650
NZ_CP048641.1\|WP_164318618.1\|1627135_1627879_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|379312
NZ_CP048641.1\|WP_164328039.1\|1616617_1617409_+\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381357
NZ_CP048641.1\|WP_164328040.1\|1621839_1622886_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|223786

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164318628.1\|1635525_1636911_-\|amino-acid-permease	gnl\|CDD\|182613	PRK10644, PRK10644, arginine/agmatine antiporter.	4.0613e-83
NZ_CP048641.1\|WP_164318630.1\|1639346_1639772_-\|hypothetical-protein	gnl\|CDD\|238206	cd00338, Ser_Recombinase, Serine Recombinase family, catalytic domain; a DNA binding domain may be present either N- or C-terminal to the catalytic domain. These enzymes perform site-specific recombination of DNA molecules by a concerted, four-strand cleavage and rejoining mechanism which involves a transient phosphoserine linkage between DNA and serine recombinase. Serine recombinases demonstrate functional versatility and include resolvases, invertases, integrases, and transposases. Resolvases and invertases (i.e. Tn3, gamma-delta, Tn5044 resolvases, Gin and Hin invertases) in this family contain a C-terminal DNA binding domain and comprise a major phylogenic group. Also included are phage- and bacterial-encoded recombinases such as phiC31 integrase, SpoIVCA excisionase, and Tn4451 TnpX transposase. These integrases and transposases have larger C-terminal domains compared to resolvases/invertases and are referred to as large serine recombinases. Also belonging to this family are proteins with N-terminal DNA binding domains similar to IS607- and IS1535-transposases from Helicobacter and Mycobacterium.	0.00696935
NZ_CP048641.1\|WP_164328042.1\|1636995_1639122_-\|hypothetical-protein	gnl\|CDD\|377198	pfam04020, Phage_holin_4_2, Mycobacterial 4 TMS phage holin, superfamily IV. These proteins are predicted transmembrane proteins with probably four transmembrane spans. The 1.E.40 is represented by the mycobacterial 4 phage holin, but it also contains many cyanobacterial. proteobacterial and firmicute proteins. Holins are encoded within the genomes of Gram-positive and Gram-negative bacteria as well as in those of the bacteriophage of these organisms. The primary function of holins appears to be transport of murein hydrolases across the cytoplasmic membrane to the cell wall where these enzymes hydrolyze the cell wall polymer as a prelude to cell lysis. When chromosomally encoded the enzymes are therefore autolysins. Holins may also facilitate leakage of electrolytes and nutrients from the cell cytoplasm, thereby promoting cell death. Some may catalyze export of nucleases.	1.07832e-10
NZ_CP048641.1\|WP_164328041.1\|1629750_1630521_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|375319	pfam17765, MLTR_LBD, MmyB-like transcription regulator ligand binding domain. This domain is found in a family of actinobacterial transcription factors. The structure shows it has a PAS domain like fold and it is bound to Myristic acid.	2.06134e-19
NZ_CP048641.1\|WP_164318620.1\|1627940_1628279_-\|4a-hydroxytetrahydrobiopterin-dehydratase	gnl\|CDD\|234845	PRK00823, phhB, pterin-4-alpha-carbinolamine dehydratase; Validated.	2.20514e-30
NZ_CP048641.1\|WP_164318616.1\|1625953_1626997_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|369778	pfam08242, Methyltransf_12, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	1.20707e-10
NZ_CP048641.1\|WP_164318614.1\|1625216_1625927_+\|VOC-family-protein	gnl\|CDD\|319937	cd08349, BLMA_like, Bleomycin binding protein (BLMA) and similar proteins. BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.	1.56803e-32
NZ_CP048641.1\|WP_164318622.1\|1628406_1629597_-\|ADP-ribosylglycohydrolase-family-protein	gnl\|CDD\|377122	pfam03747, ADP_ribosyl_GH, ADP-ribosylglycohydrolase. This family includes enzymes that ADP-ribosylations, for example ADP-ribosylarginine hydrolase EC:3.2.2.19 cleaves ADP-ribose-L-arginine. The family also includes dinitrogenase reductase activating glycohydrolase. Most surprisingly the family also includes jellyfish crystallins, these proteins appear to have lost the presumed active site residues.	7.4677e-49
NZ_CP048641.1\|WP_164318632.1\|1639874_1640654_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|225130	COG2220, COG2220, Predicted Zn-dependent hydrolases of the beta-lactamase fold [General function prediction only].	2.79872e-32
NZ_CP048641.1\|WP_164328044.1\|1642575_1643823_-\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|223513	COG0436, COG0436, Aspartate/tyrosine/aromatic aminotransferase [Amino acid transport and metabolism].	4.26124e-20
NZ_CP048641.1\|WP_164328043.1\|1641400_1642426_-\|hypothetical-protein	gnl\|CDD\|293841	cd16283, RomA-like_MBL-fold, Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain. Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	1.38223e-82
NZ_CP048641.1\|WP_164318612.1\|1622940_1624674_-\|trypsin-like-peptidase-domain-containing-protein	gnl\|CDD\|379142	pfam13365, Trypsin_2, Trypsin-like peptidase domain. This family includes trypsin-like peptidase domains.	2.46507e-10
NZ_CP048641.1\|WP_164318634.1\|1640650_1641301_+\|DedA-family-protein	gnl\|CDD\|223659	COG0586, DedA, Uncharacterized membrane-associated protein [Function unknown].	1.99161e-16
NZ_CP048641.1\|WP_164318610.1\|1617422_1621850_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|366375	pfam00931, NB-ARC, NB-ARC domain.	1.19165e-07
NZ_CP048641.1\|WP_164318624.1\|1632796_1633222_-\|OsmC-family-protein	gnl\|CDD\|274650	TIGR03562, osmo_induc_OsmC, peroxiredoxin, OsmC subfamily. pfam02566, OsmC-like protein, contains several deeply split clades of homologous proteins. The clade modeled here includes the protein OsmC, or osmotically induced protein C. The member from Thermus thermophilus was shown to have hydroperoxide peroxidase activity. In many species, this protein is induced by stress and helps resist oxidative stress. [Cellular processes, Detoxification].	5.08118e-61
NZ_CP048641.1\|WP_164318618.1\|1627135_1627879_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	2.17706e-24
NZ_CP048641.1\|WP_164328039.1\|1616617_1617409_+\|aldo/keto-reductase	gnl\|CDD\|381357	cd19131, AKR_AKR5C2, Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins. Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.	6.58396e-155
NZ_CP048641.1\|WP_164328040.1\|1621839_1622886_-\|AAA-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	1.65626e-14

>NZ_CP048641.1|WP_164328041.1|1629750_1630521_+|helix-turn-helix-domain-containing-protein
MGTLLRAWREERRVSQLELALRADSSARHISFVETGRARPSEEFVLKLAEHLDVPVRERNALLLAAGYAPRFPQTPLDDPSMDTLRAGLEQLLQGYEPYPALVVDATYHVVAANRGIAMLLDGLPEELLEPPLNAMRVVLHPRGLAAKIRNLREWRGHLLHQMERQIALHRSAELRALYDEVAAYPVADPGEDAATDWQVPYFALPLRIEHEGRVLSFVSSISTFNTPMDVTVAELAIETLLPADPATVKYLQSKA
>NZ_CP048641.1|WP_164318622.1|1628406_1629597_-|ADP-ribosylglycohydrolase-family-protein
MTNPWDPPVQVRAAGWEATVAYRARVRGCLLGGAIGDALGYAVEFTSLDGIRAAHGPGGVRGPLPDAAAGVCLISDDTQMTLFTAEALRTAHARERRKGIGGAAPELVRQAYMRWLDTQMKPGPEPRTHRAGPESRTHRAGPEPRTHQAGPEPQAHEPGPAEPADLSSQAWLYAQRAPGNACLSGLQHGYAPDPAAELGPHGPVNPESKGCGTVMRSAPFGLTRAPAGRAFELAARCAQITHGHPTGYYAAGALAAIVAHLVEGDSLEGAVLRTLRLLARYAGHEETSAALTAAVDLAAAGGPSAERVETLGAGWIAEEALGIGVYAALATHRVEDALLLAVNHSGDSDSTGSVCGNLLGALHGDHQLPDEWLRLTEGRAVIAAVADDLASECVRR
>NZ_CP048641.1|WP_164318620.1|1627940_1628279_-|4a-hydroxytetrahydrobiopterin-dehydratase
MPVEPLSQKEIEDRLAELPGWSLTSVGADAGAKAAEVKLTRSFRLASHFAATALVVHIAQVQEELGHHSDLTLGYNTVTLAVNTHSAGGALTGLDFALAGRVEALAAGHGAE
>NZ_CP048641.1|WP_164318618.1|1627135_1627879_-|class-I-SAM-dependent-methyltransferase
MLDYGKEAVRYDASRGGEPRAEAAADAVLSLLPARTRSLLDVACGTGLVTRRLAARPGLRVTGVDAAYNMARMAAERVPGAVVLGDSRRLPFPDGAFDAASAVWLLHLLSGFDEAAAVVAECARVLRPGGVLVTTVDKAASHHVGSDIDETLAGRPVRPPVDAAAQVARHAAAHGLVHEGEARFIGHGQGRSPRSTVEDLHRGWFTSIPPDGPLARRYAARLAELPDQDVHRPDPRFTLHAFRKPTV
>NZ_CP048641.1|WP_164318616.1|1625953_1626997_-|class-I-SAM-dependent-methyltransferase
MTVTERVKGHGDGHGHGGGHDHGHGGGHGHADIDWAVMAPVLEQNAEVTAPVYREVAAWLRELRGARPGDGGDRAAGVADPTLIVDAGSGPGVVTCLFAEEFPKARVIAADPEEALLERTTARAARLGLADRVGTHRAELPDGLGELPPADLIWAARSVHHVGDQGAALAALADRLAPGGTLAILEGGLAPRSLPRDFGIGRPGLQARLDAANEDWFARMRTELPGAKETTEDWPSLLKSAGLRHVATRSFLHDLPAPLDDAARAHVIATFERYRSLATNATQGAEAADGDTAAPATSAAAPAGGLTPEDAATLDRLLDPQDELSLHRRPDLFLLTAHTVHVAAKES
>NZ_CP048641.1|WP_164318614.1|1625216_1625927_+|VOC-family-protein
MAEKTIPLLPCVTVQPIVDFYTALGFETTYLQKSPYAYAVVERGTVELQFFGMKQYDPAGSISGCYILTDDVDTLHAAFRAGLKAAYGKIPSRGLPRIGPLKDMSYGVRQFLMTDPAGNSIRVGQPISEEQHHRPAPKETFARALHIADVFVDSKEDLPGAAKVIDRALGLTDERPTPAQHLRLLVLRGDIAQRLGDDALAGRLLEQAEGIALSEEERGWVQDALVRLDELRESRG
>NZ_CP048641.1|WP_164318612.1|1622940_1624674_-|trypsin-like-peptidase-domain-containing-protein
MHWRARIGPVGGGAPLGAGVLVDSERVITCAHVVDGRAEVSVVLPGVAAEARARVAWAGEWREVGDHGDLAMLVLDHPLPVPPCVFAPLGSLRPRHGRTAYALRALGFPEGHDQDGTHVTVSTSQDRQLGGEWLELDVDKGHLRRLGEGFSGAGVYDPESEQVVGIVTDADLEGEYGGTQGRMLPLDAIRRHWEGLDDLLTLDWGLAARPRRELRAALEGSEGSELPGATVSLAVRRAFPSPRLRHPPFRSVWHAVRYVAEDLIGDDRLVLLLRELRDRSPADLAARIADWMGKWLPEELEGPERPAAPPVSVGSIMFRAEPMTRGGSLDLTVCAVVDGVPVARAGPVRIRRQQLRTKAEALLAAQVGAVHDFDWMVEFIVPQGLMGEPFEEWQLREPGAARPRPLRTVPVVVRHVDRLKPLTESRLTRRRWETVRARGRTRPAPVECSESYDYQAFYDWLEDEDDLCALAYAANPVDDWLAAALDTGVPIMLWRRRDCGDAGHAHCAPGAFLDRLIEAVAALDPDELPYEVMKLRKEARSPRRGHADHCGHRLTLFWDDPERKPDPPLAMGSKGND
>NZ_CP048641.1|WP_164328040.1|1621839_1622886_-|AAA-family-ATPase
MSATWQVYTGSRTPHDRVDRLPDPPPWRRFRGGPPLPTPPGGTGNHHAAVSYRPGADAVRQVNAALYLRRPLLVTGAPGTGKSSLAYAVAHELALGKVLHWPITSRVTLRDGLYAYDPLTRLYAAERARGDGAAAGATGAAADDIGDYLRLGPLGTALLPYARPRVLLIDEIDKSDIDLPNDLLTIFEKGSYELVELARRAEPTARVMTADSTTDRVEIRDGTVTCRAFPLVVMTSNGEREFPPAFLRRCVTVDLKQPRTIDELTAIVREHLGEVVGDETGQLPQGARDVIQRFYDRRGGGLLANDQLLNAIYMCHHASFSEPPENVAELADQVMPYLSSEATGPDDA
>NZ_CP048641.1|WP_164318610.1|1617422_1621850_-|tetratricopeptide-repeat-protein
MTLDRLRATLEALGPPVTPLELAEMLWLAERLSTEVDGPWPRVGGAATPDALRHGGAGDAAHLPARPPGAPDAADAPDDQDPRPTDAPAPDEPAASPLHLPRGAARPGTDADDILVPAPQALRHELAIQRALRPLKRRVPDTRRRVLDEDATAARAASAGAGRRPWVPVLVPATERPLRLALVVDTGPAMNVWRPLAGELRAALQRTGAFRDVRLWYVTDLGSRVGLRSSPGRPAVEPGAALDPTGRQVTLVLSDCSGPHWWAGRAGAALHAWARRGPTALLQPLPERLWRRTAAPATPGRAIASRPGASNAALRFTPHDGRARRPAGALPVPVLELAPEWLADWAALVTATGDRPRDTAVTYVDATPTSRTEPRTAEGDLPIAERVLRFQLAASPTAADLAAHVALSVPALPVMRLIQQRVTPGSRPSDLAEVLLSGLLEPVDGERGLYDFVPGARTALLETLPRPESQAVTDLLTRLGAEIEARAGSTARSFRAVVPVAEGTGTRALGAAGEPFALVSEEALEVLRGRAIRVVERPVVAGPDEGGGIPEWQEVAEALWLATLNAREASAPPELTNVPLPGTGTFVGRAAEFRQLDGELLTPRSHAVDGPRAVVVHGMGGVGKTALARQWAANTVMGTSLSPVWLVTVRSGSDLTAGLADLAKAMTPAPAQATAEQLSEWAVNWLSSHADWVLVLDGVENPADIGAFLSRLGTGGRVLITSRLARGWEGVGRVLHLDVMEPAEAVAFLRARVGTDMQTADASNLAEAVGYLPLALEQAAAYMAREEITPAQYLMALERDLAEASASQAGAGHALRAALRAVDDPLAHRVLNVLAWLAPEPVPRSWLSGMAEEPELARTVRNLTRHSLLLSQDGGTLRIHPVVQGVLHESDEDDPWRSAEALEAARFEATVCLAGALPKDADDPAAWLRWQQLLPHIDELSERVAPGDENEYFATVLAEAAEFVMGQGEPERGIRMLWRAVEGRQRTPGPGYPATLRVTLWLARALRTVGRPREAVDLCESARGSAAMEDPDMVLVWTELADSYAELGEAGRAWGLFLKLRQFANEASAYEYPEWRRSCAAIAGLALTVDEPRAAVELYEATLAGCRRDLGGGHLDTIEVRSHLAAALYAAGSRERAKQEGAAVLNHLSRLYGTSHIRLIDAISEIARVHEDWEDGLPQAIQGYDEALRRSRAVRGESHPETLNLWSRLLAVLLRAGDTERTVERGNDWLSATTDALGPDHPETLRASAHLADAQWSNGAWTDAISRYKQVLNARRVVLGEDDPETWESYDRLAFALQEVGDAEGAVPLRGTVAAARSRVLGEAHPETLAAQERMALAHLGAEGADKAVELLTGVLGVRLRTHGDDFPDELVKTYNYLGYAYLEAGDHARATETYDTALRQCAQHLGDEDPRTIAMIRNLVEAYTAGGEAHMAVGLLEATVETLTQILGSAHRDVIALNDELTRLRHRRGSTDGP
>NZ_CP048641.1|WP_164328039.1|1616617_1617409_+|aldo/keto-reductase
MPQLGFGVWQVPDDEAEQAVTTALESGYRSVDTASLYENEEGTGRAIAKSGIARDKLFVTTKLRNRHQGYDSTLRAFDESLAKLGLDHVDLYLIHWPMPAKDTYIDTYKAFEKILADGRAKSIGVSNFLPEHLDRLIDATSVIPAVNQIELHPHLQQRASRAYHGEQGIATEAWSPLGQGKGLLEVPAIVAIAQKHGRTPAQIVLRWHLQLGTVVIPKSVTPSRIKENIEVFDFELDPEDMAAISALNEDRRLGPDPAAFEAP
>NZ_CP048641.1|WP_164318624.1|1632796_1633222_-|OsmC-family-protein
MATTRSAHTVWEGSLTEGSGTVTFDSSGIGQQAVSWPSRAEQANGKTSPEELIAAAHSSCFSMALSHGLTGAGTPPTKLVTSADVTFQPGTGITGIHLTVEGEVPGLDEAAFTSAAEDAKANCPVSQALTGTTITLSAKLA
>NZ_CP048641.1|WP_164318626.1|1633871_1635509_+|hypothetical-protein
MRMIYVDRGPSPVEPEKPGAAGDRDSTFGWWGAFSVETFADASPLRYTHEDATGFLEYPQKFYDRNFWFADGGVQVWAYEETFDNWQDRYGMDAVCAVYHSGHGNMDGNGVFEACLGAAWDGRTRAYSNRMALGNEKAKYVFWSTCFSLRVLGGHSPIRTWAGPNLGFRMLFGFETTSIDHPDYGRKFWDKWVSGQTYAEAWLNASWDIWKNQAPSVLAVGTTQAEAVNRLNTERYFYRDAVADNWYAWRWYNARESLTEQLTALPQGTQTVQLAPRNPSAELTQAGRIASFPAAALEEVQVDRQGVLSASSGDRVVSTGPLAVRWVRLAEPNTRNTTALPTDRAVELARAFAEEHADGAELIVDSVHDLMQNSGTKDGSEIGAPTTLQTHVTFRQAFDGVPIITPDRGVIRVGLDNDGTIVQAQLSTRQATSARREPSSQVAPPTAGGGQAPQAPAIGDPNEALAAAQESLLAELAVRGAGAGADYPSAVSREQQPEVRDVPGTFQVGYEVEGNEAYPAARKLIEIGPDDGFKTQRWVIAPLAR
>NZ_CP048641.1|WP_164318628.1|1635525_1636911_-|amino-acid-permease
MHDTGTVSPSAPAPHQEERLQDDGKHARSFSLPVATCLVMGNIIGGGIFLLPASVAPFGTISLVAFAVLTAGAIALALVFGRLARRDPRTGGPYVYAREAFGDFAGFLAAWSYWITTWVSNAALAVAAVGYLDVLIPVADHKWTACLAALTLQLLPALANFAGTRYVGAVQLVATVLKFLPLLLVAIGGLFFFDSANLGPFQASDDSPVGAVSASAAILLFSYLGVESAAVSAGEVRDPRRNVGRATVLGTLGAAVVYLLGTLAVFGTVAHDKLVASTAPFSDAVNAMFGGSWGGTAVALAALVSMVGALNGWTLLSAQTPYAAARDGLFPAAFAKKRRGVPVVGVLVTVVLASLLTVYNYTAGSSGVFEVLVLVTTFTATVPYLLATAAQIYFLISGQRERVDRGRLVRDSVLAALAFGFSMWLVAGAGYAAVYQGVLFLFVGVLVYAWMAARKQRTATQ
>NZ_CP048641.1|WP_164328042.1|1636995_1639122_-|hypothetical-protein
MSTLTMLALAGILPDFKLQSDDGDSATRIAITAALGAGAFGLLSALVWPLLVRALLLVPALVLGLLNFFLNGSLLLLALRMIPDGRGDANAETAVVVAAVMSAVASATGGALAVRDDDAYRRRLYRLADRRRRRADGARSPSTPGILFLQLDGVGHDVLTDAVGKGLMPTVARWLGRATENPETPPPPPTHRLTPWRTDWSSQTGASQLAILHGSNFDVPAFRWYEKDTGEVMVSNRPASAGELQRRAVARTGDPGLLADGGASRGNLFSGGADQLALVLSMAARRGKENRSRAGYFAYFSDPANAVRTALSFVAEVGREIGESTRARLCRRRPRVSRGGLYPFIRAFATVVERDVVVAAVIGDMLAGRAAVYADLVAYDEVAHHSGPTSGDAERVLRRLDRSLALIAQVADHAPRPYRIVLLSDHGQSPGETFRARYGLTLADLVRAGCGLPVPRRARRTHSGAEARSAVRAALRRPVEEGAGEHRPQRHAEPIVLASGNLGLVSFPDVSHRMTREEIDLRHPALLPTLANHPGVGFLLVRSEEHGALVLGARGAEVRLDDLRRADGADGPDGLGPLADFGPGAADAVRRTDSFPHTADIMVNSWYDPQEGEVLAFEEQIGSHGGLGGAQSRPFLLAPLALSPAVEDGGELVGAEAVHTVLRRWRDESRGQHKACDQHDTSVDNRRPDPAPPTAFPAADHAVQDKTH
>NZ_CP048641.1|WP_164318630.1|1639346_1639772_-|hypothetical-protein
MGHAGGAARAVRVAAIASLTPLEELDADPFLVDSRSQHAMCARWAAAQGYVVTRELVVRGLRADHAVLWNDVDAGLVDLFVVPCRRVLERALRSADEFTAECERRGVRIETAGFAEPAYDSRMKAHVHRRLSMPTAGYDGC
>NZ_CP048641.1|WP_164318632.1|1639874_1640654_+|MBL-fold-metallo-hydrolase
MRADVTVTWWGHATCTVEDSGTRVLTDPLFARRLAHLRRRRGALPPPQAALADVVLLSHLHADHLHVPSLARLAPGTRVLVPRGAARSVPGLRKLSHLRFTEVAPGDEVPAGDVVVRVVPALHDGRRLPLGPHRSPALGYVVEGRARTYFAGDTGLFDTMADEVGPVDVALLPVGGWGPYLGHGHLDPARAAEALARIAPRSAVPVHYGTYWPIGMDAVRPHEFHGPGEEFVRQAARRAPDVAVHRLGHGESVRPEVAR
>NZ_CP048641.1|WP_164318634.1|1640650_1641301_+|DedA-family-protein
MMLAAAATVTTDSTQQAVGYPSLFLLVVLGALVPVVPTGALVSSAAVVAFHQTDTSPFALLIVFGVAALAAFVGDMGLYWLGRRGMRSKNGSRWLEAIRDRAPAERLRMAQDRLDDHGVLVLVLSRLVPAGRIPVMLACLLAKMPLRRFARGNLPACLAWAVTYQLIGILGGSLFKEPWEGVALAVGLAVAISAAPTIWRRVRGTSSAPSGTGTGT
>NZ_CP048641.1|WP_164328043.1|1641400_1642426_-|hypothetical-protein
MDALGRAAFGTVRLWPRSFADRLTAPLPGLRAFARFAREGALRPRPEGLADIPRLPYEPGPLPRVDSRTVAVTWAGHASWVVRVGGLTVLTDPVWSRRILGTPARVTPVGVAWSALPRVDAVVISHNHYDHLDAPTLRRLPRDTPVFVPAGLGRWFTRRRFTRVAELDWWEGVELVPGGGAEGDSIEGGGGRRAGVRFDFVPAHHWSKRGLRDTCRSLWGGWVLTDGLGQRVYFAGDTGYGHWFSRIGERYPGIDLALLPIGAYEPRWWLRDVHCDPEEAVRAARDVGARRMAPMHWGTFLLSAEPVLQPLTRVREAWARAGLSRGDLWDLPVGGSRVLRG
>NZ_CP048641.1|WP_164328044.1|1642575_1643823_-|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MRRTDHEGRGRVRYGPPLPEPGLPVLPELSAALSAAAGRSHAQPPGGDPVLLDAASGYWSRRGLPAERGHVAAAPGAAPLLLALAAAIGGDVLLPRPCAAWWQPQVRLLGRSAYHVPTPAECGGVPDPYALLETVRRVRAEGGVPRLLVMSVADDPTATVPPPELVHEAVEAAAGEGLHIVSDETWRDTLHRPRETVLIGPAEMAPERVTVVCDLSGAFLPPALPAALARFPANGPGTALRARVLDVLSALGAAPAAPVAAAAAYALGEPDEITARLTAATRLHARVAAAVRDAVVAAGGFVRPPMAGRHLYADLGPLRAALAARGAGDAQELEDFLQEHLGMPAPGGHRFGDDIAALRVRLSTGPFLGSEPQQRLAALAAPDPLELPHVERALTLFGSAFDDLRAEAQRWEPPR
>NZ_CP048641.1|WP_164318635.1|1643950_1644826_-|hypothetical-protein
MRLSAPHLAMTLTTAALCTLAATPSAYAGDATAEVTPKHAAPGEQVTISVTCPATGGSPPQTMNANSQAFEHGTVQLQRAQHHEQTPQHQPNQSNQHSQDGTTQYDESNENGQYDEGGGRQDETGQFGGIDGFEEPLASFDAQEGLTPSDGLDPSAGIDSSGGLDPSGTTGLQGPGAAAGGIAYHGTARVAAAQSFEGGGPNAVGSGSEWAVDGTCHGDGQWKATFTVTRSGHTSTHKPDHTSPAAARGVHAGREGGFSDSPAALAAGALLVVGALGAAVHRLRRDRAYPR

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Crispr_ID: NZ_CP048641_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_2

1661705-1661804

Orphan

Consensus_repeat	Method
TTGAGGACGAGCGCGCAGCGCGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP048641_2

>merge|NZ_CP048641|2|1661705-1661804|CRISPRCasFinder
TTGAGGACGAGCGCGCAGCGCGACTGTGCGGCCACCACGGCGGCGGTGCGGCGGAGCATTTTCAGCCCGTCCGGCGTTTGAGGACGAGCGCGCAGCGCGA

>NZ_CP048641|2|2|1661705-1661804|CRISPRCasFinder
TTGAGGACGAGCGCGCAGCGCGA	CTGTGCGGCCACCACGGCGGCGGTGCGGCGGAGCATTTTCAGCCCGTCCGGCGT
TTGAGGACGAGCGCGCAGCGCGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164318666.1\|1658573_1659914_-\|NAD(P)/FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224172
NZ_CP048641.1\|WP_164318656.1\|1654892_1655954_-\|SRPBCC-family-protein	unknown	unknown	gnl\|CDD\|176859
NZ_CP048641.1\|WP_164318673.1\|1665205_1666102_-\|arginase-family-protein	unknown	unknown	gnl\|CDD\|212523
NZ_CP048641.1\|WP_164328048.1\|1660140_1661034_+\|mandelate-racemase	unknown	unknown	gnl\|CDD\|239444
NZ_CP048641.1\|WP_164318660.1\|1656836_1657598_-\|GvpL/GvpF-family-gas-vesicle-protein	unknown	unknown	gnl\|CDD\|377652
NZ_CP048641.1\|WP_164318658.1\|1656545_1656824_-\|gas-vesicle-protein	unknown	unknown	gnl\|CDD\|310007
NZ_CP048641.1\|WP_164318671.1\|1663158_1665117_-\|DUF5107-domain-containing-protein	unknown	unknown	gnl\|CDD\|375006
NZ_CP048641.1\|WP_164318681.1\|1672382_1673369_-\|LD-carboxypeptidase	unknown	unknown	gnl\|CDD\|132882
NZ_CP048641.1\|WP_164318677.1\|1666786_1667038_-\|LapA-family-protein	unknown	unknown	gnl\|CDD\|377648
NZ_CP048641.1\|WP_164318662.1\|1657594_1658029_-\|gas-vesicle-structural-protein-GvpA	unknown	unknown	gnl\|CDD\|236485
NZ_CP048641.1\|WP_164318683.1\|1673365_1675366_-\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|224423
NZ_CP048641.1\|WP_164318668.1\|1661827_1662355_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377816
NZ_CP048641.1\|WP_164318670.1\|1662501_1662861_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319962
NZ_CP048641.1\|WP_164328049.1\|1661070_1661643_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379082
NZ_CP048641.1\|WP_164318675.1\|1666158_1666719_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|224584
NZ_CP048641.1\|WP_164328047.1\|1655946_1656534_-\|DNA-primase	unknown	unknown	unknown
NZ_CP048641.1\|WP_164328050.1\|1670356_1672225_-\|CocE/NonD-family-hydrolase	unknown	unknown	gnl\|CDD\|334820
NZ_CP048641.1\|WP_164318654.1\|1654521_1654896_-\|gas-vesicle-protein	unknown	unknown	gnl\|CDD\|376379
NZ_CP048641.1\|WP_164318664.1\|1658173_1658494_-\|gas-vesicle-protein	unknown	unknown	gnl\|CDD\|368618
NZ_CP048641.1\|WP_164318679.1\|1667058_1670253_-\|NACHT-domain-containing-protein	unknown	unknown	gnl\|CDD\|368582

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164318666.1\|1658573_1659914_-\|NAD(P)/FAD-dependent-oxidoreductase	gnl\|CDD\|224172	COG1252, Ndh, NADH dehydrogenase, FAD-containing subunit [Energy production and conversion].	2.82062e-101
NZ_CP048641.1\|WP_164318656.1\|1654892_1655954_-\|SRPBCC-family-protein	gnl\|CDD\|176859	cd07817, SRPBCC_8, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.	9.82626e-38
NZ_CP048641.1\|WP_164318673.1\|1665205_1666102_-\|arginase-family-protein	gnl\|CDD\|212523	cd09999, Arginase-like_1, Arginase-like amidino hydrolase family. This family includes arginase, also known as arginase-like amidino hydrolase family, as well as arginase-like proteins and are found in bacteria, archaea and eykaryotes, but does not include metazoan arginases. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid.	4.02655e-79
NZ_CP048641.1\|WP_164328048.1\|1660140_1661034_+\|mandelate-racemase	gnl\|CDD\|239444	cd03328, MR_like_3, Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. 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. This subgroup's function is unknown.	1.0152e-126
NZ_CP048641.1\|WP_164318660.1\|1656836_1657598_-\|GvpL/GvpF-family-gas-vesicle-protein	gnl\|CDD\|377652	pfam06386, GvpL_GvpF, Gas vesicle synthesis protein GvpL/GvpF. This family consists of several bacterial and archaeal gas vesicle synthesis protein (GvpL/GvpF) sequences. The exact function of this family is unknown.	6.46828e-70
NZ_CP048641.1\|WP_164318658.1\|1656545_1656824_-\|gas-vesicle-protein	gnl\|CDD\|310007	pfam05120, GvpG, Gas vesicle protein G. These proteins are involved in the formation of gas vesicles.	3.78079e-21
NZ_CP048641.1\|WP_164318671.1\|1663158_1665117_-\|DUF5107-domain-containing-protein	gnl\|CDD\|375006	pfam17128, DUF5107, Domain of unknown function (DUF5107). This family is found in range of different bacterial species. In many proteins it lies N-terminal to a TPR-repeat region at the C-terminus.	2.50517e-29
NZ_CP048641.1\|WP_164318681.1\|1672382_1673369_-\|LD-carboxypeptidase	gnl\|CDD\|132882	cd07025, Peptidase_S66, LD-Carboxypeptidase, a serine protease, includes microcin C7 self immunity protein. LD-carboxypeptidase (Muramoyltetrapeptide carboxypeptidase; EC 3.4.17.13; Merops family S66; initially described as Carboxypeptidase II) family also includes the microcin c7 self-immunity protein (MccF) as well as uncharacterized proteins including hypothetical proteins. LD-carboxypeptidase hydrolyzes the amide bond that links the dibasic amino acids to C-terminal D-amino acids. The physiological substrates of LD-carboxypeptidase are tetrapeptide fragments (such as UDP-MurNAc-tetrapeptides) that are produced when bacterial cell walls are degraded; they contain an L-configured residue (L-lysine or meso-diaminopimelic acid residue) as the penultimate residue and D-alanine as the ultimate residue. A possible role of LD-carboxypeptidase is in peptidoglycan recycling whereby the resulting tripeptide (precursor for murein synthesis) can be reconverted into peptidoglycan by attachment of preformed D-Ala-D-Ala dipeptides. Some enzymes possessing LD-carboxypeptidase activity also act as LD-transpeptidase by replacing the terminal D-Ala with another D-amino acid. MccF contributes to self-immunity towards microcin C7 (MccC7), a ribosomally encoded peptide antibiotic that contains a phosphoramidate linkage to adenosine monophosphate at its C-terminus. Its possible biological role is to defend producer cells against exogenous microcin from re-entering after having been exported. It is suggested that MccF is involved in microcin degradation or sequestration in the periplasm.	5.20157e-96
NZ_CP048641.1\|WP_164318662.1\|1657594_1658029_-\|gas-vesicle-structural-protein-GvpA	gnl\|CDD\|236485	PRK09368, PRK09368, gas vesicle structural protein GvpA.	1.07237e-66
NZ_CP048641.1\|WP_164318683.1\|1673365_1675366_-\|S9-family-peptidase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	5.12247e-57
NZ_CP048641.1\|WP_164318668.1\|1661827_1662355_-\|hypothetical-protein	gnl\|CDD\|377816	pfam07332, Phage_holin_3_6, Putative Actinobacterial Holin-X, holin superfamily III. Phage_holin_3_6 is a family of small hydrophobic proteins with two or three transmembrane domains of the Hol-X family. Holin proteins are produced by double-stranded DNA bacteriophages that use an endolysin-holin strategy to achieve lysis of their hosts. The endolysins are peptidoglycan-degrading enzymes that are usually accumulated in the cytosol until access to the cell wall substrate is provided by the holin membrane lesion.	4.55978e-07
NZ_CP048641.1\|WP_164318670.1\|1662501_1662861_+\|VOC-family-protein	gnl\|CDD\|319962	cd16355, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	1.16997e-05
NZ_CP048641.1\|WP_164328049.1\|1661070_1661643_+\|hypothetical-protein	gnl\|CDD\|379082	pfam13238, AAA_18, AAA domain.	1.74316e-05
NZ_CP048641.1\|WP_164318675.1\|1666158_1666719_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|224584	COG1670, RimL, Acetyltransferases, including N-acetylases of ribosomal proteins [Translation, ribosomal structure and biogenesis].	3.72413e-22
NZ_CP048641.1\|WP_164318677.1\|1666786_1667038_-\|LapA-family-protein	gnl\|CDD\|377648	pfam06305, LapA_dom, Lipopolysaccharide assembly protein A domain. This family includes a domain found in lipopolysaccharide assembly protein A (LapA). LapA functions along with LapB in the assembly of lipopolysaccharide (LPS). Domains in this family are also found in some uncharacterized bacterial proteins.	0.0082049
NZ_CP048641.1\|WP_164328050.1\|1670356_1672225_-\|CocE/NonD-family-hydrolase	gnl\|CDD\|334820	pfam02129, Peptidase_S15, X-Pro dipeptidyl-peptidase (S15 family).	2.42682e-22
NZ_CP048641.1\|WP_164318654.1\|1654521_1654896_-\|gas-vesicle-protein	gnl\|CDD\|376379	pfam00741, Gas_vesicle, Gas vesicle protein.	2.94109e-15
NZ_CP048641.1\|WP_164318664.1\|1658173_1658494_-\|gas-vesicle-protein	gnl\|CDD\|368618	pfam05800, GvpO, Gas vesicle synthesis protein GvpO. This family consists of archaeal GvpO proteins which are required for gas vesicle synthesis. The family also contains two related sequences from Streptomyces coelicolor.	1.72176e-39
NZ_CP048641.1\|WP_164318679.1\|1667058_1670253_-\|NACHT-domain-containing-protein	gnl\|CDD\|368582	pfam05729, NACHT, NACHT domain. This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.	1.26909e-08

>NZ_CP048641.1|WP_164328049.1|1661070_1661643_+|hypothetical-protein
MENTEYAGHVANTGHAPEVVLIGGRSGVGKTSVGWEVAARLRAADVGHALIEGDLLDIVHPAPPGDPHRSHLTRRNLAALWANYAELGCRRLVYTNTACVLPSEEWLFTEALGTPRIVRVLLTATDDTAERRLRQRELGSELEQQLRRSAYMAHRLDTQVPPDTHRVATDDRAVGEIADEVIRRVGWTTR
>NZ_CP048641.1|WP_164328048.1|1660140_1661034_+|mandelate-racemase
MTGRDALSIPAAHDALTKAVRDTGRPGLACRAISALDIALWDLKARLLEVPLVRLLGAARDDVPVYGSGGFTTYHDTHLAAQLNGWVHGQGIPRVKIKVGEGWGRAAARDVTRVRTAREVIGQKAELYVDAGGAYTRKQAVRIGRVLAEHGVGWFEEPVSSDDLRGLSLVRDALVCDVAAGAYGCDLAYFARMIPAVDCLQADATRCGGLTEWLRAAALAQAHGLEMSARGAPHAHAAVAACVPNLRHVEWYHDHVRIESMFFDGALDPTGGTVRPDGGTGHGLRLRTPDVEEYRVA
>NZ_CP048641.1|WP_164318666.1|1658573_1659914_-|NAD(P)/FAD-dependent-oxidoreductase
MIVGAGFAGFQAARTLSRLTRRRADITLLNPTDYFLYLPLLPQVAAGVLEPRRVTVSLTGALRHVRLVLGEADGIDLARRTVNHTGPEGDRGELSYDRLVLAVGSVNKLLPVPGVAEHAHGFRGLPEALYLRDHVTRQIELAAAAEDAEVCRARCTFVVAGAGYTGVEVAAHGELFTRSLVRNRPLPDGVRPRWVLLDIAPRVLPELDRRLSDTADRVLRRRGVDVRTGTSVKEATRDGVRLDDGESVPTRTLVWCVGVRPDPLVAGIGKPLERGRLLVDPFLNVPGHPEVFACGDAAAVPDLAKPGQYTAMTAQHAWRQGKAAGHNVAASLGLGKRRSYRHHDLGFTVDLGGTSGAANPLGIPLSGPLAGAVTRGYHLAAMPGNRVRVAADWLLDAVLPRQGVQLGLVRSWSVPLDTASPELARVPGAPERPAEEQPKRLERPEE
>NZ_CP048641.1|WP_164318664.1|1658173_1658494_-|gas-vesicle-protein
MTQSPRKENRTKPEPDDLPGPVTVLRQAREQLAELTGMTAESVSSFERTEDGWELAVEVLELARVPDTMSLLATYAVTLDPQGELTGYRRTRRYERGRADPPRAGG
>NZ_CP048641.1|WP_164318662.1|1657594_1658029_-|gas-vesicle-structural-protein-GvpA
MTVVPAQQSGGAGGTSGLYDVIELILDRGLVIDAFVRVSLVGIEILKIDIRVVVASVDTYLRFAEACNRLDLEAGPRKDPGLPDLVGHITESGARGKSKGALSGAAETVSDAFRQARDEGRSEEEPARPRARRASSRSRKEDQE
>NZ_CP048641.1|WP_164318660.1|1656836_1657598_-|GvpL/GvpF-family-gas-vesicle-protein
MTTYIYGIAAATHPALPDGMGGIGEPAREVRAVRHGNLAAIVSDSPDDLRPKRRDLLAHQSVLDEAGAGGAVLPMRFGSLAQDDEAVVAVLAELAGHYEERLRALDGKAEYNVKAAHDEQAVLHQVLAENPELRAMAEANRVAGGGSYEQKLRLGEMVSAAVRAREGSDGIEVRRALEPCADAVSMGPEGTGWLANVSFLVRRDTADGFVAAVEELRKDQPHLELTVHGPLPPYSFVDPGPAQPADDAAAGVR
>NZ_CP048641.1|WP_164318658.1|1656545_1656824_-|gas-vesicle-protein
MGLIGEVLALPLAPARGTLWVLRQVVAEAERQYYDPSVIRKELALLTEQLEAGEIDDAEFDRREDVLLARLGHGSPVGGVARTDGTNGTGTS
>NZ_CP048641.1|WP_164328047.1|1655946_1656534_-|DNA-primase
MGLAVGAGYLLGRTKKAKLAFAVGTMVAGRRLQLGPGALARAVTQQLENNPQFKEIGDQLKEDLRGVGKAATGSLLDRQLEGLADRLHDRTLDVRDRLSGAVPDADEATDKAKDTGDTAADAGKSGAEKTGSGAKKTTSAARGAGKSAKKSTASRGTRQRSTQQRGTQQRSTAERGAQKRSPAKKAARARGGDDD
>NZ_CP048641.1|WP_164318656.1|1654892_1655954_-|SRPBCC-family-protein
MTDTRPSAAAHSPAADRLKDEARAYLMAQAERLLVGVGSKLGQATVRLNDVAEGRSPGFGKLALEGGRKLAAGKGPLRSAVELGGSHLKDSVKGALKGAVGRGRKSGGGKKPTVILEYVDVGVEVREAYDQWTQFQEFSTFAKGVKGATAAGDTDSDWQLKVFWSSRSWKAHVTEQVPDERIAWASEGAKGTTKGVVTFHPLGDRLTRVLLVVEYYPKGLFEKTGNIWRAQGRRTRLDLKHFARHLSIRGEASDGWRGEIRDGEVVRGHDEVTADEDTQDAEDGPYEDEASYEEDAPYEDEEPYEDEAEEVDEPEEADEAEAAEEVDDEEPDEAEEPDEADEYASAGGRRSRR
>NZ_CP048641.1|WP_164318654.1|1654521_1654896_-|gas-vesicle-protein
MTTASRLPEPYPQGGSNLADILERVLDKGIVIAGDIRINLLDIELLSIKLRLVVASVERAKEMGIDWWENDPALSSGARRTALARENEDLRRRVEQLERRELTEGGGASGAPRHDSRGEHERDR
>NZ_CP048641.1|WP_164318668.1|1661827_1662355_-|hypothetical-protein
MPVQDKNVPLPDKTLGDALSHVVHDAVRESLRDSLRTVLREELREELRAELSRATRKQRRKAALYAASGAVGLYAGAAAALSLGLVIALGLPGWAAALIVTALLAVAALLMRNAARAERGGVGGVPAAPKTPPTGGTAGFPTVPPSAGPGTPGTPETPGAGPPPPLAPKSRGPLE
>NZ_CP048641.1|WP_164318670.1|1662501_1662861_+|VOC-family-protein
MEILGTVLRVCVRDLEASVTFYERLTGSTAMRFERGGVSVASVGCFLLMSGPEAELEVLRKVAATIAVKDVDEAHATLTASGAHIVAGPVPTPAGRNLIAMHPDGAVFEYVDRNGPHTP
>NZ_CP048641.1|WP_164318671.1|1663158_1665117_-|DUF5107-domain-containing-protein
MATTVRRDVLTLPAAELGPENPLPPLRPLDEAHRLDDRDIRGLPRDMARQLAYEPLRSVLPARLRDGYGRARTPTAFETIVIENERLRVTVLPGLGGRIHSLFHKPTDRELLYRNPVFQPADFALNGAWYSGGIEWNIGATGHTALSCAPLHAARVTAPDGGEMVRLWEWERLRDTPFQVDLWLPEDSDFLHVGVRVRNPHEKPVPVYWWSNIAVPEERRVLVPADEAWHFGYARTLRKVPVPEYEGADRSYPLRGEFPADYFYDLPDGARRWIAAVDADGHGLVQTSTAPLRGRKLFLWGSGPGGRRWQEWLTEPGTGGYAEIQAGLARTQLEHVRLDAEAEFAWLESYGPLAAAPDVVHGDWAAARAEAEVRLAEALPAAAVDAAYEAWRACADTEPGEVLAVGSGWGALEVVRTQYKLPGTPFAESTLGPEQEPWLELLHSGAVPEPRRVGPPGPTLVAPHWRDMLETAPARPLAEYHLGVAQWHAGDLAQAVRSWERGLELSPSRWPLLRCLAVADHESGHLERAADRYAEAFDDLCAERRDDGVVWRGVTAALGREAVGVLLAAGRCAVARAVWDRVHPRTRASGRFRLIEAQLLLAEGEVAAARGVLEAGVEVADLREGDEVLGEVWAVVGGGAPLPGRYDFRMRP
>NZ_CP048641.1|WP_164318673.1|1665205_1666102_-|arginase-family-protein
MRNIVIIDAPSNLGLRPPAPGTVPGCYKLAGALRERGIVRRLNAFEGGVVVPPRYDRGDWKEGDGVFNAAAIAAYTPKLADRIERHVRAGDLPVVLGGDCSIQLGASLALRRLGRYGLAAVDASADFRHPGNSDGVGAAGGEELALATGRGQRDLTDIEGLRPYLRDEDVRLFGMRDEDEDRAELGELRIPTVTVGELRQWGVDDVARSALASLEDTALDGFWVHLDADVLDPSVMPAVDSPDADGLHPDELLALLRPLVRSPRCVGLNVTIYDPDLDPEGTAGDVLTDVVVAAFAQS
>NZ_CP048641.1|WP_164318675.1|1666158_1666719_-|GNAT-family-N-acetyltransferase
MLRPHTSHLAKGPRVGIRRYTRADAAEFTARARESRELHRPWLFPPTTDEAYAAYARALTADQTKAGFLVHERADGALAGFININNIVEGGFRSGALGYGAFAHAAGRGLMSEGLELVVGYAFGELRLHRLEINVQPGNAASIALARRAGFRLEGFSPDFLFIDGAWRDHQRWALTAEMTKARAGA
>NZ_CP048641.1|WP_164318677.1|1666786_1667038_-|LapA-family-protein
MSPKSSAGGSKSPSKGGVGALMTPGRVAVAAVALLTLIFIFENTRSTKIRLLIPEVTVPLWMALLGTGLIGALCGAFFVSRRK
>NZ_CP048641.1|WP_164318679.1|1667058_1670253_-|NACHT-domain-containing-protein
MARSRRWSGVPQHVTNRYEGGGAHTVVQAGVVRGGIHVHLRAEGARQLRPARRAVLAVALAAFGAQVLLRVAADWPARTAGALLVAGALWQALVALRDARADDEVFVPDDRLDAAAEVLASRLRSVYDREERLARVYDPVPLQVRWAAGDPTLSDHWRGIGGAESEQAPLDGELADVADAFRRLPMRRLVVLGAAGAGKSVLALRLARALLEPPVPAGDARAVHGSSRPVPVVLAPASWDVSACGPWEWAARQLAVQYPQIAAREDERMGLARALLESGRVLPVIDGFDEMPEGAQAEALRQLRKSLGPGRGLVLTSRPEAYARAVDAAPVLPGTAIVELLPLTVAQLTEFLPRTTRAVSGQEGPSVRTSVPGQVGPSASGRAGGADPATKWDPVLRRMAAAEAVVAVEAAQVAEAARTGKTKPRRRAAGAARRGKDPAARVLCAALSTPLMVGLARAAYSDTRADPAELLEPELFGDRDAVERHLLDAYVPAVYGIALDDRAARGPWDAHDARRWLRFLARQLQRRGSQELAWWRLDLMHRRLVSAIVPGLGLAVLIGALCWSGAGLAVGSAWPRLPLWTVFGTLTAAGLLLWAATQPRTELAGPRRLVFPRGWRPWRPVRTLTAPADIGAASGPWPLHRDDRLASLTTGVPRLVTGEAQPRLMTVALVLVVPLWFAEWWVAGLDWGHPGDFTDRVVFAAAWCLALLAQAWALTPWGRFVVARTYLAATRRLPWRLNAFLSDAHRRGVLRHSGGVYQFRHMELRDRLARHDSGGGGGGARDARGARRARSVWGVRGVSGDGDARARAELAETDFWFRTVLRIRVRSAAMSLRRSLDHGSLGVAVSLLLTTALFVWSFTALQSIPNAPGPYTSVPEACSLLGRSELRPVMPDPELAAVEPGQCVWIEQGPGRGAILRVIVKVARADRIAGAVSWADSMVRGNGKAGHPALRGVGDRATGMTEPSALDGGGHKATVFARVGNVFTMTTYDEQYADADRAMAVAGALTRRVLHNAGLPVPPGPRLKTAPLTRTAHPAPPPATPTVRDRVPLPILEPGEPPGRRSVR
>NZ_CP048641.1|WP_164328050.1|1670356_1672225_-|CocE/NonD-family-hydrolase
MFQSRRARRRARAPLAAVVGAALIAPLVLAAPPAGADDGGGGDRGRERGAVHASSGRYTVTPLKFTVPAGGRNCTVDADLYRPEGVDRAHRAPAVLATNGFGGSKEDGGTAAIGKAVAERGYVGLVYSGLGFGNSGCLISLDDPEIDGRAASGLLDFLAGERAADNGTVADFVTRDGAGDPRVGMLGGSYGGAIQLATAADDPRVDALVPLITWNDLAYSLAPNNAVDRLAGGHEVPGAAKWQWTNGFYLMGEGQPLLVPNLDPSRINALGCLHFVTEACETFRTLNSGRYPADRTRRFLDFARRVSPASYLHRVKAPTLLVQGQADTLFNLNEAEATYRTLKAQGTTAKMIWQSWGHSGGMDAPAAGELDLAKGDLGASYVGRRVLAWFDRHLRHDRSADTGPDFAYHRDWIDDPDRAYATASEVPALTRELYLSADGKLVDSPGKVKPGSREYRNRLASTSHSESSMAAMNGRPDRAPYDTKGTYLGWTTGPLTAPVDVVGAPEATLRVHSPTTERVQKSGDAADKLVLFAKLYDVAPDGTKTLVHRLIAPVRVPDVRQPFKVSLPGIVHRYAKGHRMRFVIAASDGAYGGNRGVKPVTVVSGRGEPGELRLPVVDGSPG
>NZ_CP048641.1|WP_164318681.1|1672382_1673369_-|LD-carboxypeptidase
MSAGVGRAGRPALASALVPPLVRPPRLVPGARVAVVAPSGPVPEDRLEAGLDLLRGWDLDPVVASHVLDRHGEFGYLAGADADRARDLERAWCDPSVSAVFCARGGYGAARMVELLDWDAMRAAGPKVFLGFSDITTLHEAFARRLGLVTLHGPMVAGADFLKNARAQEQLRLTLFEPERVQIIASPGRALVGGRAHGVTLGGCLSLLSADLGVPGARVSARGGLLFLEDTGEETYRIDRVLTQLLRAGWLDGVAGVALGSWEECDPYDAVRAVLLDRLGGLGVPIVEEFGFGHCDGALTVPFGIPGELDADAGTLRLDAPALAAARG
>NZ_CP048641.1|WP_164318683.1|1673365_1675366_-|S9-family-peptidase
MNDMAQTKPYGSWLSPIDAALAAAHDGGPAFVGFVGDEAWWTEPRPTEAGRRALVRRRAGGQEESVLPAPWNVRNRVIEYGGRPWAADARPGDPRGPLLVFADYADQRLYAYEPDVPEAEPRPLTPVSGVGGGLRWADPRVHLDRGEVWCVLEEFTGEEPTDVRRVVAAVPLDGSAAEDRAAVRELSDGRHGFVTGPRLSPDGAKAAWLGWDHPRMPWDGTELMVADVRADGTFDGARVFAGGPEESIVQADWAPDGRLLFVSDRTGWWNLYRAAPDGTAVALCPREEEFGGPLWQLGLSWFAPLDSGLIAVVHGTGATALGILDPETGEVVDAAGPWSEWSASLAVSGTRVAGIAASPRSAYEVVELDTRTGRARVIGAAHDDPVDPTYYPEPQIRTFLGPAGREIHAHIYPPHHPGHIAPGDELPPYVVWAHGGPTSRAPLVLDLAIAYFTSRGIGVAEVNYGGSTGYGRAYRNRLREQWGVVDVEDCASVALALADEGTADRARLAIRGGSAGGWTTAASLTTTDVYACGTILYPILDLGSWRGVDTHDFESRYLETLVGPYAEVPGRYEERSPARHADRITAPFLLLQGLDDVICPPAQCERLLERMERRGVPHAYIAFEGEGHGFRRADTVIRVLEAELSLYAQVFRLEPAGGTPTLELAK

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Crispr_ID: NZ_CP048641_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_3

1854723-1854828

Orphan

Consensus_repeat	Method
CAGCCCGTCCGGCGTTTGAGGACGAGCCGCGAAGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP048641_3

>merge|NZ_CP048641|3|1854723-1854828|CRISPRCasFinder
CAGCCCGTCCGGCGTTTGAGGACGAGCCGCGAAGCGGCGATTCGGCGGGGGTCGTCCCACCCACCCCATCCAGCCCGTCCGGCGTTTGAGGACGAGGCGCGAAGCG

>NZ_CP048641|3|3|1854723-1854828|CRISPRCasFinder
CAGCCCGTCCGGCGTTTGAGGACGAGCCGCGAAGCG	GCGATTCGGCGGGGGTCGTCCCACCCACCCCATC
CAGCCCGTCCGGCGTTTGAGGACGAGGCGCGAAGCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164318944.1\|1863778_1864471_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225107
NZ_CP048641.1\|WP_164318917.1\|1851702_1852626_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164318903.1\|1846165_1846714_-\|universal-stress-protein	unknown	unknown	gnl\|CDD\|238182
NZ_CP048641.1\|WP_164328068.1\|1848964_1849561_+\|nucleotidyltransferase-family-protein	unknown	unknown	gnl\|CDD\|133025
NZ_CP048641.1\|WP_164318908.1\|1848395_1848722_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164318914.1\|1851412_1851706_-\|SelT/SelW/SelH-family-protein	unknown	unknown	gnl\|CDD\|378415
NZ_CP048641.1\|WP_164318926.1\|1854915_1855557_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224647
NZ_CP048641.1\|WP_164318906.1\|1846800_1848312_+\|PLP-dependent-aminotransferase-family-protein	unknown	unknown	gnl\|CDD\|224089
NZ_CP048641.1\|WP_164318928.1\|1855641_1856853_+\|pyridoxal-phosphate-dependent-aminotransferase	unknown	unknown	gnl\|CDD\|181738
NZ_CP048641.1\|WP_164318898.1\|1843484_1844822_-\|allantoinase-AllB	unknown	unknown	gnl\|CDD\|163175
NZ_CP048641.1\|WP_164318901.1\|1845178_1845979_+\|IclR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224332
NZ_CP048641.1\|WP_164318919.1\|1852696_1853992_+\|VWA-domain-containing-protein	unknown	unknown	gnl\|CDD\|238733
NZ_CP048641.1\|WP_164318936.1\|1860714_1861308_+\|histidine-phosphatase-family-protein	unknown	unknown	gnl\|CDD\|366010
NZ_CP048641.1\|WP_164318941.1\|1862804_1863680_-\|oxidoreductase	unknown	unknown	gnl\|CDD\|236676
NZ_CP048641.1\|WP_164318938.1\|1861640_1862291_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164328069.1\|1857570_1858788_+\|monooxygenase	unknown	unknown	gnl\|CDD\|235980
NZ_CP048641.1\|WP_164318931.1\|1856880_1857522_+\|peptidase	unknown	unknown	gnl\|CDD\|239109
NZ_CP048641.1\|WP_164318939.1\|1862367_1862790_+\|acyl-CoA-thioesterase	unknown	unknown	gnl\|CDD\|223894
NZ_CP048641.1\|WP_164318933.1\|1858899_1860579_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|369777
NZ_CP048641.1\|WP_164318911.1\|1849782_1851405_+\|malate-synthase-A	unknown	unknown	gnl\|CDD\|236432

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164318944.1\|1863778_1864471_+\|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].	2.26884e-06
NZ_CP048641.1\|WP_164318903.1\|1846165_1846714_-\|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.	2.89265e-10
NZ_CP048641.1\|WP_164318941.1\|1862804_1863680_-\|oxidoreductase	gnl\|CDD\|236676	PRK10376, PRK10376, putative oxidoreductase; Provisional.	6.83938e-102
NZ_CP048641.1\|WP_164328068.1\|1848964_1849561_+\|nucleotidyltransferase-family-protein	gnl\|CDD\|133025	cd04182, GT_2_like_f, GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	1.49923e-53
NZ_CP048641.1\|WP_164318914.1\|1851412_1851706_-\|SelT/SelW/SelH-family-protein	gnl\|CDD\|378415	pfam10262, Rdx, Rdx family. This entry is an approximately 100 residue region of selenoprotein-T, conserved from plants to humans. The protein binds to UDP-glucose:glycoprotein glucosyltransferase (UGTR), the endoplasmic reticulum (ER)-resident protein, which is known to be involved in the quality control of protein folding. Selenium (Se) plays an essential role in cell survival and most of the effects of Se are probably mediated by selenoproteins, including selenoprotein T. However, despite its binding to UGTR and that its mRNA is up-regulated in extended asphyxia, the function of the protein and hence of this region of it is unknown. Selenoprotein W contains selenium as selenocysteine in the primary protein structure and levels of this selenoprotein are affected by selenium.	1.91603e-39
NZ_CP048641.1\|WP_164318926.1\|1854915_1855557_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|224647	COG1733, COG1733, Predicted transcriptional regulators [Transcription].	2.63061e-26
NZ_CP048641.1\|WP_164318906.1\|1846800_1848312_+\|PLP-dependent-aminotransferase-family-protein	gnl\|CDD\|224089	COG1167, ARO8, Transcriptional regulators containing a DNA-binding HTH domain and an aminotransferase domain (MocR family) and their eukaryotic orthologs [Transcription / Amino acid transport and metabolism].	1.7383e-96
NZ_CP048641.1\|WP_164318928.1\|1855641_1856853_+\|pyridoxal-phosphate-dependent-aminotransferase	gnl\|CDD\|181738	PRK09265, PRK09265, aminotransferase AlaT; Validated.	0
NZ_CP048641.1\|WP_164318898.1\|1843484_1844822_-\|allantoinase-AllB	gnl\|CDD\|163175	TIGR03178, allantoinase, allantoinase. This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.	0
NZ_CP048641.1\|WP_164318901.1\|1845178_1845979_+\|IclR-family-transcriptional-regulator	gnl\|CDD\|224332	COG1414, IclR, Transcriptional regulator [Transcription].	2.966e-71
NZ_CP048641.1\|WP_164318919.1\|1852696_1853992_+\|VWA-domain-containing-protein	gnl\|CDD\|238733	cd01456, vWA_ywmD_type, VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif. .	3.61807e-44
NZ_CP048641.1\|WP_164318936.1\|1860714_1861308_+\|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.	3.61091e-61
NZ_CP048641.1\|WP_164328069.1\|1857570_1858788_+\|monooxygenase	gnl\|CDD\|235980	PRK07236, PRK07236, hypothetical protein; Provisional.	1.43198e-70
NZ_CP048641.1\|WP_164318931.1\|1856880_1857522_+\|peptidase	gnl\|CDD\|239109	cd02549, Peptidase_C39A, A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.	6.36736e-05
NZ_CP048641.1\|WP_164318939.1\|1862367_1862790_+\|acyl-CoA-thioesterase	gnl\|CDD\|223894	COG0824, FcbC, Predicted thioesterase [General function prediction only].	8.77794e-28
NZ_CP048641.1\|WP_164318933.1\|1858899_1860579_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	1.70915e-20
NZ_CP048641.1\|WP_164318911.1\|1849782_1851405_+\|malate-synthase-A	gnl\|CDD\|236432	PRK09255, PRK09255, malate synthase; Validated.	0

>NZ_CP048641.1|WP_164318919.1|1852696_1853992_+|VWA-domain-containing-protein
MIIRKRFAAGLCALIAVLSMGLSPVAAYADDDPDHPGDADGATPKVELVLDVSGSMRARDIDGKSRMAAAKQAFNEVLDATPEDVDLGIRTLGANYSGDDRKTGCKDTEQLYPVGPLDRRDAKTAVATLSPTGFTPIGPALLKAAGDLKGGEGSHRIVLISDGEDTCQPLDPCEVAREISAKGIDLTIDTLGLVPNTKMRKQLSCIAEATGGTYTSIQHTDELSDRVGQLVDRAADPVVKPVAVEGADSCSAAPRLKPGLYTDREKFGEHRWYRVDVEPGQELRASVSVGADRAVNNDYGVLMRAVTKHDREIVRGSEAGDGRTDVISTGLRYPKPERDDDEETAETVCLQVSNSYSATSATAFADSKSKPGLPLELTVDIADAPDDASDVAAFGLGRGWWLLGALVLTGFVGGLLWGWLSRWRVAVWRTN
>NZ_CP048641.1|WP_164318917.1|1851702_1852626_-|hypothetical-protein
MLREVTAVRYLEPLRAGGSVPGLVEADDLGTYVLKFTGSAQGRKALVAEIVVGELGRRLGLRVPELVLAHFDPAVGAHEPHAEVQGLLRASAGLNLGMDFLPGARDFTPDSDLSDLDIDPLEAGKVVWLDALTANVDRTVHSSNLMVWPTFGTREPRLWLIDHGAALVFHHRWDAATVLATAEKRYDFRQHALGRYGPDTVAADAALAPRVTEELLREIVAEVPDAWIADEPGFATPAALRDAYVTYLTARARASAAWLPTDFPSRAELAAEDVLRAQATEAGRPAWLRRVPNLHGKPDPRPAKRYP
>NZ_CP048641.1|WP_164318914.1|1851412_1851706_-|SelT/SelW/SelH-family-protein
MSDSAEPHRVEIEYCTQCRWLPRAAWLAQELLTTFESELDELALKPGTGGVFVVRVDGEPVWDRREHGFPEPTAVKRLVRDRVASGRSLGHSEGKQG
>NZ_CP048641.1|WP_164318911.1|1849782_1851405_+|malate-synthase-A
MSAPAPSPLAIVDAEPLPRQEEVLTPAALAFVAELHRRFTPRRDELLTRRGERRAEIARTSSLDFLPETAAIRADDSWKVAPAPAALNDRRVEITGPTDRKMTINALNSGAKVWLADFEDASAPTWENVILGQLNLTDAYERRIDFTDERTGKSYALKDAGELATVVMRPRGWHLNERHLTDEEGRPVPGALVDFGLYFFHNAQRLLDLGKGPYFYLPKTESHLEARLWNDVFVFAQDYVGIPQGTVRATVLIETITAAYEMEEILYELRDHASGLNAGRWDYLFSIVKNFRDGGQKFVLPDRNLVTMTAPFMRAYTELLVRTCHKRGAHAIGGMAAFIPSRRDEEVNKVAFEKVKADKDREAGDGFDGSWVAHPDLVPIALASFDAVLGDKPNQKSRLREDVAVAPGDLIAIDSLDAKPTYEGLVNAVQVGIRYIEAWLRGLGAVAIFNLMEDAATAEISRSQIWQWINAGVVFENGTPATADLAREVAAAELAAIRAEIGEVAFAAGKWQEAHDLLLQVSLDADYADFLTLPAYERLR
>NZ_CP048641.1|WP_164328068.1|1848964_1849561_+|nucleotidyltransferase-family-protein
MERSGEVVGLLLAAGGGRRLGGCPKALLEHRGELFVERAARALRDGGCTRVHVVLGATADVVREQASLPGCVLVDNPDWHEGMGSSLRAGLASLRGTDAGAALVSLVDQPGIGAAAVARVLAAYRSPATLAAATYADERGHPVLFGADHWDGIAASATGDRGARAYLKEHAAAVTAVECGDVAEPYDIDTFSDLERLE
>NZ_CP048641.1|WP_164318908.1|1848395_1848722_-|hypothetical-protein
MLRSIGQRAVTGSFEDPRVTELRAAVSRLRRQLAAFPGEFPDRAIAEDELAALAAMAATGTPEPRRLRRSLLLVASSIGSVSALTDALAGVREAVETFGEFGEPPHPG
>NZ_CP048641.1|WP_164318906.1|1846800_1848312_+|PLP-dependent-aminotransferase-family-protein
MADVRVVHSVDRRLGGKRLADLVTGAVAGEKPGYRALAQAVHTLLLDGRVPLHTRLPAERELASALGVSRATVTAAYDLLRDSGFAASRRGASTWTELPEGRRPTNVAAYPPGPAGGAGGVGGVGDGMLDLAVAAPAAPAAELSEAVAAAAALLPAHAATAGYHPYGIPELRAAVAERFTRRGLPTLPDQILITTGAQQAISLVLALLGRPGDRVLVENPSYPNALDAIRRAGLRAMPVPVTDAGWDTALVESTLRQAAPRIAYLVPDFQNPTGALMGREQRVRILETARATGTWLLIDETIADIALDVPPPAPFASLAPHGVAEQVLTVGSLSKSHWGGLRIGWVRAGSRLITELAMARIPADMATPVLEQLVALHLMGGMDDVLRARLPKLRAARDALAAALTRQLPEWRWQLPPGGLSLWVDLGAPVASSLARAALGHGVRIEGGSRFGADPGTHEHRLRIPFTLAPDLYEEAAARLAAALAAGLDPAGGADPRHDDWVA
>NZ_CP048641.1|WP_164318903.1|1846165_1846714_-|universal-stress-protein
MEGLDGLGGEDGMDGIDGVEAAGRVVVGVSGVGVSGASLAALRAGARVARRDGRRLVAVLAWEPPEGEALYLRRPDPEWARHWEREAWGRLDAAFDAVFGGVPVGVEVERTVVRGPAGRVLCGVASRPGDLLVVGARGGRRWRGRVRRYVDGRAGCAVLVVPAVGVPRRLLRRVTVADVVGV
>NZ_CP048641.1|WP_164318901.1|1845178_1845979_+|IclR-family-transcriptional-regulator
MPTSSASTTDAAKSPASGGVQSLERAFDLLERMADAGGEVGLSELSASSGLPLPTIHRLMRTLVACGYVRQQPNRRYALGPRLIRLGESASRLLGTWARPYLARLVEETGETANMALLDGDEIVYVAQVPSKHSMRMFTEVGRRVLPHSTGVGKALLAHTPPEEVRALLARTGMPAATEKTITTADGFLDALEEVRRAGYAVDDNEQEIGVRCLAVSVPDSPTAAAISISGPAGRVTEAATEKIVPVLQQVAAELSVALATSAPSA
>NZ_CP048641.1|WP_164318898.1|1843484_1844822_-|allantoinase-AllB
MSGEELVLRSTRVITPEGTRPASVVVADGTIVAVRAYEAALPTRARVEDFGDDVLLPGLVDTHVHVNDPGRTEWEGFWTATRAAAAGGITTLVDMPLNSLPPTTTAAGLRTKREVAASKAHIDVGFWGGALPDNVKDLRPLHDAGVFGFKCFLSPSGVDEFPELTQDQLAVSMAEIAGFGGLLIVHAEDPHELAAAPAKAGPRYTDFLHSRPRVSEDTAIEGLIAVAKRIGARVHILHLSSSDALPLIAAAKREGVRLTVETCPHYLTLTAEEVPDGASEFKCCPPIREAANQDLLWQALADGTIDCVVTDHSPSTADLKTADFATAWGGISGLQLSLPAVWTAARERGHTLEDVVRWMSTRTADLVGLAQKGAIEAGRDADFAVLAPDETFTVDPARLQHRNRVTAYAGKTLSGVVKSTWLRGQRIVSDGEFSTPAGRLLERKN
>NZ_CP048641.1|WP_164318926.1|1854915_1855557_-|helix-turn-helix-transcriptional-regulator
MPPRQRRSYDQYCAAARALDAVGDRWTLLIVRELLAGPRRYTDLHADLPGVSTDVLASRLKDMEQVGLASRRRLAPPASSYVYELTDRGRELLPVLRALAAWGAPELAERRPTDAVRAHWFALPLLGALGSSSEEGLLEVRLDEGEFHVWVRGGGEVSYGDGPAPGEVDACVTLDAGTAVAVSRGALRFAEGVRDGRIVVVGEGAVAKVLREG
>NZ_CP048641.1|WP_164318928.1|1855641_1856853_+|pyridoxal-phosphate-dependent-aminotransferase
MEFRQSSKLSEVCYEIRGPVIEHANALEEAGHSVLRLNTGNPALFGFEAPEEIVQDMIRMLPGAHGYTDSRGVLSARRAVVQRYQALGLDDIDVDDVFLGNGVSELVTMAVQALLEDGDEVLIPAPDFPLWTAVTTLSGGKAVHYLCDEQADWYPDLDDLASKITDRTKALVIINPNNPTGAVYPREILEGMLDLARRHGLMVFADEIYDRILYDDAVHHSVATLAPDLVVLTFCGLSKTYRVAGFRSGWLVVTGPKQHARSYLEGLTMLASMRLCPNAPAQYAIQAALGGRQSIHELTAPGGRLYEQRDRAWQKLNEIPGVSCVKPRGALYAFARLAPKVHKIHDDEKFVLDLLLQEKIQVVQGTGFNWPRPDHFRILTLPYADDLDAAISRIGRFLSGYRQ
>NZ_CP048641.1|WP_164318931.1|1856880_1857522_+|peptidase
MSVTLCTTCGTPSLTQFASPDLVAKIVYEGHDRADDPAWRESGAATLEDYARWCAHLCGIACFRMALGPDAPSLFELRDGALKYGAYTEDAEGVIHGLIYAPFAEYARDVHGVEATVHRHLALDEIVQLLDAGRTVMTSVHFEIRRPERPAPGRGGHLVLLTGRTADGLLHFHNPSGIDARSRTAELSPEAFEPFFAGRGVSMVTHMGVSATR
>NZ_CP048641.1|WP_164328069.1|1857570_1858788_+|monooxygenase
MHSGRVAVVGGSVAGCAMALAAHRGGADEITVYERAAGRLAERGVGLAVHNSRYAELESAGYMDADMPWVQIVRRRWYVRDERASGPLGQQIGTMPFPFRTYNWGPLWGELRRRVPESVEFRTGTSVEAVRSSPVGAEVDADGGTERFDVVIGADGYRSVVRDAAHPGLRAEYAGYLAWRGAYPETRLADPHLWAEEDCVYVVFDGGHVIVYRIPDGAGGHRVNWVLYTAPPPGLDSLLGFTSPTSLPPGGLTDTLGAHLAYVADELLPPYWGSLVRATEPDELFLQPMYDFTAPRYARDRVLLAGDAATVARPHTGAGAVKALQDATVLESAIATATTWPEALESYDTDRTVAGRTMVDLGRRLGRALVEETPRWRDLDQPGLEAWWRRADGSGAFGGRELRSR
>NZ_CP048641.1|WP_164318933.1|1858899_1860579_-|methyltransferase-domain-containing-protein
MHPAQKFGDNPVEVRETGHYTEEYVPSFVEKWDSLIDWERRAGSEGDFFMDLLRKRGVKSVLDVATGTGFHSVRLLAAGFDTVSADGSADMLAAAFANGMKDGHVMRVVQADWRWLNRDVHGEYDAIVCLGNSFTHLFSERDRRRALAEFYAMLKHDGILVLDQRNYDAILDDGYTSKHKYYYCGEDVSVEPEYVDEGLVRMRYSFPDDSVYHLNMFPLRKDYTRRLMSEVGFQNVETYGDFQHTYRGEQPDFFVHVAEKEYRTDDEEDERYTGAVGVARNYYNSSDADTFYAKVWGGEDIHIGLYEGIDEPIADASRRTVERMAGKLGLTRDSVVLDLGSGYGGSARYLASTYGCRVLALNLSEVENQRHKELNHARGLSGLIEVVDGSFEDIPYPDDVVDVVWSQDAFLHSGNRARVLEEVSRVLRPGGQLIFTDPMAVDDCPPGVLQPILDRIHLDNMGSPGFYASELARLGFVPQGGGPAGPGGRGGFEEHREQLVTHYARVLEETRRQEADGLAGQVSHDYLTQMKKGLARWVDAGGDGHITWGILHYRRGDGA
>NZ_CP048641.1|WP_164318936.1|1860714_1861308_+|histidine-phosphatase-family-protein
MGDLLLVRHGETEWSRSGRHTSWSDVPLTDNGRAQARALAPLIGKYRVDAAFTSPRVRARETAELAGFGQARVDPDMAEWDYGAYEGITTVEIHRTHPDWFLFTDGAAPGPPEHPGESPDDVGARADRMLAKVDAALANTEGSVALFAHGHYLRVLTARRLGLPPSAGALFQLATGTVSRLSYEHGRPVLATWNVRP
>NZ_CP048641.1|WP_164318938.1|1861640_1862291_+|hypothetical-protein
MAKPTTPAQRRIIAAADPVTGRLTGTEAQLTALVRLQLAFRHPRPPHAYFLTPAGHRVRDEPVGTAPETAPVEPVAGVFAARTGTEEAPDEDGPSRAREVRGAWLGLVEMRRMTNPDGDKERPCAWERAHLPQAAAIALEAAGRVPARPSRAPARPGREGYRVTATEQPDAVAVREPTAEGVRACATVLERAGWQVSEHGEARTGRRYVLASPRRA
>NZ_CP048641.1|WP_164318939.1|1862367_1862790_+|acyl-CoA-thioesterase
MSEQFAVSVTVRGYETDSQGHLNQSVYLQYAEHARWSILRAAGIDQRDLIDKGVGPVALENTVRYRSELRAGDEVEVDCVFVWSEGKTFKVEQTITKADGTVAATVSGLGGLLDLKERRMVPAPGEYFRALASDPRVLGL
>NZ_CP048641.1|WP_164318941.1|1862804_1863680_-|oxidoreductase
MPNVNDIHASAAGHLLIGGDLPVQRMGFGAMRLPSRTWDGPPHDPDNARAVLRRAVELGVDHIDTAAFYFYKDLAANDFIREALHPYPDNLVIATKVGPDRDRDHNWLTPADPAKLKADVHRNLRQLGREQLDLVYLRFHGEEGPGNGRFEALAELREQGLIRHLGVSNATPEQLAEAQSVAPVAAVQNKFSPVDRGADAKAMVELCAGQDIAFVPFYPLGGTGAPHIEGLRRVADRHGATAAQVGLAWSLSVSPTVLAIPGTSSLAHLEENIAAAALRLDAADLAELGSA
>NZ_CP048641.1|WP_164318944.1|1863778_1864471_+|response-regulator-transcription-factor
MEHGGAAAAIVTLRGEAELVRRAGDLIASARTEYLCGATDLVTWSAGTNAVFNEGRRPRLRPGPDGLAMRKVYTRAALGDPESERRLARIAASGAHVRISSAPLAREAIVIDGRVAILAGSEARGARTYTVIREPDVVEGVRSLLYATWEAADDLADCLGPAASASARPPVLDEESRAVLAALADGLTDETAARRLGMSLRTYRRRVAALMADLGATSRFQAGVLSRRAG

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Crispr_ID: NZ_CP048641_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_4

2121742-2121865

Orphan

Consensus_repeat	Method
CGTCGGCCACACACCGGACCAGCGAACGACAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP048641_4

>merge|NZ_CP048641|4|2121742-2121865|CRISPRCasFinder
CGTCGGCCACACACCGGACCAGCGAACGACACCCGGGGCCGCCAGGCCTGGCCACGCCCCGAGCCCCGGACGACCCAAGCCCGCCCGAACACGTCGGCCACACCACCGGACCAGCGAACGACAC

>NZ_CP048641|4|4|2121742-2121865|CRISPRCasFinder
CGTCGGCCACACACCGGACCAGCGAACGACAC	CCGGGGCCGCCAGGCCTGGCCACGCCCCGAGCCCCGGACGACCCAAGCCCGCCCGAACAC
GTCGGCCACACCACCGGACCAGCGAACGACAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164319336.1\|2127895_2128387_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164319321.1\|2112130_2112874_-\|tellurium-resistance-protein	unknown	unknown	gnl\|CDD\|226696
NZ_CP048641.1\|WP_164319338.1\|2128474_2128882_-\|peptide-methionine-(R)-S-oxide-reductase-MsrB	unknown	unknown	gnl\|CDD\|376583
NZ_CP048641.1\|WP_164328106.1\|2133346_2134735_+\|PhoX-family-protein	unknown	unknown	gnl\|CDD\|253386
NZ_CP048641.1\|WP_164319328.1\|2117969_2119232_+\|DUF1266-domain-containing-protein	unknown	unknown	gnl\|CDD\|377728
NZ_CP048641.1\|WP_164319340.1\|2128895_2130278_-\|UDP-N-acetylmuramate--L-alanine-ligase	unknown	unknown	gnl\|CDD\|234757
NZ_CP048641.1\|WP_164319323.1\|2115703_2116528_+\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|131480
NZ_CP048641.1\|WP_164328105.1\|2130366_2130822_-\|indole-3-glycerol-phosphate-synthase	unknown	unknown	unknown
NZ_CP048641.1\|WP_164316718.1\|2112913_2115559_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164319319.1\|2111213_2112134_-\|protein-phosphatase-2C-domain-containing-protein	unknown	unknown	gnl\|CDD\|379325
NZ_CP048641.1\|WP_164319332.1\|2122110_2122656_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225783
NZ_CP048641.1\|WP_164328103.1\|2107149_2107599_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164319342.1\|2131033_2131852_-\|pyrimidine-reductase-family-protein	unknown	unknown	gnl\|CDD\|184482
NZ_CP048641.1\|WP_164319334.1\|2122652_2123906_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164319344.1\|2132085_2133180_+\|cell-division-protein-ZapE	unknown	unknown	gnl\|CDD\|224402
NZ_CP048641.1\|WP_164319315.1\|2107602_2109852_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|368383
NZ_CP048641.1\|WP_164319330.1\|2119364_2121671_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP048641.1\|WP_164319325.1\|2116524_2117835_+\|cytochrome-P450	unknown	unknown	gnl\|CDD\|225035
NZ_CP048641.1\|WP_164319317.1\|2109841_2111194_-\|protein-kinase	unknown	unknown	gnl\|CDD\|223589
NZ_CP048641.1\|WP_164328104.1\|2124282_2127615_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276938

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164319321.1\|2112130_2112874_-\|tellurium-resistance-protein	gnl\|CDD\|226696	COG4245, TerY, Uncharacterized protein encoded in toxicity protection region of plasmid R478, contains von Willebrand factor (vWF) domain [General function prediction only].	7.98164e-16
NZ_CP048641.1\|WP_164328106.1\|2133346_2134735_+\|PhoX-family-protein	gnl\|CDD\|253386	pfam05787, DUF839, Bacterial protein of unknown function (DUF839). This family consists of several bacterial proteins of unknown function that contain a predicted beta-propeller repeats.	4.70096e-114
NZ_CP048641.1\|WP_164319328.1\|2117969_2119232_+\|DUF1266-domain-containing-protein	gnl\|CDD\|377728	pfam06889, DUF1266, Protein of unknown function (DUF1266). This family consists of several hypothetical bacterial proteins of around 235 residues in length. Members of this family seem to be found exclusively in the Enterobacteria Salmonella typhimurium and Escherichia coli. The function of this family is unknown.	1.61686e-35
NZ_CP048641.1\|WP_164319340.1\|2128895_2130278_-\|UDP-N-acetylmuramate--L-alanine-ligase	gnl\|CDD\|234757	PRK00421, murC, UDP-N-acetylmuramate--L-alanine ligase; Provisional.	0
NZ_CP048641.1\|WP_164319323.1\|2115703_2116528_+\|alpha/beta-fold-hydrolase	gnl\|CDD\|131480	TIGR02427, b-ketoadipate_enol-lactone_hydrolase, 3-oxoadipate enol-lactonase. Members of this family are 3-oxoadipate enol-lactonase. Note that the substrate is known as 3-oxoadipate enol-lactone, 2-oxo-2,3-dihydrofuran-5-acetate, 4,5-Dihydro-5-oxofuran-2-acetate, and 5-oxo-4,5-dihydrofuran-2-acetate. The enzyme the catalyzes the fourth step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. This enzyme also acts in catechol degradation. In genomes that catabolize both catechol and protocatechuate, two forms of this enzyme may be found. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other].	3.47525e-21
NZ_CP048641.1\|WP_164319338.1\|2128474_2128882_-\|peptide-methionine-(R)-S-oxide-reductase-MsrB	gnl\|CDD\|376583	pfam01641, SelR, SelR domain. Methionine sulfoxide reduction is an important process, by which cells regulate biological processes and cope with oxidative stress. MsrA, a protein involved in the reduction of methionine sulfoxides in proteins, has been known for four decades and has been extensively characterized with respect to structure and function. However, recent studies revealed that MsrA is only specific for methionine-S-sulfoxides. Because oxidized methionines occur in a mixture of R and S isomers in vivo, it was unclear how stereo-specific MsrA could be responsible for the reduction of all protein methionine sulfoxides. It appears that a second methionine sulfoxide reductase, SelR, evolved that is specific for methionine-R-sulfoxides, the activity that is different but complementary to that of MsrA. Thus, these proteins, working together, could reduce both stereoisomers of methionine sulfoxide. This domain is found both in SelR proteins and fused with the peptide methionine sulfoxide reductase enzymatic domain pfam01625. The domain has two conserved cysteine and histidines. The domain binds both selenium and zinc. The final cysteine is found to be replaced by the rare amino acid selenocysteine in some members of the family. This family has methionine-R-sulfoxide reductase activity.	5.95831e-75
NZ_CP048641.1\|WP_164319319.1\|2111213_2112134_-\|protein-phosphatase-2C-domain-containing-protein	gnl\|CDD\|379325	pfam13672, PP2C_2, Protein phosphatase 2C. Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.	4.82693e-25
NZ_CP048641.1\|WP_164319332.1\|2122110_2122656_-\|hypothetical-protein	gnl\|CDD\|225783	COG3243, PhaC, Poly(3-hydroxyalkanoate) synthetase [Lipid metabolism].	0.00527697
NZ_CP048641.1\|WP_164319330.1\|2119364_2121671_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	4.12604e-06
NZ_CP048641.1\|WP_164319342.1\|2131033_2131852_-\|pyrimidine-reductase-family-protein	gnl\|CDD\|184482	PRK14059, PRK14059, pyrimidine reductase family protein.	6.45923e-90
NZ_CP048641.1\|WP_164319344.1\|2132085_2133180_+\|cell-division-protein-ZapE	gnl\|CDD\|224402	COG1485, COG1485, Predicted ATPase [General function prediction only].	6.16438e-61
NZ_CP048641.1\|WP_164319315.1\|2107602_2109852_+\|hypothetical-protein	gnl\|CDD\|368383	pfam05308, Mito_fiss_reg, Mitochondrial fission regulator. In eukaryotes, this family of proteins induces mitochondrial fission.	0.000822678
NZ_CP048641.1\|WP_164319325.1\|2116524_2117835_+\|cytochrome-P450	gnl\|CDD\|225035	COG2124, CypX, Cytochrome P450 [Secondary metabolites biosynthesis, transport, and catabolism].	4.89413e-73
NZ_CP048641.1\|WP_164319317.1\|2109841_2111194_-\|protein-kinase	gnl\|CDD\|223589	COG0515, SPS1, Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair].	1.00139e-17
NZ_CP048641.1\|WP_164328104.1\|2124282_2127615_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|276938	cd15831, BTAD, Bacterial Transcriptional Activation (BTA) domain. The Bacterial Transcriptional Activation (BTA) domain is present in the putative transcriptional regulator Mycobacterium EmbR and the related Streptomyces antibiotic regulatory protein (SARP) family of transcription factors, which includes DnrI and AfsR, among others. Members of this family contain an N-terminal DNA-binding domain, followed by the BTA domain, and many have diverse domains at the C-terminus. EmbR contains an C-terminal forkhead-associated (FHA) domain, which mediates binding to threonine-phosphorylated sites in a sequence-specific manner. The BTA domain of EmbR contains three Tetratricopeptide repeats (TPRs) and two C-terminal helices. The TPR motif typically contains 34 amino acids, and 5 or 6 tandem repeats of the motif generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein.	1.73183e-29

>NZ_CP048641.1|WP_164319330.1|2119364_2121671_+|tetratricopeptide-repeat-protein
MRGQEQGGHNELGGTVHGPAVQAQTVYGGIHIQSPPAAAQPPHPPWQLPPAARITDRTAELGLLERHRLRSGSAGHGDHAGLGGHASLGDRLGQGGHTLVAVSGLGGVGKTALTLAWLHALRPHFPDGQLYADLGAQSPGGPADPGEVIGRFLRALGVPAAQVPAGLAERAALYRSLTAGRRLVVLLDDAASAAQVRRLLPGGRSVTAVTSRWRMPGLTVDGCHSVRLEPLGVDEAVELLAATLSDDRVADQPEQARALVELCAGLPLAVRVAGARLASRPRRGITTMVRALTEEHDRLEELAIDGDHNVRATLDLTYQELPPDAARLYRLLGLHPGTEFSDAVAVAVLAEPGPSAGAEPGPGAGPGPGPSAPAAPATAASSSHASRALSLLDLLHDANLLTDADAHEDRHRFHDLVRLHAAAKAAQDESPWARAAALRRIADHYLATATRAERIVDPQHRTMARDHGAGPVLTEDFGEGTEAALDWQERELPNLMAVIRRARTAFPTVGWQLADALWPLFLRRKFYEEWRAAHQEGLAAAEDLGDTAAQCRMLTSGGVGELGMGCHERALEMFERAARQFRADGNALGHARTLNYRGLAHQRLGRLDEAARYFTRAAEALPGVGDVRAGGLGRLNLADVALARSRPTEAARHAAAAHTTLRAANDTYNAARAAVLLGRAHLARGEPDLAEAELTPALIALRAMSAAYETARALHALAELAEHRGTPAPARALYGEALTLYAEAGRATSPDARAAETRLNALATPPPQ
>NZ_CP048641.1|WP_164319328.1|2117969_2119232_+|DUF1266-domain-containing-protein
MYAAAEDEYHDDLFPVVPAPQDGTRWQAPADLEEHLYELVEAEDGYGYLRALAVEGVYRPVLLTDLAASPDAPPLFSVEVPDGRRVAQVYTAGFLPRPHPDIVYEYVTLGTLAREWPSDIDVMVVNTQTPCEQYYLTTDEEREVWADLHDEHHREGRIDDRVDTRRTGAPDGQVLRGLACGAHLCFANGAPWNTLDWHGAGYSNEVARLEEWWGVRDREEWRGVQDRLLDREVSPWYWDFVLGARTAVIAEQGTPVDPELWRRCVEVTLRNRVVETGGPDTPHRPGDDPELDQFVRAMRDLVGKVMRYEARFRADGLLPPDGLVATVAAWDLGRASKMARWGRGARYATHAELLTALERAAHGAQSAYTSWEDFSAGYVLGRCLHFDEEEFGTWYTSVLRAHRALTTDPDSPWLRVPFRD
>NZ_CP048641.1|WP_164319325.1|2116524_2117835_+|cytochrome-P450
MTTPQHPLPHAPDVFDPRLYAHSVPYDRYRTLRDHHPVAWQEEPAVLGWPAGPGFWAVTRHADVTAVLKDSATYSSHLGATQIRDPDPADLPFIRRMMLNQDPSPSSQLRSSRGDPIVHGRLRTLVSRAFTPRRVARFEAVARERARSLLSGAVDEARAGDGTCDLVATVTDDYALLNLADLLGVPKSDRGLLLHWTRRVIGYQDPDEAGEPVLGPDGRPVNPRSPAMLADMFAYAAELAAHKRRHPGDDILTALATTPELTTAELEMFFFLLTVAGNDTVRGAAPGGVLALAGHPGELRGLREGTAPVALAVEELLRWHPPVLSFRRTAARDTELAGRRIRRGDKVVVFHAAANRDERAFPEPDRLDLTRDPNPHVSFGDGPHVCLGAHFARLQLVVFYEELLEAVPVLHPAGPPHRLVSHFINGLKTLPLRVVD
>NZ_CP048641.1|WP_164319323.1|2115703_2116528_+|alpha/beta-fold-hydrolase
MTAFILPHELHGDGAHKVLAVHGWFADRSAYAPVLPDLDTDAFQYALVDLRGYGEAKDAVGSYTTAEGAADVLDLADRLGWERFSLVGHSMGGKVAQRVVALAPHRVRRLVGVSPVPASALPFPPEQWELFASAAHLADNRRTIIDLTTGGVRPAAWLDRMVTRSLARSDVKAFRAWLDSWAGEDFHDRVEGCQVPALAVVGALDPALPADLMRQTWLTWFTRGELVELPGVGHYAADEAPLDLIRTVEDFLRADDAAAETAGAEASQPPAADA
>NZ_CP048641.1|WP_164316718.1|2112913_2115559_-|hypothetical-protein
MAIRHLKYRLDEEPVTGTVRLVAVPESVPHSAPDAPSPAAPDEPAEPVRAAEVAEWVELAVGAGCGPYGGGLGPEARFSFSRLPDGASLLCHTVDAGRGVRAIHLTGPEAARFVEEWPVTLLATGAVRGSGGSGGSGSVGDSGDSGDSGDSGNSGDSGGFGDAGDFRDSGDDIPGPGGPFAREQLVAFARAHEPRVAPFLADVRRLFDDPAGRQLVVAEESPDTVARWIALACASLPPSYVPSLTFATRAADPGRAPQHIVGIGPDAAFDRYDATALAHHYRVHDGLGGPGSPPLTDVWATWTARLWTAGVALPGAGTSGAEASADASVAVRGPEASAEDSGAERDPKASAEANSAESDPEPDPFSPSRLVPPLLQAGLLSAEELAALPADQARAAVDALVTLVVTAPVSDDGPLPDLAALCEGLHAHAPAAAAPLALALARRRLNSVAPPELSGELAAVCAELPLSDDTKRALRAEYGGDADKALRRALLEPPAAWVEPLRIAFAVGADGGRGLTAAMSRLARDLRDTDDRARAAAVHVLEEVGLAPLTRRVLKLLGDESGVRRLDLLRDLAASEHGDWLRRHLDENSPLPLRLAEAAARWHGRGDGLRGFELFSRLTELLPERQVTDAQTLELVWRLVWRSGAPAPAELPRVVRACTVRLLVQARLGRHVKAVVTAPERVDQETVSFARELLHDPNLKRSERATASLLILAQDLADHRVSLPQGVHQLRALQVDAEQLADSVRHGVGRYVALALVRAPADQLARSPLYRYLISSGPELLKPYRQFMLDEGKRDELDHALPRQPAEICAYYFLWRPARQEGVDPYWRKVSEELLREILVPVVRGLDERALSDVATVIANLPEGENRLREWNAWRDSLREG
>NZ_CP048641.1|WP_164319321.1|2112130_2112874_-|tellurium-resistance-protein
MIHLERTSVSRTNSVSGSSEAADNFPGGAMASRPVHFIWMLDCSGSMSVNGKIGQLNFAIREAIPEMQQAADANPAASLLVRAISFASGASWHVGEPTPVDSFSWEDVHTYGGTDMGAAFKLVAGALDTPPMPQRALPPVLALASDGQPTDDWRAGLRAIDSTPWGKRAVRVAVAIGDDADKSMLKEFLGNPELEPLQAKNPRQLAAAIRWMSTAVVKDASTPKIEDARPATPVGPPLTKDGEDEIW
>NZ_CP048641.1|WP_164319319.1|2111213_2112134_-|protein-phosphatase-2C-domain-containing-protein
MTAVRETPAPAGDWELLRGAVKGVAKKYSQDRCSAKATAGGRAVVLAVADGHGSAPHFRSDMGARWAVEEFTACAEAFAHEAVRVGADAALWPGLRAEARRLPQAVGHRWQRRALLHDANAPAHGASPARRAAARERFERQGSAGTWDFTAYGSTLIGAVLTRQMLLCWQLGDGDIVVIDDGGVPHTPLSTGPDMGDETDSLCEPEPWRKTRTHWQPITGGPPPAVLLSTDGLSKSFADHQGFLDFATGVRERAAQQGVAAVQKQLQDWLERAARYSGDDTTLVAAFAAEHDGAPEQTAQEGTTPA
>NZ_CP048641.1|WP_164319317.1|2109841_2111194_-|protein-kinase
MSNGMLASGKQLVTEAGERVTVGELFGSGGQGEVYRVATPRGDRAVKWYYPQLADARQRHILEGLIEKGWDDDRFLWPESIVMDPDGKEPGFGYLMDVRPARFQELPALFKRDDCVKDATMRTLVTVCLHTVEAYRALHSKGIAYRDINWGNIFFDPRTGDVLVCDNDNAVVEGGTAGVAGTMDFMAPELVRGDRGAQPGTQTDLHSLAVLLFLILMNEHPFNGALAMRIHCMGEAAKRKLYGTDPVFVYDPVDTRNRPVVGEQPTVIATWAALPQILRDLFVQTFTDGLKVPAKRVRETQWRDALSQVLDAITQCRQCGKQNLTQPDGAAPDCWKCRQPLQLPPRLELVTATGTTLRTRRGIRLDPSARVYAHHLDGDPDRHDFRAVVGEVTEHPKQRGRYGLTNRTQTVWTVRKEDGSVREIEPGRTIALQSGLLLEFGGGVEAEVKE
>NZ_CP048641.1|WP_164319315.1|2107602_2109852_+|hypothetical-protein
MATTWRPGVRATDSGTPPPLPVLPQFPGMRGYTQLRTAIRDLGFRHAAELLREPGRQRAASGVFGTLPKAETDDGFRVLDGLWFPGRGGFWQRVDVPFVRRARDAWQTSADPRALTAAAVTDTLETLARDDPMGLRRVVLWELCCLLKDGATKGSGPNGGRTEQGSSRKGGAKQGAATTADDVAALGVHRSEARLLAAAVDAVFPADGEPRRAAEEFNDVWPSLRLRRAEHVADLLPAAPDDHVLAARLGGLRARSAKVRFLAYAARRSQEGGDPRAASAAWLRALRQATDAPELRAGLLRAATALADAPSTPAEAAVTVTKDDRRVGLTWRTAHAPRTHPAPVTYTVLLFPDGAPERATKVAEVTQVDPQDQELTVHHPDAPVGRALRYAVLPLRGDRVAGVPRVTAPVVIAPDVKDLTAVPVPGGIRLRWRPHRAAVEVEVRRHGLADAGPPHGPTVVPCAGDGAMDSAAAVGTYTYEVRCGYPAPGGRRAWSDGVRVTARVEEWPTPVEKLTAERVGEAGDRVLLRWKPARRGRSTLLPWPEGPVAAGTDVSERFARVATGLTAGGDAPDLRPEAPHPRWWDAPAQQLEVPPVPPAGRLRMTAVSVLGDRAVAGASVVVEHPDAVRDLTVRRVSADRARVRFSWPEPAVLVLVSWHDATRGVAHRVARSRHRAEGGAVELAVPETACTVSVTPLPRPDAVAVPTPPAHAELPALPPPPPPPPVAPPPPSWWDRWRRWLPRRPRATP
>NZ_CP048641.1|WP_164328103.1|2107149_2107599_+|hypothetical-protein
MLAGWLFADLLLVLALVSMADRPDPLAARDPKPSNSADASSKPKKPKPTGPRSVERKPEEFEVKGTDKGALADQIGRSTQKWRGRTAALVLTFGGGRDGTVYAHRVNSLLGKGRPEMFTKKTATDDFHDLSTDVSTALVRVYFFTEPGG
>NZ_CP048641.1|WP_164319332.1|2122110_2122656_-|hypothetical-protein
MTVRVVVAPGVVPVVAPVAAPVLTAVVTATPEARGVERVRVVLRRLGTEYVDEHVRVEVPIAGAGAGAGAGAGAGDWARLGDVLHAESAVPWHAVRLGARYPGALVVAAHHGGVCRVRVGPRGAALVLRTALPAWGARGARPGVPWPVWASLAHAFLVAGLPPRGLAGARVVCGVGVRLGW
>NZ_CP048641.1|WP_164319334.1|2122652_2123906_-|hypothetical-protein
MSVTMLEAHGHPVPVRPDVERWATRPVRRRVLAVVHTVTSGRRLLDAVRLLEGDWRVQVFFTAAPDVFSGGVADFLDELKVLVLPWSQAVQTVFDLALAAGHGGLHELHAPVVVLPHGAGHNKIVRARRGGAVAARGVYGLSRQRLVRDGSVVPEAIVLAHREELERLGRECPEALPVAEVVGDPCFDRVTASRPARALYRQALRTRAGQRLVLVCSTWGPGSLLGSGGQELLDRIVAELPPEDYRVAVLLHPHVWHTHSEWQVRGWFAGLGRGGLAVVSHRADWVGALVAADFVVGDHGSVSLYGAMTGRPVLLACLPDGDVDPGSPMAELGSFAPRLHESKPVRRQLERAAATYRADLHERVAARITSEPGRFARRMRALLYRKLRLRAPAGFPATEPARLPRVVEYDEPGSVVS
>NZ_CP048641.1|WP_164328104.1|2124282_2127615_+|tetratricopeptide-repeat-protein
MVDLLALGPLELWQDGRQHELGSPKERCVLAVLVHARGEPVSLDALMDRVWDDEPPRTAQDTLQSYLSRLRNRLGRAAGEQALLERYAPRLYRLRVAPDAVDLLRYARLRTDAAVTARQGGRQRAVELLRAAESLWRGEPLTEFTGSWARSARARLVEDHRHVREGRIRLELELGRHADLIGELHELAAQNPLAQRVIAALMLALYRSGRDDEALDLYRATRARLHEGQGIEPGTELQELHVRILEQDRTLMTPAAPESGGAPGPSGAGQGRPPHVPDARAERPASGGRAADDAPADRRPTAEEPLTNLPRDMGHFTGRASELRILLGVSGTPRALPLTVVHGMPGVGKTALALHAAHRLAEACPDGRFYVDLRGYGPLPPYDPAEALAVLLHAAGVPGELPGSLDARVTRWREWTARRRVLVVLDNARDADQVRPLLPGAGTCRAVVTSRNRLTGLAGATPLYLEVLSTTEAATLFTRVAGPGRLPADTSALTRTVAACGRHPLALQLLASQFRHRDSWSLDHLTDRLVQAADPLDEFDSDAVASAFSLSYAELTPKAAQLLRRLALHPGPDITLGAATALAADAPDREEGREGGAPGREADQDPAHAARTRKTLDQLLDRNLVEEPVTDRYRLHDLTRAFGLRMATRDEPHSARRAALTRLLNCYLTGAYRAAVRTDPHHRILPPEPHLTCPYAPDFGDADEAAAWLSVERGNLLAVARTAAAESPEHAALFPHVLAKSLRLWGTWDLASELFEAAVSAARTRDDQVALARTLVEHADVLTQKDHGKALHRATEALFLFQELNDVRGRADALLQSGRAHFAAGQGSTCLRVLRAAHTLYRQVEDPYGQADVANMMGVALHSAGRHREALDQFRTVLRVHERTGHLYGQMRALNNVGEVYRLDGRHEEARTHFERSLRLAHSVGGRQERANLLANLGSVCQDTGRVEQALTYFRRALASYRAASDARGESDTLISLGSAYAANSRPGEALWHFAEAERIAWSIGSPLDLQAALLGTGTALRQLGRYEAALDAHHEALRIAREAGSPLGAARALDGLARTSPHTQNASSARGFAEDALELYGRLGCAGRARDLRLALAEPGETSAARSTT
>NZ_CP048641.1|WP_164319336.1|2127895_2128387_-|hypothetical-protein
MTAVREAIHGKGAFRKELPTRLAKGPDKDWDGFLHFAEGIVLVGLALGWAYMGVDQEKPLYIGGGLVLAVALLVGTLFVVRDDAREKAVERAGLPRADYFWLPARYCGGCESVFCPQGEPWRGVLTPEQFKRLVWSEAGYADQLAAGDKAKDAEVPPGTVVGR
>NZ_CP048641.1|WP_164319338.1|2128474_2128882_-|peptide-methionine-(R)-S-oxide-reductase-MsrB
MSYDIEKPDEEWRAELTPAEYQVLRQAGTEPAFRGEYTDTTTKGVYSCRACGAELFTSHEKFESHCGWPSFYDPKDTDAVELIEDRTHGMVRTEVRCARCGSHLGHVFEGEGYATPTDQRYCINSISLRLAADEG
>NZ_CP048641.1|WP_164319340.1|2128895_2130278_-|UDP-N-acetylmuramate--L-alanine-ligase
MPTAMDRPHFIGIGGAGMSGIAKILAQRGAKVAGSDAKDSATADALRALGARVDIGHAAEHLASDATCVVVSSAIRADNPELARAAELGIPVVHRSDALASLMDGRRPIAVAGTHGKTTTTSMLAVTLSALGLDPSYAIGGDLDVPGSNALHGAGDIFVAEADESDRSFHKYTPEVAIVLNVELDHHANYASMDEIYESFETFAGKIVPGGTLVVSADQAGAVELTRRLRDLGQLKVVTYGESETADLRIHKITARGLTSEVTVFLDGKLLTFTVSVPGRHYANNAVAALAAGIALGIPSRNLAAALKSYTGVKRRLQLKGEAAGVQVVDSYAHHPTEMTADLEAMRSAAGDSRILVLFQPHLFSRTQELGTEMGQALALADSSVVLDIYPAREDPIPGITSALIIDAARAAGAEVLAAGDRADAVREIAGMAKPGDLVLTMGAGDVTDLGPRILAELSK
>NZ_CP048641.1|WP_164328105.1|2130366_2130822_-|indole-3-glycerol-phosphate-synthase
MIEKALTSADVEFVTTLHGDEPVTFHVLLQPRGDQADRLLRAIDDVALGELDDAVREGEVPEGQEAVEPAERALQVSLVALRATGSAAEGRLVEAHPLDVLQEAVDDLGADEVIVLTEPHLVEEFFHRDWASRARHKVGVPVLKLFAHSES
>NZ_CP048641.1|WP_164319342.1|2131033_2131852_-|pyrimidine-reductase-family-protein
MRRLFPVTDHTAAPTSAKTSPDEVVADREWSLDELADAYAYPAGPLDPAGTGAWLRANMVSTLDGAAQHDGRSQPISNATDMRIFGTLRGLADAVVVGAETVRQEGYRPARAREAFAARRAAAGQAPAPAIVVVSASLDLDFSLPLFTAPLTPTYVVTGAAASSDRMAAARAAGAEVVTAGEGAGADPARVVRALAERGLTRLLTEGGPRLLGQFVAAQALDELCLTVSPMLTAGGAQRIAGGPGLAAPERFVLASILEEAGFLFTRYRRGL
>NZ_CP048641.1|WP_164319344.1|2132085_2133180_+|cell-division-protein-ZapE
MSATTSAAGPSPIPEAAPVSLSAREPQVPADRLVAEMVPPPRFSTARFDTYIPDPGQPSQSEAVRVLSTFAAGLGGAHATGAGKRRWFARAKQTVPAGPRGVYLDGGYGVGKTHLLASLWHATPAEPALKAFGTFVELTNLVGALGFQQTVRTLGGHRLLCIDEFELDDPGDTVLVSTLLGKLVDAGVALAATSNTLPGKLGEGRFASADFLREIQGLSAHFKALRIDGEDYRHRGLPEAPAPYSEEQVTKAAYATEGASLDDFPHLLDHLARVHPSRYGALTDDLKAVCLTDVTPVPDQSTALRLVVLADRLYDREVPVLASGVPFDRLFSEEMLNGGYRKKYFRAISRLTALARDAKGLVQS
>NZ_CP048641.1|WP_164328106.1|2133346_2134735_+|PhoX-family-protein
MRSGAEPSATTRRQVLARTGALGASIAFTGALSELFAGTATAATQGRTGYGPLVPDPDGLLDLPKGFRYQVLSREGEPLRSGEGKVPSNHDGMAAFRGRRGGVHLVRNHENRATAKLGVPTVKGLTYDPAAKGGCTALALDRHGRVVDERVAIAGTAVNCAGGPTPWGTWLTCEETEDKAGTSGYTKDHGFIFEVDPVDPRRTGAVPLTAMGRFQHEAVAVDPWRGVVYETEDAFQKPFGLFYRFLPNKPEGGRGSLRAGGRLQAMRVPGVPDLSAIQETGATFDGVEWADVPDPLAAQTPIRHQDFGPKGITHAQKLEGCYWGGRCVYFVSSFAHSAEGSAADHFGQVWRYDPARRRLTLVIVFGPDTDIQLPGESPDNICLAPSGGLMVCEDGGGTQHVYGVTRGGKVYAMARNAQNLGTPEEPEWGEFAGVAFSPDHDTMYVNCYTPGTTFAVTGPWRR

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Crispr_ID: NZ_CP048641_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_5

3609076-3609170

Orphan

Consensus_repeat	Method
CCTGTGGTGCGGCGGCTGCCCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP048641_5

>merge|NZ_CP048641|5|3609076-3609170|CRISPRCasFinder
CCTGTGGTGCGGCGGCTGCCCGCCCGGCGGGGGTGGCCTGTCGTGCGGCGGCTGCCCGCCCGGCGGAGACGTCCTGTCGTGCGGCGGCTGCCCGC

>NZ_CP048641|5|5|3609076-3609170|CRISPRCasFinder
CCTGTGGTGCGGCGGCTGCCCGC	CCGGCGGGGGTGGCCTGTCGTGCGGCGGCTGCCCGCCCGGCGGAGACGT
CCTGTCGTGCGGCGGCTGCCCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164321454.1\|3610849_3611275_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319898
NZ_CP048641.1\|WP_164328256.1\|3614869_3615589_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|131997
NZ_CP048641.1\|WP_164328253.1\|3609376_3610330_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|187759
NZ_CP048641.1\|WP_164321444.1\|3599192_3600947_+\|succinate-dehydrogenase-flavoprotein-subunit	unknown	unknown	gnl\|CDD\|236185
NZ_CP048641.1\|WP_164328255.1\|3614190_3614607_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164321457.1\|3618571_3619315_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_CP048641.1\|WP_164321453.1\|3610380_3610719_-\|cupin	unknown	unknown	gnl\|CDD\|380358
NZ_CP048641.1\|WP_164321449.1\|3602488_3603214_-\|respiratory-nitrate-reductase-subunit-gamma	unknown	unknown	gnl\|CDD\|376889
NZ_CP048641.1\|WP_164328257.1\|3615631_3616102_-\|carboxypeptidase-regulatory-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|379297
NZ_CP048641.1\|WP_164321456.1\|3611900_3613298_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863
NZ_CP048641.1\|WP_164321451.1\|3603213_3603762_-\|nitrate-reductase-molybdenum-cofactor-assembly-chaperone	unknown	unknown	gnl\|CDD\|225091
NZ_CP048641.1\|WP_164321452.1\|3603758_3605396_-\|nitrate-reductase-subunit-beta	unknown	unknown	gnl\|CDD\|224063
NZ_CP048641.1\|WP_164321446.1\|3600946_3601708_+\|succinate-dehydrogenase-iron-sulfur-subunit	unknown	unknown	gnl\|CDD\|235652
NZ_CP048641.1\|WP_164328252.1\|3597586_3598138_+\|2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline-decarboxylase	unknown	unknown	gnl\|CDD\|184333
NZ_CP048641.1\|WP_164321438.1\|3595681_3597292_-\|family-20-glycosylhydrolase	unknown	unknown	gnl\|CDD\|119334
NZ_CP048641.1\|WP_164321442.1\|3598675_3599167_+\|succinate-dehydrogenase-hydrophobic-membrane-anchor-subunit	unknown	unknown	gnl\|CDD\|239580
NZ_CP048641.1\|WP_164328254.1\|3613316_3613625_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164321447.1\|3601861_3602485_+\|Uma2-family-endonuclease	unknown	unknown	gnl\|CDD\|368559
NZ_CP048641.1\|WP_164321455.1\|3611234_3611831_-\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP048641.1\|WP_164321440.1\|3598286_3598667_+\|succinate-dehydrogenase,-cytochrome-b556-subunit	unknown	unknown	gnl\|CDD\|239581

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164321454.1\|3610849_3611275_+\|VOC-family-protein	gnl\|CDD\|319898	cd06587, VOC, vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.	7.93041e-09
NZ_CP048641.1\|WP_164328256.1\|3614869_3615589_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|131997	TIGR02952, RNA_polymerase_sigma-70_factor_ECF_subfamily, RNA polymerase sigma-70 factor, TIGR02952 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building, bidirectional best hits and one-to-a-genome distribution, to represent a conserved family. This family is found in a limited number of Gram-positive bacterial lineages.	1.27008e-21
NZ_CP048641.1\|WP_164328253.1\|3609376_3610330_+\|hypothetical-protein	gnl\|CDD\|187759	cd09319, TDT_like_1, The Tellurite-resistance/Dicarboxylate Transporter (TDT) family. The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes members from all three kingdoms, but only three members of the family have been functionally characterized: the TehA protein of E. coli functioning as a tellurite-resistance uptake permease, the Mae1 protein of S. pombe functioning in the uptake of malate and other dicarboxylates, and the sulfite efflux pump (SSU1) of Saccharomyces cerevisiae. In plants, the plasma membrane protein SLAC1 (Slow Anion Channel-Associated 1), which is preferentially expressed in guard cells, encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. SLAC1 is essential in mediating stomatal responses to physiological and stress stimuli. Members of the TDT family exhibit 10 putative transmembrane alpha-helical spanners (TMSs).	3.21068e-61
NZ_CP048641.1\|WP_164321444.1\|3599192_3600947_+\|succinate-dehydrogenase-flavoprotein-subunit	gnl\|CDD\|236185	PRK08205, sdhA, succinate dehydrogenase flavoprotein subunit; Reviewed.	0
NZ_CP048641.1\|WP_164321453.1\|3610380_3610719_-\|cupin	gnl\|CDD\|380358	cd02230, cupin_HP0902-like, Helicobacter pylori HP0902 and related proteins, cupin domain. This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.	1.56922e-14
NZ_CP048641.1\|WP_164321449.1\|3602488_3603214_-\|respiratory-nitrate-reductase-subunit-gamma	gnl\|CDD\|376889	pfam02665, Nitrate_red_gam, Nitrate reductase gamma subunit. This family is the gamma subunit of the nitrate reductase enzyme, the gamma subunit is a b-type cytochrome that receives electrons from the quinone pool. It then transfers these via the iron-sulfur clusters of the beta subunit to the molybdenum cofactor found in the alpha subunit. The nitrate reductase enzyme, EC:1.7.99.4 catalyzes the conversion of nitrite to nitrate via the reduction of an acceptor. The nitrate reductase enzyme is composed of three subunits. Nitrate is the most widely used alternative electron acceptor after oxygen.	6.10569e-118
NZ_CP048641.1\|WP_164328257.1\|3615631_3616102_-\|carboxypeptidase-regulatory-like-domain-containing-protein	gnl\|CDD\|379297	pfam13620, CarboxypepD_reg, Carboxypeptidase regulatory-like domain.	2.46811e-09
NZ_CP048641.1\|WP_164321456.1\|3611900_3613298_+\|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.	3.7954e-53
NZ_CP048641.1\|WP_164321451.1\|3603213_3603762_-\|nitrate-reductase-molybdenum-cofactor-assembly-chaperone	gnl\|CDD\|225091	COG2180, NarJ, Nitrate reductase delta subunit [Energy production and conversion].	1.08253e-33
NZ_CP048641.1\|WP_164321452.1\|3603758_3605396_-\|nitrate-reductase-subunit-beta	gnl\|CDD\|224063	COG1140, NarY, Nitrate reductase beta subunit [Energy production and conversion].	0
NZ_CP048641.1\|WP_164321446.1\|3600946_3601708_+\|succinate-dehydrogenase-iron-sulfur-subunit	gnl\|CDD\|235652	PRK05950, sdhB, succinate dehydrogenase iron-sulfur subunit; Reviewed.	2.90593e-146
NZ_CP048641.1\|WP_164328252.1\|3597586_3598138_+\|2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline-decarboxylase	gnl\|CDD\|184333	PRK13798, PRK13798, putative OHCU decarboxylase; Provisional.	2.86488e-42
NZ_CP048641.1\|WP_164321438.1\|3595681_3597292_-\|family-20-glycosylhydrolase	gnl\|CDD\|119334	cd06564, GH20_DspB_LnbB-like, Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.	6.3327e-89
NZ_CP048641.1\|WP_164321442.1\|3598675_3599167_+\|succinate-dehydrogenase-hydrophobic-membrane-anchor-subunit	gnl\|CDD\|239580	cd03500, SQR_TypeA_SdhD_like, Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase D (SdhD)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.	2.86905e-45
NZ_CP048641.1\|WP_164321457.1\|3618571_3619315_+\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	2.09758e-72
NZ_CP048641.1\|WP_164321447.1\|3601861_3602485_+\|Uma2-family-endonuclease	gnl\|CDD\|368559	pfam05685, Uma2, Putative restriction endonuclease. This family consists of hypothetical proteins that are greatly expanded in cyanobacteria. The proteins are found sporadically in other bacteria. A small number of member proteins also contain pfam02861 domains that are involved in protein interactions. Solutions of several structures for members of this family show that it is likely to be acting as an endonuclease.	1.46788e-28
NZ_CP048641.1\|WP_164321455.1\|3611234_3611831_-\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	3.51644e-17
NZ_CP048641.1\|WP_164321440.1\|3598286_3598667_+\|succinate-dehydrogenase,-cytochrome-b556-subunit	gnl\|CDD\|239581	cd03501, SQR_TypeA_SdhC_like, Succinate:quinone oxidoreductase (SQR) Type A subfamily, Succinate dehydrogenase C (SdhC)-like subunit; SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. Members of this subfamily reduce low potential quinones such as menaquinone and thermoplasmaquinone. SQR is also called succinate dehydrogenase or Complex II, and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are similar to the Thermoplasma acidophilum SQR and are classified as Type A because they contain two transmembrane subunits as well as two heme groups. Although there are no structures available for this subfamily, the presence of two hemes has been proven spectroscopically for T. acidophilum. The two membrane anchor subunits are similar to the SdhD and SdhC subunits of bacterial SQRs, which contain heme and quinone binding sites. The two-electron oxidation of succinate in the flavoprotein active site is coupled to the two-electron reduction of quinone in the membrane anchor subunits via electron transport through FAD and three iron-sulfur centers. The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes.	2.05288e-40

>NZ_CP048641.1|WP_164321452.1|3603758_3605396_-|nitrate-reductase-subunit-beta
MRVLAQIAMVMNLDKCIGCHTCSVTCKQTWTNRSGMEYVWFNNVETRPGQGYPRRYEDQEKWRGGWELNRRGALKLKSGGRFHALATIFSNPVLPEIKDYYEPWTYEYKNLTDAPLGDDYPVAEPRSLITGKPMKIEWSSNWDDNLGGGAEGVAADPMVAKAQARETADRAAVQVKAAFEQTFMFYLPRICEHCLNPACVASCPSGAMYKRTEDGIVLVDQDRCRGWRKCVTGCPYKKVYFNHRTGKAEKCTLCYPRLEVGLPTVCSETCVGRLRYLGVVLYDADKVTAAASTPDEKALYEAQLGVFLDPADPEVRRAAERDGIPHDWIEAARRSPAYALISTYRVALPLHPEYRTMPMVWYVPPLSPVVEALTGTGHDGEDAGNLFGAIDTLRIPLEYLAELFTAGDVGPVRAALERLAAMRSYMRGVNLGDPADPSVPARVGMTPQDIEDMYRLLAVAKYEERYVIPTAAVGDARRLEESAVPDGCGLDVPGGPGMLPSGPPGAGPFGDDSGTYQGLPLVTIENFHASRRRQTADDVSAEEEL
>NZ_CP048641.1|WP_164321451.1|3603213_3603762_-|nitrate-reductase-molybdenum-cofactor-assembly-chaperone
MTDLAVLYQGAAHCLCYPDSEVRERLPLVRAAVPELHPFLDEFAGWSPTAAMEHYVRVFDFKNRHSLYLSWWLDGDTRRRGASLVAFKETYRAHGLSVTGEELPDYLPAVLEFTARTGDRTLLTSHRAGLELVRLALTDDGTPYALILDAICATLPGPSPKDRVEARALARSGPPTETVGLD
>NZ_CP048641.1|WP_164321449.1|3602488_3603214_-|respiratory-nitrate-reductase-subunit-gamma
MDTFLWGVLPYVALVLLIAGTLWRYRYDKFGWTTRSSQVYESRLLNIASPAFHYGILFVLVGHLMGLFVPESWTNAVGLKERAYHLLSLYGGTAAGVLAVAGIALLLYRRRTNTPVFRATTRNDKLMYAVLLAAVIMGMWAKLTNSSPNSGYNYRETIAPWARSIFTLRPDISAMEGVPLTYRIHAVIGLTLIALVPFTRLIHMFSAPVQYLFRPYVVYRSRGAGELGRRKERRGWEKVDS
>NZ_CP048641.1|WP_164321447.1|3601861_3602485_+|Uma2-family-endonuclease
MSAASVEQPYEDEEPFSLTAIADEIMERHPGYRVEIIGGHLLVTPSPDAPHARALTKLMRPFIASGLDDGDIEVLQNVGLWLPTGIEDYAIPDLAVVDADIDDHLVENNAYDPVCFRLVLEVTSSNWRDDLKTKVTAYAEAKVPVYVVVDRKHQRLHVLTDPKGGEYGNHQVHAPGQVIALPDSIGAKVSLDVAEILKASQPKRRTD
>NZ_CP048641.1|WP_164321446.1|3600946_3601708_+|succinate-dehydrogenase-iron-sulfur-subunit
MATPTMDKVEAEAAASDHLITVTFRIRRFNPEVSADAVWEDFQLEIDPKERVLDGLHKIKWDLDGTLTFRRSCAHGICGSDAMRINGKNRLACKTLIKDINPAKPITVEPIKGLTVLKDLVVDMDPFFQAYRDVMPFLVTSGNEPTRERLQTAEDRERFDDTTKCILCAACTSSCPVFWNDGQYFGPAAIVNAHRFIFDSRDEAGEQRLEILNDKDGVWRCRTTFNCTDACPRGIEVTKAIQEVKRALITRRF
>NZ_CP048641.1|WP_164321444.1|3599192_3600947_+|succinate-dehydrogenase-flavoprotein-subunit
MKIHKYDTVIVGAGGAGMRAAIEATKRSRTAVLTKLYPTRSHTGAAQGGMAAALANVEEDNWEWHTFDTIKGGDYLVDQDAAEILAKEAIDAVLDLEKMGLPFNRTPDGTIDQRRFGGHSRNHGEAPVRRSCYAADRTGHMILQTLYQNCVKEGVEFFNEFYVLDQLIVEEDGVKKSAGVVAYELATGEIHVFQAKSVIYASGGTGKFFKVTSNAHTLTGDGQAACYRRGLPLEDMEFFQFHPTGIWRMGILLTEGARGEGGILRNKDGERFMEKYAPVMKDLASRDVVSRSIYTEIREGRGCGPEGDHVYLDLTHLPPEQLDAKLPDITEFARTYLGIEPYTDPIPIQPTAHYAMGGIPTNVEGEVLSDNTTVVPGLYAAGEVACVSVHGANRLGTNSLLDINVFGRRAGIAAAEYSAKADYVELPENPAELVVSLVEQLRDSTGTERVADIRKELQETMDANVMVFRTEQTIKTAVEKIAELRARYKNVSVQDKGRRFNTDLLEAIELGNLLDLAEVMAVSALARKESRGGHYREDYPNRDDVNFMRHTMAYREVADDGKDSIRLDYKPVVQTRYQPMERKY
>NZ_CP048641.1|WP_164321442.1|3598675_3599167_+|succinate-dehydrogenase-hydrophobic-membrane-anchor-subunit
MSDITLQKSDGSGVGPVEGISLYDADNPAPVIEAPRKRTSKTPRSTRGNFEMAAWLFMRLSGVVLVVLVLGHLLIQLVLDGGVSKIGFAFVAGRWASPFWQVWDLLMLWLAMLHGANGLRTVINDYAERPNTRLWLKGLLYTATVFTILLGTLVIFTFDPNIR
>NZ_CP048641.1|WP_164321440.1|3598286_3598667_+|succinate-dehydrogenase,-cytochrome-b556-subunit
MPAGTLYRGREGMWSWVAHRVTGVLIFFFLFVHVLDTALVRVSPEAYDDVVATYKTPLVALLEYGLVAAILFHALNGLRVIAVDFWSKGPRYQKQMLWTVMGVWIVLMVGALYPVLGHAVREVFGS
>NZ_CP048641.1|WP_164328252.1|3597586_3598138_+|2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline-decarboxylase
MHPLNTASPESAERTLTTCCGSRHWAHRLAAHRPYPDLDALLAAADEAAYDLAPDDLTEALAAEPLEPALPPGTGYGAAATALRAATAAYESRFGHAFVICLDGVARSEALDHLLASIRGRLGNDPEEERAVAADELRRLARGRLTRLVREQAQHAVAGAPEQPAPPAAQRGEAHRDSPYVPV
>NZ_CP048641.1|WP_164321438.1|3595681_3597292_-|family-20-glycosylhydrolase
MPRGLAVGAGVVAAGAVALTVGLWPDEGGGSDGGAGNAARGNGERTTSSAPPRAPEPTKSYAPSEAPATIPAVRAHESARGPGWRPGDGGRIVVGDGRLADEARLLAGELRLKYGGEAKPRAGDVRLELSKGDRGAGGGAESYTLTVKNRVVRIAGPAEAGVFYGTRTLKQAVADGRTAPEGVVRDQPAKPRRGFMIDTARKHFSAEWIEDRIRDLGDLKYNEIGLHFSDDQAFRIASESHPEIVSADHLTKDQVRRIVDLAASRHITVVPEIDSPGHLGAVIRAHPDLQLRNTGGAPTQGAVDISKPKAAEIVDDLLREYDELFPGARWHLGADEYQALTVRDPEASFPQLAAAARDRLGPGARVQDLATAWLNDRAKTVGPGRQVRAWNDGFFRGGVTRVDDRVEVAYWTGKELGSREPVEYLRDGRDVVNYNDEFLYYVLGQPNDFRYPTGQRIYEQWTPRVVRGTQPVPASYDRQILGATFAVWCDLANSQTQDEVARGIRMPLRATAQKLWDAREPTRSWAEFEGLAGRLG
>NZ_CP048641.1|WP_164328253.1|3609376_3610330_+|hypothetical-protein
MATGILSVGLFLTGHDVLSEILLAIASLLWVLLAADFTDLIARDRARWTKSAITPPALTAVAATTVVGTRFSLLGWQWLAIALLVIAAVVWPVLLLAVVRHWQRGMPGGVFLVCVATQGLSVLAATLYFAGKGEWLGDAALALFGLGLLLYADALLRFDFRQVWEGAGDQWVAGGALAISALAASKLTASPLWTGTGHEFLRNLTYVLLALALAWYATLAAAEAVRPRLHYDVRRWATVFPLGMTAVATLSTGVVTDVPWLRTLGRVLLWVAVAVWGVVWVGFAWARVGGPRGGAPTPPLPETGAPPQTPLLKRRRG
>NZ_CP048641.1|WP_164321453.1|3610380_3610719_-|cupin
MPDTQDLTALAEEHLNQARTAAHGRSARLIVHDGALRQSVIALAAGSALDEHSTPPAASLQVLRGKVRLTTESGDTDIVLAAGQLCRVPQERHGLLGLEDSVVLLTAVTATG
>NZ_CP048641.1|WP_164321454.1|3610849_3611275_+|VOC-family-protein
MSDNQPSSGAPGTDLLGIDNALFPVGDLDEAVGFYERAGFPIAYRLDEAGLAILKAGAETPGVLLRVEDGIGRRPPAWPASRLWLEVGDARAKARALGEAGIPALTEPFSTATGWTVEITDPWGNVVGFTDYSKRPELARS
>NZ_CP048641.1|WP_164321455.1|3611234_3611831_-|MarR-family-transcriptional-regulator
MTPDETKSPGVSRAHDEPRDWTDGHVAQWLPVLPGLDPDIEGAVTRVKRLTVHLRRVREQSLVDFDLERHEFDTLHKLSGRGGRATPSELAADLDLAPASVTGRLDGLERRGLLRRTPSKTDRRRVDVELTEEGRAVWLGAMDVLGHEEYRLLGVLSGEERAQLSDLLRRIMVVAEGGDAGGAGVTNSGPAPASWSSP
>NZ_CP048641.1|WP_164321456.1|3611900_3613298_+|MFS-transporter
MPHTEPRPPGPSRLLRHNHPFRLFFIGRSLSLIGDAVIPAALALAVLRVTGSASALALVLGCAMGARLLLLPLGGVLGDRFDARKIALTTDLVRCATQLFVGVQLLSGSPELWHMAAAEAVSGAATAFALPTLPTLVTAMVDGKDRHAANTALGVVKSGTRVGGPALAGALVLVAGPGSAFLLQGLCFAASACLLSAVRMRRTDPGQETAPGQGDQGGQDRRSLRKDLVEGWHEVRSRDWYWTSLVAHAAWNGAAAVLTTLGPVLAVRELGGEGVWVAMLQTGAVGLLLGSLLAGRAHPRRPILMANLGLATYALPLILLAAGAPAPATIAAYGVAQAGLGFLSPVWETSVQAAIPSGVLARVTSYDWLLSMAAMPLGYVLGPLAADAWGPSVPLYAAALTVGVVCAGTAAVPGVRDFRQPPATPTGSAASDKADSPSDAKADSPTETKAPTSTDAAPLESAPRP
>NZ_CP048641.1|WP_164328254.1|3613316_3613625_-|hypothetical-protein
MARSRPPVAAVTYEITGTGSADISYLARNERGHGGRPAVEAGVRLPWRKTVFVPAGERPVVSVRLDEGGGEARCALAVAGKHRHRDAAAGAFGRATCSVRVG
>NZ_CP048641.1|WP_164328255.1|3614190_3614607_+|hypothetical-protein
MRGYARRFVARVTQRNRLPLDFSVRSLRVVDFVLDGLRKSGRERAEVAETLSGFGAYVGEVLVRRAGATWIDFDASQREFFGQAVGVRMPDGRVWSPLGKVVNRYEVGAAESLQTFYLTLPGRHPATAPGEEREPARR
>NZ_CP048641.1|WP_164328256.1|3614869_3615589_+|sigma-70-family-RNA-polymerase-sigma-factor
MGDAALTRALADAGQGDEAAFALVYQWVHPGLLGYVRGIVGDESEDVASEAWLQIARDLERFSGDGADFRRWAAAIARNRARDHIRRRMSRPRLSLTDGDALDVPDARDTAEEVLEALATDDTVDLVAALPPDQGKAVFLGVLVGMDSPSAARVLGKRPGAVRMALHRGLRRLRAQLSGTAERRERREHREEGGGPDPGRRHCRNSGGRPCGRAATAVPVVPLAAPWARVVVGARASRP
>NZ_CP048641.1|WP_164328257.1|3615631_3616102_-|carboxypeptidase-regulatory-like-domain-containing-protein
MCGAVNPYEAAHAYEYESRDASGDPAKALPAYDAHDPATPYGPRRPGQSADSGAGLPEDPGPHASVVHGFIVTPDGDPIHSVTLTLLSKGGRQLDRVSSLADGSYILAAPAPGVYLLAATAPGYASRARHIMLGDGPLTYDLELVEAVGGGVSAVT
>NZ_CP048641.1|WP_164321457.1|3618571_3619315_+|response-regulator-transcription-factor
MSHAEGHRGTHVAAAGDADTAPGRATVLVVEDEPSIADVLAIALRFHHFEVMTAGTVREALAAAERTRPDCALLDVMLPDGDGRALGRELRARRPELALVFLTARDAPAEVVGALGFGDDYITKPFNIDEVVARIGAVLRRVRPNDVLPQRPPLRYGDLELDETTYVVRRGGGSVQLTPTEYALLRFLVRNGGQVVPKEQLLRHVWNIEHSAESTVVETYVSYLRRKLDQVGPPLITTRRGVGYGLA

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Crispr_ID: NZ_CP048641_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_6

4448409-4448504

Orphan

Consensus_repeat	Method
CCGCTGTACGACGACTTACGCCAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP048641_6

>merge|NZ_CP048641|6|4448409-4448504|CRISPRCasFinder
CCGCTGTACGACGACTTACGCCACGCCTCGCCGCTGAGGGGCGCGCACTCGACGCAGTCGCCTCCGGTGTTTCCGCTGTACGAGGACTTACGCCAC

>NZ_CP048641|6|6|4448409-4448504|CRISPRCasFinder
CCGCTGTACGACGACTTACGCCAC	GCCTCGCCGCTGAGGGGCGCGCACTCGACGCAGTCGCCTCCGGTGTTT
CCGCTGTACGAGGACTTACGCCAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164328348.1\|4443395_4444058_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380061
NZ_CP048641.1\|WP_164322695.1\|4446055_4446715_+\|NAD(P)-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|224996
NZ_CP048641.1\|WP_164328351.1\|4456240_4457134_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176106
NZ_CP048641.1\|WP_164322697.1\|4447329_4447554_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|226181
NZ_CP048641.1\|WP_164322716.1\|4454920_4455541_+\|alkylmercury-lyase	unknown	unknown	gnl\|CDD\|183911
NZ_CP048641.1\|WP_164322687.1\|4442152_4443151_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|224001
NZ_CP048641.1\|WP_164322691.1\|4444541_4445414_-\|LLM-class-flavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|274680
NZ_CP048641.1\|WP_164322685.1\|4441739_4442093_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164322703.1\|4449480_4449867_+\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|340413
NZ_CP048641.1\|WP_164322708.1\|4450383_4451163_+\|glucose-1-dehydrogenase	unknown	unknown	gnl\|CDD\|235500
NZ_CP048641.1\|WP_164322714.1\|4454462_4454924_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164322718.1\|4455551_4456181_-\|MarC-family-protein	unknown	unknown	gnl\|CDD\|225006
NZ_CP048641.1\|WP_164322693.1\|4445596_4445977_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224647
NZ_CP048641.1\|WP_164328349.1\|4446776_4447232_-\|winged-helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224759
NZ_CP048641.1\|WP_164322699.1\|4447579_4448161_-\|DUF2975-domain-containing-protein	unknown	unknown	gnl\|CDD\|378586
NZ_CP048641.1\|WP_164322720.1\|4457337_4458648_+\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|238868
NZ_CP048641.1\|WP_164322689.1\|4444173_4444521_+\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|379266
NZ_CP048641.1\|WP_164322712.1\|4453588_4454347_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|367243
NZ_CP048641.1\|WP_164322705.1\|4449902_4450391_+\|cupin-domain-containing-protein	unknown	unknown	gnl\|CDD\|380376
NZ_CP048641.1\|WP_164322710.1\|4451865_4453416_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|129794

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164328348.1\|4443395_4444058_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|380061	pfam17932, TetR_C_24, Tetracyclin repressor-like, C-terminal domain. TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain. This entry represents the C-terminal domain present in family members such as HTH-type transcriptional repressor KstR2 as well as fatty acid metabolism regulator proteins. In Mycobacterium smegmatis, KstR2 is involved in involved in cholesterol catabolism, while YsiA in Bacillus subtilis is involved in fatty acid degradation.	4.85233e-07
NZ_CP048641.1\|WP_164322697.1\|4447329_4447554_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|226181	COG3655, COG3655, Predicted transcriptional regulator [Transcription].	1.56894e-22
NZ_CP048641.1\|WP_164328351.1\|4456240_4457134_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176106	cd08414, PBP2_LTTR_aromatics_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators involved in the catabolism of aromatic compounds and that of other related regulators, contains type 2 periplasmic binding fold. This CD includes the C-terminal substrate binding domain of LTTRs involved in degradation of aromatic compounds, such as CbnR, BenM, CatM, ClcR and TfdR, as well as that of other transcriptional regulators clustered together in phylogenetic trees, including XapR, HcaR, MprR, IlvR, BudR, AlsR, LysR, and OccR. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	1.20746e-34
NZ_CP048641.1\|WP_164322687.1\|4442152_4443151_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|224001	COG1075, LipA, Predicted acetyltransferases and hydrolases with the alpha/beta hydrolase fold [General function prediction only].	5.55153e-27
NZ_CP048641.1\|WP_164322691.1\|4444541_4445414_-\|LLM-class-flavin-dependent-oxidoreductase	gnl\|CDD\|274680	TIGR03619, F420_Rv2161c, probable F420-dependent oxidoreductase, Rv2161c family. Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes a domain found in a distinctive subset of bacterial luciferase homologs, found only in F420-biosynthesizing members of the Actinobacteria. [Unknown function, Enzymes of unknown specificity].	6.108e-39
NZ_CP048641.1\|WP_164322695.1\|4446055_4446715_+\|NAD(P)-binding-domain-containing-protein	gnl\|CDD\|224996	COG2085, COG2085, Predicted dinucleotide-binding enzymes [General function prediction only].	2.93369e-40
NZ_CP048641.1\|WP_164322703.1\|4449480_4449867_+\|ATP-binding-protein	gnl\|CDD\|340413	cd16936, HATPase_RsbW-like, Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains. This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.	7.53555e-17
NZ_CP048641.1\|WP_164322708.1\|4450383_4451163_+\|glucose-1-dehydrogenase	gnl\|CDD\|235500	PRK05557, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Validated.	2.21078e-76
NZ_CP048641.1\|WP_164322716.1\|4454920_4455541_+\|alkylmercury-lyase	gnl\|CDD\|183911	PRK13239, PRK13239, alkylmercury lyase MerB.	1.06551e-44
NZ_CP048641.1\|WP_164322718.1\|4455551_4456181_-\|MarC-family-protein	gnl\|CDD\|225006	COG2095, MarC, Multiple antibiotic transporter [Intracellular trafficking and secretion].	1.96458e-17
NZ_CP048641.1\|WP_164322693.1\|4445596_4445977_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|224647	COG1733, COG1733, Predicted transcriptional regulators [Transcription].	1.14604e-35
NZ_CP048641.1\|WP_164328349.1\|4446776_4447232_-\|winged-helix-turn-helix-transcriptional-regulator	gnl\|CDD\|224759	COG1846, MarR, Transcriptional regulators [Transcription].	5.59068e-05
NZ_CP048641.1\|WP_164322699.1\|4447579_4448161_-\|DUF2975-domain-containing-protein	gnl\|CDD\|378586	pfam11188, DUF2975, Protein of unknown function (DUF2975). This family of bacterial proteins have no known function. These proteins are likely to be integral membrane proteins. The proteins contain a highly conserved glutamic acid close to their C-terminus.	1.76581e-05
NZ_CP048641.1\|WP_164322720.1\|4457337_4458648_+\|SGNH/GDSL-hydrolase-family-protein	gnl\|CDD\|238868	cd01830, XynE_like, SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. SGNH hydrolases are 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 found in other serine hydrolases.	3.81376e-86
NZ_CP048641.1\|WP_164322689.1\|4444173_4444521_+\|DoxX-family-protein	gnl\|CDD\|379266	pfam13564, DoxX_2, DoxX-like family. This family of uncharacterized proteins are related to DoxX pfam07681.	1.8735e-09
NZ_CP048641.1\|WP_164322712.1\|4453588_4454347_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|367243	pfam02909, TetR_C, Tetracyclin repressor, C-terminal all-alpha domain.	4.89696e-13
NZ_CP048641.1\|WP_164322705.1\|4449902_4450391_+\|cupin-domain-containing-protein	gnl\|CDD\|380376	cd06121, cupin_YML079wp, Saccharomyces cerevisiae YML079wp and related proteins, cupin domain. This family includes eukaryotic, bacterial, and archaeal proteins homologous to YML079wp, a Saccharomyces cerevisiae cupin-like protein of unknown function that structurally resembles plant seed storage and ligand-binding proteins (canavalin, glycinin, auxin binding protein) as well as the bacterial RmlC epimerase. YML079wp is non-essential in yeast and localizes to the nucleus and cytoplasm. The presence of a hydrophobic ligand within a well-conserved binding pocket inside the cupin beta-barrel and sequence similarity with bacterial epimerases suggests a possible biochemical function for YML079wp and its homologs. Also included in this family are Shewanella oneidensis So0799, Agrobacterium fabrum Atu3615 and Branchiostoma belcheri Bbduf985. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.	2.81899e-62
NZ_CP048641.1\|WP_164322710.1\|4451865_4453416_-\|MFS-transporter	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	2.70891e-70

>NZ_CP048641.1|WP_164322699.1|4447579_4448161_-|DUF2975-domain-containing-protein
MNTRLTRTLSSVTFAMAVLCGLVFLGTGLSHMLDDGAVCVKTSFWANASLGKLPIGEGVEAGSSTTRLCQNDPSVGQRAADLGGELPWLLFGALALLLFSRLLDAVLAKGPFTDVVARRLSVLGWVVAVGTPLAGLVVGWSKSWLAGSMAPVIGSGPEVAGPQALILAGLAAVIMGKIMREGVRMREDLEGTI
>NZ_CP048641.1|WP_164322697.1|4447329_4447554_-|helix-turn-helix-transcriptional-regulator
MPEEEIHGIRIHLDRVLAERGMTLTELSARVDITVVNLSVLKNGRAKAIRFSTLSRICEVLQCQPGDLITHDSV
>NZ_CP048641.1|WP_164328349.1|4446776_4447232_-|winged-helix-turn-helix-transcriptional-regulator
MEYSHEDAGLVNQPIGYWTWAANKTLMAYVRGRLAAIGITQPQWWMLHQALHSENGVTRDEVISAHRANLDVGAGIAPDLDLLVERKLLVLDADSRLHITDEGRALHQRAAETQQASRRHVHADVSDEEYLITLKVLQRMIRNAGGDVSPG
>NZ_CP048641.1|WP_164322695.1|4446055_4446715_+|NAD(P)-binding-domain-containing-protein
MKIGVLGTGNMADALATHWVRAGHDVFVGGRDAEKARLLAARMGRDVRHGSLREAAAYGDVVLVALPYGAGADVVRELRAELEGTVLLDCANPVGPDFRLLTEGGPSAAHQLASAAPDAHVVKAFNLCHEDVWRMNPPVFDGRPLAVPVCGDDATALALAGTLVRDVGCEPVAGGGLDRAGLLEATAALFIGLWVAEKADVRAIAPPLEYATGPRAGSA
>NZ_CP048641.1|WP_164322693.1|4445596_4445977_-|helix-turn-helix-transcriptional-regulator
MKPNASDASEAAPDGFLADCRARLAFDLLSHTWNPVLIWVLRHGPLRPGELRARIGGISPKVLTETLRRLEFNGLVTRIAYDESPPRVEYELTVLGRTLLAPIDAFGAWAFEHGDEVMAAQERMGG
>NZ_CP048641.1|WP_164322691.1|4444541_4445414_-|LLM-class-flavin-dependent-oxidoreductase
MRFSINIPNFGDFADARTVARVAVAAEEAGWDGLFVWDHVVHDKVVQRGKPFGDPWMLLTAAALATERIRLGTLVTPVARRRPQQLARQVATLDVLSGGRVTFAAGLGGPVADEYASFGEPTDPRVLAGLLDEGLGLLDRYWSGEPVTHQGTHFRVDDVQLLPATAQRPRPPVWIAGFWPNRPPMRRAARWDGAVPLFESAKHGEIPPLGEFRELVAYVEGKRERLGAQGAYEFVLGGATPGDADHAGELLAPLRDAGATWWDERQLQTGPGIDRLDPVLRRIEQGPPRL
>NZ_CP048641.1|WP_164322689.1|4444173_4444521_+|DoxX-family-protein
MSTAHVAVTLVAAAMTGFSATSVFLRAKWVVEPMADYGIPMSWLPWLGTAKAAGAIGLLVGLFLPVVGIAAAVALVLYFAGAVVAVVRARWYAHIPFPLVYAAPVVGALVLGFGS
>NZ_CP048641.1|WP_164328348.1|4443395_4444058_+|TetR/AcrR-family-transcriptional-regulator
MRNARRPARAYGGKSAEQRRAERRRRLLEAAVELFGAGPGAYRAASVATLCARADLSTRQFYEEFRNLEEVLAVLHGHIQKAAQGAIVEALATATEGSVRERADVAFHAYARVLTANPHLIRIAFVEVTGVSPELEKQRLEARRGWVDLLVAALDEAVAQGEIGARDYRIAALGFVAAVNGLLYDWTAGYVDASLDTIVEELLLMFMGLLQPPEPAAPRK
>NZ_CP048641.1|WP_164322687.1|4442152_4443151_-|alpha/beta-fold-hydrolase
MNTPSAPTRPRRAAHRRAAAALVPLALAATALTATAAPAQATSQTGEQPRKQYPVGGVAEGVSNFLFSPNAVSGVNDWNCKPTAAHPNPVVLVHGTGVNLGANWVKMGPTLANEGHCVFAFNYGMGSPLNLGGRVGGLTSIAKSAETMRDFVDKVLAATGAKKVNVLGHSQGGMMPNYYLKRLGGAQKVDRLVALAPTNHGTTLSGLVNLGKALGLLGVVNSAFDHLNLSGLKDQEEGSDFQKALWADGDTVPGVRYTVIATKYDLVASPYSNGFLKGDKVRNIALQDQCPKNPVGHVGLFTDGPTTQNVVNALGADKPDFKPACQDYGLPF
>NZ_CP048641.1|WP_164322685.1|4441739_4442093_+|hypothetical-protein
MTAMDERPVSTAHTLISEIEGHLLAESARAESRAAAETFAQRLDWLSPAERAEVERLYAEDHLTLTRQAWRHIAGRCLDVRGEYEDRYRMLRQRVLAGGLLAASGMVACVVVVLTAR
>NZ_CP048641.1|WP_164322703.1|4449480_4449867_+|ATP-binding-protein
MSFTVGEHSVQPLRRILTMYLEGWGLAALTEGATLALSELVTNVVRHVPDRRCAVLILRRPGGIRVEVSDASPELPAPPAPPGHSPDGGELAEDGRGLLLVEAATTRWGVTVLPERAGKTIWFEYDDV
>NZ_CP048641.1|WP_164322705.1|4449902_4450391_+|cupin-domain-containing-protein
MAKSPVTAEELAARYGLEPLPFEGGRFRQTWAAPPDASGHPAGTAIIMLLTATAGDFSAMHRLPTDEVWHFYQGDPLDLLLLWPDGRDELRILGDGDGEEFQLVVPAGTWMGARVRNGGEWSLFGTTMAPGFLESDYEGGDPDELAARYPQQAELIRRLCRV
>NZ_CP048641.1|WP_164322708.1|4450383_4451163_+|glucose-1-dehydrogenase
MSDPQLPSLEGRVALVTGASGLLGGGIARSFARAGAAVVLHCNQRVERAREVAEEIGKAGGEAVVVSADLSEERECRRLVEESHRWRGRLDSLVNNAGIQPVQGLEGMTAEDWRGLYDANVTSAFSCTQAAAEVMAGQERPGGSVTHIASIEGHQPAVGHAHYSASKAALIMFARAAAVEYGARGVRVNSVSPGLVGHPTLASDWPEGVERWGRAAPLRRLGRPEDIGSACVFLASDAASWITGTDLVVDGGVSARSTW
>NZ_CP048641.1|WP_164322710.1|4451865_4453416_-|MFS-transporter
MTGSETKTVDGKGQARDPKRWLILVVLCLSTLVLVVDNMVLTVAVPPIAQDLDASASDLQWILDSYMLVFAGLLLTSGSLSDRFGRRRVMLIGLVVFGAASLLATVADSPEQLIAGRVLMGVGGALIMPSTLSILITVFDEDERPKAIAAWSAVAMVGLVGGPVLGGALLDHFWWGSVFLINIPIAVLAIVAALALMSESKGPWRKADPVGMVLSVVGMVALVWTITEWPKEGFGDPKVYVAAIVTVVALAGFGLWETRVAEPMVPLSLFRNRVFTGASFSIVLLTFANGGLMLVLTQYLQFVLDYSPTDTGWAFAPLAVASLVFNTLGATLGQKLGNRVMLATGLAIIAAGFFTLTTLERGDGFGIVTLAMVLMGMGGGLAMPAAQAALMGAVPTEHAGVGSALNDTVQQGGAALGVAVLGSILSSTYGNAMPADAPGKADESIVEAFAEAARSGNAALLDTARDAFTDAMSASFVVGASGVLVAAALSVFLMRPRPEADTPAPAPEDAVTPVGR
>NZ_CP048641.1|WP_164322712.1|4453588_4454347_+|TetR/AcrR-family-transcriptional-regulator
MPRAAQPTKQPTGEPIGSVWTRPQRPRREQPALSRDQIVAEAIALLDSDGIEALSMRKLGTRLNAGATSLYTHVANKDELIELVVDQIYGEIEVPTPASPEEWRTAAVACGNNVRAAILRHPWIASLLGEMGMAYLGPNMMRLSESMLGLFETGGFDLRRSNVALNTIWSYVIGTSATEAAWLTMLARSGRSEQEWVEVVTAAAETAMEPYPRVRGLHALQTETEVDETRRSNFDLGLDCILDGLEAQRGGA
>NZ_CP048641.1|WP_164322714.1|4454462_4454924_+|hypothetical-protein
MDSAKSGPSGSSLWASGGTMFAGVLMLVNGVLGVLAGITGIAKDDVYTRLGDYVYKFNLTTWGWIHLVLGVLIAVTGWGILKGAEWARAAGVGLAAVGMVAQFLWLPYTPLWALISLALSAFVIWALCTDSGGAGSDGADSGGARTGGANTGR
>NZ_CP048641.1|WP_164322716.1|4454920_4455541_+|alkylmercury-lyase
MTPPVSALSDHLVAKWTSPQGARLMAAGAKIVDGLLELGPLTHERAGRMLGWPPQEVLPRFEAMDFRLETDPDGNIIGAGVSLNEARPHSMELRGRTVYGWCAMDTLMFPLALDEAVSHITSRCAATGEPVRATVTPSGVRDVHPATAAVTLAPATGADIREVFCNRVNFYADEALANQVTGRDSDLAVCSTAEAWAVGRRLADLF
>NZ_CP048641.1|WP_164322718.1|4455551_4456181_-|MarC-family-protein
MNALTYSAAFVTFFSVVGPPKVLLAFAALAQAHPTAELRRIALASTAAAILVALVVGFTAPWLLELFHISTPALQLAGGVIFFVYAVGLVLGVHIGSEDPGDAPPSLVGGVRDLLMPYIVSPLAITAVLIEAAARDTWSWRSTVVGAYVSVLALDLLCVVVLTRLLRRTHHAVIELSGRLLGLLLAAVGADLVLDGLYSLGVESLGRRE
>NZ_CP048641.1|WP_164328351.1|4456240_4457134_-|LysR-family-transcriptional-regulator
METFLTLAEELHFGRTAERLLLSQARVSQTVKKLERKIGAPLFERTSRVVRMSPLGRQLYDDLEPLHRGMEEAVARAKDVARGVEGELGVGFLGSGAGTLTQPILELFRERVPGCDVRMREAQFKDPLGALRAGDVDVLFTCLPVEEPDLTVGPIVINEPRVLAMPLRHPLAGRTSLAWEDLAGETFFGVVNGAPAYWWDFHVPPRTPSGRVIRRGQAVASFQEMMTLVATGQGVSPVIASVEKYYARPDITFVPVHDLPTADVALIWRTGDTGPRTEAFIGAVRDVVAANGGPAAF
>NZ_CP048641.1|WP_164322720.1|4457337_4458648_+|SGNH/GDSL-hydrolase-family-protein
MISRARTTAVAIALALTAGAAVTTAQASQGGHGTGNSVENKKAAAAWTAAWAASPQRPSTGFKANWSENGFDDQTVRQVVRVTEGGDRARIRLSNAYGASPLHIASATVARTEGTKGAGVEKGSVRRLTFGGKTSATVPAGGALASDEAGLDLDRFESVTVTLHLARTTGPATFHAQSFATSYRAAGNHVGDTGAGAFKESTESWYYLSGVDVRSDKGGQGRAPRRDGIVLFGDSITDGFASSTDRNRRWSDALAERLAKAGTPRPVLNSGIGGNLVLNDSAWYGDKGTNRIGRDVLDQPGAGTVVVLEGLNDIGFSESDTPTYKPAPVISADQLIAGHRKLIRAAHDKGLKAVGGTLLPLGGSDHYGKHAAAVSDAFNKWVRTSGEYDSYIDFDKALADPKDPERIRPAYDSGDHLHPNDAGYRAMARAADLNSL

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Crispr_ID: NZ_CP048641_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_7

5552698-5552768

Orphan

Consensus_repeat	Method
GCCGCGTTTGTGGGCAGGCGTTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP048641_7

>merge|NZ_CP048641|7|5552698-5552768|CRISPRCasFinder
GCCGCGTTTGTGGGCAGGCGTTCTGGGAGGGGGGCCGGACGCCCGTCCGCTGCGTTTGTGGGCAGGCGTTC

>NZ_CP048641|7|7|5552698-5552768|CRISPRCasFinder
GCCGCGTTTGTGGGCAGGCGTTC	TGGGAGGGGGGCCGGACGCCCGTCC
GCTGCGTTTGTGGGCAGGCGTTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164324348.1\|5556884_5559020_-\|PTS-transporter-subunit-EIIA	unknown	unknown	gnl\|CDD\|224218
NZ_CP048641.1\|WP_164324337.1\|5548927_5549305_+\|DUF3499-domain-containing-protein	unknown	unknown	gnl\|CDD\|378788
NZ_CP048641.1\|WP_164324336.1\|5546517_5548011_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164324355.1\|5569978_5571289_-\|DUF58-domain-containing-protein	unknown	unknown	gnl\|CDD\|224635
NZ_CP048641.1\|WP_016642094.1\|5542297_5542561_+\|WhiB-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|376791
NZ_CP048641.1\|WP_164324334.1\|5542765_5546521_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|224137
NZ_CP048641.1\|WP_164324349.1\|5559388_5560843_+\|adenosylhomocysteinase	unknown	unknown	gnl\|CDD\|377487
NZ_CP048641.1\|WP_164324345.1\|5554544_5555696_+\|mannose-6-phosphate-isomerase,-class-I	unknown	unknown	gnl\|CDD\|185085
NZ_CP048641.1\|WP_164328480.1\|5561888_5562938_-\|RDD-family-protein	unknown	unknown	gnl\|CDD\|377640
NZ_CP048641.1\|WP_164324353.1\|5563094_5564102_+\|stage-II-sporulation-protein-M	unknown	unknown	gnl\|CDD\|376676
NZ_CP048641.1\|WP_164324346.1\|5555802_5556777_+\|cation-transporter	unknown	unknown	gnl\|CDD\|223131
NZ_CP048641.1\|WP_164324332.1\|5540986_5541490_-\|cysteine-dioxygenase	unknown	unknown	gnl\|CDD\|380416
NZ_CP048641.1\|WP_164324330.1\|5539996_5540953_-\|2-phospho-L-lactate-transferase	unknown	unknown	gnl\|CDD\|237443
NZ_CP048641.1\|WP_164324341.1\|5551288_5552653_+\|phosphomannomutase/phosphoglucomutase	unknown	unknown	gnl\|CDD\|236557
NZ_CP048641.1\|WP_164324339.1\|5549539_5551156_+\|L-lactate-permease	unknown	unknown	gnl\|CDD\|224535
NZ_CP048641.1\|WP_164324351.1\|5561106_5561730_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164324342.1\|5552949_5553126_+\|Trm112-family-protein	unknown	unknown	gnl\|CDD\|225391
NZ_CP048641.1\|WP_164324343.1\|5553261_5554440_+\|mannose-6-phosphate-isomerase	unknown	unknown	gnl\|CDD\|378434
NZ_CP048641.1\|WP_164328478.1\|5538419_5539847_-\|coenzyme-F420-0:L-glutamate-ligase	unknown	unknown	gnl\|CDD\|183957
NZ_CP048641.1\|WP_164328479.1\|5548149_5548617_-\|metallopeptidase-family-protein	unknown	unknown	gnl\|CDD\|240574

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164324348.1\|5556884_5559020_-\|PTS-transporter-subunit-EIIA	gnl\|CDD\|224218	COG1299, FruA, Phosphotransferase system, fructose-specific IIC component [Carbohydrate transport and metabolism].	8.05644e-121
NZ_CP048641.1\|WP_164324337.1\|5548927_5549305_+\|DUF3499-domain-containing-protein	gnl\|CDD\|378788	pfam12005, DUF3499, Protein of unknown function (DUF3499). This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 125 to 163 amino acids in length.	3.63532e-59
NZ_CP048641.1\|WP_164324341.1\|5551288_5552653_+\|phosphomannomutase/phosphoglucomutase	gnl\|CDD\|236557	PRK09542, manB, phosphomannomutase/phosphoglucomutase; Reviewed.	0
NZ_CP048641.1\|WP_164324355.1\|5569978_5571289_-\|DUF58-domain-containing-protein	gnl\|CDD\|224635	COG1721, COG1721, Uncharacterized conserved protein (some members contain a von Willebrand factor type A (vWA) domain) [General function prediction only].	1.99829e-50
NZ_CP048641.1\|WP_016642094.1\|5542297_5542561_+\|WhiB-family-transcriptional-regulator	gnl\|CDD\|376791	pfam02467, Whib, Transcription factor WhiB. WhiB is a putative transcription factor in Actinobacteria, required for differentiation and sporulation.	4.04301e-28
NZ_CP048641.1\|WP_164324334.1\|5542765_5546521_+\|glycosyltransferase	gnl\|CDD\|224137	COG1216, COG1216, Predicted glycosyltransferases [General function prediction only].	1.98777e-32
NZ_CP048641.1\|WP_164324349.1\|5559388_5560843_+\|adenosylhomocysteinase	gnl\|CDD\|377487	pfam05221, AdoHcyase, S-adenosyl-L-homocysteine hydrolase.	0
NZ_CP048641.1\|WP_164324345.1\|5554544_5555696_+\|mannose-6-phosphate-isomerase,-class-I	gnl\|CDD\|185085	PRK15131, PRK15131, mannose-6-phosphate isomerase; Provisional.	4.58841e-110
NZ_CP048641.1\|WP_164328480.1\|5561888_5562938_-\|RDD-family-protein	gnl\|CDD\|377640	pfam06271, RDD, RDD family. This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. This region contains two predicted transmembrane regions. The arginine occurs at the N-terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this region is unknown. However this region may be involved in transport of an as yet unknown set of ligands (Bateman A pers. obs.).	7.26037e-19
NZ_CP048641.1\|WP_164324346.1\|5555802_5556777_+\|cation-transporter	gnl\|CDD\|223131	COG0053, MMT1, Predicted Co/Zn/Cd cation transporters [Inorganic ion transport and metabolism].	1.0391e-40
NZ_CP048641.1\|WP_164324332.1\|5540986_5541490_-\|cysteine-dioxygenase	gnl\|CDD\|380416	cd10548, cupin_CDO, cysteine dioxygenase, cupin domain. This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.	6.82103e-24
NZ_CP048641.1\|WP_164324330.1\|5539996_5540953_-\|2-phospho-L-lactate-transferase	gnl\|CDD\|237443	PRK13606, PRK13606, LPPG:FO 2-phospho-L-lactate transferase; Provisional.	1.77148e-171
NZ_CP048641.1\|WP_164328478.1\|5538419_5539847_-\|coenzyme-F420-0:L-glutamate-ligase	gnl\|CDD\|183957	PRK13294, PRK13294, F420-0--gamma-glutamyl ligase; Provisional.	0
NZ_CP048641.1\|WP_164324339.1\|5549539_5551156_+\|L-lactate-permease	gnl\|CDD\|224535	COG1620, LldP, L-lactate permease [Energy production and conversion].	2.04664e-137
NZ_CP048641.1\|WP_164324353.1\|5563094_5564102_+\|stage-II-sporulation-protein-M	gnl\|CDD\|376676	pfam01944, SpoIIM, Stage II sporulation protein M. SpoIIM is on e of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalized through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell. The four proteins working in sequence are SpoIIB, pfam05036, SpoIIM, SpoIIP, pfam07454, and finally SpoIID, pfam08486. D, M and P are in a complex with each other and the complex assembles in a hierarchical manner such that M, which serves as a membrane anchor, recruits P to the septum and P, in turn, recruits D to the septum.	2.07946e-41
NZ_CP048641.1\|WP_164324342.1\|5552949_5553126_+\|Trm112-family-protein	gnl\|CDD\|225391	COG2835, COG2835, Uncharacterized conserved protein [Function unknown].	3.88084e-14
NZ_CP048641.1\|WP_164324343.1\|5553261_5554440_+\|mannose-6-phosphate-isomerase	gnl\|CDD\|378434	pfam10432, bact-PGI_C, Bacterial phospho-glucose isomerase C-terminal SIS domain. This is the C-terminal SIS domain of a bacterial phospho-glucose isomerase EC:5.3.1.9 protein which is similar to eukaryote homologs to the extent that the sequence includes the cluster of threonines and serines that forms the sugar phosphate-binding site in conventional PGI. This domain contributes a good proportion of the active catalytic site residues. This PGI uses the same catalytic mechanisms for both glucose ring-opening and isomerisation for the interconversion of glucose 6-phosphate to fructose 6-phosphate. It is associated with family SIS, pfam01380.	4.28566e-16
NZ_CP048641.1\|WP_164328479.1\|5548149_5548617_-\|metallopeptidase-family-protein	gnl\|CDD\|240574	cd12954, MMP_TTHA0227_like_1, Minimal MMP-like domain found in a group of hypothetical proteins from alphaproteobacteria and actinobacteria. The subfamily includes some uncharacterized bacterial proteins which show high sequence similarity with Thermus thermophilus hypothetical protein TTHA0227. However, they do not contain the conserved HExxH (x could be any amino acid) motif. They may not have any zinc metallo-peptidase activity.	6.69328e-27

>NZ_CP048641.1|WP_164324341.1|5551288_5552653_+|phosphomannomutase/phosphoglucomutase
MTADLSQLVKAYDVRGVVPDQWDESLAELFGAAFARVTEATAIVIGHDMRPSSPGLSGAFARGAAALGVDVTEIGLCSTDQLYYASGALNLPGAMFTASHNPAQYNGIKMCRAGAAPVGQDTGLAEIRALVEGWSESGAPESAATPGTLTRRDTLTDYAAYLRSLVDLTSIRPLKVVVDAGNGMGGHTVPTVFEGLPLTLVPMYFELDGTFPNHEANPLDPANIVDLQKRVREEGADLGIAFDGDADRCFVVDESGAPVSPSAITALVASRELAKHGGSGTVIHNLITSWSVPEVVRENGGTPVRTRVGHSFIKEEMAKTGAIFGGEHSAHYYFRDFWNADTGMLAALHVLAALGGQDGPLSGLVAQYDRYAGSGEINSTVDDQKARLAAIRTTYESREDITIDELDGLTITSTDWWFNVRASNTEPLLRLNVEARDEKTMTGVRDEALAIIRG
>NZ_CP048641.1|WP_164324339.1|5549539_5551156_+|L-lactate-permease
MYVQELEPVADSLGLSALVATLPLLTVLVLLGAVRMKAHRAGLIGLAVAAAVAWLAYGMPLGQTASSAAQGAVFGLFPILWIVVNALWVYRMTVRTRHFDILRRSFGRLSDDPRIQALVVAFCFGALLEALAGFGAPVAICSVMLVALGFDPVRAAVVALVANTAPVAFGAMGTPVVTLAQVTGIPLDTVATVVGRQTPLLALVVPLLLVVLVDGRRGLRETWMPAAACGFAFAAAQFAASNYVSAQLADIGAALAGAGALVAVPGARKPAAEPVRAAVLTGVRSEDLDHDDPRADVLRAYAPYALIVAIFSIAQIPPVKDFLAEATRAFDWPFLNVGDPAGDPVGGNVFSLPLVSTGGTLVLLAGVGTAAVLGVHARVAVREWVATVRELRFAILTVTSVLALAYVMNLSGQAATIGHFVADAGAGLAFLSPVLGWFGVAVTGSDTSANALFGSLQVTAAEQSGLSPELLAAANSSGGVLGKMISPQNLTIACAAVGLAGKEGDLLRKVLPWSLGLLLVMCLIVVGQSTPVLGWMLP
>NZ_CP048641.1|WP_164324337.1|5548927_5549305_+|DUF3499-domain-containing-protein
MSPVRRCSRTACGRPAVATLTYVYADSTAVLGPLATYAEPHCYDLCAEHSERLTAPRGWEVVRLADGSGPSRPSGDDLEALANAVREAARPQERAAEAGGSGARGADPMEVARRGHLRVLRSPES
>NZ_CP048641.1|WP_164328479.1|5548149_5548617_-|metallopeptidase-family-protein
MDDPVQPRSTDPRPRRRDRHGRGMRGPVAPPQVPLSASRAEAFTDLVQDSVERLERRWPQLTEIDFLVLDVPPTSGGVGEGGADDDWGAGTVPLGGTISASEGRPARVVIYRRPVEIRTKGRDERAALVHEVVVEQVAELLGLSPESVDPRYGEE
>NZ_CP048641.1|WP_164324336.1|5546517_5548011_+|hypothetical-protein
MNRTTVSLIAVAAALAAVTGFASVNAPDGGDDGAKAAKRLPVERTSLLCPEPSTSDLAETSYTAFTPSSGGAGSGGKAELLPAPKELTDAPQGGKGKHKDTKPFLSQKAPGKPVTGEESGAEAPALVGRADGALAPGWTVQQTTTVSAGSGRGVQGANCVAPDTEFWFPGASTAKGRSDYIHLTNPDDSAAVVDVELYGPDGGIKADVGQSIQIQPHSSVPVLLSTLTGKPHTNLAMHVVARSGRVAAAVHSSDDKLGGDWLPASTDPAPSLVLPGIPEDATSVRLVAFAPGADDADLKVRLASPTGPITPAGHETLHVKAGMTAAIDLGDVTKGEAGSLLLTPTEKAVPVVAALRVTRGKGDKQETAFIPATAPVGDRATAADNRAKGSTLSLVAPGKTARVKVTASPGAEAGDPVTKTYTVKGGTTLSVAPPVPSGLKGPYALTVEPESGGPVHAARTLELPENGIPMFTIQTLPDDRGTVSVPEAEQDLEVLQK
>NZ_CP048641.1|WP_164324334.1|5542765_5546521_+|glycosyltransferase
MSVHSHQAGHEGAAAGFDPSRAAGFDPASPPEFPRHVVTAVLVSHDGARWLPDAVAGLLGQDRPVQNAVAADTGSADDSARLLTEALGPDRVLHLARRSGFGTAVEEAVRTAAVLTPEDLPYLKRPSGWDPVSRTWRDETYDMPELPHGEPEQWLWLLHDDCAPEPGALAELLRAVETEREAGNEVAIVGPKLRGWYDRRQLLEVGTSIAHSGRRWTGLDRREQDQGQHDHVRPVLCVSTAGMLIRREVFERLGGFDRRLPLMRDDVDLCWRAHAAGHRVLVAPDAVVRHAEASSRERRTVDCVGRTATSPHRVDKAGAAYTLLVNSRTAVLPWVFVRLVLGTVLRTLAYLVGKAPGQALDEVAGLFGTLLRPERILAGRKRRGRPVVDAGEMRPLFPPPGATVRATVEQVASNLVGRSDPEVSAAGRHGVVESGPGGDDADFLEIEQFARIKRVARKPGPVLFVVLLFASLIACRALLGGGALAGGALLPAPADASGLWSRYLDGWHPVGIGGTEAAPPYLAILGFLSSLLFGSTGLAVTVLLVGAVPLAGFAAYFASRPLVASRLLRAWASVAYAFLPAATGALAGGRVGTAVLAILLPLIARAGVSASGLAAADGARGSWRATWAYALLLTVTTAFTPIVWPIALVLGLALLAVRRGDITAYGLRFLAALGTPLLLLAPWSLSLLPFGFFKEAGLEYGTGAASALDLLGASPGGPGTVSGLLLIGIVLAALGALLRGERQAAVRTAWAVALVALVFAALSNGSAWAGPATLAYGIALLSAAALGADGARARVAEQSFGWRQPVAALIAFTAAAGPLLAAAGWMIGGADGPVERRDPVQVPAFVAEESGTQDQARTLVLDSASAAEVSYTLVRGAGARLGDAELAAADGTDGRLDRIVARLLAGSGADQADQLGGYAVRYVLVRDGAPRQLSRTLDATPGLTRLSQEDGSALWRVDRQVARAAVVPKTGDPEPVAAGPVELHTKIPDGQEGRVLRLADSADPGWTATLDGHALTRTTVDGWAQGFELPASGGRLDVTYASPAAHTAWLWTQGALAVVLVVLALPGRRRDVDDDLPEEPVVPAQPVTGEGRRARRLRAQSEQAGEDGRAAAPDEEGLGAVPAQAPAYDEWQTPAPAGGADYGTYGGEQPYQGGQYGSYEQPYQADLYQAGAPQSGQYDPYAYGGAYGGEQQGYGQTYDPTDPAYAQQDAASYAQQAQQPQAQQPQAQQPPPMPRQPPPGTDSERPDGSQQ
>NZ_CP048641.1|WP_016642094.1|5542297_5542561_+|WhiB-family-transcriptional-regulator
MTELVQELLVEDADEELGWQERALCAQTDPESFFPEKGGSTREAKKVCLACEVRSECLEYALANDERFGIWGGLSERERRRLKKAAV
>NZ_CP048641.1|WP_164324332.1|5540986_5541490_-|cysteine-dioxygenase
MNSDSDLQIAGDILEVPHLLQPAREHPVTVAEFAGLARAIAADRSQWEHLVEYDAASRWYHRLRTGPGYEVWLLSWVPGQSSGLHDHGRSSGVLTLLEGELTERTERGTRALGSGAQRVFAPGYVHEVVNDSLEPAVSLHVYYPGLTEMPMHTARCEARAPQDPVTA
>NZ_CP048641.1|WP_164324330.1|5539996_5540953_-|2-phospho-L-lactate-transferase
MRIVVLAGGIGGARFLRGLKKAAPDAAITVIGNTGDDIHLFGLKVCPDLDTVMYTLGGGINEEQGWGRTDETFKVKEELAAYGVGPGWFGLGDRDFATHIVRTQMLAAGYPLSAVTEALCERWQPGVRLIPMSDDRVETHVAVEVDGERKAVHFQEYWVRLRASVDAHAIVPVGAEQAKPAPGVLEAIADADVVLFPPSNPVVSVGTILAVPGIREAIAEAGVPVVGLSPIVGDAPVRGMADKVLAAVGVETTAAAVAEHYGSGLLDGWLVDTVDAGVVERVESAGIRCRAIPLLMTDEDAAATMAREALTLAEEVRA
>NZ_CP048641.1|WP_164328478.1|5538419_5539847_-|coenzyme-F420-0:L-glutamate-ligase
MERPGGVPAFRVWAVGGVPEVRPGDDLAKLIAAAEPGLADGDVVLVTSKIVSKAEGRVVAAADREAAIDAETVRVVARRGTLRIVENRQGLVMAAAGVDASNTPAGTVLLLPEDPDASARAVRAGLRAALGVDVGVIVTDTFGRPWREGVTDVAIGAAGVRVLDDLRGGVDAYGNPLSATVVATADELAAAGDLVKGKAAGLPVAVVRGLGHVVVSRSAVAPGAPGVLGALGGAERGAAQGELGADGEVTHGVGAEDRGARDLVRSARNDMFRLGTSEAVREALSLRRTVREFTDEPVDPGAVRRAVAAAVTAPAPHHTTPWRFVLLESADSRVRLLDAMRDAWVADLRRDGKSEESIARRVRRGDVLRNAPCLVVPCLVMDGAHSYGDARRDGAEREMFVVAAGAGVQNFLVALAGERLGSAWVSSTMFCRDVVRGVLGLPEGWDPMGAVAVGHAVAPAAGRVGRSVEDFIEVR
>NZ_CP048641.1|WP_164324342.1|5552949_5553126_+|Trm112-family-protein
MPLEAGLLEILACPACHAPLKETDTELVCTAESTECGLAYPVRDGIPVLLVDEARRPA
>NZ_CP048641.1|WP_164324343.1|5553261_5554440_+|mannose-6-phosphate-isomerase
MLDESLLDAPEALARADLHDLLRGAAEAGARVRTAVRHATESGLTELKPDGRPRAVLIAGPGTAATGVADLIGTLAGTACPVVRLAPTGVAPAAGALRWALPGWTGPVDLLLIVTPDGSEPGLTLLAEQAYRRGCTVVAVAPPRSPLAESVEGSHGLTVPMAASPVAYEAAQREPFTQEDLSREAPATAPGTLWALLTPLLVLLDRTGLIAAPVDTLQKVADRLDSVAERCGPAIATYSNPAKTLATELSETLPLIWSEGQSAGMAGRRFAAALAELAGHAALAAELPEALAAHTTLLAGGPVGGGDGDDFFRDRVEEPASLRARVVLLREHPADAGGLTAAPTARELVHSHDTALSELEPADGGDLERLAELIAITDFAAVYLALASGDRS
>NZ_CP048641.1|WP_164324345.1|5554544_5555696_+|mannose-6-phosphate-isomerase,-class-I
MDRLTNTVRPYAWGSTTAIAQLLGVEPTGEPQAEMWMGAHPGAPSRTERGPLNEVIDEDPAHELGPRAVAKFGPRLPFLLKILAAGAPLSLQVHPNLEEAKEGYDDEERRGVPLDAPHRNYKDANHKPELICALTPFDGLCGFRAPAEAADLLAGLGVDSLKPYVDLLHAKPEEAALREVLTAVLSADPDDMAKTVAEAATAAERLGGDYAPYAAVARHYPGDPGVIAAMLLNYVQLQPGEAMFLGAGVPHAYIQGLGVEIMANSDNVLRCGLTPKHVDVPELLRVVRFEATDPGVLRPEASPDGEEVYETPIDEFRLSRFVLPESGAAHDLTAETPQILLCTAGAVRAGDIALTPGQSAFVPAGEKAEVSGTGTVFRATVVA
>NZ_CP048641.1|WP_164324346.1|5555802_5556777_+|cation-transporter
MSASGGTKAIVAALVANLAIAVAKFVAFLFSGSSSMLAESVHSLADSGNQGLLLVGGKKAQREATPQHPFGYGRERYIYAFLVSIVLFSVGGMFAIYEGYEKIKHPHEIEHWYWPVGVLIFAIIAESFSFRTAIKESNALRGKLTWTQFVRRAKAPELPVVLLEDLGALVGLVLALGGVGLALATGDGVWDGIGTLCIGVLLILIAIVLAAETKSLLLGEAAGTEEVEKIEQALVDGDTVTRLIHMRTLHLGPEELLVAAKVAVRHDDTAREIADAINAAEDRIRAAVPIARVIYLEPDIYSEEAAAAGTNPAKSPGGSPEGDH
>NZ_CP048641.1|WP_164324348.1|5556884_5559020_-|PTS-transporter-subunit-EIIA
MTSPADPPAGGGPSGQKRLKLLAVTACPTGIAHTYMAAEKLQQAAEGLGIDMKVETQGSIGAENVLTDNDVRDADGVIIAADKDVDLARFAGKRVLSVGVSEGISNPERLIEQVQGAPVHGGSGGGGGGGDAAQASTGDGGRERSVAYKALMNGVSYMIPFVVVGGLLIAISLSLGGHTDPKGGLVIPDDSFWMHVNEIGVIGFKLMVPILSGYIAYAIGDRPALVPGMIGGWIANTGELYDSEAGAGFIGAIVTGFLAGYLVLWIKKVEVPKFARPIMPIIVIPIIATSALGLFFIYVIGKPISWVFEHLTDWLSGMTGTSAILLGAILGLMIAFDMGGPVNKTAFLFGAGLIATGNQTVMGMCAAAIPVMPLGQGLATLIRKRLYSEQERETGLAALFMGMFGISEGAIPFAAARPAQVIPANMLGGAVAGAVAGLASVEDAVPHGGPIVAVLGAIGGVPMFLVAVAIGTVVTALTTVTLVDISERRRRGEPLVGGAGGPGAGEPVLAGVGAGAAVAGGGVGSGAGSTAKSPAAPAPSAPTPSAPAPQAPADAAAPGGEVLSGYLTEQTVKVQLAADEKEAAIREMAGLLARTGKVGDVEELVRTALRREAQGTTGLGEEIAIPHAKTDAVTAPVVGFARSAEGIEWGSMDGTKAKLIFMISVPEAAAGDEHLRILALLSRKLMDVGFRERLVAAPDEAAILEVLREVQ
>NZ_CP048641.1|WP_164324349.1|5559388_5560843_+|adenosylhomocysteinase
MTAANGQDFKVADLSLAEFGRKEITLAEHEMPGLMAIRKEFAAAQPLAGARIMGSLHMTVQTAVLIETLVALGAEVRWVSCNIFSTQDHAAAAIAVGPKGTPDNPQGIPVFAWKGETLEEYWWCTEQALTWPNSPTGGPNMILDDGGDATLLVHKGVEYEKDGKVPAIETAESDEHRVILQTLHRTLGENPQKWTQLASEIRGVTEETTTGVHRLYEMHRDGQLLFPAINVNDAVTKSKFDNKYGCRHSLVDGINRATDVLIGGKTAVICGYGDVGKGCAESLRGQGARVIITEIDPICALQAAMDGYQVTTLDEVVETADIFITTTGNKDIIMAADMAKMKHQAIVGNIGHFDNEIDMAGLAKLPGIVKDEVKPQVHTWKHPDGKVLIVLSEGRLLNLGNATGHPSFVMSNSFADQTLAQIELFTKPDEYPTDVYVLPKHLDEKVARLHLDSLGVKLTTLRPEQASYIGVEVEGPYKPDHYRY
>NZ_CP048641.1|WP_164324351.1|5561106_5561730_+|hypothetical-protein
MPRGRYSLHDPHDHTPLGEEHFQCAPGPSGWRYVAQRTTPSGDHSGSVDLTLDELGRPIRLELHASGWQVRAAALDGVTWVRSDPSGAHATENNAPAHAVTGTSPAFLVATARLLRLAPASPATRVRLVAFTDPVLAPRTLDQSWALLKREAHATDNGPLTVDEYQVTALDTGEQHTVHLTGDVVLAAPGIELENLESPPSAFGSEG
>NZ_CP048641.1|WP_164328480.1|5561888_5562938_-|RDD-family-protein
MTGEAVALELRPAKLPSRALAVLIDMVVAWSVYLAVTLGLLAAAGSLDDAAVAAIAVGTFVLVLVGVPIAVETLSHGRSLGKLACGLRVVRDDGGPIRFRHALVRGAVGVVEILLTFGVIACIASLVSERGRRLGDVFAGTLVVRERVPTGRMAYVPAPPPWLAGRFAELDLSAVPDGLWLAIRQYLTRMGQLDPQVGWAMAERLASDVVARTGAPAPEGVPPAAFLAAVVHERQAREARRAFGAQGVGMPGAAPGAPYAPGAPGVPSVSGAPTGRPGAQAGPFAPPGAAPVGPPVYASPTAPATQPPQPSQPAPGSGTPAPAAPAPPRPATPAPEERAQPTTGFVPPA
>NZ_CP048641.1|WP_164324353.1|5563094_5564102_+|stage-II-sporulation-protein-M
MDLDVFVSAHRAEWDRLDALLRRQRRLTGPEVDELVVLYQRTATHLSLIQSSAPDPQLTGRLTQLVARARSAVTGTRRASWRDATRFLTHGFPAAVYRSRHWWVPTALLSIALAAVLGWWIGTHPEVQSSIAAPSELRDLTRPGGEYETYYSSHPAASFAAQVWTNNAQAAAMCLVLGAFLCVPVIWILFQNMLNLGAGIGLMSSADRLDTFLGLVLPHGLLELTAVFVAAGTGLRLGWTLIDPGPRTRRTAMAEEGRAALGMAIGLALILLISGAIEGFVTPSGLPTWARIGIGIAAELAFLAYVYVLGGRAARAGETGDVDEAERSAAVPAAA
>NZ_CP048641.1|WP_164324355.1|5569978_5571289_-|DUF58-domain-containing-protein
MPVTGRTALLAALGSLPVGILEPGWTGILAVNAPLALACACDFALAAPVRRLVLTRSGDTSVRLGEPADVHLTLTNPTNRPLRAELRDAWPPSSWQPGTEVTASRQRWDVPTGERRRFTTRLRPTRRGDHQADRVTIRSRGPLGLFTRQGSHKVPWTLRVLPPFASRKHLPSKLARLRELDGRTSVLIRGQGTEFDSLREYVPGDDTRSIDWRATARQSSVAVRTWRPERDRHILLVLDTGRTSAGRVGDAPRLDASTDAALLLAALASRAGDRVDLLAYDRRVRALVQGKAAGDVLPSLVNALATLEPELVETDARGLTATALRAAPRSSLIVLLTSLEAAPIEEGLLPVLSRLTQRHTVLVASVADPYITQMAKARGTTEAVYDAAAAAQAQAERQRTAEQLTRHGVTVVDATPDNLAPALADAYLSLKAAGRL

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Crispr_ID: NZ_CP048641_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_8

5748143-5748264

Orphan

Consensus_repeat	Method
CCCTGGCTCTGGCCCTGGTCCTGACC	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP048641_8

>merge|NZ_CP048641|8|5748143-5748264|CRISPRCasFinder
CCCTGGCTCTGGCCCTGGTCCTGACCCTGAGTCTGGCCCTGGTCCTGACCCCCGGTCGGTCCCTGGTTCTGGCCCTGGTCCTGACCTCCGGTCGGTCCTTGGTTCTGGCCCTGGGTCTGGCC

>NZ_CP048641|8|8|5748143-5748264|CRISPRCasFinder
CCCTGGCTCTGGCCCTGGTCCTGACC	CTGAGTCTGGCCCTGGTCCTGA
CCCCCGGTCGGTCCCTGGTTCTGGCC	CTGGTCCTGACCTCCGGTCGGT
CCTTGGTTCTGGCCCTGGGTCTGGCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164324565.1\|5747101_5747458_+\|co-chaperone-GroES	unknown	unknown	gnl\|CDD\|197951
NZ_CP048641.1\|WP_164324580.1\|5758619_5760659_-\|TNT-domain-containing-protein	unknown	unknown	gnl\|CDD\|379424
NZ_CP048641.1\|WP_164324573.1\|5754025_5754877_+\|DUF1707-domain-containing-protein	unknown	unknown	gnl\|CDD\|377959
NZ_CP048641.1\|WP_164324568.1\|5751281_5752103_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|226953
NZ_CP048641.1\|WP_164324561.1\|5746095_5746563_-\|thioredoxin-dependent-thiol-peroxidase	unknown	unknown	gnl\|CDD\|224146
NZ_CP048641.1\|WP_164324574.1\|5755076_5756408_-\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|238868
NZ_CP048641.1\|WP_164324581.1\|5760941_5761367_-\|RICIN-domain-containing-protein	unknown	unknown	gnl\|CDD\|379501
NZ_CP048641.1\|WP_164324559.1\|5745256_5745859_+\|RdgB/HAM1-family-non-canonical-purine-NTP-pyrophosphatase	unknown	unknown	gnl\|CDD\|234648
NZ_CP048641.1\|WP_016638888.1\|5743371_5743605_+\|PTS-transporter-subunit-EIIB	unknown	unknown	gnl\|CDD\|238130
NZ_CP048641.1\|WP_164324558.1\|5744735_5745134_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164324576.1\|5756634_5757993_+\|DUF445-domain-containing-protein	unknown	unknown	gnl\|CDD\|377281
NZ_CP048641.1\|WP_164324554.1\|5740318_5741569_-\|PTS-transporter-subunit-EIIC	unknown	unknown	gnl\|CDD\|273920
NZ_CP048641.1\|WP_164324555.1\|5741820_5743146_-\|PTS-transporter-subunit-EIIC	unknown	unknown	gnl\|CDD\|273920
NZ_CP048641.1\|WP_164324578.1\|5758064_5758505_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|317917
NZ_CP048641.1\|WP_164324566.1\|5747634_5747955_+\|multidrug-efflux-SMR-transporter	unknown	unknown	gnl\|CDD\|171110
NZ_CP048641.1\|WP_164328496.1\|5761784_5762273_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164324563.1\|5746725_5747058_+\|DUF3618-domain-containing-protein	unknown	unknown	gnl\|CDD\|378834
NZ_CP048641.1\|WP_164324556.1\|5743822_5744554_+\|ribonuclease-PH	unknown	unknown	gnl\|CDD\|178914
NZ_CP048641.1\|WP_164324571.1\|5753001_5754015_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213234
NZ_CP048641.1\|WP_164324569.1\|5752095_5752995_+\|transporter	unknown	unknown	gnl\|CDD\|253605

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164324565.1\|5747101_5747458_+\|co-chaperone-GroES	gnl\|CDD\|197951	smart00883, Cpn10, Chaperonin 10 Kd subunit. The chaperonins are 'helper' molecules required for correct folding and subsequent assembly of some proteins. These are required for normal cell growth, and are stress-induced, acting to stabilise or protect disassembled polypeptides under heat-shock conditions. Type I chaperonins present in eubacteria, mitochondria and chloroplasts require the concerted action of 2 proteins, chaperonin 60 (cpn60) and chaperonin 10 (cpn10). The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between six to eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides as isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.	3.44739e-27
NZ_CP048641.1\|WP_164324580.1\|5758619_5760659_-\|TNT-domain-containing-protein	gnl\|CDD\|379424	pfam14021, TNT, Tuberculosis necrotizing toxin. This is the C-terminal domain secreted by Mycobacterium tuberculosis (Mtb). It induces necrosis of infected cells to evade immune responses. Mtb utilizes the protein CpnT to kill human macrophages by secreting its C-terminal domain (CTD), named tuberculosis necrotizing toxin (TNT) that induces necrosis. It acts as a NAD+ glycohydrolase which hydrolyzes the essential cellular coenzyme NAD+ in the cytosol of infected macrophages resulting in necrotic cell death. CpnT transports its toxic CTD from the cell surface of M. tuberculosis by proteolytic cleavage, where the toxin is cleaved to induce host cell death. Structural analysis determined that the TNT core contains only six beta-strands as opposed to seven found in all known NAD+-utilizing toxins, and is significantly smaller, with only two short alpha-helices and two 3/10 helices. Furthermore, the putative NAD+ binding pocket identified Q822, Y765 and R757 as residues possibly involved in NAD+-binding and hydrolysis based on similar positions of catalytic amino acids of ADP-ribosylating toxins. While glutamine 822 residue was detected to be highly conserved among TNT homologs.	2.67393e-28
NZ_CP048641.1\|WP_164324573.1\|5754025_5754877_+\|DUF1707-domain-containing-protein	gnl\|CDD\|377959	pfam08044, DUF1707, Domain of unknown function (DUF1707). This domain is found in a variety of Actinomycetales proteins. All of the proteins containing this domain are hypothetical and probably membrane bound or associated. Currently, it is unclear to the function of this domain.	4.3906e-23
NZ_CP048641.1\|WP_164324568.1\|5751281_5752103_+\|ABC-transporter-permease	gnl\|CDD\|226953	COG4587, COG4587, ABC-type uncharacterized transport system, permease component [General function prediction only].	2.83028e-29
NZ_CP048641.1\|WP_164324561.1\|5746095_5746563_-\|thioredoxin-dependent-thiol-peroxidase	gnl\|CDD\|224146	COG1225, Bcp, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones].	1.08905e-67
NZ_CP048641.1\|WP_164324574.1\|5755076_5756408_-\|SGNH/GDSL-hydrolase-family-protein	gnl\|CDD\|238868	cd01830, XynE_like, SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. SGNH hydrolases are 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 found in other serine hydrolases.	1.66898e-82
NZ_CP048641.1\|WP_164324581.1\|5760941_5761367_-\|RICIN-domain-containing-protein	gnl\|CDD\|379501	pfam14200, RicinB_lectin_2, Ricin-type beta-trefoil lectin domain-like.	5.62001e-06
NZ_CP048641.1\|WP_164324559.1\|5745256_5745859_+\|RdgB/HAM1-family-non-canonical-purine-NTP-pyrophosphatase	gnl\|CDD\|234648	PRK00120, PRK00120, dITP/XTP pyrophosphatase; Reviewed.	1.67132e-103
NZ_CP048641.1\|WP_016638888.1\|5743371_5743605_+\|PTS-transporter-subunit-EIIB	gnl\|CDD\|238130	cd00212, PTS_IIB_glc, PTS_IIB, PTS system, glucose/sucrose specific IIB subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIB PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation.	4.91354e-23
NZ_CP048641.1\|WP_164324576.1\|5756634_5757993_+\|DUF445-domain-containing-protein	gnl\|CDD\|377281	pfam04286, DUF445, Protein of unknown function (DUF445). Predicted to be a membrane protein.	8.65316e-136
NZ_CP048641.1\|WP_164324554.1\|5740318_5741569_-\|PTS-transporter-subunit-EIIC	gnl\|CDD\|273920	TIGR01998, N-acetylglucosamine_and_glucose_PTS, PTS system, N-acetylglucosamine-specific IIBC component. This model represents the combined B and C domains of the PTS transport system enzyme II specific for N-acetylglucosamine transport. Many of the genes in this family also include an A domain as part of the same polypeptide and thus should be given the name "PTS system, N-acetylglucosamine-specific IIABC component". This family is most closely related to the glucose-specific PTS enzymes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids].	2.24846e-138
NZ_CP048641.1\|WP_164324555.1\|5741820_5743146_-\|PTS-transporter-subunit-EIIC	gnl\|CDD\|273920	TIGR01998, N-acetylglucosamine_and_glucose_PTS, PTS system, N-acetylglucosamine-specific IIBC component. This model represents the combined B and C domains of the PTS transport system enzyme II specific for N-acetylglucosamine transport. Many of the genes in this family also include an A domain as part of the same polypeptide and thus should be given the name "PTS system, N-acetylglucosamine-specific IIABC component". This family is most closely related to the glucose-specific PTS enzymes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids].	1.82103e-130
NZ_CP048641.1\|WP_164324578.1\|5758064_5758505_+\|hypothetical-protein	gnl\|CDD\|317917	pfam15599, Imm63, Immunity protein 63. A predicted immunity protein with an alpha+beta fold and a conserved E+G and ExxY motifs. Proteins containing this domain are present in bacterial polymorphic toxin systems as an immediate gene neighbor of the toxin gene, which usually contains toxin domains of the Ntox40, Tox-CdiAC and Tox-ARC families. The protein is also found in poly-immunity loci in polymorphic toxin systems.	4.67557e-10
NZ_CP048641.1\|WP_164324566.1\|5747634_5747955_+\|multidrug-efflux-SMR-transporter	gnl\|CDD\|171110	PRK11431, PRK11431, quaternary ammonium compound efflux SMR transporter SugE.	1.644e-28
NZ_CP048641.1\|WP_164324563.1\|5746725_5747058_+\|DUF3618-domain-containing-protein	gnl\|CDD\|378834	pfam12277, DUF3618, Protein of unknown function (DUF3618). This domain family is found in bacteria, and is approximately 50 amino acids in length.	1.8328e-09
NZ_CP048641.1\|WP_164324556.1\|5743822_5744554_+\|ribonuclease-PH	gnl\|CDD\|178914	PRK00173, rph, ribonuclease PH; Reviewed.	6.72087e-172
NZ_CP048641.1\|WP_164324571.1\|5753001_5754015_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213234	cd03267, ABC_NatA_like, ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA. NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.	7.59903e-128
NZ_CP048641.1\|WP_164324569.1\|5752095_5752995_+\|transporter	gnl\|CDD\|253605	pfam06182, ABC2_membrane_6, ABC-2 family transporter protein. This family acts as the transmembrane domain (TMD) of ABC transporters. The family includes proteins responsible for the transport of herbicides.	6.06772e-65

>NZ_CP048641.1|WP_164324566.1|5747634_5747955_+|multidrug-efflux-SMR-transporter
MAWVLLVVAGLLEVGWSIGMKFTDGFTRLWPSVFTGAGIVASMFLLSYAAKTLPIGTAYGVWVGIGAAGAAVVGMLALGEPTTAARIFFVCLLLVAVVGLKATSGH
>NZ_CP048641.1|WP_164324565.1|5747101_5747458_+|co-chaperone-GroES
MSAKTHEPSSHDDKLPIRMLHDRVLVRQDTAEGERRSGGGILIPATAAVGKRLAWAEVVAVGQNVRTVEPGDRVLYDPEDRAEVEVRGVAYVLMRERDLHAVAADRFEGSEDSTGLYL
>NZ_CP048641.1|WP_164324563.1|5746725_5747058_+|DUF3618-domain-containing-protein
MSDADADARTPAQIEADIKLRRDQLAETLDEIGVRVHPKTIVGDAKAKIASSVDQSLGRAYVGANRFVSDVKAQFVAEDGAPRVERIVPVALVVVGLVGLLAVGSRRRRG
>NZ_CP048641.1|WP_164324561.1|5746095_5746563_-|thioredoxin-dependent-thiol-peroxidase
MSERLQPGDTAPAFTLPDADGKEVSLADHKGRKVIVYFYPAALTPGCTKQACDFTDNLDVLAAAGYDVIGVSPDKPEKLAKFREKENLKVTLVGDPSKATLEAYGAFGEKKLYGKTVTGVIRSTIVVDGTGKVEHAFYNVKATGHVAKIIRDLGV
>NZ_CP048641.1|WP_164324559.1|5745256_5745859_+|RdgB/HAM1-family-non-canonical-purine-NTP-pyrophosphatase
MTRLILATRNAGKLTELKAILADARLDHELVGAEAYPDIPDVKETGVTFAENALLKAHALAKATGLPAVADDSGLCVDVLGGAPGIFSARWAGRHGDDRANLELLLAQLGDIDDPHRGAHFACAAALALPDGTERVVEGRLLGTLRHTPSGTGGFGYDPVLQPEGDTRTCAELTPDEKNAISHRGKAFRALVPVVRELLG
>NZ_CP048641.1|WP_164324558.1|5744735_5745134_+|hypothetical-protein
MAARHRRTVTAIATVLIAVTAGAGLVACDPVDKAIDCAKTADEIHDNIQDMQEAVQDAALDPGDADKSLDDIEDNLDNIRDKSDDSDVDKAIDHLEKAVDNIRDSTKDGGDKTPDMSPVGDAAKELTKVCTD
>NZ_CP048641.1|WP_164324556.1|5743822_5744554_+|ribonuclease-PH
MSRIDGRTPEQLRPITIERGWSKHAEGSVLISFGDTKVFCTASVTEGVPRWRKGSGEGWVTAEYSMLPRSTNTRGDRESVRGKIGGRTHEISRLIGRSLRAVIDYKALGENTIVLDCDVLQADGGTRTAAITGAYVALADAVAWAQGKKLIKAGRKPLTGTVSAVSVGIVGGVPLLDLCYEEDVKADTDMNVVCTGDGRFVEVQGTAEAEPFAREELNALLDLAVGGCVDLAAYQNEALEKVK
>NZ_CP048641.1|WP_016638888.1|5743371_5743605_+|PTS-transporter-subunit-EIIB
MASKAEKIVAGLGGIDNIEEVEGCITRLRTEVNDPGLVDEAALKAAGAHGVVKMGTAIQVVIGTDADPIAADIEDMM
>NZ_CP048641.1|WP_164324555.1|5741820_5743146_-|PTS-transporter-subunit-EIIC
MSSDAAAVPRNVPQKKWWNGLFQGLQKMGRSLQLPIAVLPAAGILNRLGQPDVFGDDGLGWTNVAKVFAAAGGALLDSSLGLPLLFCIGVAIGMAKKSDGSTALAAVAGFLVYYAVLRAFPDDCPAGADFAGAGMWSGVCVAEDGTPAQAAYQNPGVFGGIVMGLLSAWFWQRYHRVKLVDWLGFFNGRRLVPIIMAFVGLIFAGLCVWVWPPIGDGLTSFSKWLVDLGWLGSGIFGVANRALLTVGLHQFLNTFVWFQFGDYTKADGTVVHGDINRFLAGDPTAGQFTSGFFPIMMFALPAAALAITHAARPERRKVVGGMMLSVGLTSFVTGITEPIEYSFLFIAPALYAIHALLTGVSMAVTWGLGVKDGFSFSAGLIDYVINWSLATKPWLIIPIGLCFAAVYYVLFLFVIKKFNLATPGREPEEEAKALDEEQTKA
>NZ_CP048641.1|WP_164324554.1|5740318_5741569_-|PTS-transporter-subunit-EIIC
MSTATAKAAPAKKRGSSLLQGLQKVGRSLQLPIAVLPAAGILLRLGQPDVFGADGLGWGKVATVFANAGDAVFANMPLLFCIGVAIGFAKKADGSTALAALVGFLVYTNVLKAFPVTEAKITKGADIAATYNDPKVFGGIIMGLISAVVWQKFHRTKLVDWLGFFNGRRLVPILMAFIGTALGVFFGLAWGPVGDAITSFGEWMTDLGSVGAGIFGVVNRALLPVGMHQFVNTVAWQEIGSFTDSAGAVWHGDIQRFMHGDPTAGQFMSGFFPIMMFALPAVALAITHTARPERRKVVGGMMMSLALTSFVTGITEPIEFAFMFIAPALYVIHAVLTAVAMTVTWALGVHHGFTFSAGAIDYILNWKFAEKPWMIIPIGLVFAAIYYVVFRFAIVRFNIPTPGREPEEEIEDLTKA
>NZ_CP048641.1|WP_164324568.1|5751281_5752103_+|ABC-transporter-permease
MFVGTGRFRLYAAVAAGSFRRFATYRIATVAGVFTNTVFGVILTYTYIALWDEKPGLGGYDQAQALTYVWLGQALLTTVAVMGGGFEDELMARIRTGDVAIDLYRPADLQAWWLAGDVGRAAFQCLARGAVPMAFGALCFQLALPGDVLTWLAATLAVLLGVVVSFALRFLVALSAFWLLDGAGVSQVAWLASTFFSGMLLPLNVFPGALGEIARALPWSALIQVPADVFLGKHQGMDLLATYAFQVGWAAVLLTAGRLLQAVATRRVVVQGG
>NZ_CP048641.1|WP_164324569.1|5752095_5752995_+|transporter
MAELLRHEKGRAGDLAGPDRLADGVPDRPLDRARDGLRAYRMIAAMWIRSTMAYRASFAMTAFGNLAATALDFVAILLMFSQVDALGGYRLPEVAFLYGASSTAFGLADLAIGSMDRLGRRVRDGTLDTLLVRPAPVLAQVAADRFALRRLGRVTQGLLILGFALLALDVTWTPLKVLLIPLMLVSGAAIFMSVFIAGAAFQFLAQDASEVQNAFTYGGNTLLQYPPSVFGKDLVRGATFLVPIAFVNWLPGLYVLGRPYPLDLPPWAAFTPPLVAVACCALAGLAWRAGLRSYRSTGS
>NZ_CP048641.1|WP_164324571.1|5753001_5754015_+|ATP-binding-cassette-domain-containing-protein
MDTALNPDPDRDPVPDPDADFIALDGIEKVFDVRKKTGFLRRERHQVRAVDGITFRVPRGEMVGYIGPNGAGKSTTIKMLTGILTPSGGRLRVAGIDPARERTRLARRIGVVFGQRTTLWWDLPLIDSYRLMHRMYRIPDRRYAENLDRCVQLLDLGELLDVPVRQLSLGQRMRGDIAAALLHDPEVLYLDEPTIGLDVVSKAKVRTFLRDLNAESGTTVLLTTHDLTDIEQLCKRVMVIDHGRLMYDGPLAGLHEVGESERTLVVDLERELPPLEVESARVVKVEGPRQWLAFPAAASAAPLVAAVAACYPLVDLSVREPDIEAVIAKMYADRATS
>NZ_CP048641.1|WP_164324573.1|5754025_5754877_+|DUF1707-domain-containing-protein
MTDAEPTPPPEEPPSSGRDASGPPPAAQQPAAQPPAVRSAPAEPSHAELRASDADRERVAEVLREAVAEGRLDMEEFGERLDAVYQARTYGELAPLTRDLPSAVAPAPKVSMVKRPEDGDSGEIDWAERVVDGEPSSTGAVAIWGGFSRKGGWTVGRLFTSFAMWGGGEIDLREARFAERDVVIRCFALMGGIQVTVPPELDVTVKGFGIMGGFGDDATGAGTPGSPRVVVTGFALMGGVGVERKLRKEVRARLKEERRELQARRREERHALHARRREERRGR
>NZ_CP048641.1|WP_164324574.1|5755076_5756408_-|SGNH/GDSL-hydrolase-family-protein
MTKRHGYALLAAVLAVIVVVSAAIYIGVTGTDDDTKDQLSASPRGPRNSAAPASSGTWVGTWSASPAGAEPGTESHGMAGRSVRNVVHTSVGGESARITLSNLYGTQPLTITHASVAVAAASNNPAAAVDTLRRLTFRGDTSVVIPPGQQIVSDAARLRVPHDADLLVTTFSPATSGPVTYHPHARQISYVADGDHTEDPSGSAYHEQSPYWRYLSAVDVLSSESDGTVVVIGDSITDGISSTMGTNRRWTDVLADRLREESGAPRYSVVNQGISGNRVLSDGRPGLRGGPGANPSGLSRFHRDVLGRTGVKAVVIALGINDILRNRETDARRIADGLRELTRQAHARGLRVVGATLTPFGGHRGFTPALEGVRRSVNDEIRSGKVFDEVVDFDKALRDPYDPRALLDRYDSGDHLHPSDGGFRRMAQTFNLTHLKGTSAAEL
>NZ_CP048641.1|WP_164324576.1|5756634_5757993_+|DUF445-domain-containing-protein
MERTKTAESAGTGRDMHARAGRPPSTGGGPSGPGAFSEADQEKQRGVRRMKLTATGLLLFVAVVYVLAKWAQNTGAGAWAGYVAAAAEAGMVGALADWFAVTALFRHPLGIPIPHTAIIPKKKDQLGASLGDFVGENFLSQTVVRQRLRAVGIGSRLGTWLAEPEHADRVTAELATALRGALTVLRDSDVQAVVGEAITRRADAQEIAPGLGKMLEKVVADGGHKRVVDLVCVRAHDWLVTHGDSVMVAVQGGAPGWTPRFVDKKVGERVYKELLRFVTEMRDMPEHPARGALDRFLTDFASDLQSDTDTRARVEHLKREVLARGEVQDLIASAWSAVRQMIVAAAEDERSELRLRVRAALLSLGRRMSTDARLQEKVDGWVEGAAVYVVTTYRDEITSLITDTVAGWDAEHTSKKIEAHIGRDLQFIRINGTVVGSLAGLVIYTVSRALGG
>NZ_CP048641.1|WP_164324578.1|5758064_5758505_+|hypothetical-protein
MTITEAEITAGARAIASALRVAPDTVIPFHPPLDGWPYAELHDGKVHYLVRERADVDLIAVYTDLDDFLYQLAEEATSGLARDWELAHRTGSVEDPDFDPRIAWVAKQLQLLNTVNPAWAERFRATVETRFSGLGLHDVDRHPVDS
>NZ_CP048641.1|WP_164324580.1|5758619_5760659_-|TNT-domain-containing-protein
MKNPISLRSPQRRASVVAGVIALATLFGPAAAHAAALDDLRTTTAATGAGSSATAPVDERPSATPPHVFGEPAPRSSGAPSAAAAANRAPNTPKAPEVGPPFKQASGVWQTNTLTPTFRNTVVDPDKDKTTSTFEVWTAKADGTAGSKVNLTDDNKFDVLVSGFAASGTPASVTVPKGKLKDGSTYLVRSSAYDGSAYEADWSPWAKFKVAVPPVVPPGPVTDGRDDVPADVKAQWQKLAKDALASYDKDQAELARIKSGGSIASGAAAVKQLNMNDVKLPDNGYFGVPRQFMAARVYDSRATDNPTVSMVGACEGALHCTQKFRLDYTLRVDTFYCTAQDAAANVGSKCPENELHWVGFSAEAQSEEFTREYNRITDGFDKFLDQMVGDLPKIFTQCVTGDTSTTEPPVVAAPRPPAVGVLRATADQCAEAGMQLGALLPLGRVGGAAKVVSDPLVEVNFTAAQIAKAKGALNELKLAQGKNQYATALRDVIGAAVKADNTGGLSFTLKQVIDLPKITANMRPEPQKLMAGYKPMGNMTIEQWFHKFWDKDANWFKYPPQNGFEGAAKVHLPKVGDHMDRFGGPNGGFLAPRDGTPYTERALPPSNVSADASAKGPGYHAYRWARDWGPAEVAQYGNIQGGKIAPWFGQPGGGTQYLLPKGINVQWLLDNRYIAEVTD
>NZ_CP048641.1|WP_164324581.1|5760941_5761367_-|RICIN-domain-containing-protein
MAPIIPDGEYWIRNAAFEDLYVDLSGSSTSPNTPISGWELHKGTNQKWRISTTNGVNQYVIKSAAGESYISQSDIRIYPPLIAGQPVPLQWSIEPVGENLFRIAFVYANGVITLPSNRKGTQLNLEEWVGERNQKWLFESA
>NZ_CP048641.1|WP_164328496.1|5761784_5762273_-|hypothetical-protein
MNVPTPRRNALRLLRNAFRPLRGRPFAERWATRLLGAGAGAAAYLLFIPWDLRNRVETPGAINETSPVTDTGITLLVVTVVALAAYFGFRDRVRWILPVVAAPPAALLYASFATHKTLDASPWPVAWLVFVMAGSGVVLAVAGCARQFREDGAAGGSAGSGV

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Crispr_ID: NZ_CP048641_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_9

6435485-6435593

Orphan

Consensus_repeat	Method
CTCGTCCTCAAACGCCGGACGGGCTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP048641_9

>merge|NZ_CP048641|9|6435485-6435593|CRISPRCasFinder
CTCGTCCTCAAACGCCGGACGGGCTGGAGGGGGTGGGCTGCGCTGGGCGGGTGGGGCAGGCCCTGACGTCGGCCCTGGACGGCCTCGTCCTCAAACGCCGGACGGGCTG

>NZ_CP048641|9|9|6435485-6435593|CRISPRCasFinder
CTCGTCCTCAAACGCCGGACGGGCTG	GAGGGGGTGGGCTGCGCTGGGCGGGTGGGGCAGGCCCTGACGTCGGCCCTGGACGGC
CTCGTCCTCAAACGCCGGACGGGCTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164325474.1\|6427286_6427865_+\|TMEM165/GDT1-family-protein	unknown	unknown	gnl\|CDD\|225030
NZ_CP048641.1\|WP_164325495.1\|6441548_6442793_-\|cytochrome-P450	unknown	unknown	gnl\|CDD\|225035
NZ_CP048641.1\|WP_164325497.1\|6443036_6444206_+\|steroid-3-ketoacyl-CoA-thiolase	unknown	unknown	gnl\|CDD\|181145
NZ_CP048641.1\|WP_164328574.1\|6429996_6431991_+\|DHA2-family-efflux-MFS-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|341045
NZ_CP048641.1\|WP_164325493.1\|6435690_6437112_-\|glycine-betaine/L-proline-transporter-ProP	unknown	unknown	gnl\|CDD\|340924
NZ_CP048641.1\|WP_164325476.1\|6428045_6428702_+\|HAD-IA-family-hydrolase	unknown	unknown	gnl\|CDD\|319829
NZ_CP048641.1\|WP_164325484.1\|6433238_6433724_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164325506.1\|6449908_6451144_-\|terpene-cyclase/mutase-family-protein	unknown	unknown	gnl\|CDD\|238362
NZ_CP048641.1\|WP_164325478.1\|6428746_6429475_-\|peptidoglycan-binding-protein	unknown	unknown	gnl\|CDD\|366659
NZ_CP048641.1\|WP_164328576.1\|6446129_6448019_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213192
NZ_CP048641.1\|WP_164325504.1\|6448021_6449245_-\|energy-coupling-factor-transporter-transmembrane-protein-EcfT	unknown	unknown	gnl\|CDD\|223692
NZ_CP048641.1\|WP_164325480.1\|6432030_6432582_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP048641.1\|WP_164325482.1\|6432758_6433214_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164325486.1\|6433856_6434183_-\|antibiotic-biosynthesis-monooxygenase	unknown	unknown	gnl\|CDD\|225209
NZ_CP048641.1\|WP_164325502.1\|6445272_6446133_-\|ECF-transporter-S-component	unknown	unknown	gnl\|CDD\|378961
NZ_CP048641.1\|WP_164325490.1\|6434696_6435371_-\|O-methyltransferase	unknown	unknown	gnl\|CDD\|226607
NZ_CP048641.1\|WP_164325500.1\|6444505_6444925_-\|transglycosylase-SLT-domain-containing-protein	unknown	unknown	gnl\|CDD\|381605
NZ_CP048641.1\|WP_164328575.1\|6439726_6441355_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164328577.1\|6449204_6449876_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164325488.1\|6434273_6434669_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164325474.1\|6427286_6427865_+\|TMEM165/GDT1-family-protein	gnl\|CDD\|225030	COG2119, COG2119, Predicted membrane protein [Function unknown].	1.89677e-24
NZ_CP048641.1\|WP_164325495.1\|6441548_6442793_-\|cytochrome-P450	gnl\|CDD\|225035	COG2124, CypX, Cytochrome P450 [Secondary metabolites biosynthesis, transport, and catabolism].	1.64746e-97
NZ_CP048641.1\|WP_164328574.1\|6429996_6431991_+\|DHA2-family-efflux-MFS-transporter-permease-subunit	gnl\|CDD\|341045	cd17502, MFS_Azr1_MDR_like, Saccharomyces cerevisiae Azole resistance protein 1 (Azr1p), and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This subfamily is composed of multidrug resistance (MDR) transporters including various Saccharomyces cerevisiae proteins such as azole resistance protein 1 (Azr1p), vacuolar basic amino acid transporter 1 (Vba1p), vacuolar basic amino acid transporter 5 (Vba5p), and Sge1p (also known as Nor1p, 10-N-nonyl acridine orange resistance protein, and crystal violet resistance protein). MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. This subfamily belongs to the Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters (MMR-like MDR transporter) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.7166e-90
NZ_CP048641.1\|WP_164325493.1\|6435690_6437112_-\|glycine-betaine/L-proline-transporter-ProP	gnl\|CDD\|340924	cd17366, MFS_ProP, Proline/betaine transporter of the Major Facilitator Superfamily of transporters. This subfamily is composed of Escherichia coli proline/betaine transporter, also called proline porter II (PPII), and similar proteins. ProP is a proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response. The ProP subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) 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.	0
NZ_CP048641.1\|WP_164325476.1\|6428045_6428702_+\|HAD-IA-family-hydrolase	gnl\|CDD\|319829	cd07527, HAD_ScGPP-like, subfamily of beta-phosphoglucomutase-like family, similar to Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). This subfamily includes Saccharomyces cerevisiae DL-glycerol-3-phosphate phosphatase (GPP1p/ Rhr2p and GPP2p/HOR2p) and 2-deoxyglucose-6-phosphate phosphatase (DOG1p and DOG2p). GPP1p and GPP2p are involved in glycerol biosynthesis, GPP1 is induced in response to both anaerobic and hyperosmotic stress, GPP2 is induced in response to hyperosmotic or oxidative stress, and during diauxic shift; overexpression of DOG1 or DOG2 confers 2-deoxyglucose resistance. These belong to the beta-phosphoglucomutase-like family whose other members include Lactococcus lactis beta-PGM, a mutase which catalyzes the interconversion of beta-D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and Escherichia coli 6-phosphogluconate phosphatase YieH. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	7.20386e-69
NZ_CP048641.1\|WP_164325497.1\|6443036_6444206_+\|steroid-3-ketoacyl-CoA-thiolase	gnl\|CDD\|181145	PRK07850, PRK07850, steroid 3-ketoacyl-CoA thiolase.	0
NZ_CP048641.1\|WP_164325478.1\|6428746_6429475_-\|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.	1.55632e-09
NZ_CP048641.1\|WP_164328576.1\|6446129_6448019_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213192	cd03225, ABC_cobalt_CbiO_domain1, First domain of the ATP-binding cassette component of cobalt transport system. Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.	2.08206e-78
NZ_CP048641.1\|WP_164325504.1\|6448021_6449245_-\|energy-coupling-factor-transporter-transmembrane-protein-EcfT	gnl\|CDD\|223692	COG0619, CbiQ, ABC-type cobalt transport system, permease component CbiQ and related transporters [Inorganic ion transport and metabolism].	4.16536e-12
NZ_CP048641.1\|WP_164325480.1\|6432030_6432582_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	3.48691e-12
NZ_CP048641.1\|WP_164325486.1\|6433856_6434183_-\|antibiotic-biosynthesis-monooxygenase	gnl\|CDD\|225209	COG2329, COG2329, Uncharacterized enzyme involved in biosynthesis of extracellular polysaccharides [General function prediction only].	1.06761e-21
NZ_CP048641.1\|WP_164325502.1\|6445272_6446133_-\|ECF-transporter-S-component	gnl\|CDD\|378961	pfam12822, ECF_trnsprt, ECF transporter, substrate-specific component. Energy-coupling factor (ECF) transporters consist of a substrate-specific component (known as the S component), and an energy-coupling module. The substrate-binding component is a small integral membrane protein which captures specific substrates and forms an active transporter in the presence of the energy-coupling AT module.	3.23704e-12
NZ_CP048641.1\|WP_164325490.1\|6434696_6435371_-\|O-methyltransferase	gnl\|CDD\|226607	COG4122, COG4122, Predicted O-methyltransferase [General function prediction only].	3.24581e-58
NZ_CP048641.1\|WP_164325500.1\|6444505_6444925_-\|transglycosylase-SLT-domain-containing-protein	gnl\|CDD\|381605	cd13402, LT_TF-like, lytic transglycosylase-like domain of tail fiber-like proteins and similar domains. These tail fiber-like proteins are multi-domain proteins that include a lytic transglycosylase (LT) domain. Members of the LT family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, and the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL). LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.	0.000565323
NZ_CP048641.1\|WP_164325506.1\|6449908_6451144_-\|terpene-cyclase/mutase-family-protein	gnl\|CDD\|238362	cd00688, ISOPREN_C2_like, This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system.	5.09188e-14

>NZ_CP048641.1|WP_164325490.1|6434696_6435371_-|O-methyltransferase
MSTNPTHWTKVDSYFTDLLTPADPVLTAALQDSEAAGLPAINVAPNQGKLLHLLAQLQGAHRILEIGTLGGYSTIWLARALPADGHLLTLEYSPKHAEVAAANLTRAGLDKITEIRTGPALDSLATLHAESPAPFDLVFIDADKANNPHYVEWSLKLTRPGSLIIVDNVVRGGEVTNPKSDDPSIQGTRAALELIASHPKLDGTAVQTVGTKGYDGFALARVLD
>NZ_CP048641.1|WP_164325488.1|6434273_6434669_+|hypothetical-protein
MLELTMAVVTGEADAGATAGMLMAEADSEPGAVLRVGRDRNVCRLAPPQDWLFVSRTHLEFRCRVDGTWTVTWVRGSQPDPASEVRLLAGGSAVALAYGATTPLPRGGSGEVVVRDRSGPRSVSVGFYHEV
>NZ_CP048641.1|WP_164325486.1|6433856_6434183_-|antibiotic-biosynthesis-monooxygenase
MSVVKINVLTVPAEQRETLEQRFASRAGAVESSDGFEWFELLRPVEGTDQYLVYTRWRDEASFQAWMEGPMKASHQGQADGGDRPKPASSSAAVWTFEVVQQAAPKSQ
>NZ_CP048641.1|WP_164325484.1|6433238_6433724_-|hypothetical-protein
MKYRVITAGIGILAVLGLILATSGTAFALPTVSAQAPRPAPTAEYENLTAREWALIAKDPDAHTGERYVVYGVVTQSDSATGTEILRANVDGIRHVDAYEYPTNTVLTGDASAFAKIVEDDSFTAKVEVSGSLTYETQIGGETTAPELQVDSITVTVPASR
>NZ_CP048641.1|WP_164325482.1|6432758_6433214_+|hypothetical-protein
MTGTGCTADSADSDGSANPTEKPHPKPAKNTPAYDDQKLGDRVERALATRIDDTGTDPALVESGLERVGDGIHTRPKLPRGAPYKLSVACAGKGRITLTIRAAKPSRQTVSCDAVPSTQRITGSRNNLEIDTAGAPGATGMVGWRVSRVAD
>NZ_CP048641.1|WP_164325480.1|6432030_6432582_-|GNAT-family-N-acetyltransferase
MSWTVSPEPVGSAAAVALWRAYYTEVSDRWYELHEGRRTDPAELEREIAADTGAGLVPPGGVLLVARWDGEPGGTAGVRLVGVGGGGGGCVGAGVEGAVVTAELTRVFVAAGLRGKGGGSVLLAAAEEAARSLGAGRVRLDTRHDLVEARALYERHGYVEGPPHNSDQYAEHWFRKELSVGGG
>NZ_CP048641.1|WP_164328574.1|6429996_6431991_+|DHA2-family-efflux-MFS-transporter-permease-subunit
MGGGVLVSIGALLLGMLLAALDQTIVSTALPTIVSDLGGLDHLSWVVTAYMLAATAATPLWGKLGDQYGRKKLFQTAIVIFLIGSALCGVAQNMPQLIGFRALQGLGGGGLMVLSMAIVGDLVSPRERGKYQGLFGAVFGATSVLGPLLGGLFTEHLSWRWVFYVNLPIGVVALVVIAAALHIPASRARHTIDYLGTFLIASVATCLVLVASLGGTTWAWGSAQIIGLAVLGVVLGVWFVAVERKAAEPVIPLKLFRIRTFTLTAVISFVVGFAMFGAMTYLPTFLQVVQGVTPTMSGVHMLPMVAGLLIASTASGQIVSRTGRWKVFPIAGTGVTTLGLLLLHQLDENSPTGEMSAFFFVFGLGLGLVMQVLVLIVQNAVSYEDLGVATSGATFFRSIGASFGVAIFGTVFTSRLGDKLTDALRGQDLPAGVGVDALKADPRGIAELPADVRPGVLNAYASSITDVFLYAAPVALVAFVLAWFLREDKLRGAVTAPDPTQTLASNPVERSSYEEVARALSLLGTRAGRREVYVRITERAGYDLLPAASWMLLRIARHGHVEPATLAERSMVPLTVVTEASRQLEERRLALREGLGLRLSDSGREVAAKLAAAREESLAELLGDWWGPGRPTDLMQLVEELGAEMCGSDAERPVGGGPGRGPGR
>NZ_CP048641.1|WP_164325478.1|6428746_6429475_-|peptidoglycan-binding-protein
MTLPEPSAPLPALTSTPLPPEAPAAADTAPAEASPAYERSARRVRTGLFAGAGAVFAAVAVFAGGALSGGNGGGDRGDGSDGTTDRALPDTAADTPDAPSGEPAPRKASRPAPRPTSSHAAPTPTRTPSASASRSLPVRNAPVTSPSRSTARATGSVGPAPSSRRPTPTATLRLGDQGDDVTELQHRLRQLFLYMGPPDGTYTRPVADAVTRYQWARGVTTDPHGTYGPKTRKSLESETNAP
>NZ_CP048641.1|WP_164325476.1|6428045_6428702_+|HAD-IA-family-hydrolase
MTAANVLTARALLLDMDGTLVNSDAVVERCWRQWSAKHGLDADEVMRVVHGRQGYASMALLLPERSMEENYAENREMLAQETADMDGVVPVPGAPEFMASLAGLPHALVTSADVGLSTGRMAAAGLSLPEIRVTAENVGASKPDPEGFLKGAAELGFDPADCVVFEDSGAGIAAGHAAGMRVVGVGPRAGEYEPTVWVDDLTQVRVSADAGFVRLTFN
>NZ_CP048641.1|WP_164325474.1|6427286_6427865_+|TMEM165/GDT1-family-protein
MISISVTALVFGVVFLAELPDKTALAGLVLGTRYRASYVFVGVAAAFAVHVVLAVAAGSVLTLLPQQLLHALTGVLFLGGAAVLLMKKGEDEEEVRAPKNQSFWRVSGAGFMLILIAEFGDLTQIMTANLAARYDDPLSVGLGAVLALWAVAGLGIVGGKALMKRVPLALITKIAAVLMLGLGLWSLYEAIA
>NZ_CP048641.1|WP_164325493.1|6435690_6437112_-|glycine-betaine/L-proline-transporter-ProP
MRTATPVAPRPKAAPSPTEPAPAEATVTDPALVKRAVKAAALGNAMEWFDFGVYSYIAVTLGKVFFPSGNPTAQLLSTFGAFAAAFLIRPVGGMVFGPLGDRVGRQKILALTMIMMAAGTFAIGLIPSYATIGVWAPILLLAARLVQGFSTGGEYAGASTFIAEYAPDKKRGFLGSWLEFGTLAGYIGGAGLVTLMTALLSSEDLQSWGWRIPFLIAGPMGLIGLYLRMRLEETPAFAAELEKAHKDEQTRPKVRVRDMVTGQWRALLLCMGLVLVFNVTDYMLLSYMPSYLTSELKYDETHGLLVILVVMALMMCAQPFVGALTDRVGRRPVIAAGCAGFLLLSIPALLLIRAGSLWAIGLGLSALGLLLVCFTASMPSALPALFPTPVRYGSLSIGFNISVSVFGGTTPLVVTALIGATGDVMMPAYYMMAAAVVGGVAVWYMTESAGRPLPGSPPAVETEREARALAGRR
>NZ_CP048641.1|WP_164328575.1|6439726_6441355_-|hypothetical-protein
MVSADLSILPTGSSPTERKNPFRALRTFYRRHRIAVLATAPTLPLYALWAAFLATGGGDLAAQQAWARFAEEHGSAAYSLFWYGGMHTANYSLISPYLMAAIGVKTVTVLSGVAGAWLVAVLIERSGVRRPLWPAVLASLAVWCNVASGRTTFALGLAFGLGAVLAVLRGRRLTVAVICSALATMASPVAGLFLLVAGAGYFFVREWGRALALLAPPVVVVGVTTLLFPFKGEHLMWADRIFPPVFFSLVLVVAGPREWRVLRCGAGVYAAGTVLTYLIPSPIGTNVERLAELVAPALLLAALLSPALPIMRRMALVTALVLSTAWVAQKTADDLEVSTIVPAWATDTQAVVRELERLGADRGRVEVVPARNHREATALAPYVNMARGWNRQLDIERGRLFYDGSFSATTYRAWLDKWAVGFVVLPSGRPDGPALDEAALVKSGPKWLEPVWKDKHWRIFRVRNAVPMASAPASVVRSTSTDVVVRVPERGSVSVRIVYSPWLRAEGACLKRHGEFTQLTVRAPGTYRISSGYGRSPRPSAC
>NZ_CP048641.1|WP_164325495.1|6441548_6442793_-|cytochrome-P450
MPCPALPDGFDFTDPDVLQARVPFPEFTLLRRSEPVRWIAQRPGISGFDDAGYWAVTRHADVKYVSTHPELFSSNLNTAVIRFNESISRDQIEVQKMIMLNMDPPEHTRVRQIVQRGFTPRAIRSLEDALRSRSHKIVEAALENAADDGSFDFVTNVAVELPLQAIAELIGVPQEDRSKIFDWSNKMAAYDDPEYAITEEVGAEAAMEIVSYAMHLAAARKECPAKDIVSQLVAAEDEGNLSSDEFGFFVILLAVAGNETTRNAITHGMHAFLTHPDQWELFKRERPVTTAEEIVRWGTPVVSFQRTATQDTELGDARIKKGDRVGIFYSSANHDPEVFENPDVFDITRDPNPHLGFGGGGPHFCLGKSLAVLEINLIFNAVAEAMPQLRLTGDPRRLRSAWLNGVKELQVSTR
>NZ_CP048641.1|WP_164325497.1|6443036_6444206_+|steroid-3-ketoacyl-CoA-thiolase
MAAEPVIVEAVRTPIGKRGGALANLHPAYLLGETYRELLGRTGIHADCVEQIVGGAVTQAGEQSANPARTAWLTMGLPYETGATTVNCQCGSSQQASHMVANMVAGGVIDVGISCGVESMSRVPLGSASRNGPGKPFPDEWNIDLPNQFEAAERIARKRGLSRENVDSLGLISQERAGVAWGEERFKRETFAVQVPTTEAEQAAGQGMWRLVDRDEGLRDTSMDALGRLKPVMPTAVHTAGNSSQISDGAAALLWTSKRMARALRLRPRARVVAQALVGADPHFHLDGPIDATRAVLGKAGMSLKDIDLVEINEAFAAVVLSWAQVFGQDLEKVNVNGGAIALGHPVGATGARLLTTALHELERADKEFALVCMCAGGAVATATILQRL
>NZ_CP048641.1|WP_164325500.1|6444505_6444925_-|transglycosylase-SLT-domain-containing-protein
MTVSILRRIASPKKAIAAGAVAAAATGMVFAAAPAQAAPAAATSDSAKAVAQRMIADDAQFQCFDRIVSHESGWDVNAKNASSGAYGLVQALPGSKMASAGADWQTNPETQIKWGHEYMKDRYGSPCGAWDHWQANGWY
>NZ_CP048641.1|WP_164325502.1|6445272_6446133_-|ECF-transporter-S-component
MNDAHQTHLDRPDHSDRQVRPVRLGPRSVAALGLVTAIGIVAFGWPLFAGGDSSLSAHAKDAPWLFAALLPLLLGVVVATIADVGLDAKAIAMLGVLAAAGAALRPLGAGTAGIEPMFFLMVLSGRVLGPGFGFVLGSVSMFASALLTGGVGPWMPFQMLAMGWVCMGAGLLPGPDTLRGRGELYVLGAYGAVSSVLYGTVMNLQGWPYIGGLATGVSFVPGDPVGENLARFLAYCLATSLGWDLPRAVVTVALSLTLGPAVLKALRRATRRAAFETPVTFEPSRR
>NZ_CP048641.1|WP_164328576.1|6446129_6448019_-|ATP-binding-cassette-domain-containing-protein
MIRFEDVSVRYEGAAGPTVRGVDLAVPEGELVLLVGPSGVGKSTLLGTVSGLVPHFTGGTLRGRVTVAGRDTRTHKPRELADVVGTVGQDPLAHFVTDTVEDELAYGMESLGLAPDVMRRRVEETLDLLGLADLRDRPITTLSGGQQQRVAIGSVLTPHPRVLVLDEPTSALDPAAAEEVLAVLQRLVHDLGTTVLMAEHRLERVVQYADQVLLLAAPGEPPLLGDPAEVMAVSPVYPPVVDLGRLAGVTPLPLTVRDARRRTAGLRERLVGVAPGEGRPVGASAAEGAAVASEPRPEPGPAEAVAPASGASGRASRWRRIGGKGRGGGAEVTAPDAARPDSAAPDASDAEAAKAGEAVQEAAPAGAPPAARVSGLAVYRGRVEALRRVDLDVCAGETVALMGRNGAGKSTLLSTLVGLLAPTSGTVRVGGATPHRTTPRELIRRVGLVPQEPRDLLYADTVAAECAAADHDADAAPGTCRDLVAELLPGIADDTHPRDLSEGQRLALALAIVLTARPPLLLLDEPTRGLDYAAKARLVTILRGLAAEGHAIVLATHDVELAAELAHRVVILAEGEVVADGPTADVVVSSPSFAPQVTKVLAPQPWLTVTQVRRALRAAAPGTGEGTTP
>NZ_CP048641.1|WP_164325504.1|6448021_6449245_-|energy-coupling-factor-transporter-transmembrane-protein-EcfT
MPPPSGRPAAAVADPAPEDRPARRLRLAPQAHRSNALHPGAWWLWALGLATAASRTTNPLLIGLLIGVAGYVVAARRTSAPWARSYGAFVKLALVVIGIRLVFAIVLGSPIPGTHLIVTLPEVPLPDWAQGVRIGGRVTAEGVVFALYDGVRLAGLLICVGAANALASPARLLKSLPGALYEVGVAVVVAMTFAPNLIADVQRLRAARRLRGRPDKGVRGLLQVGLPVLEGALERSVALAAAMDARGFGRTADVPARVRRTTAVLTLGGLMGVCAGTYGLLTADGTTYGLPVLGVGLAAALGGLWLGGRRSVRSRYRPDRWGLRAWLVAGSGAAVATLMIAASSSASDALHPGVVPLVAPTLPLLPAAAILIGLLPAFVAPVPPPAEAPVSARSAKPPRMPAKEKTS
>NZ_CP048641.1|WP_164328577.1|6449204_6449876_-|hypothetical-protein
MAALLTTVLTLFVGTLLAAGPAHAADYRYWSFWQQGKDGAWVYATQGPSIARPDDGDVEGFRFAVSANSGSAEKPRGAADFGAICADTPAKDGHKRIALVIDFGTPGDAPGGEQPPKPRTACTSVDSDGTSADALAAVAKPLRYNSGALLCAISGYPKQGCGEQVSGKESGGKGDKSESAQGNGDNGDSGGDDGGPSVGLLAGIAAIVALGAAAVWQARRRRG
>NZ_CP048641.1|WP_164325506.1|6449908_6451144_-|terpene-cyclase/mutase-family-protein
MNVRRSAAALAVAVAALGTAAAPAALADDASPSPKGPLPSGLYGKKDPQFDGVFRQSYALLAQKTVGVTPADKAVDWLTGQQCSSGGFAAYRADATEPCDSKTQVDSNSTAAAIQALHAVGNESNTVKKSLDWLKSVQNQDGGWGYNPGLPSDANSTGIVIGALAAVGEKPASAKSQKGKSPLDALTKLAMDCGKDGGAFGLADAKSGKLTPNADATAAGVLGGLGQGLVPAKGKEAGSAPKCAKPDTAGQAARNGTGYLLKSLAKTGHLTSAMPGAKDQPDVGNTADAVVALAAAGQAEQAKKSAEWLSKNSAAWAKDSGPAAYSQLVFAALAADMDVRDFGGADLVKQLNAQGPTPKAISEVATGAKVKDEKDEDDGSGVSVWWIVGVGLVAGAGIGFLLSGRKKKNQL

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Crispr_ID: NZ_CP048641_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP048641_10

6951055-6951153

Orphan

Consensus_repeat	Method
GCTGAACGGGCGAGAGCCTGAACAAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP048641_10

>merge|NZ_CP048641|10|6951055-6951153|CRISPRCasFinder
GCTGAACGGGCGAGAGCCTGAACAAGCTGGACGAGCGAGAGCTGAACAAGCTGGACGAGCGGGAGCTGAACGGGCTGAACGGGCGAGAGCTGAACAAGT

>NZ_CP048641|10|10|6951055-6951153|CRISPRCasFinder
GCTGAACGGGCGAGAGCCTGAACAAG	CTGGACGAGCGAGAGCTGAACAAGCTGGACGAGCGGGAGCTGAACGG
GCTGAACGGGCGAGAGCTGAACAAGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP048641.1\|WP_164325957.1\|6946937_6950018_+\|excinuclease-ABC-subunit-UvrA	unknown	unknown	gnl\|CDD\|234734
NZ_CP048641.1\|WP_164325958.1\|6951175_6951739_-\|YceI-family-protein	unknown	unknown	gnl\|CDD\|377274
NZ_CP048641.1\|WP_164325959.1\|6951852_6952713_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|375319
NZ_CP048641.1\|WP_164325963.1\|6955657_6956305_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372083
NZ_CP048641.1\|WP_164325953.1\|6943304_6944573_-\|MHS-family-MFS-transporter	unknown	unknown	gnl\|CDD\|340927
NZ_CP048641.1\|WP_164325961.1\|6953960_6954380_+\|Rieske-(2Fe-2S)-protein	unknown	unknown	gnl\|CDD\|239550
NZ_CP048641.1\|WP_164328632.1\|6950216_6951044_+\|crotonase/enoyl-CoA-hydratase-family-protein	unknown	unknown	gnl\|CDD\|236205
NZ_CP048641.1\|WP_164325960.1\|6952753_6953731_-\|carbohydrate-kinase	unknown	unknown	gnl\|CDD\|238572
NZ_CP048641.1\|WP_164325950.1\|6938757_6940713_+\|TerD-family-protein	unknown	unknown	gnl\|CDD\|132992
NZ_CP048641.1\|WP_164328633.1\|6960265_6961390_+\|uridine-diphosphate-N-acetylglucosamine-binding-protein-YvcK	unknown	unknown	gnl\|CDD\|211689
NZ_CP048641.1\|WP_164325964.1\|6956310_6957183_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164325954.1\|6944852_6945314_+\|type-II-3-dehydroquinate-dehydratase	unknown	unknown	gnl\|CDD\|237270
NZ_CP048641.1\|WP_164325949.1\|6938098_6938677_+\|TerD-family-protein	unknown	unknown	gnl\|CDD\|376767
NZ_CP048641.1\|WP_164325962.1\|6954465_6955425_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP048641.1\|WP_164325956.1\|6946001_6946700_-\|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme	unknown	unknown	gnl\|CDD\|236578
NZ_CP048641.1\|WP_164325952.1\|6942172_6943273_+\|ionic-transporter-y4hA	unknown	unknown	gnl\|CDD\|223464
NZ_CP048641.1\|WP_164325951.1\|6940994_6942014_+\|TerC-family-protein	unknown	unknown	gnl\|CDD\|274743
NZ_CP048641.1\|WP_164325965.1\|6957321_6959445_+\|excinuclease-ABC-subunit-UvrC	unknown	unknown	gnl\|CDD\|234792
NZ_CP048641.1\|WP_164325966.1\|6959441_6960377_+\|RNase-adapter-RapZ	unknown	unknown	gnl\|CDD\|235450
NZ_CP048641.1\|WP_164325955.1\|6945335_6945992_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293792

Protein	Function_ID	Function_description	E-value
NZ_CP048641.1\|WP_164325957.1\|6946937_6950018_+\|excinuclease-ABC-subunit-UvrA	gnl\|CDD\|234734	PRK00349, uvrA, excinuclease ABC subunit UvrA.	0
NZ_CP048641.1\|WP_164325958.1\|6951175_6951739_-\|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.	2.24078e-51
NZ_CP048641.1\|WP_164325959.1\|6951852_6952713_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|375319	pfam17765, MLTR_LBD, MmyB-like transcription regulator ligand binding domain. This domain is found in a family of actinobacterial transcription factors. The structure shows it has a PAS domain like fold and it is bound to Myristic acid.	9.09684e-36
NZ_CP048641.1\|WP_164325963.1\|6955657_6956305_+\|hypothetical-protein	gnl\|CDD\|372083	pfam12385, Peptidase_C70, Papain-like cysteine protease AvrRpt2. This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defense responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.	3.52897e-09
NZ_CP048641.1\|WP_164325953.1\|6943304_6944573_-\|MHS-family-MFS-transporter	gnl\|CDD\|340927	cd17369, MFS_ShiA_like, Shikimate transporter and similar proteins of the Major Facilitator Superfamily. This subfamily is composed of Escherichia coli shikimate transporter (ShiA), inner membrane metabolite transport protein YhjE, and other putative metabolite transporters. ShiA is involved in the uptake of shikimate, an aromatic compound involved in siderophore biosynthesis. It has been suggested that YhjE may mediate the uptake of osmoprotectants. The ShiA-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) 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.	5.58935e-153
NZ_CP048641.1\|WP_164325961.1\|6953960_6954380_+\|Rieske-(2Fe-2S)-protein	gnl\|CDD\|239550	cd03467, Rieske, Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.	6.32575e-21
NZ_CP048641.1\|WP_164328632.1\|6950216_6951044_+\|crotonase/enoyl-CoA-hydratase-family-protein	gnl\|CDD\|236205	PRK08259, PRK08259, crotonase/enoyl-CoA hydratase family protein.	3.8816e-157
NZ_CP048641.1\|WP_164325960.1\|6952753_6953731_-\|carbohydrate-kinase	gnl\|CDD\|238572	cd01167, bac_FRK, Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.	6.17244e-84
NZ_CP048641.1\|WP_164325950.1\|6938757_6940713_+\|TerD-family-protein	gnl\|CDD\|132992	cd06974, TerD_like, Uncharacterized proteins involved in stress response, similar to tellurium resistance terD. Tellurium resistance terD like proteins. This family is composed of uncharacterized proteins involved in stress response, such as the tellurium resistance proteins, chemical-damaging agent resistance proteins, and general stress proteins from a variety of organisms. The tellurium resistance proteins are homologous terA,-D,-E,-F,-Z,-X gene products, which confer tellurium resistance mediated by plasmids. Currently, the biochemical mechanism of tellurium resistance remains unknown. The family also contains several ter gene homologues, YceC, YceD, YceE, for which there is no clear evidence for any involvement in the tellurium resistance. A putative cAMP-binding protin CABP1 shows a significant similarity to the terD protein and is also included in this family.	3.77692e-22
NZ_CP048641.1\|WP_164328633.1\|6960265_6961390_+\|uridine-diphosphate-N-acetylglucosamine-binding-protein-YvcK	gnl\|CDD\|211689	TIGR01826, Putative_gluconeogenesis_factor, conserved hypothetical protein, cofD-related. This model represents a subfamily of conserved hypothetical proteins that forms a sister group to the family of CofD, (TIGR01819), LPPG:Fo 2-phospho-L-lactate transferase, an enzyme of cytochrome F420 biosynthesis. Both this family and TIGR01819 are within the scope of the pfam01933. [Hypothetical proteins, Conserved].	3.84265e-94
NZ_CP048641.1\|WP_164325966.1\|6959441_6960377_+\|RNase-adapter-RapZ	gnl\|CDD\|235450	PRK05416, PRK05416, RNase adapter RapZ.	3.7918e-165
NZ_CP048641.1\|WP_164325954.1\|6944852_6945314_+\|type-II-3-dehydroquinate-dehydratase	gnl\|CDD\|237270	PRK13015, PRK13015, 3-dehydroquinate dehydratase; Reviewed.	3.85465e-86
NZ_CP048641.1\|WP_164325949.1\|6938098_6938677_+\|TerD-family-protein	gnl\|CDD\|376767	pfam02342, TerD, TerD domain. The TerD domain is found in TerD family proteins that include the paralogous TerD, TerA, TerE, TerF and TerZ proteins It is found in a stress response operon with TerB and TerC. TerD has a maximum of two calcium-binding sites depending on the conservation of aspartates. It has various fusions to nuclease domains, RNA binding domains, ubiquitin related domains, and metal binding domains. The ter gene products lie at the centre of membrane-linked metal recognition complexes with regulatory ramifications encompassing phosphorylation-dependent signal transduction, RNA-dependent regulation, biosynthesis of nucleoside-like metabolites and DNA processing linked to novel pathways.	2.53087e-53
NZ_CP048641.1\|WP_164325956.1\|6946001_6946700_-\|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme	gnl\|CDD\|236578	PRK09583, PRK09583, mycothiol-dependent maleylpyruvate isomerase; Reviewed.	4.14287e-75
NZ_CP048641.1\|WP_164325952.1\|6942172_6943273_+\|ionic-transporter-y4hA	gnl\|CDD\|223464	COG0387, ChaA, Ca2+/H+ antiporter [Inorganic ion transport and metabolism].	5.14744e-83
NZ_CP048641.1\|WP_164325951.1\|6940994_6942014_+\|TerC-family-protein	gnl\|CDD\|274743	TIGR03718, R_switched_Alx, integral membrane protein, TerC family. Rfam model RF00080 describes a structured RNA element called the yybP-ykoY leader, or SraF, which may precede one or several genes in a genome. Members of this highly hydrophobic protein family often are preceded by a yybP-ykoY leader, which may serve as a riboswitch. From the larger group of TerC homologs (pfam03741), this subfamily contains TerC itself from Alcaligenes sp. plasmid IncHI2 pMER610 and from Proteus mirabilis. It also contains the alkaline-inducible E. coli protein Alx, which unlike the two TerC examples is preceded by a yybP-ykoY leader.	3.2612e-140
NZ_CP048641.1\|WP_164325965.1\|6957321_6959445_+\|excinuclease-ABC-subunit-UvrC	gnl\|CDD\|234792	PRK00558, uvrC, excinuclease ABC subunit UvrC.	0
NZ_CP048641.1\|WP_164325955.1\|6945335_6945992_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293792	cd06262, metallo-hydrolase-like_MBL-fold, mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.	3.28844e-41

>NZ_CP048641.1|WP_164328632.1|6950216_6951044_+|crotonase/enoyl-CoA-hydratase-family-protein
MPAAADVPVRIERQGPVTTVVLSRPHARNAVDGPTAKALADAFRAFDADPEASVAVLWGEGGTFCAGADLKALGTPDGNVVAEVTSETSETSETSENGANDGPMGPTRLDLSKPVIAAVSGHAVAGGLELALWCDLRVAEEDAVFGVFCRRWGVPLIDGGTVRLPRIVGEGRAMDLILTGRPVDATEALGMGLVNRVVPKGSARAAAERLAAEIAAFPQTCLRHDRLSAREQHGLPERQALAGELRHGLHALGEATEGAARFAAGAGRHGAFGEH
>NZ_CP048641.1|WP_164325957.1|6946937_6950018_+|excinuclease-ABC-subunit-UvrA
MADRLIVRGAREHNLKNVSLDLPRDSLIVFTGLSGSGKSSLAFDTIFAEGQRRYVESLSSYARQFLGQMDKPDVDFIEGLSPAVSIDQKSTSRNPRSTVGTITEVYDYLRLLFARIGKPHCPECGRPITRQSPQAIVDKVLELPEGSRFQVLSPLVRERKGEFVDLFADLQTKGYSRARVDGETIQLSEPPTLKKQEKHTIEVVIDRLTVKDSAKRRLTDSVETALGLAGGMVVLDFVDLPEDDPERERMYSEHLYCPYDDLSFEELEPRSFSFNSPFGACPDCTGIGTRMEVDPELIVPDEDKSLDEGAIHPWSHGHTKDYFGRLVGALADALGFSTDMPWAGLPQRAKKALLHGHKTQIEVRYRNRYGRERVYTTAFEGAVPFVKRRHSEAESDASRERFEGYMREVPCPTCEGTRLKPIVLAVTVMGKSIAEVSAMSISDCADFLAELKLGARDKKIAERVLKEVNERLRFLVDVGLDYLSLNRAAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNHRLIETLVRLRDMGNTLIVVEHDEDTIKVADWVVDIGPGAGEHGGKVVHSGSLKELLDNEKSVTGQYLAGKRSIPVPDLRRPADPTRRLTVHGARENNLRDIDVSFPLGVLTAVTGVSGSGKSTLVNDILYTHLARELNGARSVPGRHTRVDGDDLVDKVVHVDQSPIGRTPRSNPATYTGVFDHVRKLFAETTEAKVRGYLPGRFSFNVKGGRCENCSGDGTIKIEMNFLPDVYVPCEVCHGARYNRETLDVHYKGKSIAEVLDMPIEEALGFFEAVPAIARHLKTLHDVGLGYVRLGQSAPTLSGGEAQRVKLASELQKRSTGRTVYVLDEPTTGLHFEDISKLITVLSGLVDKGNTVIVIEHNLDVIKTADWVVDMGPEGGSGGGLVIAEGTPEQVAGVPASHTGKFLRDIIAPDRISDAGVPPARKATRKAPAKKTVAAATSTAKKTVTKAAAKKTTTAKSAATKATASKTAASKPAAKKSAAKKTATRTRKT
>NZ_CP048641.1|WP_164325956.1|6946001_6946700_-|maleylpyruvate-isomerase-family-mycothiol-dependent-enzyme
MIDHVRDLASVRDATERLLAAAAALDNVSMAEPSRLPGWTRGHVLAHVARNADALVNVLAGRPMYVSGEARDADIERDAPRAMEVQLADLRESAARLGAQAALPADWSRTITMRNGVTDSASRVPFRRWVELELHHVDLGVGYELEDIPADFLEREIDFLTDRFSGNAEVAATNVTDGTRAWPTGRVADKPEVTVSGPAPALVGWLAGRRDHSALAVELTVEGGPLPALPPL
>NZ_CP048641.1|WP_164325955.1|6945335_6945992_-|MBL-fold-metallo-hydrolase
MTYSGAVKVGGPADVHELRDLMISKVAVGPMDNNAYVLRCRATDEQLLIDAANDAHTLLTLIGGDGIKAVVTTHQHGDHWQALAEVVAATGARTYAGREDAEGIPTPTDVLVDDGDTIAFGRISLTARHLVGHTPGSIALVYDDPHGHPHVFTGDCLFPGGVGNTWKDPERFTSLIEDVETKIFGTLPDETWVYPGHGKDTTLGAERPHVQEWRARGW
>NZ_CP048641.1|WP_164325954.1|6944852_6945314_+|type-II-3-dehydroquinate-dehydratase
MPHTLATAPVMILNGPNLNLLGKRQPEIYGTDTLADVEAMCAKAAAAHGGTVDLRQSNHEGELVDWIHEAREHHVGIVINPAAYSHTSVAILDALNTCDGMPVVEVHISNIHQREAFRHHSYVSQRADGVIAGCGVQGYVFGVERVAALVARG
>NZ_CP048641.1|WP_164325953.1|6943304_6944573_-|MHS-family-MFS-transporter
MLRLAAASLAGTAIEFYDFFVYGTAAALVLGPLFFPTFSPLAGTLAAFATFGVGFVARPLGSVLFGHLGDRRGRRPVLVISLLLTGVATVAVGCVPTYESIGAAAPVLLLVLRFAQGVGLGGEWGGAVLLTAEHAPPERRALWASFPQVGPAIGFLLANGVMLVLSATLTDAQFASWGWRIPFWGAGLLAVAGLALRASLAESPDFLEVREHARVPLVEVARHHWRLVLLTAGALAVGYAVFYAVTTWSLSYGVERLGVSRTVMLACIMGAVVVKGALTPVAALLGDRYGRRPMCLVGCSAVALWMFPMVALLATGEPFLMFLGFLVALLAFVVMFSVVAAYLPELYEPRVRCTGAAVGYNLAGVLGGALTPLVATAAARGEGTPWGVAAYLTAVAVLSLGCFALLPETLPAREEAVVPATG
>NZ_CP048641.1|WP_164325952.1|6942172_6943273_+|ionic-transporter-y4hA
MIPRLRAVTARWTAAVPVLGVVLLALTWGRDLSGVVVALVTAVLAGAVLAAVHHAEVIAHRVGEPFGSLVLAVAVTIIEVALIVTLMADGGDKSSTLARDTVFAAVMITCNGILGLCLLTGALRHRVAVFNSEGTGAALATVATLATLSLVLPTFTTSKPGPEFSTSQLTFAALASLVLYGLFVATQTVRHRDYFLPVTKEGDVVDGDDHAEGPSARTALISLGLLALALVGVVGLAKGVSPTIESGVESAGLPHAVVGVIIALLVLLPETIAAVRAARRDRVQTSLNLALGSAMASIGLTIPAVAIASVWLSGPLVLGLSSTHMVLLVLTVLVGTLTVVPGRATPLQGGVHLVLFAAYLELAINP
>NZ_CP048641.1|WP_164325951.1|6940994_6942014_+|TerC-family-protein
MDVSMTLWAATVLGLCALIAVDFFIGRKPHDVSIKEAGTWTIVWIVLAVLFGIGLLIAGESQASGEFFAGFITEKSLSVDNLFVFILIMAKFSVPSHLQQRVLLFGVLIALVLRAIFIAAGAAVIANFSWVFYIFGAFLIYTAWKLVQEARAGEEEEDWEENRLLKSIEKKFGVSDRYEGTKLFIKKNGKKVMTPLMVVMLAIGTTDVLFAMDSIPAIFGLTQDPYIVFTANAFALMGLRQLYFLIGGLLKKLVHLSYGLSVILGFIGVKLVLHALHENGVHVPEISIPVSLGVICGVLIVTTITSLMANKKQAQLEAAEAGEGDIQKDSKDDKDSIEA
>NZ_CP048641.1|WP_164325950.1|6938757_6940713_+|TerD-family-protein
MTAELVRGQNHPLPGTRLEIRVSAGKPIVAGATLCDDRRTVRGTAWVAHPGAPTLPGLEVSRQAAADHRLAVDLGALPDGAHHVNVLLALPVGAAGPVAFGSVAAPFVAVTGLDGTEIASYTITDLSAESAVVALELYRRQDAWKVRAVGQGYAGGLADMLADQGLPQAQELASTINDAVARGLARSVAAPPPRPADEARVRAAAQGHTAPGQQPAPPEPAADPAGKAIAPTPQPGEGDTPQQPGDGSVNYTHPRRQTSAPPPPPPTAAPAAPGQSAQPVAGDATGWSLEERLYNQVWGMFEDLARTAAAYRSAVDFAESRMDQELDKVLSDPRSRIGNTGDAARAAARARHGDLVDQARAALDRDLAQLAAEAEVVEPALPPAFADWSSPVWQGYRAPMEIPMALRLGNLHLPESPDLRIPMLVRLPLERGLWIDSGRSGADSLADADQLRRLGLDSAVAHAARLLASYPPGEFTVHVIDAAGTGASAFAPLVRAGVLAGPPATGAAGVTAALTRLTQRVDLVQMAVRGGVADALPQDLDTGEQLLVVNDFPHGFDDRAVTQLRYLADEGPAVGVHLMMVADREDASEYGPLLDPLWRALLRVTPVPDDHLADPWVGHAWTYEPPMVPPGSQVLTHVLDRVGEARRTGSR
>NZ_CP048641.1|WP_164325949.1|6938098_6938677_+|TerD-family-protein
MTVNMTKGQAISLQKNDGGALTSVRMGLGWQAAPRRGLFGTRTREVDLDASAVLFADKQPVDVVFFRHLVSDDGSVRHTGDNLVGGVGQGGDDEAILVDLQRVPVHIDQIVFTVNSFTGQTFQEVQNAFCRLVDETNGQELARFTLDGGGQYTAQIMAKVHRAGAGWQMTALGNPANGRTFQDLMPAILPHL
>NZ_CP048641.1|WP_164325958.1|6951175_6951739_-|YceI-family-protein
MTFETNTADATTALPLPVGRWALDPLHSAVNFTIRHLGISKVRGRFTQFDAELVVGGALDTTAVNATIALASIDTGNPDRDAHVRASDLLDVEKRPTMAFRSTGITGSGEDWTMAGDLTIGDVTRPVTLAVEFGGLGEFGDTRHAGFEATGEIRRSEYGLTFAPGMLGEAVKIQLDMQFLEPGKAEA
>NZ_CP048641.1|WP_164325959.1|6951852_6952713_+|helix-turn-helix-domain-containing-protein
MSDNELGAFLRARREAVTPTEVGLPSGPRRRTPGLRRSEVATLAGISVEYLTRLEQGRDRNPSPSVLGSLADVLRLTVEERIHLRRLEKASNGADDPCCSAAPPPALSVRPTVRALVDLLEPTPAVLLNRLSDVLAYTTGYERIARPLGLLDGERPNLLRFVFTDERARTAFTEWDRVADEQIAHLRSESPMIDPHVMQFVDELTVLAGAPFSDRIEAVPGLPRRSGVQSLDHPEAGALRLSYESLALPDVDGQRLLVHLPADDATSAALDRLNGRQPGGLRAVSG
>NZ_CP048641.1|WP_164325960.1|6952753_6953731_-|carbohydrate-kinase
MIVVAGEALIDLVPQGTGSPSGGAASPSGGASQSGSLPALAPRLGGGPYNTAVALGRLGSPTAFCSRVSLDAFGEALLAGLRAADVDVSYVQRGAEPTTLAVASVGADGSAGYSFYVDGAADRLFAVPRRIPDSVRALSFGTCSLVLEPGASAYEELLRREAARGVFTALDPNIRAVLIPDADAYRARFKNWLPSVALLKVSEEDARWLGGTPEEWLASGPVAVVVTRGGDGLSVFTRDGGEVCVPGVPVDVVDTIGAGDTVNAALLHGLAARGALSAHAVAGLGVDAWAEVLRFAARAAAITCSRAGAEPPYARELGEDGGFAG
>NZ_CP048641.1|WP_164325961.1|6953960_6954380_+|Rieske-(2Fe-2S)-protein
MSGTSPARRTVLRAAALVPAAGLGLTACSSGDGGSRSAPTKPVDLGAADEVPVGGSKLYTDDHVVVSRIADDEYKAFSSICTHAQCPIEKLQGSKLTCQCHGSQFDARNGKVLREPAVTPLEELPVKVAGGKIVAGPGA
>NZ_CP048641.1|WP_164325962.1|6954465_6955425_-|hypothetical-protein
MRNVSPPTTALADDTPADLATALRTGPFHVALRAAIAARRLPLQRVRHHLARAGVNVGVTSLSYWQQGARRPQRPESLRAVRALEEILQLPEESLIRLLARADERTDTERPAARSYRSLVEASDVLQSLIADLGSPLDGGLHTIGHHERIRIGPRRELLGRDSQHVVRAHTDGIDRYLAIHHGDPGCAPEHMEVRALENCRTGRVRWHHDTGVLVAELLFDARLRAGDTHLFCYGFEDGTAGTSAEYVRGFSFTGGQYALQVRFAEDALPARCHRFTQRSTAAPRLGRQELTLSGSHRSVHLVEPQVRAGLIGIGWDWE
>NZ_CP048641.1|WP_164325963.1|6955657_6956305_+|hypothetical-protein
MHHTSSGSSRRRRLTALAVAAAAFLAVPAATAVAAPHDTSSTVAPAASGAADPSVLAAKRLNITMQAQQKTNWCWAAAGNTIATYLGKNYSQNQFCNAAFGRNQNTECPNNQATLGNVQTGLRWAGINSGSYVTGWLRYPTVQAEINANRPIETRILWSNGGGHMHTIYGYDTANDWVYWGDPWPSSDRYNWASHSWYVNNNTFSWTHSLYRIGA
>NZ_CP048641.1|WP_164325964.1|6956310_6957183_+|hypothetical-protein
MNRHVSRTSLKAVLAGSAAALFLGVAAPHATADSGPAAPPAPSDASRNAAHDAAEAPKTLDTLSRFFAREGAVTKAAAEPRVAGDKAVPVYYLSPDFVAGKKDAPIARMQFLASKAVSSDGQEASLWAVRQGGSWQIVNIATGDDETHYARVGADKAPGGTVFLEPQINGWYVTKGTRVLPLDKDARRAVGAEGTTVVAYQKRVHKAYGDKLPGSAYGKSGKAGGFTEEPSGGAAAASGAKSDSGARTESASASSDGAVTVASTVAGAGALVALGLSGVALVRRRSRRLG
>NZ_CP048641.1|WP_164325965.1|6957321_6959445_+|excinuclease-ABC-subunit-UvrC
MADPSSYRPKPGQIPDSPGVYKFRDEHRRVIYVGKAKSLRQRLASYFQDLANLHPRTATMVTTAASVEWTVVATETAALQLEYTWIKEYDPRFNVKYRDDKSYPYLAVTMNEEFPRVQVMRGQKKKGVRYFGPYGHAWAIRDTVDLLLRVFPVRTCSAGVFKNAARTGRPCLLGYIGKCSAPCVDRVSAEEHRELAEEFCDFMAGRTGTYIRRLERRMTDAAEDMEYERAARLRDDMGALRKAMEKSAVVLADATDADLIAVAEDELEAAVQIFHVRGGRVRGQRGWVTDKVEAVTTGDLVEHALQQLYGEETGDAVPKEVLVPALPDPADPVQEWLTQRRGSNVSLRIPQRGDKKALMETVARNAQQSLMLHKTKRASDLTTRSRALEEIAAALELDSAPLRIECYDISHLQGDDVVASMVVFEDGLGRKSEYRRFQIKSFEGQDDVRSMHEVITRRFRRYLAEKEKTGEWSPEDAQEAPDAQDVQDIQGGLTEEDGRPKKFAYPPQLVVVDGGQPQVAAAQRALDELGIDDIAVCGLAKRLEEVWVPGEDDPVILPRTSEGLYLLQRVRDEAHRFALTYQRSKRAKRFKASPLDAVPGLGEARKQTLVKHFGSVKRLRSATIDQICEVPGIGRKTAEAVLAAFAQAAPAAPAVNTATGEIMEEEEPATAGDSDHGEEPAGAGDSPDDSEVPTRVGTAETRRGMET
>NZ_CP048641.1|WP_164325966.1|6959441_6960377_+|RNase-adapter-RapZ
MSEHDEGGEQVSTGTTIEPGEAAEAAIPELVIISGMSGAGRSTAAKCLEDLGWFVVDNLPPALIPTMVELGARSQGNVARIAVVVDVRGRRFFDNLRQSLADLESKHVTRRIVFLESSDDALVRRFESVRRPHPLQGDGRIVDGIAAERELLRELRGDADLVIDTSSLNVHELRAKMDAQFAGDEEPELRATVMSFGFKYGLPVDADLVVDMRFLPNPHWVPELRPFTGLNEEVSAYVFNQPGAKEFLDRYTELLQLIAAGYRREGKRYVTIAVGCTGGKHRSVATSEKLTARLTAAGIETVLVHRDMGRE
>NZ_CP048641.1|WP_164328633.1|6960265_6961390_+|uridine-diphosphate-N-acetylglucosamine-binding-protein-YvcK
MYGRQAPLRGHVREADRPSDRRRDRDRPRPPGHGARMKPNRRVLRLNRLGRKRGAQPKVVALGGGMGLSASLAALRRITGDVTAVVTVADDGGSSGRLRDELGVLPPGDLRKALAALCGDDDWGQTWARVIQHRFQSKGDLHEHAVGNLLIVALWEQLGDHVQALDLVGRLLGAHGRVLPMSAVPLELQALVKGHDPERPDDVDTVCGQATVALTPGEVQSVHVVPQDPPAVPEAVAAVLDADWVVLGPGSWFSSVIPHLLVPELLDALTETKARRILSLNLAPQPGETEGFSPQRHLEVLARHAPKLALDVVLADEAAVPDRGSLTDAAKRFGATVELAPVARQDGSPKHDPELLAAAYDRIFRMHGRIGPWR

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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_CP048641_8	8.1\|5748169\|22\|NZ_CP048641\|CRISPRCasFinder	5748169-5748190	22	NZ_CP031650	Pantoea agglomerans strain TH81 plasmid unnamed1, complete sequence	288156-288177	2	0.909
NZ_CP048641_8	8.2\|5748217\|22\|NZ_CP048641\|CRISPRCasFinder	5748217-5748238	22	NZ_CP012182	Pseudonocardia sp. EC080610-09 plasmid pBCI2-1, complete sequence	304781-304802	2	0.909
NZ_CP048641_8	8.2\|5748217\|22\|NZ_CP048641\|CRISPRCasFinder	5748217-5748238	22	NZ_CP012185	Pseudonocardia sp. EC080619-01 plasmid pBCI1-2, complete sequence	743777-743798	2	0.909
NZ_CP048641_7	7.1\|5552721\|25\|NZ_CP048641\|CRISPRCasFinder	5552721-5552745	25	NZ_CP023712	Rhodococcus ruber strain YC-YT1 plasmid unnamed1, complete sequence	77713-77737	3	0.88

1. spacer 8.1|5748169|22|NZ_CP048641|CRISPRCasFinder matches to NZ_CP031650 (Pantoea agglomerans strain TH81 plasmid unnamed1, complete sequence) position: , mismatch: 2, identity: 0.909

ctgagtctggccctggtcctga	CRISPR spacer
ctgagtctggccctggccctgt	Protospacer
****************.****

2. spacer 8.2|5748217|22|NZ_CP048641|CRISPRCasFinder matches to NZ_CP012182 (Pseudonocardia sp. EC080610-09 plasmid pBCI2-1, complete sequence) position: , mismatch: 2, identity: 0.909

ctggtcctgacctccggtcggt	CRISPR spacer
ctggtcctgatctccggtcggc	Protospacer
**********.**********.

3. spacer 8.2|5748217|22|NZ_CP048641|CRISPRCasFinder matches to NZ_CP012185 (Pseudonocardia sp. EC080619-01 plasmid pBCI1-2, complete sequence) position: , mismatch: 2, identity: 0.909

ctggtcctgacctccggtcggt	CRISPR spacer
ctggtcctgatctccggtcggc	Protospacer
**********.**********.

4. spacer 7.1|5552721|25|NZ_CP048641|CRISPRCasFinder matches to NZ_CP023712 (Rhodococcus ruber strain YC-YT1 plasmid unnamed1, complete sequence) position: , mismatch: 3, identity: 0.88

tgggaggggggccggacgcccgtcc	CRISPR spacer
ggggaggggggccggacgccccgcc	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