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_AP022569	Mycobacterium cookii strain JCM 12404	5 crisprs	WYL,cas4,DEDDh,csa3,DinG,cas3	1	3	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_AP022569_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP022569_1

581714-581794

Orphan

Consensus_repeat	Method
CGGGGCGTTTCCGCCGCCTGCCCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP022569_1

>merge|NZ_AP022569|1|581714-581794|CRISPRCasFinder
CGGGGCGTTTCCGCCGCCTGCCCCGCCGCCTGCCCCGCCGCCGGGCGCAGCGGGTGCGGGTGCGTTTCCGCCGCCTGCCCC

>NZ_AP022569|1|1|581714-581794|CRISPRCasFinder
CGGGGCGTTTCCGCCGCCTGCCCC	GCCGCCTGCCCCGCCGCCGGGCGCAGCGGGTGC
GGGTGCGTTTCCGCCGCCTGCCCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP022569.1\|WP_163774981.1\|572744_575861_+\|isoleucine--tRNA-ligase	unknown	unknown	gnl\|CDD\|235681
NZ_AP022569.1\|WP_163774991.1\|585524_588416_+\|MMPL-family-transporter	unknown	unknown	gnl\|CDD\|129913
NZ_AP022569.1\|WP_163774989.1\|584233_585037_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|223377
NZ_AP022569.1\|WP_163774987.1\|582643_583051_-\|group-1-truncated-hemoglobin	unknown	unknown	gnl\|CDD\|381253
NZ_AP022569.1\|WP_163774988.1\|583209_584226_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|235962
NZ_AP022569.1\|WP_163774983.1\|578781_579483_+\|signal-peptidase-II	unknown	unknown	gnl\|CDD\|237810
NZ_AP022569.1\|WP_163774984.1\|579479_580406_+\|RluA-family-pseudouridine-synthase	unknown	unknown	gnl\|CDD\|161659
NZ_AP022569.1\|WP_163774995.1\|596126_596564_+\|nitroreductase-family-deazaflavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|281995
NZ_AP022569.1\|WP_163774985.1\|580887_581643_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|369777
NZ_AP022569.1\|WP_163774992.1\|588428_591971_+\|DNA-polymerase-III-subunit-alpha	unknown	unknown	gnl\|CDD\|235554
NZ_AP022569.1\|WP_163774982.1\|577793_578714_-\|asparaginase	unknown	unknown	gnl\|CDD\|199208
NZ_AP022569.1\|WP_163781241.1\|575873_576386_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP022569.1\|WP_163774980.1\|571675_572482_+\|thioesterase-family-protein	unknown	unknown	gnl\|CDD\|379298
NZ_AP022569.1\|WP_163781242.1\|576440_577829_+\|DNA-polymerase-IV	unknown	unknown	gnl\|CDD\|235118
NZ_AP022569.1\|WP_163774979.1\|571201_571576_+\|amino-acid-binding-protein	unknown	unknown	gnl\|CDD\|227090
NZ_AP022569.1\|WP_163774994.1\|594672_595899_-\|fatty-acid-desaturase	unknown	unknown	gnl\|CDD\|239583
NZ_AP022569.1\|WP_163774993.1\|591980_592802_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|225852
NZ_AP022569.1\|WP_163774990.1\|585036_585468_+\|SRPBCC-family-protein	unknown	unknown	gnl\|CDD\|378454
NZ_AP022569.1\|WP_163781247.1\|592852_594670_+\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|223953
NZ_AP022569.1\|WP_163781245.1\|580408_580861_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP022569.1\|WP_163774981.1\|572744_575861_+\|isoleucine--tRNA-ligase	gnl\|CDD\|235681	PRK06039, ileS, isoleucyl-tRNA synthetase; Reviewed.	0
NZ_AP022569.1\|WP_163774991.1\|585524_588416_+\|MMPL-family-transporter	gnl\|CDD\|129913	TIGR00833, Putative_membrane_protein_ActII-3, Transport protein. The Resistance-Nodulation-Cell Division (RND) Superfamily- MmpL sub family (TC 2.A.6.5)Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. This sub-family includes the S. coelicolor ActII3 protein, which may play a role in drug resistance, and the M. tuberculosis MmpL7 protein, which catalyzes export of an outer membrane lipid, phthiocerol dimycocerosate. [Transport and binding proteins, Unknown substrate].	0
NZ_AP022569.1\|WP_163774989.1\|584233_585037_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|223377	COG0300, DltE, Short-chain dehydrogenases of various substrate specificities [General function prediction only].	1.88636e-101
NZ_AP022569.1\|WP_163774987.1\|582643_583051_-\|group-1-truncated-hemoglobin	gnl\|CDD\|381253	cd00454, TrHb1_N, truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 1 (N). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. They are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). Typical of the TrHb1s (N) group is a protein matrix tunnel. It includes a Mycobacterium tuberculosis TrHb1, Mt-trHbN, which is encoded by the glbN gene. Mt-trHbN is expressed during the Mycobacterium stationary phase, and plays a specific defense role against nitrosative stress. The cyanobacterium Synechococcus sp. PCC 7002 TrHb1 GlbN, is constitutively expressed, and likely also protects cells from reactive nitrogen species.	3.88235e-37
NZ_AP022569.1\|WP_163774988.1\|583209_584226_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|235962	PRK07201, PRK07201, SDR family oxidoreductase.	9.24879e-136
NZ_AP022569.1\|WP_163774983.1\|578781_579483_+\|signal-peptidase-II	gnl\|CDD\|237810	PRK14764, PRK14764, lipoprotein signal peptidase; Provisional.	2.11488e-100
NZ_AP022569.1\|WP_163774984.1\|579479_580406_+\|RluA-family-pseudouridine-synthase	gnl\|CDD\|161659	TIGR00005, Ribosomal_large_subunit_pseudouridine_synthase_D, pseudouridine synthase, RluA family. In E. coli, RluD (SfhB) modifies uridine to pseudouridine at 23S RNA U1911, 1915, and 1917, RluC modifies 955, 2504 and 2580, and RluA modifies U746 and tRNA U32. An additional homolog from E. coli outside this family, TruC (SP\|Q46918), modifies uracil-65 in transfer RNAs to pseudouridine. [Protein synthesis, tRNA and rRNA base modification].	1.5638e-114
NZ_AP022569.1\|WP_163774995.1\|596126_596564_+\|nitroreductase-family-deazaflavin-dependent-oxidoreductase	gnl\|CDD\|281995	pfam04075, F420H2_quin_red, F420H(2)-dependent quinone reductase. This family of proteins is found in the genera Mycobacterium and Streptomyces. Member protein Rv3547 has been characterized as a deazaflavin-dependent nitroreductase. Rv1558 is an F420H(2)-dependent quinone reductase involved in oxidative stress protection.	9.94327e-59
NZ_AP022569.1\|WP_163774985.1\|580887_581643_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	2.1218e-12
NZ_AP022569.1\|WP_163774992.1\|588428_591971_+\|DNA-polymerase-III-subunit-alpha	gnl\|CDD\|235554	PRK05673, dnaE, DNA polymerase III subunit alpha; Validated.	0
NZ_AP022569.1\|WP_163774982.1\|577793_578714_-\|asparaginase	gnl\|CDD\|199208	cd08964, L-asparaginase_II, Type II (periplasmic) bacterial L-asparaginase. Asparaginases (amidohydrolases, E.C. 3.5.1.1) are enzymes that catalyze the hydrolysis of asparagine to aspartic acid and ammonia. In bacteria, there are two classes of amidohydrolases. This model represents type II L-asparaginases, which tend to be highly specific for asparagine and localized to the periplasm. They are potent antileukemic agents and have been used in the treatment of acute lymphoblastic leukemia (ALL), but not without severe side effects. Tumor cells appear to have a heightened dependence on exogenous L-aspartate, and depleting their surroundings of L-aspartate may starve cancerous ALL cells. Type II L-asparaginase acts as a tetramer, which is actually a dimer of two tightly bound dimers. A conserved threonine residue is thought to supply the nucleophile hydroxy-group that attacks the amide bond. Many bacterial L-asparaginases have both L-asparagine and L-glutamine hydrolysis activities, to a different degree, and some of them are annotated as asparaginase/glutaminase.	1.80465e-97
NZ_AP022569.1\|WP_163774979.1\|571201_571576_+\|amino-acid-binding-protein	gnl\|CDD\|227090	COG4747, COG4747, ACT domain-containing protein [General function prediction only].	2.57621e-12
NZ_AP022569.1\|WP_163774980.1\|571675_572482_+\|thioesterase-family-protein	gnl\|CDD\|379298	pfam13622, 4HBT_3, Thioesterase-like superfamily. This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.	2.80212e-49
NZ_AP022569.1\|WP_163781242.1\|576440_577829_+\|DNA-polymerase-IV	gnl\|CDD\|235118	PRK03348, PRK03348, DNA polymerase IV; Provisional.	0
NZ_AP022569.1\|WP_163774994.1\|594672_595899_-\|fatty-acid-desaturase	gnl\|CDD\|239583	cd03506, Delta6-FADS-like, The Delta6 Fatty Acid Desaturase (Delta6-FADS)-like CD includes the integral-membrane enzymes: delta-4, delta-5, delta-6, delta-8, delta-8-sphingolipid, and delta-11 desaturases found in vertebrates, higher plants, fungi, and bacteria. These desaturases are required for the synthesis of highly unsaturated fatty acids (HUFAs), which are mainly esterified into phospholipids and contribute to maintaining membrane fluidity. While HUFAs may be required for cold tolerance in bacteria, plants and fish, the primary role of HUFAs in mammals is cell signaling. These enzymes are described as front-end desaturases because they introduce a double bond between the pre-exiting double bond and the carboxyl (front) end of the fatty acid. Various substrates are involved, with both acyl-coenzyme A (CoA) and acyl-lipid desaturases present in this CD. Acyl-lipid desaturases are localized in the membranes of cyanobacterial thylakoid, plant endoplasmic reticulum (ER), and plastid; and acyl-CoA desaturases are present in ER membrane. ER-bound plant acyl-lipid desaturases and acyl-CoA desaturases require cytochrome b5 as an electron donor. Most of the eukaryotic desaturase domains have an adjacent N-terminal cytochrome b5-like domain. This domain family has extensive hydrophobic regions that would be capable of spanning the membrane bilayer at least twice. Comparison of sequences also reveals the existence of three regions of conserved histidine cluster motifs that contain the residues: HXXXH, HXX(X)HH, and Q/HXXHH. These histidine residues are reported to be catalytically essential and proposed to be the ligands for the iron atoms contained within the homolog, stearoyl CoA desaturase.	4.32714e-43
NZ_AP022569.1\|WP_163774993.1\|591980_592802_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|225852	COG3315, COG3315, O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport, and catabolism].	6.58815e-38
NZ_AP022569.1\|WP_163774990.1\|585036_585468_+\|SRPBCC-family-protein	gnl\|CDD\|378454	pfam10604, Polyketide_cyc2, Polyketide cyclase / dehydrase and lipid transport. This family contains polyketide cylcases/dehydrases which are enzymes involved in polyketide synthesis. It also includes other proteins of the START superfamily.	3.65217e-14
NZ_AP022569.1\|WP_163781247.1\|592852_594670_+\|AMP-binding-protein	gnl\|CDD\|223953	COG1022, FAA1, Long-chain acyl-CoA synthetases (AMP-forming) [Lipid metabolism].	0

>NZ_AP022569.1|WP_163774985.1|580887_581643_-|methyltransferase-domain-containing-protein
MTRAFDDLVSEASAVPIDGWDFSWLDGRASEERPSWGYQRQMSARLATASAALDLDTGGGEVLAGARIFPPTMVALETWPPNAALATKLLHPRGVVVVAARDEPRLPFADEAFDLVTSRHPITVRWNEIARVLRPGGSYFAQQIGPATMAELVEYFIGPQPQKWAELHPDAQRAGAQAAGLQVVDMRLERQRAEFFDVGAVIYFLRKVVWTVPDFSVDRYREPLRRLHERIESDGPFVAHATRLLVEARKP
>NZ_AP022569.1|WP_163781245.1|580408_580861_-|hypothetical-protein
MRMSMAGMGLMGVVAGASTAGILGVVRLVGDTWLPRLAASSEQKHQMISQLHSQRHDSVQRWRAGLANARDSYRRWADGPRDADAPNVVGDEWFEGLRPHLPAAGAAAEFRTAHEVHCDNATVAMLSLEIGRIEREWVDEAKSFPRRVRS
>NZ_AP022569.1|WP_163774984.1|579479_580406_+|RluA-family-pseudouridine-synthase
MTDRSMPVPEGLAGMRVDAGLARLLGLSRTAAAALAEDGGVELDGVQAGKSDRLTPGAWLQVRLPEPPAPVENTPVDIEGMTILYSDDDIVAVDKPAGVAAHASVGWTGPTVLGGLAAAGYRITTSGVHERQGIVHRLDVGTSGVMVVAISERAYTLLKRAFKQRTVDKRYHALVQGHPDPSSGTIDAPIGRHRGHDWKFAVTSDGRHSRTHYDTIEAFVAASLLDVHLETGRTHQIRVHFAALHHPCCGDLTYGANPKLAKKLGLERQWLHARSLSFTHPGDGRQMEIVSPYPQDLQHALDVLRAEG
>NZ_AP022569.1|WP_163774983.1|578781_579483_+|signal-peptidase-II
MTDQPTGPAEPVTEADTAEDAQAPAPRRRQPLLLSVAAVVLALDIVTKVLAVRLLTPGQPVPIIGDTITWTLVRNSGAAFSMATGYTWMLTVIASAVVVGIFWMGRRLVSPWWAVGLGMILGGAMGNLVDRFFRSPGPLRGHVVDFLSIGWWPVFNVADPSVVGGAILLVTLSALGYDFDTVGRRRPGDDGSGDDAERSDAADDEAEERRRWSAGEATDAADASDGDTADRSL
>NZ_AP022569.1|WP_163774982.1|577793_578714_-|asparaginase
MSRVTVIATGGTIASSAQADGVARPTRGGAQLAAGLDVDVVDVMAKDSSELTPADWDVIGTAARAAADGGAQGVVVLHGTDTLEETALWLDLTYAGDIPLVMTGAMRSADDPDADGPANLRDAVTVASDPAARNLGVLVSFAGRILQPWGLHKVATGHAFESRLLGSVDTAVTFAQDKARPYLGELSAAGAPRVDIVAAYPGGDAVAMDACVAAGAHGIVLAALGSGNAGAAMIDGVRRHCRAGVDVAVSTRVVGGRVSPGYGPGRDLVDAGAVMVSGLPPSQARVLLMAAQAAGLPLRDVVARLF
>NZ_AP022569.1|WP_163781242.1|576440_577829_+|DNA-polymerase-IV
MLHLDMDAFFASVEQLTRPTLRGRPVLVGGLGGRGVVAGASYESRVFGARSAMPMHQARRLIGVTAVVLPPRGVVYGVASRRVFDTVRAMVPVVEQLSFDEAFGEPPELVGASATDVEQFCAELRRRVLDETGLVASVGAGSGKQIAKIGSGLAKPDGIQVIRRDDEKRLLDGLAVRKLWGIGPVAEEKLHRLGIDTIGQLAALSEAEVANILGATIGPALHRLARGIDDRPVAERAEAKQISAESTFAADLTTLEELREAIAPIAEHAHQRLCRDGRGARTVTVKLKKSDMSTLTRSATLPYATTDAAALAALARRLLLDPHQIGPIRLLGVGFSGLSGVRQESLFPDLELAMSDADLGTDTAHPGPDAAVPRALDAEDWRVGDDVIHRDLGHGWVQGAGHGVLTVRFETRGSGPGPARTFPSGTDDITRANPVDSLDWPEYVAGIAETTSEQAGDDVAQR
>NZ_AP022569.1|WP_163781241.1|575873_576386_-|hypothetical-protein
MRTPASPEHQGRRAQQWWARVRDEWRARLEPGEQATVLAWAAFTVTFAGLRALTHWIRAGHGPSGGGMSVGGRHFHHYNLGIALLAGVGAMGLRGTERQRRHPAAAIAFGSANAMIVDELALLLDLKDVYWANDGRKSVDAAVGLIAVGGTIVAGLPFWPHARRALQSVR
>NZ_AP022569.1|WP_163774981.1|572744_575861_+|isoleucine--tRNA-ligase
MTENTYPKPAGGAPDLPALELEVLDYWAADDTFRASVAGRAEAPEYVFYDGPPFANGLPHYGHLLTGYVKDIVPRYRTMRGYKVERRFGWDTHGLPAELEVERQLGITDKSQIDAMGIAAFNDACRESVLRYTDEWRAYVTRQARWVDFDNDYKTLDLPYMESVIWAFKQLWDKGLAYEGYRVLPYCWRDETPLSNHELRMDDDVYQSRQDPALTVGFAVTEGDLAGAHLLVWTTTPWTLPSNQAVAVNPDVNYVQVRAGEHRVVLAEPRLAAYAREFNDEPEVLGTYRGSDLVGIRYRPPFPYFMDSLNAFQVLAADFVTTDDGTGIVHLAPAYGEDDKATADEVGIVPVTPVDARGRFDATVPDYQGQQVFDANPQIIRDLKNRTGPAAANGAVLIRQETYDHPYPHCWRCRNPLIYRAVSSWFIKVSDFRDRMVELNQQITWYPEHVKDGQFGKWLQGARDWSISRNRYWGTPIPVWVSDDPAYPRIDVYGSLDELERDFGTRPDNLHRPYIDELTRPNPDDPTGQSTMRRIPDVFDVWFDSGSMPYAQVHYPFENRDWFDTHYPGDFIVEYIGQTRGWFYTLHVLATALFDRPAFKTCVAHGIVLGSDGQKMSKSLRNYPDVSEVFDRDGSDAMRWFLMASPILRGGNLIVTEQGIRDGVRQVLLPFWNAYSFLALYAPKVGTWRADSRHVLDRYILAKLAVLRDDLTAQLDACDISGACEQLRQFTEALTNWYVRRSRSRFWEEEADAIDTLHTVLEVTARLAAPLLPITTEIIWRGITAERSVHLSDWPAAGLLPADAELVAAMDQVREVCSVASSLRKAKKLRVRLPLPKLTVAVDNPGALEPFTDLIADELNVKAVELTDDIDRYGRFELTVNARVAGPRLGKDVQAAIKAVKSGAGVVNPDGTLTAGPAVLQPEEYSSRLVAADPEYTAPLPDGAGLVVLDATVTPELEAEGWAKDRIRELQELRKTAGLEVSDRISVVMLVPAARADWAATHRELIAGEILATSFVFGEPEQGAAEIGDGVRVAIVKA
>NZ_AP022569.1|WP_163774980.1|571675_572482_+|thioesterase-family-protein
MPGPHALDRALELEVVDADVVRGRTRPEWANMVGPFGGITAAVLLRAIESHPDRLGEPVALTVNFAAPIVDGEFEISRRAPRTNRTNQHWIAELSQDGDVKTTATAVFGIRRDTWSDTQATSPEAPPPEQVARSDHENLPTWVRLYDMRFAEGSFSGGHVDVGPSSTTTLWVRDAAGRPVDFPAIAAVSDIFFPRVFLRRGMVPSGTISLTTYFHVGQPHLDALGADYILGTAHANRFDRGFFDQSAQLWSRDGALVATTYQIVYFKG
>NZ_AP022569.1|WP_163774979.1|571201_571576_+|amino-acid-binding-protein
MATDLTLYLDDEPGELALVGDALGKAGVNIAGLCAVTSGGGQAEVHILVHDATSAFEALQSAGIKVAEEQEVIVLDVKDQPGALGEIVHKLGAAKINLETAYLATNTRLVLRADDLAEAKAALA
>NZ_AP022569.1|WP_163774987.1|582643_583051_-|group-1-truncated-hemoglobin
MGILARFRKPGTATLYDTIGGRDALEVVVEDFYCRVLDDDLLAGFYAGADMKRVKAKQVEFLSSLLGGSVSYSGLSMRQAHEGRGITMHHFAMVAAHLADSLCAAGLHPDTITEILRAVAPLAGDIASDDIKAVV
>NZ_AP022569.1|WP_163774988.1|583209_584226_+|SDR-family-NAD(P)-dependent-oxidoreductase
MNLGDLTGLVEKPFAAVSNLVNTPNSAGRYRPFYLRNLLDAVQGRTLRESVDDTITLITGGSSGIGEAAAKKIAAAGGEVVLVARTQENLDKVADDIRSDGGIAHVYPCDLSDMDAIAAMADKVLADLGGVDVLINNAGRSIRRSLALSYDRIHDYQRTMQLNYLGAVQLILKFIPGMRERGFGQIINVSSVGVQTRAPRFGAYIASKAALDSLCDALQAEVVDDDVKFTTVHMALVRTPMISPTKMYDKFPALTPDQAAGVITDAIVQRPRRASSPFGQFAALADAVNPAVMDRVRNRAFSMFDDSSAAKGDESDSGATNFDNRSETFVRATRGIHW
>NZ_AP022569.1|WP_163774989.1|584233_585037_+|SDR-family-NAD(P)-dependent-oxidoreductase
MSLPKPNNQAAVVITGASSGIGTELARGLARRGYPLVLVARRKERMDELADELRGQYSVGVDVQPLDLSDSAAREKLAHRLRTEPVAGLCNSAGFGTSGIFQELPIERESEEVVLNSLTLMELTHAALPGMVERGAGAVLNIASIAGFQPMPYMAVYSATKAFVQTFSEAVHEELSGTGVSVTVLCPGPVPTEWGEIANAERFSIPIAQVSPHDVAEAAIAGMVDGKRSVVPGIVPKAVSIGGRYMPRTLLLPGLRLGNRLRGGPSH
>NZ_AP022569.1|WP_163774990.1|585036_585468_+|SRPBCC-family-protein
MAAVDVKADVPMSPQDMWDRVSDLSELGDWLSMHEGWRSELPDELSEGIEVVGVARAKGFRNRVTWTVTTWQPPQRVALSGSGKGGAKYTVTLTVSPTKRGSNLGLRLELGGRALFGPVGAAAARAVKGDAEKSLKKFVELYG
>NZ_AP022569.1|WP_163774991.1|585524_588416_+|MMPL-family-transporter
MLRGAEEATATGSRGVFGWIGVVVVRWPWAVIGAWIALAVVLSMIFPSLTEMAERRPVAILPPEAPVLQTTRQISEAFHQSGSENENVLLVVLTDENGLDPSDLSTYRTLADNLRPDTRDIVMLQDFVATPALRDAMTSKDHKAWYLPMVLSGWVGTPELHAAYGRVADIVKKSVAGSTLTAHLTGPAATGDDMMFIGIKDMHAIEGAVVLMVLIILFVIYRNLVTMMLPLVTIGVSVGVAQSVVAGVAELGLGVSSQTITLMTTMMAGAGVDYAVFLISRYHDSLRQGMPSDQAVVRALTSIGKVIAGSAATVSITFMGMVFTHLGSFRNVGPCLAISIALAFLAAVTFLPALMVLVGRRNWIKPRRDVATRFWRRLGIHIVRRPISHLVGSLVVLAILAGCAFLAHFNYDDSKTLPQSVESAVGYRTLGRHFPLNATIPEYLVVQSEQDLRKPANLSALNQLEQRVRQMPAVAAIHGAPVPKPKSSDKSDSEVNDSWTDSALDGGKKDKSNDDGAGSFPNVTNLLYSVGATGNAAADLGLPAIPGMAQVDVGDDTTNFVNTVRGIGFAMSVDIAEIANTVNGAPVTVLDVVAVTDRDGGALKKLSDFAGQLESLPDADNIESAARNVRQILDNVITDLRTLGNDGAHENERPTPPPPDPHNYADAIKQMIDQVKDLMKQTAHTGGGLTSALTSFISPDGHTARYLVQTNLYPFGTGAMDQIRQITDTARGTHPEPALTGASISVSGITAMLRDTRAYYFEDISLIVVMTILIVFVILVMILRAIVAPLYLIASVVISYLSAFGIGVVVFQFLLHEELTWSIPGLTFIVLVAMGADYNLLLISRLREESPHGIRSGVIRTVRSTGGVITAAGVIFAASMFGMLLASISTLVQAGFIIGVGLLLDTFLVRTITVPAIAVLCGKANWWPSRPLPPPPPQRPEPIPVPESETHSATRREHVGVQP
>NZ_AP022569.1|WP_163774992.1|588428_591971_+|DNA-polymerase-III-subunit-alpha
MSQSFVHLHNHTEYSMLDGAAKVAPMLAEAQRLEMPAIGMTDHGNMFGASEFYNGATAAGIKPIIGIEAYIAPGSRFETRRVLWGDPGQKSDDVSGSGSYTHMTMVAENATGLRNLFKLSSLASFEGQLGKWPRMDAELIAEHAAGIIATTGCPSGEVQTRLRLGHHREALEAAAKWREIFGPENFFLELMDHGLSIERRVRDGLLEIGRTLNIPPLATNDCHYVTRDAAHNHEALLCVQTGKTLSDPNRFKFDGDGYFLKSAAEMRAIWDGDVPGACDSTLLIAERVTSYADVWAPCDRMPVFPVPDGHDPSSWLRHEVDAGLRRRFGDAQPDGYAQRAAYEIEVICDKGFPSYFLIVADLINYARSVDIRVGPGRGSAAGSLVAYALGITDIDPIQHGLLFERFLNPERASMPDIDIDFDDRRRGEMVRYAADKWGHDRVAQVITFGTIKTKAALKDSARIHYGQPGFAIADRITKALPPPIMAKDIPLSGITDPNHERFKEAAEVRSLIDTDPDVRTIYQTARGLEGLIRNAGVHACAVIMSSEPLTEVIPLWKRPQDGAIITGWDYPSCESIGLLKMDFLGLRNLTIIGDAIGNIKANRGIDLDLESLALDDPATFELLGRGETLGVFQLDGGPMRDLLRRMQPTGFEDIVAVLALYRPGPMGMNAHNDYADRKNNRQAIKPIHPELEEPLREILAETYGLIVYQEQIMRIAQKVAGYSLARADILRKAMGKKKREVLEKEFEGFSEGMQANGFSAKAIKALWDTILPFADYAFNKSHAAGYGLVSYWTAYLKANYPAEYMAGLLTSVGDDKDKAAVYLADCRKLGITVLPPDVNESGLNFASVGADIRYGLGAVRNVGSNVVASLINTRTAKGKFTDFSDYLNKVDIAACNKKVTESLIKAGAFDSLKHPRKGLFLVHTDAVESVLGTKKAEAMGQFDLFGGDPNDGGVGADSVFTIRVPDDEWDDKHKLALEREMLGLYVSGHPLNGIAHLLTSQVDTAIPAILDGDVANETMVKVGGILASVNRRVNKNGMPWASAQLEDLTGGIEVMFFPHTYSAVGGEIVDDAVVLVTAKVAIRDDRIALIANDLVVPDFSNAQLNRPLAVSLPTRQCTIDKVSALKQVLARHPGTSQVHLRLISGERTTTLELDASLRVTPSPALMGDLKALLGPGCLGG
>NZ_AP022569.1|WP_163774993.1|591980_592802_-|class-I-SAM-dependent-methyltransferase
MGNAISRLTPVELTAFVTQYARALDSRWPTPILGDTLADDIVSKIAYDFDAMGVPSSAVRQTALRAKMLDDRVRRFVAEHPDAVVVDLGAGLGTAMMRVAPPPTVDWYSVDLPNVIALRDELVPEGEQAHSVAASLTDDSWTDQIPSDRPTVLIADGLLAFLPESVVVTLFRRIPEYFSSGEIAMNDYGRVGRLNIAAMKIVFSAVGTQWAYRGFSDPHVPESWSPRLRLVEETSLSHAPEIDLYPVAARVSTRLMGMTKSGARTARILRYRF
>NZ_AP022569.1|WP_163781247.1|592852_594670_+|AMP-binding-protein
MSMPTTMCEAFQRSAAVKPDAVALRTPGDTQTMTWREFAAGVRRVAAGLAGIGVRHGDTVSLMMANRIEFYPLEVGAQHLGATSFSVYNTLPAEQLTYVFGNAGTKVVICEEQYVDRIRASGAPIEHIVCIDGAPDGTMSLDELYAAAAEDFDFDATWRAVRPDDVITLIYTSGTTGNPKGVEMTHTNLLFEAAALGAVLDVRPDDRTTSYLPSAHIADRMMALYNQQLYGTQVTVVSDVREIAAALPDARPTVWAAVPRVWEKLKAAIEFAVAHEQDDVKRQALQWAMSVAGKRAAAMLADRPLPDDVAAEWAQADELVLSKLRERLGLDQLRWAVSGAAPIPRETLAFFAAIGIPIAEVWGMSELSCVASVSHPREARLGTVGKLLPGLESMIADDGEYLVRGPLVMKGYRKEPAKTAEAIDADGWLHTGDILDEDADGFLRIIDRKKELIINAAGKNMSPANIENTVKAACPMVGAMVAIGDGRPFNTALLVFDADSVGPYAERHGLADASPEALAAHPEVLAQISAGVAEGNSKLSRVEQIKRFRVLPNLWEPGGDEITLTMKLKRKPIMAKYAAEIEELYDSEPGPEIHQPKGASATQPA
>NZ_AP022569.1|WP_163774994.1|594672_595899_-|fatty-acid-desaturase
MAIAEVPEYAHLSDADVAALAAELDTIRCDIETSRGTRDRRYIRRAIALQRGLEVAARLIILASKTKGGWAVGTVALAAAKCIENMELAHNISHGQWDWMNDPEIHSATWEWDMVGPSSHWMSSHNHRHHMFTNVIGVDDDLGFGVLRVTPEQEWRPGNLFQPLRAVLLAAAFEWGVAFHDLYSMQERETTQAAKSAHKKTMFRKMIRQSVKDYVIFPALGRRRWRRALGATVVANGLRNAWAYIVIVCGHFADGAEKFTASVLDDETKPQWYLRQMLGTANFRAGPVLAFMSGNLCYQIEHHLFPDLPSNRLPEIAGRVQALCDKYDLPYTTGSFIRQYLLTVRTICKLALPVGVLAATADDAPETASENKFRNRARQSDLAVAGDGVRHSGLATAVSAHRTRRKAS
>NZ_AP022569.1|WP_163774995.1|596126_596564_+|nitroreductase-family-deazaflavin-dependent-oxidoreductase
MPLEGEYAPSPWDWSREQADKYAESGGTDAADMKGKPIILLTTVGAKTGKLRKTPLMRVEHDGEYAVVASLGGAPKNPVWYYNIAKNPRVELQDGSVTQDYDAREVFGDEKAVWWERAVEAWPDYADYQQKTDRQIPVFVLTPVQ

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Crispr_ID: NZ_AP022569_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP022569_2

2690717-2690793

Orphan

Consensus_repeat	Method
TGAGTACCGCCGACGACGATGCAGAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP022569_2

>merge|NZ_AP022569|2|2690717-2690793|CRISPRCasFinder
TGAGTACCGCCGACGACGATGCAGAGCGAAGCGATGCTGAGGAGCGGCGCCTGAGTACCGCCGACGACGATGCAGAG

>NZ_AP022569|2|2|2690717-2690793|CRISPRCasFinder
TGAGTACCGCCGACGACGATGCAGAG	CGAAGCGATGCTGAGGAGCGGCGCC
TGAGTACCGCCGACGACGATGCAGAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP022569.1\|WP_163776638.1\|2689454_2690288_+\|sulfurtransferase	unknown	unknown	gnl\|CDD\|225450
NZ_AP022569.1\|WP_163776646.1\|2700284_2700680_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380033
NZ_AP022569.1\|WP_163776642.1\|2694048_2695128_-\|phosphoribosylformylglycinamidine-cyclo-ligase	unknown	unknown	gnl\|CDD\|235439
NZ_AP022569.1\|WP_163776630.1\|2682470_2683403_-\|phosphate-ABC-transporter-permease-PstA	unknown	unknown	gnl\|CDD\|273373
NZ_AP022569.1\|WP_163776643.1\|2695193_2696747_-\|amidophosphoribosyltransferase	unknown	unknown	gnl\|CDD\|236113
NZ_AP022569.1\|WP_163776636.1\|2688330_2688747_+\|thioredoxin-family-protein	unknown	unknown	gnl\|CDD\|239245
NZ_AP022569.1\|WP_163776640.1\|2692615_2693710_+\|folate-binding-protein-YgfZ	unknown	unknown	gnl\|CDD\|223431
NZ_AP022569.1\|WP_163776641.1\|2693844_2694012_+\|DUF3073-family-protein	unknown	unknown	gnl\|CDD\|378620
NZ_AP022569.1\|WP_163776644.1\|2696928_2698497_-\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224154
NZ_AP022569.1\|WP_163776645.1\|2698580_2699180_+\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|188483
NZ_AP022569.1\|WP_163776647.1\|2700676_2702950_-\|phosphoribosylformylglycinamidine-synthase-subunit-PurL	unknown	unknown	gnl\|CDD\|234921
NZ_AP022569.1\|WP_163776634.1\|2686520_2687282_-\|winged-helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|223816
NZ_AP022569.1\|WP_163781737.1\|2691703_2692567_-\|aminodeoxychorismate-lyase	unknown	unknown	gnl\|CDD\|236114
NZ_AP022569.1\|WP_163776635.1\|2687415_2688222_+\|mannan-chain-length-control-protein-LmeA	unknown	unknown	gnl\|CDD\|378597
NZ_AP022569.1\|WP_163776639.1\|2690289_2690592_+\|DUF1416-domain-containing-protein	unknown	unknown	gnl\|CDD\|377793
NZ_AP022569.1\|WP_163776633.1\|2685633_2686524_-\|mycothiol-synthase	unknown	unknown	gnl\|CDD\|132489
NZ_AP022569.1\|WP_163776631.1\|2683399_2684434_-\|phosphate-ABC-transporter-permease-subunit-PstC	unknown	unknown	gnl\|CDD\|273992
NZ_AP022569.1\|WP_163776632.1\|2684430_2685543_-\|phosphate-ABC-transporter-substrate-binding-protein-PstS	unknown	unknown	gnl\|CDD\|273374
NZ_AP022569.1\|WP_163776637.1\|2688969_2689431_+\|DUF4395-family-protein	unknown	unknown	gnl\|CDD\|379566
NZ_AP022569.1\|WP_163776648.1\|2702986_2703796_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|375319

Protein	Function_ID	Function_description	E-value
NZ_AP022569.1\|WP_163776638.1\|2689454_2690288_+\|sulfurtransferase	gnl\|CDD\|225450	COG2897, SseA, Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism].	5.78271e-109
NZ_AP022569.1\|WP_163776646.1\|2700284_2700680_-\|hypothetical-protein	gnl\|CDD\|380033	pfam17844, SCP_3, Bacterial SCP ortholog. This domain is found in MSMEG_5817 gene product from M. smegmatis. It has been shown to be vital for mycobacterial survival within host macrophages. Crystal structure revealed a Rossmann-like fold alpha/beta two-layer sandwich forming a highly hydrophobic interface cavity and with high structural homology to the SCP family. Hence, it has been suggested that this domain may be involved in the interaction of apolar ligands through its hydrophobic cavity. Alanine-scanning mutagenesis of the hydrophobic cavity of MSMEG_5817 protein demonstrated that the conserved Val82 residue plays an important role in ligand binding.	3.33679e-46
NZ_AP022569.1\|WP_163776642.1\|2694048_2695128_-\|phosphoribosylformylglycinamidine-cyclo-ligase	gnl\|CDD\|235439	PRK05385, PRK05385, phosphoribosylaminoimidazole synthetase; Provisional.	2.98124e-179
NZ_AP022569.1\|WP_163776630.1\|2682470_2683403_-\|phosphate-ABC-transporter-permease-PstA	gnl\|CDD\|273373	TIGR00974, 3a0107s02c, phosphate ABC transporter, permease protein PstA. This model describes PtsA, one of a pair of permease proteins in the ABC (high affinity) phosphate transporter. In a number of species, this permease is fused with the PtsC protein (TIGR02138). In the model bacterium Escherichia coli, this transport system is induced when the concentration of extrallular inorganic phosphate is low. A constitutive, lower affinity transporter operates otherwise. [Transport and binding proteins, Anions].	1.83829e-83
NZ_AP022569.1\|WP_163776643.1\|2695193_2696747_-\|amidophosphoribosyltransferase	gnl\|CDD\|236113	PRK07847, PRK07847, amidophosphoribosyltransferase; Provisional.	0
NZ_AP022569.1\|WP_163776636.1\|2688330_2688747_+\|thioredoxin-family-protein	gnl\|CDD\|239245	cd02947, TRX_family, TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.	3.08768e-24
NZ_AP022569.1\|WP_163776640.1\|2692615_2693710_+\|folate-binding-protein-YgfZ	gnl\|CDD\|223431	COG0354, COG0354, Predicted aminomethyltransferase related to GcvT [General function prediction only].	8.68077e-82
NZ_AP022569.1\|WP_163776641.1\|2693844_2694012_+\|DUF3073-family-protein	gnl\|CDD\|378620	pfam11273, DUF3073, Protein of unknown function (DUF3073). This family of proteins with unknown function appears to be restricted to Actinobacteria.	6.22213e-18
NZ_AP022569.1\|WP_163776644.1\|2696928_2698497_-\|FAD-dependent-oxidoreductase	gnl\|CDD\|224154	COG1233, COG1233, Phytoene dehydrogenase and related proteins [Secondary metabolites biosynthesis, transport, and catabolism].	3.68594e-73
NZ_AP022569.1\|WP_163776645.1\|2698580_2699180_+\|TetR-family-transcriptional-regulator	gnl\|CDD\|188483	TIGR03968, transcriptional_regulator_TetR_family, mycofactocin system transcriptional regulator. Members of this family are TetR family putative transcriptional regulators that occur in genome contexts near proteins of the mycofactocin system. These include the precursor peptide (TIGR03969), a radical SAM peptide maturase (TIGR03962), and a putative carrier protein (TIGR03967). [Regulatory functions, DNA interactions].	1.27404e-23
NZ_AP022569.1\|WP_163776647.1\|2700676_2702950_-\|phosphoribosylformylglycinamidine-synthase-subunit-PurL	gnl\|CDD\|234921	PRK01213, PRK01213, phosphoribosylformylglycinamidine synthase subunit PurL.	0
NZ_AP022569.1\|WP_163776634.1\|2686520_2687282_-\|winged-helix-turn-helix-domain-containing-protein	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].	1.15088e-45
NZ_AP022569.1\|WP_163781737.1\|2691703_2692567_-\|aminodeoxychorismate-lyase	gnl\|CDD\|236114	PRK07849, PRK07849, aminodeoxychorismate lyase.	2.5608e-146
NZ_AP022569.1\|WP_163776635.1\|2687415_2688222_+\|mannan-chain-length-control-protein-LmeA	gnl\|CDD\|378597	pfam11209, DUF2993, Protein of unknown function (DUF2993). This family of proteins with unknown function appears to be restricted to Cyanobacteria.	1.75536e-14
NZ_AP022569.1\|WP_163776639.1\|2690289_2690592_+\|DUF1416-domain-containing-protein	gnl\|CDD\|377793	pfam07210, DUF1416, Protein of unknown function (DUF1416). This family consists of several hypothetical bacterial proteins of around 100 residues in length. Members of this family appear to be Actinomycete specific. The function of this family is unknown.	8.86938e-49
NZ_AP022569.1\|WP_163776633.1\|2685633_2686524_-\|mycothiol-synthase	gnl\|CDD\|132489	TIGR03448, mycothiol_MshD, mycothiol synthase. Members of this family are MshD, the acetyltransferase that catalyzes the final step of mycothiol biosynthesis in various members of the Actinomyctes, Mycothiol replaces glutathione in these species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs].	3.21379e-132
NZ_AP022569.1\|WP_163776631.1\|2683399_2684434_-\|phosphate-ABC-transporter-permease-subunit-PstC	gnl\|CDD\|273992	TIGR02138, phosphate_transport_system_permease_protein_PstC, phosphate ABC transporter, permease protein PstC. The typical operon for the high affinity inorganic phosphate ABC transporter encodes an ATP-binding protein, a phosphate-binding protein, and two permease proteins. This family consists of one of the two permease proteins, PstC, which is homologous to PstA (TIGR00974). In the model bacterium Escherichia coli, this transport system is induced when the concentration of extrallular inorganic phosphate is low. A constitutive, lower affinity transporter operates otherwise. [Transport and binding proteins, Anions].	2.70631e-81
NZ_AP022569.1\|WP_163776632.1\|2684430_2685543_-\|phosphate-ABC-transporter-substrate-binding-protein-PstS	gnl\|CDD\|273374	TIGR00975, precursor_PBP-3_PstS-3_Antigen_Ag88., phosphate ABC transporter, phosphate-binding protein. This family represents one type of (periplasmic, in Gram-negative bacteria) phosphate-binding protein found in phosphate ABC (ATP-binding cassette) transporters. This protein is accompanied, generally in the same operon, by an ATP binding protein and (usually) two permease proteins. [Transport and binding proteins, Anions].	1.61318e-88
NZ_AP022569.1\|WP_163776637.1\|2688969_2689431_+\|DUF4395-family-protein	gnl\|CDD\|379566	pfam14340, DUF4395, Domain of unknown function (DUF4395). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 142 and 168 amino acids in length. There are two completely conserved C residues that may be functionally important.	7.15061e-36
NZ_AP022569.1\|WP_163776648.1\|2702986_2703796_-\|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.	2.92348e-29

>NZ_AP022569.1|WP_163776639.1|2690289_2690592_+|DUF1416-domain-containing-protein
MCSAPKQGQTLPASVDLEKETVITGRVVDGSGQTVGGSFVRLLDSSGEFTAEVVASATGDFRFFAAPGSWTLRALSAAGNGDAIVEPKGAGIHEVDVKIA
>NZ_AP022569.1|WP_163776638.1|2689454_2690288_+|sulfurtransferase
MARSDVLVSADWAQSNLDADHVVFVEVDEDASAYDDGHIAGAVKLDWRTDLQDPVRRDFVDAQQFSKLLSDRGIANDDTVILYGGNNNWFAAYAYWYFKLYGHEDVKLLDGGRKKWQLDGRAFSTDKVERPATSYTAKPADNSIRAFRDEVLAAIHEKNLVDVRSPDEFSGKILAPAHLPQEQSQRPGHIPGAINVPWSKTANDDGTFKSDDELAKLYADAGLDGKKETIAYCRIGERSSHTWFVLQELLGHHNVKNYDGSWTEYGSLVGAPIELGS
>NZ_AP022569.1|WP_163776637.1|2688969_2689431_+|DUF4395-family-protein
MSNINTADQVDVRGPRFAAWVTTLVLVAGLLVSGVSTVAAAIILGVQAVIFAIGATAGPRRHPYGLIFAKLVAPRVAPVREREPVAPLKFAQLVGLIFAVVAVAGFASSASLLGVIATGAALVAAFLNAAFGICLGCQLYPLVVRLKPAASTS
>NZ_AP022569.1|WP_163776636.1|2688330_2688747_+|thioredoxin-family-protein
MTAAIVGLVAALVLAAVIGWLLNRRSGDLRATDPGTAEKVDTSDLGLSRDGPTVVHFSATWCSPCKQVRRVVDQVCDDLGDVAHLEIDMDDNPGAAKRLSVLSLPTTFIFDADGRQRYRTAGVPKADDLRSTLAPLLA
>NZ_AP022569.1|WP_163776635.1|2687415_2688222_+|mannan-chain-length-control-protein-LmeA
MRMRKVLLAAAAVLLTAVIVLVAAAGVDFGTSIYAEYRFARSVRQSARLGFDPFVAIIAFPLIPQAMRDHYRQLEIKASAVDRPVIGKATLEATMHSVDLTDASWLIGPNAKFKVGKLESRIIIDSRHLGLYLGIRDLIVEAPPQVTNSSTGGTTESGISGSHGLVFTGTPRAAHFDKRVSVAVDLSMADKTTLVFTPTGVMTGPNTANEPVPDDKRDAVLATFAGRLPDQRLPFDVAPTHEGARGSDVIIEGITTGLTITLDGFNQA
>NZ_AP022569.1|WP_163776634.1|2686520_2687282_-|winged-helix-turn-helix-domain-containing-protein
MDLLLLTSEPHPDVVLPSLSLLAHTVRTAAPDVSSLLEAGSADILIVDARLDLPAARGLCRLLGSTGRSIPAVVVVNEGGLVAVNADWGLDEILLPSTGPAEIDARLRLLVGRRGNLQDQEGVGKVSLGELVIDESTYTARLRGRPLDLTYKEFELLKYLAQHAGRVFTRAQLLHEVWGYDFFGGTRTVDVHVRRLRAKLGPEYEALIGTVRNVGYKAVRPTRRLPSGEADGHDSEAEIDNYRDPLPDPLHSQ
>NZ_AP022569.1|WP_163776633.1|2685633_2686524_-|mycothiol-synthase
MTSPQWRAGLAAEDQQRIREIITAASDVDKVAPVGEQVLRELAQQRTGHLVAVSGGRVVGYLNLATGPGSGMAELVVHPDARRQGIGAAMIRAALAKTDGKNQFWAHGTLESAQATASALGLEPVRELVQMRRSLHGVTEPMVPDGVRIRTYAGTADDAELLRVNNAAFATHPEQGGWSAADLDERRAESWFDPEGLFLAFDPHTDALLGFHWTKVHSDQAGLGEVYVVGVDPAAQGSGLGGLLTAVGIAHLARQLGGSAEPTVMLYVDADNTAALKTYRRLGFNQFSVDTAYAAR
>NZ_AP022569.1|WP_163776632.1|2684430_2685543_-|phosphate-ABC-transporter-substrate-binding-protein-PstS
MRRDGLGAALAKALTTGVVGCVVLAGCGSDKNLSGVSPAPTGPVDCGGKSDLTAEGSTAQQNAIALFNKEWAELCPGKNIAYNPTGSGAGREQFIARHVDFAGSESPLSREQIEPATQRCNGNPAWHLPMVFGPVALAYHVDGVTSLVLNSDVLAKIFSGVITDWSDPAIAALNAGVALPDSKITPIYRSDSSGTTDNFQKYLAAAAPNSWTKGAGSEFQGGVGEGAQKSAGIVQAVKSTPGAIGYVEKGFADQSGLPYARIDSGRGGVALTDDAARKAIDGATFAGDGDDLKLDLKSIYSTTVAGAYPLVLATYEIVCSDGYDASTSAAVKSFFTIAADNGQGGLSAAGYVPLPDKFKQRLLAAIRAIQ
>NZ_AP022569.1|WP_163776631.1|2683399_2684434_-|phosphate-ABC-transporter-permease-subunit-PstC
MTTPDPNTAGSGEVIAAPFRQPRVTPTLPWGTTAPHRGERLYRRVSAGSGVLIVVLVSAIGLFLLWRAIPALARDKENFFTYGGNWVTTNTSAMHFGIFDLVQVTVCVALFALVLAMPIALGIAIFLTQYSPRRMAGPLAYMVDLLAAVPSIIYGVWGLYVLAPQLRPVATWLNEHLGGVFLFATGNASVAGGGTVFTAGIVLAVMILPIITAVTREVFIQTPQNQVEAALALGATRWEVVKTTVLPFGRSGYISGAMLGLGRALGETVALLIILRGTQAAFGWSLFDGGYTFATKIAATASEFNNQYKAGAYIAAGLVLFLLTFVVNALARAGTRGRAGGDAR
>NZ_AP022569.1|WP_163776630.1|2682470_2683403_-|phosphate-ABC-transporter-permease-PstA
MTSILDRPLKARRFTGVSLRRRAANVVATVLVTSSVALALVPLIWVLYSVVTKGFRTVKSTVWWSHSQADMTAFLAGGGAYHAIVGTVLQGLVCAAISIPIGLFVAIYLVEYGGDSTLAKLTTFTVDILTGVPSIVAALFIYALFIATLGFPRSGFAVSLSLVLLMLPVIVRATEEMLRIVPLDLREASYALGVPKWKTITKIVLPAGLSGIITGVFLALARVMGETAPLLLLVGYSQVMNFDMSSGFMGSLPGMMYDQTAAGAGSNPIPTDRLWGAALTLIVLIAVINLGARVGSRVFAPEKLGRSSHG
>NZ_AP022569.1|WP_163781737.1|2691703_2692567_-|aminodeoxychorismate-lyase
MIVTLDGKVHPVDAPLLFADDLAAVRGDGVFETLLVRDGAACLVDAHLGRLAHSAKLLDLPEPDLTAWRHAIDVAARQWTRDTDDEAAMRLVYSRGRESGSAPTAYVTVNPVAERIAAVRRDGLAAITLPRELPSAGVEAMPWLLAGAKTLSYAINMAALRHAARRGAGDVVFVSSDGYILEGPRSTVVIATAGDDGNVCLLTPPPWYPILRGTTQQALFTVARAKGYDCDYRALRVADLFAAQGIWLVSSMTLAARVHTLDGRQLPSAPIAAEFAGLVDAAIVSDR
>NZ_AP022569.1|WP_163776640.1|2692615_2693710_+|folate-binding-protein-YgfZ
MSAVPAPETGPDAGAIWHYGDPLGEQRTAETGAVLVDRSHRGVLTLTGADRQTWLHSISTQHVAELADGASTQNLSLDGQGRVEDHWLQTELGGVSYLDTEPWRAAPLLDYLRKMVFWSDVAVAPADLAVVSLLGPKLSERAVLDALGLDTLPAEMTATPLAGGGFARRMTEAVPGQVELDVLVGRGDVADLQRRLTQAGVRPAGVWAYEAHRVAAIRPRLGVDTDERTIPHEVGWIGGPGLGAVHLDKGCYRGQETVARVHNLGKPPRMLTLLHLDGSVDRPVTGDPVLAGGRAVGRLGTVVEHVDLGPVALALLKRGIPADTALSTGADADVAAMIDAASLPTLDGPGAGRLAVERLRGTVR
>NZ_AP022569.1|WP_163776641.1|2693844_2694012_+|DUF3073-family-protein
MGRGRAKAKQTKVARELKYSSPQTDFDRLQQELSGSGNDDADQSEGDDPWSDERR
>NZ_AP022569.1|WP_163776642.1|2694048_2695128_-|phosphoribosylformylglycinamidine-cyclo-ligase
MTDRGKDPANPGVTYASAGVNIEAGDRAVDLFKPLALKATRPEVRSKLGGFAGLFALRDYREPLLAGSSDGVGTKLAVAQAMDKHDTVGLDLVAMVVDDLVVCGAEPLFLLDYIALGRIVPERLNAIVGGIAEGCVRAGCALLGGETAEHPGLIEPDHYDISATGVGVVEAEDVLGPERVKPGDVLIAMGSSGLHSNGYSLARKVLLEIDRGNLAGHVEEFGRTLGEEMLEPTIIYAKDCLALAAETQVRTFCHVTGGGLAGNLERVIPNGLVAEADRGTWTPAPVFAMIAQRGRVARAEMEKTFNMGVGMIAVVAPEDTDRALAILTARHLNCWVLGTINKGGKEGPRAKLVGQHPRF
>NZ_AP022569.1|WP_163776643.1|2695193_2696747_-|amidophosphoribosyltransferase
MTTELPVPDENPPGEECGVFGVWAPGEQVAKLAYYGLYALQHRGQEAAGIAVADGSQVLVFKDLGLVSQVFDEQTLAAMDGHVAVGHCRYSTSGSTTWENAQPVFRNTAAGTGVALGHNGNLVNSADLVTRAREAGLISAKAPGAANTDSDMLGALLAHGAADSSLEQAALELLPTVRGAFCLTFMDENTLYAARDPYGVRPLSLGRLDRGWVVASETAALDIVGASFVRDIEPGELLAIDADGVRSTRFANPEPKGCIFEYVYLARPDSTIAGRSVHGARLEIGRRLARESPIDADLVIGVPESGIPAAVGYAQESGIPYGQGLMKNAYVGRTFIQPSQTIRQLGIRLKLNPLKEVIRGKRLIVVDDSIVRGNTQRALVRMLREAGAVEVHVRIASPPVKWPCFYGIDFPSPAELIANAVEDEDEMLEAVRHAINADTLGYISLRGLTAATEQPTSRLCSACFDGKYPIDLPRETALGKNVIEQMLANAARGVGHPDIAALEISPEAEQAAVLRHP
>NZ_AP022569.1|WP_163776644.1|2696928_2698497_-|FAD-dependent-oxidoreductase
MSDYDAIVVGAGHNGLTAAAILQGAGLRTLCLEANTYSGGMAATVELIDGFRYEIAGSVQFPTAPQITKELGLDALPTVDAEVMSVNIGESGEEPMVFYRDPMQLMTHLGEKHGADAIMGMAELIAWSQGPAKALGRFEVRTPPKTLDEMYACAANEAERAAIHQMLFGSAMDAIDRCLPDREKHAIMRGMLAFLAVNSTYRGPYTPGSATCLAFALAVPDDNTAMMTKLAGGIGALTEHLHELFVSRGGEMRFRTKVDKILVENDRVTGVRLRDGSTISAPVVVSNLAPDLTLTDLVGADCLPADLIARLSGRDHRAAFIQMHFALDGLPEFAPPYELLNEPGMQQSIGIFGSPEEQQRQWEMCTHGLVPDNPSLGMQIPSCMDPGLAPAGKHAASAYAYAFPVEASRDQHGRLKNEMAQRVIEKITRVAPNFRDIVIRHITFAPYHMQTMFGAPSGDFCHGLLHPDLMGPNRPGPKGFIDLPIPVEGLYLASAGCHGGPGITFTPGYNAAYQALDDRAVG
>NZ_AP022569.1|WP_163776645.1|2698580_2699180_+|TetR-family-transcriptional-regulator
MTEPTNLHELRRRSTHVALRRVALAQFASKGFANVTVTQLATEAGVTERTFFRHFPSKEAVLFQDYDTHLEWLAEALSQRPASESLFDAVLASVATFPHDVEVVRQAALARSTLISAERIAAHLRVVQSSFATVLTDFIKTRYAGVANLDLVAEVAGATLAAALVMAVQRWGDDGCTGDLGEIVATSVDLVRSGFAPLA
>NZ_AP022569.1|WP_163776646.1|2700284_2700680_-|hypothetical-protein
MSAARQHADPAKTRDAVRVIEGWLRDDTGPAPNRVALAAAVRLTARTLAAAAPGASVEVRIPPFVAVQCISGPRHTRGTPPNVVETDPRTWLLLATGLLQLTEASAAGTVQLSGSRANEIQIWLPLVRLAG
>NZ_AP022569.1|WP_163776647.1|2700676_2702950_-|phosphoribosylformylglycinamidine-synthase-subunit-PurL
MIDTVEHAAATPDHPQPFRELGLKEDEYQRIRDILGRRPTDAELAMYSVMWSEHCSYKSSKVHLRYFGETTTEQMRAGMLAGIGENAGVVDIGDGWAVTFKVESHNHPSYVEPYQGAATGVGGIVRDIMAMGARPVAVMDQLRFGAADAPDTRRVLDGVVRGIGGYGNSLGLPNIGGETVFDACYAGNPLVNALCVGVLRTEDLHLAFASGAGNKIILFGARTGLDGIGGVSVLASETFGGDESGGGRKKLPSVQVGDPFMEKVLIECCLELYSAGLVIGIQDLGGAGISCATSELASAGDGGMHIDLDTVPLRAANMTPAEILSSESQERMCAVVAPENVDAFMAVCRKWEVLATTIGEVTDGDRLRITWHGETVVDVPPRTVAHEGPVYQRPVARPESQDALNADRSTGLTRPKTGDELRATLLALLGSPHLCSRSYITEQYDRYVRGNTVLAEHADGGVLRVDETTGRGIAISTDASGRYTYLDPYTGAQLALAEAYRNVAVTGATPVAVTNCLNFGSPEDPGVMWQFSEAVRGLADGCVALGIPVTGGNVSFYNQTGTTAIMPTPVVGVLGVLDDVSRRLPTSFGTQPGETLILLGDTRDELDGSIWAQVTADHLGGLPPTVDLAREQLLADVLSTACRDGLVSAAHDLSEGGLAQAIVESALAGETGCRIVLPEDADPFVMLFSESAGRVLVAVPHTEETRFQELCAARGLPATRIGVVDRGSDAVEVQGLFTVPLAELRSTSEGVLAALLR
>NZ_AP022569.1|WP_163776648.1|2702986_2703796_-|helix-turn-helix-domain-containing-protein
MSQATVGVLLREWRTRRRVSQLDLSLSVGVSARHLSFIETGRSRPSPEMVIALAEGLDIPLRERNTLLLAAGFAPRYQSRRLEDSALSPARDAVARLLEAHDPYPGVVIDRCWNIVGANAAASALTAGLPDELLGPPANVYRLSLHPDGLAGRTVNFDEWGGYLLHQLRRTVALTGDPAVRTLEKEVSAYPGVEALTARGAPPDATSLLVPFVLDVGGGQRLSMFTTLTTFGTPLDVTLAELAVELFYPADDASADLLRASRERTGQGI

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Crispr_ID: NZ_AP022569_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP022569_3

2982522-2982622

Unclear

Consensus_repeat	Method
CTGCATCGTCACCGGCGCAGATCA	CRISPRCasFinder

1 spacers

cas3

The CRISPR arrays of NZ_AP022569_3

>merge|NZ_AP022569|3|2982522-2982622|CRISPRCasFinder
CTGCATCGTCACCGGCGCAGATCATTCGCGCCGCTCTCCCCCGCGAGCGGGAGGTACCCCCACCTCATCGCCACGCCCTGCGTCGTCACCGGCGCAGATCA

>NZ_AP022569|3|3|2982522-2982622|CRISPRCasFinder
CTGCATCGTCACCGGCGCAGATCA	TTCGCGCCGCTCTCCCCCGCGAGCGGGAGGTACCCCCACCTCATCGCCACGCC
CTGCGTCGTCACCGGCGCAGATCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP022569.1\|WP_163776904.1\|2986040_2986889_+\|HAD-IB-family-hydrolase	unknown	unknown	gnl\|CDD\|273654
NZ_AP022569.1\|WP_003925183.1\|2977020_2977224_-\|cold-shock-protein	unknown	unknown	gnl\|CDD\|224197
NZ_AP022569.1\|WP_163776906.1\|2988085_2989738_-\|dipeptide-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224048
NZ_AP022569.1\|WP_163776905.1\|2987336_2988089_-\|oxidoreductase	unknown	unknown	unknown
NZ_AP022569.1\|WP_163781793.1\|2995348_2996008_-\|trypsin-like-peptidase-domain-containing-protein	unknown	unknown	unknown
NZ_AP022569.1\|WP_163776894.1\|2972706_2973120_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP022569.1\|WP_163776897.1\|2977560_2979897_+\|DEAD/DEAH-box-helicase	cas3	mkCas0139_cas3_CAS-I	gnl\|CDD\|274800
NZ_AP022569.1\|WP_163781789.1\|2981905_2982439_-\|type-II-secretion-system-F-family-protein	unknown	unknown	gnl\|CDD\|366122
NZ_AP022569.1\|WP_163776900.1\|2981686_2981893_-\|DUF4244-domain-containing-protein	unknown	unknown	gnl\|CDD\|379429
NZ_AP022569.1\|WP_163776895.1\|2973273_2976081_-\|type-I-DNA-topoisomerase	unknown	unknown	gnl\|CDD\|236048
NZ_AP022569.1\|WP_163776908.1\|2990581_2991508_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223674
NZ_AP022569.1\|WP_163776902.1\|2983410_2984574_-\|TadA-family-conjugal-transfer-associated-ATPase	unknown	unknown	gnl\|CDD\|200328
NZ_AP022569.1\|WP_163776907.1\|2989734_2990589_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|224094
NZ_AP022569.1\|WP_163776909.1\|2993215_2995174_+\|acetate--CoA-ligase	unknown	unknown	gnl\|CDD\|234677
NZ_AP022569.1\|WP_163776896.1\|2976236_2976815_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP022569.1\|WP_163776899.1\|2981035_2981569_-\|flp-pilus-assembly-TadE/G-like-family-protein	unknown	unknown	gnl\|CDD\|274799
NZ_AP022569.1\|WP_163781788.1\|2971041_2972688_+\|HAMP-domain-containing-protein	unknown	unknown	gnl\|CDD\|143636
NZ_AP022569.1\|WP_163781791.1\|2991509_2993105_-\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|173853
NZ_AP022569.1\|WP_163776898.1\|2980019_2981039_+\|DUF5593-domain-containg-protein	unknown	unknown	gnl\|CDD\|376047
NZ_AP022569.1\|WP_163776903.1\|2984570_2985659_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274798

Protein	Function_ID	Function_description	E-value
NZ_AP022569.1\|WP_163776904.1\|2986040_2986889_+\|HAD-IB-family-hydrolase	gnl\|CDD\|273654	TIGR01490, Uncharacterized_protein_Rv3661/MT3761, HAD-superfamily subfamily IB hydrolase, TIGR01490. This hypothetical equivalog is a member of the IB subfamily (TIGR01488) of the haloacid dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The sequences modelled here are all bacterial. The IB subfamily includes the enzyme phosphoserine phosphatase (TIGR00338). Due to this relationship, several of these sequences have been annotated as "phosphoserine phosphatase related proteins," or "Phosphoserine phosphatase-family enzymes." There is presently no evidence that any of the enzymes in this model possess PSPase activity. OMNI\|NTL01ML1250 is annotated as a "possible transferase," however this is due to the C-terminal domain found on this sequence which is homologous to a group of glycerol-phosphate acyltransferases (between trusted and noise to TIGR00530). A subset of these sequences including OMNI\|CC1962, the Caulobacter crescentus CicA protein cluster together and may represent a separate equivalog. [Unknown function, Enzymes of unknown specificity].	5.33741e-83
NZ_AP022569.1\|WP_003925183.1\|2977020_2977224_-\|cold-shock-protein	gnl\|CDD\|224197	COG1278, CspC, Cold shock proteins [Transcription].	6.71742e-36
NZ_AP022569.1\|WP_163776906.1\|2988085_2989738_-\|dipeptide-ABC-transporter-ATP-binding-protein	gnl\|CDD\|224048	COG1123, COG1123, ATPase components of various ABC-type transport systems, contain duplicated ATPase [General function prediction only].	0
NZ_AP022569.1\|WP_163776897.1\|2977560_2979897_+\|DEAD/DEAH-box-helicase	gnl\|CDD\|274800	TIGR03817, DECH_helic, helicase/secretion neighborhood putative DEAH-box helicase. A conserved gene neighborhood widely spread in the Actinobacteria contains this uncharacterized DEAH-box family helicase encoded convergently towards an operon of genes for protein homologous to type II secretion and pilus formation proteins. The context suggests that this helicase may play a role in conjugal transfer of DNA.	0
NZ_AP022569.1\|WP_163781789.1\|2981905_2982439_-\|type-II-secretion-system-F-family-protein	gnl\|CDD\|366122	pfam00482, T2SSF, Type II secretion system (T2SS), protein F. The original family covered both the regions found by the current model. The splitting of the family has allowed the related FlaJ_arch (archaeal FlaJ family) to be merged with it. Proteins with this domain in form a platform for the machiney of the Type II secretion system, as well as the Type 4 pili and the archaeal flagella. This domain seems to show some similarity to PF00664 but this may just be due to similarities in the TM helices (personal obs: C Yeats).	1.10065e-05
NZ_AP022569.1\|WP_163776900.1\|2981686_2981893_-\|DUF4244-domain-containing-protein	gnl\|CDD\|379429	pfam14029, DUF4244, Protein of unknown function (DUF4244). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 66 and 95 amino acids in length. There is a conserved EYA sequence motif.	3.98689e-15
NZ_AP022569.1\|WP_163776895.1\|2973273_2976081_-\|type-I-DNA-topoisomerase	gnl\|CDD\|236048	PRK07561, PRK07561, DNA topoisomerase I subunit omega; Validated.	0
NZ_AP022569.1\|WP_163776908.1\|2990581_2991508_-\|ABC-transporter-permease-subunit	gnl\|CDD\|223674	COG0601, DppB, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	1.81571e-99
NZ_AP022569.1\|WP_163776902.1\|2983410_2984574_-\|TadA-family-conjugal-transfer-associated-ATPase	gnl\|CDD\|200328	TIGR03819, heli_sec_ATPase, helicase/secretion neighborhood ATPase. Members of this protein family comprise a distinct clade of putative ATPase associated with an integral membrane complex likely to act in pilus formation, secretion, or conjugal transfer. The association of most members with a nearby gene for a DEAH-box helicase suggests a role in conjugal transfer.	7.27583e-167
NZ_AP022569.1\|WP_163776907.1\|2989734_2990589_-\|ABC-transporter-permease-subunit	gnl\|CDD\|224094	COG1173, DppC, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	5.08087e-80
NZ_AP022569.1\|WP_163776909.1\|2993215_2995174_+\|acetate--CoA-ligase	gnl\|CDD\|234677	PRK00174, PRK00174, acetyl-CoA synthetase; Provisional.	0
NZ_AP022569.1\|WP_163776899.1\|2981035_2981569_-\|flp-pilus-assembly-TadE/G-like-family-protein	gnl\|CDD\|274799	TIGR03816, tadE_like_DECH, helicase/secretion neighborhood TadE-like protein. Members of this small, highly hydrophobic protein family occur in a pilus/secretion-like region that usually is next to an uncharacterized DEAH-box helicase, in Actinobacteria. Members show sequence similarity to the TadE-like family described by pfam07811. The function is unknown. [Unknown function, General].	7.92845e-16
NZ_AP022569.1\|WP_163781788.1\|2971041_2972688_+\|HAMP-domain-containing-protein	gnl\|CDD\|143636	cd07302, CHD, cyclase homology domain. Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.	3.10749e-43
NZ_AP022569.1\|WP_163781791.1\|2991509_2993105_-\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|173853	cd00995, PBP2_NikA_DppA_OppA_like, The substrate-binding domain of an ABC-type nickel/oligopeptide-like import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding domain of nickel/dipeptide/oligopeptide transport systems, which function in the import of nickel and peptides, and other closely related proteins. The oligopeptide-binding protein OppA is a periplasmic component of an ATP-binding cassette (ABC) transport system OppABCDEF consisting of five subunits: two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Similar to the ABC-type dipeptide and oligopeptide import systems, nickel transporter is comprised of five subunits NikABCDE: the two pore-forming integral inner membrane proteins NikB and NikC; the two inner membrane-associated proteins with ATPase activity NikD and NikE; and the periplasmic nickel binding NikA, which is the initial nickel receptor that controls the chemotactic response away from nickel. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains 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 ligand binding domains of ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	4.29019e-116
NZ_AP022569.1\|WP_163776898.1\|2980019_2981039_+\|DUF5593-domain-containg-protein	gnl\|CDD\|376047	pfam18621, DUF5628, Family of unknown function (DUF5628). This is a domain of unknown function found in Actinobacteria.	2.55279e-47
NZ_AP022569.1\|WP_163776903.1\|2984570_2985659_-\|hypothetical-protein	gnl\|CDD\|274798	TIGR03815, CpaE_hom_Actino, helicase/secretion neighborhood CpaE-like protein. Members of this protein family belong to the MinD/ParA family of P-loop NTPases, and in particular show homology to the CpaE family of pilus assembly proteins (see ). Nearly all members are found, not only in a gene context consistent with pilus biogenesis or a pilus-like secretion apparatus, but also near a DEAD/DEAH-box helicase, suggesting an involvement in DNA transfer activity. The model describes a clade restricted to the Actinobacteria.	1.43219e-83

>NZ_AP022569.1|WP_163781789.1|2981905_2982439_-|type-II-secretion-system-F-family-protein
MVRARATKAMPAKRAGRPSVRGPDPLAVASSLDVLAVCLAAGMAVSTAAAATAPSAPPVLARVLRRAADLLVLGAAPDVAWSTPPDLPPSSLDPQTDALLRLARRSSTSGVALAEAVAALAAQCRQDAVHAAAATAERAAVLIAGPLGLCFLPAFVCLGVAPVVAGLAGDLMQSGLL
>NZ_AP022569.1|WP_163776900.1|2981686_2981893_-|DUF4244-domain-containing-protein
MKLVTMFRVLEARAALLAADESGMSTVEYAIGTIAAAAFAAILYTVVTGDSVVTALTNIIARALNTKA
>NZ_AP022569.1|WP_163776899.1|2981035_2981569_-|flp-pilus-assembly-TadE/G-like-family-protein
MPPARLPGWLRAVTSARRSPPPAAWHPTAPPSSCVATAISSSRPSPPGRGCFRCCTSPRLARRWSSRRGEQGSATVVAAAMVAALLAVTGGAGYLGAAVVARHQAQAAADLAAVAAATGLVSGAEAACEQAKAVAREMRVSTTDCDVDDLDVIVSVEVRLAVSRWGSARAAARAGPA
>NZ_AP022569.1|WP_163776898.1|2980019_2981039_+|DUF5593-domain-containg-protein
MTTDWLLVETLGREPAVVALGRQLQNLVPITAFLRRKGGRAAIQSAIAESLHTSQSLVSLTPKKDRVIHTEPVVMSDGRVHGVHVWSGPAGDEPPERPIPGPLKWDMTLGVATDTPESLANAGRNVEAEDSEERALAECWPSGELKPNEGRALGAAVRSEPGHTVCDTWDGVDWQGRYIRVSFVARNGLEAGADGRDHLVARGMNWRAEEAERPQPSDRLAQQILRGLAQPGVHRALFDPHTWTLLKWLDEPCPFYDWRRIAADSPKLHPSDEAKMATMQAEFAHGTTWGVLRMPGCDGGWVPVHVTVNRVEIGDDTFAGLASLRQPTAAEVADAALTD
>NZ_AP022569.1|WP_163776897.1|2977560_2979897_+|DEAD/DEAH-box-helicase
MVTFGSELLAAAVAGTDAGEQPLRHVAELPARHGRQRPWPTWVEPDVLRAFTDRGVNSPWLHQVAAADLAHAGRHVVISTGTASGKSLVYQLPILNALATEPRARALYISPTKALGHDQLRAAHALTAAIPRLNDVAPTAYDGDSPTEVRRFARERSRWLFSNPDMVHLALLRNHARWAVFLRGLRFVVVDECHYYRGVFGSNVAMVLRRLLRLCARYSADPSRTPTVIFASATTSEPGATATELIGQPVEEVTEDGSPQGARTVALWEPALRTDLVGENGAPVRRSAGSESARVMADLIAEGARTLTFVRSRRGAELTALAARARLEDIAPELVEKVASYRAGYLPEDRNELERALLDGRLRGLATTNALELGIDIAGLDAVVMAGFPGTVTSFWQQAGRSGRRGQGALVLLVARDDPLDTYLVHNPAALLDKPIERVVIDPTNPYILGPQLLCAATEFPLDDVEVRTLGAEVVAQQLVDDGLLRRRSGKYYPAPGVDPHPAVDIRGSTGNQIVIVETDTGRLLGTADTGRAAASVHPGAVYLHQGESYLVDSLDFDEGMAFVHGEDPGYATFARELTDIEVTGTGERSTFGSVTLGLVPVRVTNRIVGYLRRRLTGEVIDFVELDMPPHMLETTAVMYTITPEALYGNGIDPIRIPGSLHAAEHAAIGLLPLVASCDRGDIGGLSTAVGPESDGLPSVFVYDGYPGGAGFAEQGFRRASTWLGATAAAIEACECPSGCPSCVQSPKCGNGNDPLDKAGAVQVLDAVLSALAQNLQS
>NZ_AP022569.1|WP_003925183.1|2977020_2977224_-|cold-shock-protein
MPQGTVKWFNAEKGFGFIAPEDGSADVFVHYTEIQGSGFRTLEENQRVEFEVGQSPKGPQATGVRSI
>NZ_AP022569.1|WP_163776896.1|2976236_2976815_-|hypothetical-protein
MSQLSFFSAESVPPAVSDLTGVLAAAGQIVTVGSGARLSVVVDQTWRAVALGQMIEEAGLTAEITETDEKTPLVRTAVDNRLRPIAVEWTRGAVKTVPPLWLPGSRELRAWVLAAGSPEADRYLLGLDPHAPDTHSPLASALMRIGIAPTLIGTRGARPALRISGRRRLSRLVENVGEPPDTVEALPYWPHV
>NZ_AP022569.1|WP_163776895.1|2973273_2976081_-|type-I-DNA-topoisomerase
MAEGDRGGPSRGNGASRRLVIVESPTKARKLAGYLGSNYIVESSRGHIRDLPRAAADVPAKYKSQPWARLGVNVDEDFEPLYIISPDKKSTVSELKGLLKDVDELYLATDGDREGEAIAWHLLETLKPRIPVKRMVFHEITEPAILEAAENPRDLDNDLVDAQETRRILDRLYGYEVSPVLWKKVAPKLSAGRVQSVATRIIVQRERDRMAFRSAAYWDVVAELDASVSDPKAQPPTFTARLTSVDGLRVATGRDFDSLGAVRKPDEVTVLDEASAVSLATGLRGSQLSVGSVEEKPYTRRPYPPFMTSTLQQEAGRKLRFSAERTMSIAQRLYENGYITYMRTDSTTLSQSAIDAARTQARQLYGEEYVYPSARQYTRKVKNAQEAHEAIRPAGETFATPDAVHRELDGDEFRLYELIWQRTVASQMADARGTTLSLRINGESDGRQIQFSASGRTITFAGFLKAYVETVDELAGGEADDAESRLPQLTQGQRVDATKLTPDGHSTNPPARYTEASLIKALEELGIGRPSTYSSIIKTIQDRGYVHKKGSALVPSWVAFAVTGLLEQHFGRLVDYGFTAAMEDELDAIASGQEHRTNWLNNFYFGGDHGVADSIARSGGLKKLVGVNLEGIDAREVNSIKLFDDAQGRAVNVRVGKNGPYLERMVVGDDGEPTPQRANLHDSLTPDELTLDVAEELFSTPQEGRTLGVDPDTGHEIVAKDGRYGPYVTEVLPKSEDDDDGTAGQPAKKGKKPTGPKPRTGSLLRTMDLQTVTLEDALRLLSLPRVVGVDPQSGEEITAQNGRYGPYLKRGTDSRSLATEEQMFDITLDEALKIYAEPKRRGRQAAAAPPLRELGNDPASGKPMVIKDGRFGPYVTDGETNASLRKGDDVLSITDDRAAELLADRRARGPVKKTAKKTARKSPAKKAAKKAVKRS
>NZ_AP022569.1|WP_163776894.1|2972706_2973120_-|hypothetical-protein
MRSAARHCITAGAALVGLSVIIAAPAAPPLSDVQVPAVQLSGNSHENPDANSPSVADLLQVMNGSESPVVVQNITESETGVFEGDTPAIVPGLSELLNLGTDPAGVTDPQGKAFIDLGPLVPGVVTPAPAGPPPAGG
>NZ_AP022569.1|WP_163781788.1|2971041_2972688_+|HAMP-domain-containing-protein
MTIERFGYFLVAADRYGGQVSTAAGLPGRISGFVQWFVRTPWPVFTLSQLQADIIGALLVLGFLRYGLPPEDRIELQKLPTLNLATFAGSIVLLFLIGTAISARLLVPVFRWQRRDGLLTDTDPTATALARSRALRTPFYRTVINLASWCIGGTIFIVASWPVAKHAAPVVAVATALGATATAIIGYLQSERVLRPVAVAALRGGLPENIRASGVIGRQMLAWALSTGVPVLTIVLAVVADKAEYLHGPPEKLLNPILLLALLALGIGLASTLLVAMSIADPLRQLRWALGEVQRGNYNAHMQIYDASELGLLQAGFNDMVRDLAERQRLRDLFGRYVGEDVARRALERGTELGGQERDVAVLFVDLVGSTKLASTRPPAEVVSMLNEFFRVVVDTVGRHGGFVNKFQGDAALAIFGAPIEHPDASGGALAAARELHDELLPVIGSAEFGIGVSSGRAIAGHIGALARFEYTVIGDPVNEAARLTELAKLEDGHVLASAVAVSGALDAEALCWDVAEVVALRGRTAPTQLARPLNLAAPEEAPREMSS
>NZ_AP022569.1|WP_163776902.1|2983410_2984574_-|TadA-family-conjugal-transfer-associated-ATPase
MTDSLIDRVRERLASESAPLRPKVVADAIRAESGGVLGDTELLSNLRILQTELTGAGILEPLLCADGTTDVLVTAPDAVWVDDGTGLRRSRIEFADEAAVRRLAQRLALSAGRRLDDAQPWVDGQLTGLGVGGFAVRLHAVLPPVAMGGTCLSLRVLRPATQDLSALIAAGAIAPTAAGLIDEIITARLAFLVSGGTGAGKTTLLSAMLNAVSPDERIICVEDAAELAPPHPHLVKLVARCANVEGVGEVTVRQLVRQALRMRPDRIVVGEVRGAEVVDLLAALNTGHDGGAGTVHANNPGEVPARLEALGALGGLDRDALHSQLAAAVQVLLHVARDRSGRRRLSEIAMLRQSAGRVRAATVWHADRGPTDELAELRRLLQDRTRP
>NZ_AP022569.1|WP_163776903.1|2984570_2985659_-|hypothetical-protein
MTTTSARGILAVLGDPALRDDLDRVAAAVGVRVVHASNVLPASRKAWSAAAAIVLDEAAAVECGQSGMPRRAHVIVVCGDEPEPVTWAAAIEVGATQVLRMPAQERDLVRELADASESVRDGGSRSAVVAVIGGRGGAGASLFAVAMASVAANAMLLDLDPWGGGIDLLLGAETTPGVRWPDLTLQGGRLNWSAVREALPRHRGVTVLSGTRQDCEYDGHAVHSVVDAGRRGGVTVVCDLPRRLTGSTEIALEAADLVVVVCPCDVRSCAATATIAPVLAAVNPNLGLVVRGPSPGGLRADEVAAIAGVPLLASMRPHPRLAEQIEVGGLRLPRRSALAKAARRVLAVLPAHPAVRPEGIAA
>NZ_AP022569.1|WP_163776904.1|2986040_2986889_+|HAD-IB-family-hydrolase
MTVNDSAADQQTPSTPSGPSPRTAAFFDLDKTIIAKSSTLAFSKPFFAQGLINRRAVLKSSYAQFLFLLSGADHDQMDRMRVHLTNMCTGWDVEQIKSIVNETLHDIVTPLVFAEAADLIASHKLCGRDVVVVSASGEELVAPIARALGATHAMATRMVVEDGKYTGEIGFYCYGEGKVQAIRELAAREGYPLEHCYAYSDSITDMPMLEVVGHPSVVNPDRALRREAASRGWPVLAFSRPVSLRDRIPAPSGAALATTAAVGISALAAGALTYSLLRRLAL
>NZ_AP022569.1|WP_163776905.1|2987336_2988089_-|oxidoreductase
MTDPLAPLMELPGVAAASDQAREALGRAHRHRSNLRRWPVTAAEAALRSARASAVLDGGGRKLDDQIDVSAIGDPVFAGALRVAQALEGGETNLVGVWQRAPLQALARLHMLAAADRVDESRLGRPRTDADVGPRLELLAGIVTGGTAAPAPIIAAVAHGELLTLAPFGTADGVVARAVSRLVTIATGLDPHGLGVPEVAWMRRAADYREAARGFADGTPAGIAKWLVLSCRALRTGAQEALTIADSLTQ
>NZ_AP022569.1|WP_163776906.1|2988085_2989738_-|dipeptide-ABC-transporter-ATP-binding-protein
MNSTDLPLLSVTGLDVRFGDDAPAVRQVDVAVRAGQTVAIVGESGSGKSTTAAAILGLLPPGGRITAGRIMFDGIDLTTADRRRLRSVRGSGIGYVPQDPMTNLNPVWRVGFQVREALRANNVDRRAVQLLADAEMPDPELRAMQYPHQLSGGMCQRALIAIGLAGRPQLLIADEPTSALDVTVQRQVLDHLQRLTGDLGTAVLLITHDLALAAERAEQLIVMHQGSVVETGAAQLVLRDPQHPYTQRLVAAAPSMRDITTATRARRRIRRAAGVRAGRDLAQDVIVVSDLTKVYRPSRGAPWRKVDVRAVDKVSFRLRRATTLAIAGESGSGKSTLARMILGLLQPTSGTVVFDGKEVSDSAGRDEALAFRRRIQPVFQNPYGSLDPTYSVFRTIEEPLRIHRVGDRRKRRKSVHELADQVALPSSLLARRPRELSGGQRQRVAIARALALRPEVVVCDEAVSALDVVVQAQILDLLAELQAELGLTYLFISHDLAVIRQIADEVLVMHAGRVVERGATKDVFTRPSHDYTRQLLAAIPGTGAGYSGSR
>NZ_AP022569.1|WP_163776907.1|2989734_2990589_-|ABC-transporter-permease-subunit
MAEVLAGGGFWRGLRRRPQFVIAAVLIGFVVVVAAFPALFTTADPGYADPNQSLLAPSAAHWFGTDLQGHDIYARTVYGARASVTVGLGATLVVFVVGGALGALAGFYGGWLDAVVSRIADVFFAIPLLLAAIVLMQVMHHRTVWTVIAILSLFGWPQVARIARGAVLTVRDSDYVLAAKALGMSRFGTLVRHVVPNAVGPVIAVSTIALGLFIVTEATLSYLGVGLPPSVVSWGGDINVDQIRLRAGSPILFYPAGALAITVLAFMIMGDVLRDALDPTSRRR
>NZ_AP022569.1|WP_163776908.1|2990581_2991508_-|ABC-transporter-permease-subunit
MGWYIARRVAAMLPVFLGATLLIYGMVFLLPGDPIAALGGDRPLSPAVAAQLRAQYHLNDPFWLQYLHYLGGIVHGDLGHAYSGLPVSTVLAQAFPVTFRLALIALAVEALFGVGFGVIAGLRQGGVFDGAVLIVSLIIIAVPIFVLGFLAQFVFGVRLGLAAVTVGDQPTFSRLLLPGIVLGAVSFAYVVRLTRSAVADNAHADYVRTAIAKGLSRPRVVTVHILRNSLIPVVTFLGADLGALMGGAIVTEGIFNIHGVGGVLYQAVTRQEAPTVVSIVTVLVVVYLVTNLAVDLLYAALDPRIRYG
>NZ_AP022569.1|WP_163781791.1|2991509_2993105_-|ABC-transporter-substrate-binding-protein
MAAVAVALLAVAPLVGCGAGDVRTDVVIVNAGEPQNPLIPTNTNDSNGGRIVDRLFAGLMSYDANGSPSPEVAESIETADDVNYRITLKSGWTFSDGSPVTAHSFVDAWNFGALSTNAQLQQSFFSPIAGFDEVAAAKPTTTTMSGLQVVNEREFTVRLKGPTIDFKLRLGFSPFYPLPESAYMDMARFGQHPVGNGPYQLADERRIPAWQHNVKLDLVTNPGYHGNRTSQNKGLRFVFYANLDTAYADLLSSNLDVLDTIPPSVLTVYRRDLGDRAVSAPAAVNLTLDTPMRLPHFGGEEGRLRRLALSAAINRSQICQKIFSGARAPARDFTASSLPGYDPDIDGNSALNFDPDRARRLWAQADAISKWTGRYAIAYNTDGSHQEWVDAVANSIKNTLGVDALGAPQPTFAGFRTQITTHTISTAFRAGWQGDFPSMLEFLEPLFATGASANDVGYSNPRFDAAIGEAEAAADLPQSYALANGAQRILLADMPVVPLWYTVAVAGHSPAVGQVRLTWNGLPDYEHIVKA
>NZ_AP022569.1|WP_163776909.1|2993215_2995174_+|acetate--CoA-ligase
MRVTETHAPLSYPPSAEFTAQANAAEGLYRDAEQDRLAFWAEQANRLSWATPFSQVLDWSEAPFAKWFADGKLNVAYNCVDRHVEAGNGDRVAIYWEGEQIGDSRSLTYRDLQDEVGKAANALTGLGLVAGDRVAIYLPMIPEAIVAMLACARLGLMHSVVFAGYTANALRARIDDAEAKLVITADGQFRRGKPAPLKNAVDDAVASADTVEHVLVVRRTGIEVDWKQGRDVWWHDVVDSASPEHDPEAFDAEHPLFLLYTSGTTGKPKGIVHTSGGYLTQASYTHHNIFDIKPETDVFWCTADIGWVTGHTYGVYGPLSNGVTEIFFEGTPDTPSQHRHFQIIEKYGATIYYTAPTMVRTFMKWGREFPDAHDLSSLRLLGTVGEPINPEAWRWYRTVIGGDSAPIVDTWWQTETGAAMISPLPGVAATKPGSAMAALPGISAKVVDDHGDELAPPSTDEGEHAAGYLVLDQPWPSMLRGIWGDPDRFRETYWSRYAEHGYYFAGDSARYDSDGAIWVMGRIDDVMNVSGHRISTAEVESALVGHAGVAEAAVVGATDDTTGQAICAFVVLTADHADTAGAEIIDELRAEVAKEISPIARPRELHVVPELPKTRSGKIMRRLLRDIVEKRELGDTSTLLDPGVFDAIRAAK
>NZ_AP022569.1|WP_163781793.1|2995348_2996008_-|trypsin-like-peptidase-domain-containing-protein
MVTVVSAGLSAAPASADDRVPLGGGSGIVVNGDSLCTLTTIGTDPKGELIGFTSAHCGGPGAQVAAEAAKERGVLGTMVSGNDGLDYAVIQFDRAKVAPVANVAGFVITGIGPDPAFGQVACKQGRTTGNSCGVTWGPGQDPGTILMQVCGQPGDSGGPVTVDNRLVGMIHGAFSENLPICVTKYIPLHTPAVVQSFNAILADLQSKGRMGAGFVPVPA

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Crispr_ID: NZ_AP022569_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP022569_4

3195594-3195679

Orphan

Consensus_repeat	Method
AGCTCCGCCAACATCGGGTTGGGCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP022569_4

>merge|NZ_AP022569|4|3195594-3195679|CRISPRCasFinder
AGCTCCGCCAACATCGGGTTGGGCGCGCGCTTTGATTTTGCTTTCGCCGACGGCCCAGGCAGCTCCGCCAATATCGGGTTGGGCGC

>NZ_AP022569|4|4|3195594-3195679|CRISPRCasFinder
AGCTCCGCCAACATCGGGTTGGGCGC	GCGCTTTGATTTTGCTTTCGCCGACGGCCCAGGC
AGCTCCGCCAATATCGGGTTGGGCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP022569.1\|WP_163777097.1\|3184215_3184890_-\|isoprenylcysteine-carboxylmethyltransferase-family-protein	unknown	unknown	gnl\|CDD\|224931
NZ_AP022569.1\|WP_170308201.1\|3174011_3180902_+\|amino-acid-adenylation-domain-containing-protein	unknown	unknown	gnl\|CDD\|237108
NZ_AP022569.1\|WP_163777106.1\|3200030_3200963_+\|homoserine-O-succinyltransferase	unknown	unknown	gnl\|CDD\|235433
NZ_AP022569.1\|WP_163781842.1\|3147535_3149722_-\|acyltransferase-family-protein	unknown	unknown	gnl\|CDD\|224748
NZ_AP022569.1\|WP_163781845.1\|3151628_3162578_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|225858
NZ_AP022569.1\|WP_163777108.1\|3200967_3202254_+\|aminotransferase-class-V-fold-PLP-dependent-enzyme	unknown	unknown	gnl\|CDD\|225428
NZ_AP022569.1\|WP_163777114.1\|3204826_3205738_-\|phytanoyl-CoA-dioxygenase-family-protein	unknown	unknown	gnl\|CDD\|368580
NZ_AP022569.1\|WP_163781849.1\|3204543_3204789_-\|acyl-carrier-protein	unknown	unknown	gnl\|CDD\|180828
NZ_AP022569.1\|WP_163777110.1\|3202396_3204061_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274428
NZ_AP022569.1\|WP_163781847.1\|3196288_3196612_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP022569.1\|WP_163777104.1\|3198745_3200029_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235010
NZ_AP022569.1\|WP_163777093.1\|3168404_3170039_+\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|380465
NZ_AP022569.1\|WP_163777098.1\|3185220_3194934_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|235624
NZ_AP022569.1\|WP_163777090.1\|3163629_3163878_+\|MbtH-family-NRPS-accessory-protein	unknown	unknown	gnl\|CDD\|377081
NZ_AP022569.1\|WP_163777085.1\|3149929_3151216_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|224732
NZ_AP022569.1\|WP_163777102.1\|3196923_3198741_+\|FAD/NAD(P)-binding-protein	unknown	unknown	gnl\|CDD\|379196
NZ_AP022569.1\|WP_163777088.1\|3162643_3163495_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379312
NZ_AP022569.1\|WP_163777112.1\|3204070_3204544_-\|4'-phosphopantetheinyl-transferase-superfamily-protein	unknown	unknown	gnl\|CDD\|223807
NZ_AP022569.1\|WP_163777092.1\|3163867_3168418_+\|amino-acid-adenylation-domain-containing-protein	unknown	unknown	gnl\|CDD\|237108
NZ_AP022569.1\|WP_163777116.1\|3205830_3206760_+\|TIGR03621-family-F420-dependent-LLM-class-oxidoreductase	unknown	unknown	gnl\|CDD\|200301

Protein	Function_ID	Function_description	E-value
NZ_AP022569.1\|WP_163777097.1\|3184215_3184890_-\|isoprenylcysteine-carboxylmethyltransferase-family-protein	gnl\|CDD\|224931	COG2020, STE14, Putative protein-S-isoprenylcysteine methyltransferase [Posttranslational modification, protein turnover, chaperones].	5.27526e-23
NZ_AP022569.1\|WP_170308201.1\|3174011_3180902_+\|amino-acid-adenylation-domain-containing-protein	gnl\|CDD\|237108	PRK12467, PRK12467, peptide synthase; Provisional.	0
NZ_AP022569.1\|WP_163777106.1\|3200030_3200963_+\|homoserine-O-succinyltransferase	gnl\|CDD\|235433	PRK05368, PRK05368, homoserine O-succinyltransferase; Provisional.	7.15413e-59
NZ_AP022569.1\|WP_163781842.1\|3147535_3149722_-\|acyltransferase-family-protein	gnl\|CDD\|224748	COG1835, COG1835, Predicted acyltransferases [Lipid metabolism].	5.44712e-59
NZ_AP022569.1\|WP_163781845.1\|3151628_3162578_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|225858	COG3321, COG3321, Polyketide synthase modules and related proteins [Secondary metabolites biosynthesis, transport, and catabolism].	0
NZ_AP022569.1\|WP_163777108.1\|3200967_3202254_+\|aminotransferase-class-V-fold-PLP-dependent-enzyme	gnl\|CDD\|225428	COG2873, MET17, O-acetylhomoserine sulfhydrylase [Amino acid transport and metabolism].	0
NZ_AP022569.1\|WP_163777114.1\|3204826_3205738_-\|phytanoyl-CoA-dioxygenase-family-protein	gnl\|CDD\|368580	pfam05721, PhyH, Phytanoyl-CoA dioxygenase (PhyH). This family is made up of several eukaryotic phytanoyl-CoA dioxygenase (PhyH) proteins, ectoine hydroxylases and a number of bacterial deoxygenases. PhyH is a peroxisomal enzyme catalyzing the first step of phytanic acid alpha-oxidation. PhyH deficiency causes Refsum's disease (RD) which is an inherited neurological syndrome biochemically characterized by the accumulation of phytanic acid in plasma and tissues.	1.03786e-21
NZ_AP022569.1\|WP_163781849.1\|3204543_3204789_-\|acyl-carrier-protein	gnl\|CDD\|180828	PRK07081, PRK07081, acyl carrier protein; Provisional.	5.11208e-29
NZ_AP022569.1\|WP_163777110.1\|3202396_3204061_+\|hypothetical-protein	gnl\|CDD\|274428	TIGR03101, hydr2_PEP, exosortase A system-associated hydrolase 2. This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.	7.67003e-07
NZ_AP022569.1\|WP_163777104.1\|3198745_3200029_+\|hypothetical-protein	gnl\|CDD\|235010	PRK02186, PRK02186, argininosuccinate lyase; Provisional.	3.14403e-27
NZ_AP022569.1\|WP_163777093.1\|3168404_3170039_+\|AMP-binding-protein	gnl\|CDD\|380465	cd19543, DCL_NRPS, DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.	2.99933e-142
NZ_AP022569.1\|WP_163777098.1\|3185220_3194934_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|235624	PRK05850, PRK05850, acyl-CoA synthetase; Validated.	0
NZ_AP022569.1\|WP_163777090.1\|3163629_3163878_+\|MbtH-family-NRPS-accessory-protein	gnl\|CDD\|377081	pfam03621, MbtH, MbtH-like protein. This domain is found in the MbtH protein as well as at the N-terminus of the antibiotic synthesis protein NIKP1. MbtH and its homologs were first noted in gene clusters involved in non-ribosomal peptides and other secondary metabolites by Quadri et al. This domain is about 70 amino acids long and contains 3 fully conserved tryptophan residues. The structure of the PA2412 protein shows it adopts a beta-beta-beta-alpha-alpha topology with the short C-terminal helix forming the tip of an overall arrowhead shape. MbtH proteins have been shown to be required for the synthesis of antibiotics, siderophores and glycopeptidolipids.	1.05743e-33
NZ_AP022569.1\|WP_163777085.1\|3149929_3151216_+\|glycosyltransferase	gnl\|CDD\|224732	COG1819, COG1819, Glycosyl transferases, related to UDP-glucuronosyltransferase [Carbohydrate transport and metabolism / Signal transduction mechanisms].	1.48692e-66
NZ_AP022569.1\|WP_163777102.1\|3196923_3198741_+\|FAD/NAD(P)-binding-protein	gnl\|CDD\|379196	pfam13454, NAD_binding_9, FAD-NAD(P)-binding.	1.49129e-26
NZ_AP022569.1\|WP_163777088.1\|3162643_3163495_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	7.87679e-17
NZ_AP022569.1\|WP_163777112.1\|3204070_3204544_-\|4'-phosphopantetheinyl-transferase-superfamily-protein	gnl\|CDD\|223807	COG0736, AcpS, Phosphopantetheinyl transferase (holo-ACP synthase) [Lipid metabolism].	2.91381e-32
NZ_AP022569.1\|WP_163777092.1\|3163867_3168418_+\|amino-acid-adenylation-domain-containing-protein	gnl\|CDD\|237108	PRK12467, PRK12467, peptide synthase; Provisional.	0
NZ_AP022569.1\|WP_163777116.1\|3205830_3206760_+\|TIGR03621-family-F420-dependent-LLM-class-oxidoreductase	gnl\|CDD\|200301	TIGR03621, F420_MSMEG_2516, probable F420-dependent oxidoreductase, MSMEG_2516 family. Coenzyme F420 is produced by methanogenic archaea, a number of the Actinomycetes (including Mycobacterium tuberculosis), and rare members of other lineages. The resulting information-rich phylogenetic profile identifies candidate F420-dependent oxidoreductases within the family of luciferase-like enzymes (pfam00296), where the species range for the subfamily encompasses many F420-positive genomes without straying beyond. This family is uncharacterized, and named for member MSMEG_2516 from Mycobacterium smegmatis. [Unknown function, Enzymes of unknown specificity].	3.23885e-84

>NZ_AP022569.1|WP_163777098.1|3185220_3194934_+|SDR-family-NAD(P)-dependent-oxidoreductase
MVESSILAELRERANLQPGETAFTYVDYEQDWAGVAESLTWSQLYRRTQNVAQELRACGSTGDRAVILAPQGLGYVTSFLGALEAGLIAVPLSVPLGGASDERVSSVLRDASPAAILTTSSVARNSAEYIQSKPGESAPSVIEVDLLDLDRQVGPAVEADSRPDIAYLQYTSGSTRTPAGAVVSHENILANFEQINVGFFGGAAPTDTTVVSWLPFYHDMGLYLGILFPVLTGHPALITSPVAFLQRPARWMQALASSSHAFSGAPNFAFELAARKTSDDDMAGLDLGGVSSILNGSERVQPATLQRFAERFAGFNFHPRMLRPAYGMAEATVYIATREVGQPPEIVHFESEKLTAGQAQRCSSDDGTPLVSYGVPKSPMVCIVDPETSTECPAGTVGEIWTQGDNVAKGYWGKPPGTEGMFGATLVGTAGASEGRWLRTGDLGFFSEGELFVIGRIKDLLIVYGRNHSPDDVEGTIQEITKGRSVAIAVPDDGGVEKLVAIVELKHRDESEEAAMQRMGVVRREVATAISKVHGLSVADLVLVPQGSIPITTSGKVRRRDCVQLYLHDEFNRLDGLIRRPGQHMVDDAGAGPGVDSGWTQRLHTLRKQQHDLLVGLVCSQAALVLGHPSPNDIDPECAFGDLGFDSVKATELLDRLNTVTELALPPTLAFDCPTPDELATHLGQLLSGSVSAAPTVASRVQTDEPVAVVGMACRFPGGVDSPAALWDLVANGTDAVGEFPADRGWNLADLFDPDPDAVGKTYTRAGGFVADAAGFDADFFGISAREAQTMDPQQRLLLEVCWEALETARIDPAALAGSETGVFVGAWSQSYGAGGSDGVEGYGLTGLSTSVASGRVAYALGLQGPAITVDTACSSSLVATHLACQSLRNGESTLALAGGVTVMTTPAVFTEFARQRGLAADGRCKAFSANADGTGWGEGAAVLVLERLSDARRNNHPVLAVVAGSAINQDGASNGLTAPNGPAQQRVIAQAVANAGIGLDQVDAVEAHGTGTTLGDPIEAGALIATYGLSRDPEHPLWLGSIKSNIGHTQAAAGAAGLIKMIEALNHQSLPPTLNVDGPSPHIDWSAGTVRLLTEPTPWPVADHPRTAAVSSFGISGTNAHMILQQAPTSPAGSADAEPATEQAHHGAEFELAMWPVSARTPAALRAQADRLHQHLVCHPDLDLADVAYSLGSTRTHHSYRAMITAPVAAADPREDLLDALHALRTDQPHPQLTQHHYVAHLRGKTVFVLPGQGGQYPGMGRELYEHHRVFADMVDDCDKALRPFTGWSVREVLCGDEAAPSLDRVDVVQPALFTMMVSLAEVLSHYGIVPDAVIGHSQGEIAAAYIAGVLSLPEAAEVVARRSQALSALCGAGGMASVLLGADQLAPRLQPWGEALSISAINGPSHTIISGDPAGLEEFTAACERDGIHVRPIAVDYAAHSAQVEPVRERLLAELADLTPAHSRIPLYSTVASALSADPLDTTKMDGDYWYRNLREPVRFYDSVVERLAAGEHTFVELSPHPVLAPAITDTLAQSAAGRTQSAMVITLHRDRPDQDNLATALAQLHNHGHSPSWSALYPQARTVGLPTYPFEHRRYWLSPTSTDDASGLGLDRAEHPLLGAVATLADEDQVMISGRLSPNTQNWLVGHQVNDTVVFPATGFIEVILRAGELAGSPVIDELVLHSALILSERMPTDLQIVVRPLDEQGQRRFSVHSRTGGQSGVWTLHASGTLGADQPTAEVSLPPAPGVEALDQDDFYERLAHRGYRYGGLFRSLRGIGTDPAQPEVAYAEVALPAGTDVTGYGIHPALLDAALHPLASLLDRAGEADSASLRLPYAFSGITLYATAATQLHVHLTRTADDTFELRATDPTGTPVITIRALTFRAVSDQIGRPTSMAGLSDSLFELSWPPVPELPDPSAARPPAWAVCTDSPEQLPANLSGGTIHTDLTTVTPGPDLVIWQLPKEKVGGEAEPLGRVHSLTRNVVAQLQSWLARPETADTRLVIVTRHAVGVSAYDGVPDLAHAAVWALIHTAQNEHPDRIILLDTDDTVATEDNLLTVAAARPAGEPQLALRDGVIHIPRLTRTRNLTPPDAPDWQLGTTSKGDLTKLTLLPTDPTTTLAPGQIRVQVGAAGLNFRDVVVALGAIDDDGMGSEAAGVVLDAAPGTSLRRGDAVMGLFPHNAFAPTAVTDEHMVVPIPAGWSLTQAASAPIVFLTAYIALVEIAGLSAGQRVLIHGGAGGVGQAAIQIARHLGAEVFATAHPNKHHVLSDLGVDPGHIASSRTLDFVDAFNGTTGGQGMDVVLNSLSGDFVDASLRLLPRGGRFIEIGKTDIRVAGDVAAAHPGVDYHVYDLSSASAESLQPAWTALTEMFAAGVLKPLPTTSYGLLNAPQAFRDMSQARHTGKIVLIPPAVLNPEGTVLITGGTGMLGALFAEHLVTRYGIRHLLLVSRSGPDAPGAGELKERLARLGAHVAITACDASDPAELAALLDSIDAGHPLTAVIHTAGVLDDAMVTELTPGQLDAVLAAKADAAWHLHRLTADRDLAAFVLFSSAAGILGSPGQANYAAANAVLDALARQRNHTQRQATSVAWGYWQTPSGMTGHLNATDLSRLSSSGLIPITSEHGAALFDAALTRQRPNVVASPINIGTLTRHARHHTLDPVLSALTRVRPQAATASPRTLAARLATQRPQQRLETLTAMVTATTAAVLAHPDPDALDPDRHFKDLGIDSLTALELRNTLNQRTGLVLPATLALDYPTPTTLASHLAELLTDAVEPAVPAAQVSTRSDKPADNALAPVDQASFLAMRATHAALIQVIWIYDGAVNVDGLRRFQRNLGCGLLGRTIERSPLPFARDRWVKAAASEDIDMAATPRRRADVDAWADEQARRPIDPEWGPGWHLGVLPLEGGGTAVSLVASHTIVDAVGLGQAIEDAAAGRTRDLGYPRPKSRTRRRALREDLQQTVKELPDLAQALAAVVRRARSDRKGFTASIKVAPPAPRTASDDQAVEVPALTAYIDLAEWDARAKSLGASSTSLVAGVASRLAVRVGRVHDDGTVILRFPLTLRTEDDTRGNALTIVDVPVDPSHAATDLGDMHAKITHAMLAAIENSDDAVLATLPLATLVPRWVNRGLAAMAAGGAGLPVTCSNLGDLSPAANRPDGTDADFAYMRNLSPDIKKSTLEHMGGQLFVGSGRARGKMGIRISAYILGRPNTKDDLRESVSRTFAEFDLDAEIDC
>NZ_AP022569.1|WP_163777097.1|3184215_3184890_-|isoprenylcysteine-carboxylmethyltransferase-family-protein
MKTIPKLLVFGLAEFAVFGVMLFVPAGTFDYWQAWVFLVVVALSVWIPPIYLLRANPAALQRRMRGGPTAEGRVAQKVVIAGLYSSLAAMVVVSVLDHRFRWSPVPTALCLVGDVLVALGLGVVALVIVQNSYAASTVRVEAGQTVISTGLYGMVRHPMYTGNVIMLIGIPLALGSYWGLVFVIPGLIVLALRLRDEEKLLEEELKGYHEYTQTVRYRLVPLVW
>NZ_AP022569.1|WP_170308201.1|3174011_3180902_+|amino-acid-adenylation-domain-containing-protein
MYRTGDLVRWRADGQLQYLGRADEQLKIRGYRIEPGEIEAAMAALDGVEQAVVIAREDHPGVTRLVGYVTGTAEAATVRAALAERLPGYMVPATLVALTALPLTVNGKLDKRALPVPEYDDADRYRAPSTPAEEILAGIYAHVLGLERVGVDDSFFDLGGDSLSAMRLVAAINNDMGSGLKVRAVFEAPAVAQLALRIGADEDLLEPLVAVERPAVVPLSFAQSRLWFIDQLQGPSPVYNLAVALRLRGRLDPDVLATALSDVVGRHESLRTLFAAPDGVPQQSVIEREQADFGWQVVDATGWPASRLEEALGEAARHTFDLATEIPLRAQLFQVADDEHVLVAVAHHIAADGWSVAPLVNDLGTAYACRCAGRAPDWAELPVQYIDYTLWQRAQFGDLDDSHSRIGGQLGYWQQALAGMPERLALPTDRPYPPVADQCGATVAVDWPVELQQQVVRMAREHNATSFMVLQTALAVLLAKLSASSDVAVGFPIAGRRDPALDGLVGFFVNTLVLRLDLAGDPTVADLLAQARQRSLAAYEHQDVPFEVLVDRLNPTRSLTHHPLVQVMLAWQNLPGDSGHPTAAVPLGDLQVTPIPVDTRAARVDLSFSLAERWDMAGEPAGIGGAVEFRTDVFDAASIQTLVERLRRVLAAMTADPTQRLSAVDVLDRAEHARLEEWGNRAALTAPVSAPTSIPTVFAAQVRRAPQQVAVRWDGGSMSYLELDQASNRLAHWLIGRGVGPGRRVALVLPRSADAIVAIFAVLKTGAAYVPIDPAVPEARIAFVLDDAEPIAAITTAGLADRLDGHGLLVVDVDDPAVAGQPSTALPAPAPDDIAYLIYTSGTTGTPKGVAIPHRNVTRLLEVLDAELGMSAGQVWTQCHSLAFDFSVWEIFGALLHGGRLLMVPDSVVRSPEDFHALLVAEQVNVLSQTPSAFYALQTADRLSPELGRQLKLDAVVFGGEALEPQRLGAWLDSHPGSPRLINMYGITETTVHASFREILGGDVDSTVSPIGVPLAHLGFVVLDTSLQPVPAGVVGELYVAGAGTAYGYVGRAGLTATRFVACPFGNAGSRMYRTGDLVWWGADGQLRYVGRADEQVKIRGYRIELGEVQAALSELQGVDQAVVIAREDRPGDKRLVGYVTGTADPATARAVLAERLPAYMVPAAVVVLDALPLTVNGKLDTRALPAPEYQEGEQYRAPADAVEEILAGIYAQVLGLERVGVDESFFELGGDSILSMQVVARARAAGVVCRPRDVFVEQTVARLARVAGVASDAGEVIDEGVGPLPATPIICWLAGVDGPTDQFNQAVLVQAPVGVTEADVTTVLQALLDRHAMLRLRVDDDGAGGWSLTVPEAGSVDARACLQTVDALSDEAVVAARSRLDPTAGVMLSALWVVPTAQLVVIIHHLAVDGVSWRILLEDLNLAWAQHRTGQPVVLPTGGMSFARWASLLADHARRPEVVARADAWRQIAAVPAAALPAVQPAVDTYACAGNLSVELDTDTTRMLLGEVPAAFHAGINDILLIAFALACAEFLGTGSAPIVIDAEGHGRHDELAADVELSRTVGWFTTKYPVSLTAGGLSWAQVVAGEAGLGALIKDAKEQLRALPDPLTYGLLRYLNPDVDLEGSDPAIGFNYLGRLGATGVEASGDIWEIREDGYLVTGVALAIPMPLMHTVELNAGTVDTDTGPRLRAGWTWAPSALSHAQIDRLSRLWFDALTGICAHVRRGGGGLTPSDIAPAHLSQQQIDELCRHHQVADILALTPLQHGLLFHASIAPGSGDDVYAVQLDITLNGRLDPHRLREALNTVVTRHPHLVARFCPQFDEPVQVVPANPVAPWRYVELDPDGVDVEEQIQQVCAAERDAVFNLTDQPAFRAALIRTGEAQHRFVLTNHHIVLDGWSLPILQSELFASYYGQRLPAAVPYRRFIAWLAGRDREAARTAWREVLEGFETPTLVGPPDRLGLGRRAVTSSLVPEQTTRAIGELARSSHTTVNTVLQCAWAQLLVWLTGHHDVAFGAVVSGRPAEVAGADAMIGLLINTVPVRATITDATSTTDLLDQLHRAHNHTLEHQHLALSDIHHLTGQARLFDTVFVYENYPTDAATMSGADGLVVTELTNRDYYHYPLTIQAVPGRELDLRVQFRTDVFDTADIQAMMERLQQLLVAMTADPAQPLSSVDLLGDGKRWALQPATTTPESAPENHDDGVGDRPAASLVEQILAGVYGQVLAVDHVGLDESFFDLGGDSLSAMRVIAAINTTLDIDLAVTTLFEAPTIRRLSRQLGHADVARQVPTANPAGDL
>NZ_AP022569.1|WP_163777093.1|3168404_3170039_+|AMP-binding-protein
MRIADVLPLTPLQQGLLFHASTARGSGDDVYAVQLVIGLRGGLDAHRLRDALYAVVMRHPHLAARFSERFDEPVQIVPADPWVPWRYVDVGAEGGAVEDQIEQVCAAERAAVCELGDRPVFRAVLIRTGDDEHRFVLTNHHIVMDGWSLPILVGELFASYAGQPLAPAGPYRRFVTWLAGRDAATARAAWAQVLAGVDTPTVVGPPGRCGLGRRAVASCQLPGQLTEAVTELARSCHTTVNIVLHAAYAQLLMGWTGQHDVVFGTTVSGRPVELAGAESMVGLLINTIAVRATATATTTTAGLLDQLHHAHHHTLDHQHLALSDIHRLTGHEQLFDTLFVYENYPLDTTAALGIDGLAVTGYSTREYNHYPLAIQALPGPALTLRAEYDTEVFDPATIDTLLARFTALLGAMTTNPHTALSCIDVLDPAEHARLHHWGNQAVLTAPAPPAASIPELFATQVARVPHAVAVSDGQLSMTYRELDQAANRLAHLLIAHHAGPGQRVALLLPRTTHAIVAILAILKTGAAYLPIDPHYPTPDRFPAR
>NZ_AP022569.1|WP_163777092.1|3163867_3168418_+|amino-acid-adenylation-domain-containing-protein
MALNKSALPLTRGQLDIWLAQETGHSSIDWQLGVLVRFDGEIQPDLLTQAIRHVVAEAEPVRATIFEDDGQVFQRAVDDADVEVAFHDLSDTRHPVQEARAIAASIQQTPMPPSGPLFSFALFRTWVDEFYLFGCFHHIVVDGSGITLLAHRIATVYAAIVSGAPIPPAFFGSLQDLVRYESEYEGSAEYLDDEAYWAQNLAPESDPNYRLPNAAGKVDPHSPSAPVRLDPAVLRHVQELSETWNMPRSSVITAACALLVRGWCAESSEVVLDFPVSRRVRRESKTLPGMISGAVPLVLSVSPGATVAEFCAHVDTRVREALQHQRYPVHALERKAHPGRSDHRVNRVSINFMPSKMTMDFAGVEASASFTNPGQVGDFGLIFSGAGDQLFLSTAGAEGPFSNFDVADLARRLSRLLVAMTADPSRRLSSMDLLDDSEHAGLDGWGNRAALDQPTPAPVSIQTAFAAQVARVPEAVAITDGERSWTYREVEQAANRLAHLLVCEGVGPGQRVALLLERSAEAVVAMLAVSKTGAAYVPIDPSVPVARMEFVLTDAAPIAAITTAELRPRLDGHDLRVVDVNDSAVSAQPDTALPGPAPDDIAYLIYTSGTTGTPKGVAIPHRNVTRLLQTLDSDLELAGQVWSQCHSLAFDFSVWEIWGALLYGGRVVVVPDAVVRSPEELHALLVAEQVSVLSQTPSAFYALQTADALQPELGRQLKLQAVVFGGEALEPQRLTSWLQAHPGFPRLINMYGITETTVHASFREILGSDVDNVVSPIGVPLAHLGFFVLDAWLQPVPAGVVGELYVAGAGAAYGYVGRTGLTGTRFVACPFGGPGARMYRTGDLVWWGADGHLRYVGRADQQVKIRGHRIELGEVQAALSALDGVEQAVVIAREDRPGDKRLVGYVTGTTDPAVARTELAERLPAYMVPAVVVALDALPLTVNGKLDTRALPAPEYQDADHYRAPAHAVEEILAGIYAQVLGLERVGVDESFFELGGDSILSMQVVSRARAAGLVCRPRDVFVEQTVARLARVVEGAVTSVDEGIGPVVATPIMRWLASVDGPVQHFNQTTVVQAPAGATEADVVVLLQALLDRHAMLRLRAEDDGAGGWSFHVPEAGSVDARDCLLTVEALSDAAMLTAGSRLNPAAGIMLSAIWVTSTARLVSIVHHLAVDGVSWRILLEDLNIAWAQHHHGQQVELPAPGTSFARWSELLAEHASRPEVVQQAPAWRQVAATPAALPAVRPEVDTYANVGQLSMALDAEVTRVLLGEVPTAFHTGIHEILLIAFALACAEFLGTGAAPVGIDVEGHGRHNELAPDIDLSRTVGWFTTKYPVALAVGGLSWTQVVDGDAGLGALIKDAKEQLRALPDPLTYGLLRYLNPEVDLNESDPPIGFNYLGRLGAGAGESGDGWQISWDGLSNIDAGLRLPMPLAHTVELNAGIIDTDFGPFLRAAWWWAPSALDHAQVSRLGQLWFDALTGICANVRRGGGGLTPSDLAVGGLSQQQIDELERLYADR
>NZ_AP022569.1|WP_163777090.1|3163629_3163878_+|MbtH-family-NRPS-accessory-protein
MSINPFDDGDGSFFVLVNDEEQHSLWPAFAEVPAGWRVVYGEGDRAACLDYIEQNWTDIRPKSLREGLASRQGVSIGTPNGS
>NZ_AP022569.1|WP_163777088.1|3162643_3163495_+|methyltransferase-domain-containing-protein
MANGSEPAVAMSAHLADDLLSTTAGGWRNFYNLLSRRLEAVGVADSSFFLNYGYVPTDSDNESAFVIRDGTFNANSVRLVFEVIGSLDLNNRTVVEIGCGRGGNSRTVAEKFSAHVIGIDMSSEAIAFCEKTHVGSSIDFKVGDALNIPLGDAVCDAVLNIESSHSYGNLPKFLGEVRRICRTEAWFLHTDFLSPEDWDYVRMRLKALGFAVEDDRDITANVLASRDQASNNWEQVYGDGNPRVANFLALPGSAIYEQMRAGLLEYRILRSQLRAPTTSASTG
>NZ_AP022569.1|WP_163781845.1|3151628_3162578_+|SDR-family-NAD(P)-dependent-oxidoreductase
MGGGFAVVGYALRVPGAADADEFWEVLQQGRDAVSEVPADRWDVEEFFDPDPDAPGKIVSRRAGFIDDVAGFDAPFFGLSKRETMLIDPQHRLLLETAWRAVEHSGTAPSALANTQTGVFMGLGTHDYLGLISEQLSYAEIEAYVAIGTSAAAGAGRISYGLGLQGPAVTVDTACSSSLVAVHQACQALRFGECDLALAGGVNVLLSAKTAMTFSHAHMLAPDGKCKTFDAAADGYVRGEGCGVIVVKRLEDAIRDGDRIRAVIRGSAVNQDGASGGLTVPNGVAQQRVINEALQCAGVAAGDVNYLEAHGTGTSLGDPIEVQAAGAALGNGRDADQPLLIGSVKTNIGHLEAAAGIAGLIKVILSLEHEELPKHLHFQKPSPHIPWDRLPVRVVDQTLPWTRNGRPRIAGVSSFGFSGTNSHIIVQEAPEAAGQLAAAPSDDRRFSVLPLSARSPEALAELAQSYRDWLSDRPEASLADVCFTAGVGRSHLEHRAALVVNSTESAREALAALADDRPAPGLVRGECADKPRTAWLFTGQGSQYPGMARELFETEPVFAETMARCAAVVADVLERPLLDVIFETDGPDNQDTLRQTSYAQPALFAVEMGLARLWQSWGFEPDVVLGHSVGQYSAACVAGVFSLEDGALLMAERGRLFGSLPAGGRMVAIFAAAERVESLTDEFPSLSVAAYNGANTVLSGPSQDLEQAVARLEADGVRCDWLDTSHAFHSALLDPILDEFESYANRFEFGPPQRTLVCNRTGAALGRNAKLDGAYWRRHARQPVEFAKSVRTLADLHCTMLLEIGPQPVLTAAALRAWPDPATAPRAIPSLRKNTADLRQITEALANAYIVGHVPDFGALQQAPARKLDLPTYPFQHRQYWFREQRVKHVQAPDETHAMRTDTVRLLEDGRIDELAALLDGASANEQALDLLKQLAAQHNQQRNAQSITDSRYEIRWEKSAATPAKAPAAQGDEPAWLLISDDAEAVQPLVDALTARGQRHRILRLPASDADEQRLEAELRESASDDLRILNLAALDSGAAPSTESLERMQFHVLSGTRRLFRAAAAAELRAPIWLITHGAQRVTGADSVSPVQSCLWGFGRAASLEHPRLWGGLADLSGGGIDEWSRLIDQLVSAPRGEDQIALRDQAVYVARLTRRTGQPIATPLQLRYDATYLVTGGLGAVGMEIAGYLATHGARHLVLTSRRAPSEAAQQRIDALQEQSGCAVRVVTADVASPRDVARLLATVQAELPPLAGIVHAAGEIGTTPLQDLDDAEIDRVFSGKVWGAWRLSEATADLPLDFFLSTSSIASVWGSFGQTAYGAANAFLDGLAWRQREHGVPGISVNFGPWAAAGMADEDARAHLDKRGVRTLSPADALAGMAELMQASSGRGATNGIVAKIDWPSFLPLYQLTGKRSFLEQLQREVPQSASAPTSAGATRLVERLTNAPVQQRKKLVVDYLRDVVAEVTRIDAAEIRDEAGFFAVGMDSLMAVELRTRVERAVGKELPATLAMDYPRLVDVADYLLDDVLSISAPAAATAPAQPNPVMTTRSDEPIAIVALACRFPGAPDPEAYWDLLAGGVDAIREIPDDRFDVDEYYDPDPEAPGKIYTRYGGYLDSIDGFDPEFFGISPREAVWMDPQQRLMLEIAWEGLERAGYSPASLRGSRTGVFVGVAANEYSQLLNANSVETIEAHFITGNALNVIAGRVAFALGLEGPAMAVDTACSASLVAVHQACQALHSGDCDMALAGGVNVLVSPASIVATSRARMLAADGRCKTFDAAANGYARSEGCGILVLKRLSDAEREGDQICAIIRGSAVNQDGASSGLTVPNGGAQQRLIAATLARAGVEGRDVDYLEAHGTGTSLGDPIEVQAAAAVYGAGRDSDRPLLIGSAKTNIGHLESAAGIAGLIKVVLSLQHEMLPQNLHFENPSPNIPWDSLPVRVVDKQIPWHANGRPRRAGTSSFGFSGTNAHVLIEEAPHSDDAAAAREPDTTAEPVGVLPLSARSPEALVSLAQRYATWLEAHPDVDITDMCFTAGVGRSHFEHRAALVVDSVQGARELLSGLAENRLGPGAVRGVCGDPPKTAWLFTGQGSQYPDMARELFDSEPVFADTVKQCADAVDGMLPRPLLDVLFDLDGDTGEPGKGLGHTSFAQPALFAVEMGLARLWQSWGIEPDVVLGHSVGQYAAACVAGVFSLEDGARLMAERGRLFGDLPEGGRMVAVFADPRQVERAAEDFPQISVAAYNGPNTVLSGPATDLEKIVATLSADEIRCTWLDTSHAFHSELLEPALDEFESYAKGFEFAVPTLPLVCNRTGAVLTAETPLDAQYWRRHSRQPVQFAESVHAVAKLGCSVLMEIGPQPVLTGAALQAWPDSSAAPRAVVSLRKGTDAQRQMAEALAAVYVAGHRPNFAALQHHRQHALELPTYPFQRRRFWPKTSDFRVDGPAVSGILGSVKDLASGDAVYTSRWSIKSQPWLSHHVIYGTVVVPGATYATMALAAVGTPAQVRNVFFYEPIILGDKTSREVQLTVHPVAEEGGWTFQVHSRPYGERDAEWSLNADGRVVSGLDDEPAPEPTESIDAACERLGRTRPQQLFDTFADMELMWGPTWSTSLKSLWAGDGEAVGDIAIGDELAEQLGTEPIHPVLLDLCTGIAFPAFPAVLTAAETGVPDLFLPLRYGRVVLREKLPKRFYCRARWQSGGTESETQVFDLDFVDRDGRQLGEIREFTVKRAPREALLRGLGGDATRNLYTFGWQEVAPPASGSTAGIADGTWLIAGFDELVAKHSGFVAVDHATDPELWKRLFTQAEEGGAPVSGVVWRSAARPGVEESSTDFTARLESEIDQLLTVVHTLQSQHDVKLTGGLWIVTERAVATEPGEPVDPVQSALWGFGRTVITEQPALRCRLVDCDSFEDAGQLLAGLLGTPAEEPELALRQGKYLVPRLLPWARSGHLPIPRATDYILEPTERGAIDNLHLVETAVAPPSAGQVQIRVEAAGLNFRDVLNVLGLYPGDPGLIGGDLSGIVTEVGEGVTGFEVGQRVFGFMQGCFTTRVNVPAQFLSPLPNGVSAVGAATIPAGALTTRLAFDWAQVGPGDRVLIHAASGGVGLAAIQIAQQRGATVFATASTYKRATLRKMGVEHVYDSRSTDFADQILADTGGAGVDVVLNSLTNEGFIAATVRATAQGGRFAEIAKRDIWTPDQMAAVRPDIAYEIVALDATIEEEPERVGKLLAELADSMGRGELLPLAAEVYPLTEAKTAFRRMQQARHIGKIVLQMPKPLQPKGDRSYLITGGLGALGLFTAAHLAQLGAGDIVLTGRHLPDADAQREIDDITERYRCRIHTFVADVGDEQQVAGLLERIRAELPPLAGVAHLAGVLDDALLSQQSLDRFQTTLGPKALGAWHLHRLTKNDDLEFFVVYSSASSVLGSPGQANYATANALLDGLVADREAQGLPAAGINWGPWAKGGMATSHAARANLSAQGLIPLEPSAALNALDEVLAHGITQATVIKANWQRAAKGLGGSRPSILDHVLPSAGAATHGDSELLRQLHEVPEMERGSFLTEYLRHEVQNFLRLAQPPAATSRFLELGTDSLMAVEFSNRLLPQFGGAFTISATAVFDYPTIGSLAEYLAGQVPESAGAETVDASESTQ
>NZ_AP022569.1|WP_163777085.1|3149929_3151216_+|glycosyltransferase
MKFVLASWGSRGDVEPNLAVGRELVRRGHDVCMAVPPDLVDFTEAAGVPAVGFGPEARSILDSHREFWTCFFSHPWRVRKLVRSRLDIAAPLLRGWQEMSTTLMSLADGADLLFTGINFEDAAANVAEHYDIPLATLHYFPLRPNGQTLRFLPAPLARAAVAAFWWVTWRGMKKAEDAQRRELGLPKATGSAPRRITERGSLEIQAYDEACFPGLAAEWAKWDCQRPFVGTLTLELATAADDEVASWIAAGTPPIYFGFGSIPVESPSDTIAMIAAACARLGERALIGAAGTDFGNVPHFEHVKVVGTMNYATVFPACRAVVHHGGSSTTPIAMRAGVPQLILFWDMVHAVYGAAVKRLKVGSARRFSTATEEALVHDLRLILGPDYVSRARELATRITEPAKSAAAAADRLEDFARLARTGRTERSV
>NZ_AP022569.1|WP_163781842.1|3147535_3149722_-|acyltransferase-family-protein
MRQADSISPAQDLRGRRSEQKRFRPDIEGLRAVAVLAVVLFHAEVPGVGGGYVGVDVFFVISGFLITGLLWREANTTGTVRLRSFYGARARRLLPASATVGVVTMGASVVLLPALQVKSVIWDGITSALYVGNYWFIMRGVDYFASHKALSPFQHYWSLGVEEQFYLVWPALIIGTAWLIRRVRRRTRAEATSSQRPYLVVLALTAVVSFALSLAATPLAPPVAFFSLPTRAWQLAIGGLVALTVGRWQRLSPRAGAITGWAGLALILLACGGLSSATLYPGIAALLPTVGAALVIAAGCASPEGGCGRVLGLSPMRAIGRISYSWYLWHWPVLLLVPALLGHPLGLAARVAAALLAGGLALLTLRFIENPLRFAAPIRRSPGRSLALGGAATAVAVCVGLALLHVVPTPIGRGTPAAALKVTTAPVPAGAGLAAYDAAAQRAVAQVQAAVAASVDIKAVPSNLDPSFADVEAEQKAYMGSGCLRTPTQGGQPECATGDTESTTTVAVVGDSHAAIWNPAFKQAAADRHWRLETLAKAACPLMDLRVTNSFRPLVELLEHCEQWRAEIMTRLRAEHPRLVVVSAFRGYGADESMTGFNAYDPTWIDGLTRIVQQLRSIGAKVLVLGPVPDPHFDVPTCLSAHLDDVTACLPRRSKAVNESGIAAESAAAKAGGGQYADVTDLFCTADRCPVIVGNTLIYVDSSHLTFEYSRLLAPVMGALADRALAHG
>NZ_AP022569.1|WP_163781847.1|3196288_3196612_+|hypothetical-protein
MQTGGSPNAPGAAITVALCGGWDHPPPCPLAPHYVSNVRTGETVTLRVLFATEAENEARVRALIGGALETGRLTGPDGEVATWQLRSASPGEIRADEREHAAHLVAH
>NZ_AP022569.1|WP_163777102.1|3196923_3198741_+|FAD/NAD(P)-binding-protein
MIEMAIVGLGSWGLCVMERTVSRARQVGKPVRLHLIEPAQLGGGVYSAEQPDFLVLNNACGQLSLYAAPDGDALPPYAVGLHPWAVVRGYRWVGYECRIGAGGDPILPTDYLPRRLMGEYLAWFYDTLVSYAPPNLEIVRHYAAAVDISPALHGHEAVLLDNGATLTVDHVVLTSGHTWNDEAGADGGVRYLRPYPIDYLDQCAPAGSSLAVAGMGLVGFDVLAALTIGRGGTFEGRSDRSDRLRYVPSGHEPTITLYSRSGAPYCAKSATGVDPYGQYQPVVCTPEEFTALTHPGGSPLRRHVDFRAELLPLVFAEMQARYYIQCAILAGGDGAASEVRTVLRQGWVDGYYEKAVDVLEPRYGRFDPAAHLFAGSDRHYTSAADYQAQVYDMIDDDLTEALRPGGSPVKAAQEVLRILRDQLRSVIEFGGLSLDSYVEFQANVRGRINRLEAGVPPMRSQQLLGLLDAGVVRIPLGPGPKAAACPDGVRLSSTALDEPTAMTADGVVRGYLDMPSLARSGSPLLNRLYAKGRLTQLSYGDTPVGSVAINEEFHPYDTEGRLQPKLSVLGVLTEGVRYFTHYLPSPRSRLRAVYDAQACVEAVIG
>NZ_AP022569.1|WP_163777104.1|3198745_3200029_+|hypothetical-protein
MTDTESLMTGRAQPLVAVGYGPRCVPVMQLAEAAAGICDLLWMIDTAVPGMSEMTDLLNRFGPVVDLKGMTVEQTFKTLADWAPDGMTTYLDAGMVELAYVAEDLGLPFHSPATAAALTDKARQRQALADAGLDMPACHLVRPYQSERELSAIEAEVGWPAVLKPRSAQGSRCTFLARDRAELANLLVALGPNRRDMVLEGYLLDDPARAGEPYAGYVSVESVVADGVISHLALTGRFPPAENFRETGFFIPAALDADSRWAVLKLATRAIEALRVRTGCLHTEVKFTPDGPRIIEVNGRVGGGVPEMLERAAGVKLLDLTLRVALGEPVSVDGPVATERIGYRFFLQPPTVSATVTAIEGINDFTDRAEVDTVSVHQGPGAALDWRDGSGNHIVAVVGSTDDEEQLQAAYRLLHQEVTVTYADVRY
>NZ_AP022569.1|WP_163777106.1|3200030_3200963_+|homoserine-O-succinyltransferase
MGIQLADGPAQWTCALVNNMPDAAFCATERQFISLLDGGSGCRTVGVTRYAMAGVPRGERIRTHIAAEYRPFEDIFSDPPDLLVVTGANPLESRIEDEAYWSDLHGLLKWASEHVRTMVLSCLSAHAALAVFDGVERTVLPEKCTGVFAQQADQSHPLAAGFGGPVLLPHSRHNAVPVDTVVAAGYAVALQSEAAGWSVVTRTVGQSDVVLVQAHPEYDPTSLVREYLRDARRYVSHERDEPPCLPRDCLVGADWHRLRLLHKKVVGDRNPDLLDAFPFDQVAAHAPWQWRGTALRLYANLLATIPMRSV
>NZ_AP022569.1|WP_163777108.1|3200967_3202254_+|aminotransferase-class-V-fold-PLP-dependent-enzyme
MHDETIAIHGGYTPDGTRAVAVPIYQTVAHDFIDAAHAGAVLDLETPGFHYNRLNNPTLDVLEQRICALEGGTAALVVASGMAAVSYAILTVASAGSNIVVAPQLYGATFTYFAHVLPTLGIEARFAVDDRAESIAPLIDDNTRAVFCETIGNPAGNVVDLEAVAAVAHASGVPLIVDNTVATPLMLKPFEHGADVVVHSLTKFVGGHGTTLGGAIVDGGRFPWADHPDRFPMFNQPEPAFHGVVFARDFPERPFTVRARSTQLRNSGATLSPFNAFMLLQGLETMALRLERHEANARAVAEYLAADPRVAWVSFAGFPDHPYHHLVERYLHGRVPSIITFGVTGGYDAGLAFFDALLLVKRLLNLGDAKTLAIHPASTTHRQLSDDELVKAGIKPETIRLSIGIEHIDDIIDDIDQALAKATVGHID
>NZ_AP022569.1|WP_163777110.1|3202396_3204061_+|hypothetical-protein
MDSARLHRILADGLARRGFAVLHFDYLGLGDSAYAQDRDDAVANWVASVGHALDYLTLVGAQSTTAIGIRAGCLIVDEYLNRSHTVNRVVLLDPPGTGRRYLREHTALFRLSVGEDAVTAGEVSIMGGRLTDHAAGEFAALQLSANPVSTHGVDNVLLVGRPAETDRRVTALASSEGVDSIVSEGLPDCARPRDMLLPIPYAAVDSIVEWIDRHVSNGTHRAVPQYLDTVTMPADGPDGVDVIERIERIGPNGLFAIRTLPRRRSAAPARTVLFFVTAKDFHVGPAREWVELSRRIAASGAQAMRWDPAGMGLSGRIHRDPYRFVFTKADITDAIAVARHACHDVAELELVGICSGSWYAAQVVRNVGARSAILVNLVAWSWRITPNWLSQWDIRRKALRANAPRDTGGSHLGSWTARLRAPLAPARGATKSFMHNHLPRSVLHVLSWIGLVYLPESVLTTLVRRGTDLTLIAAPEDTEHFLARGGQGALDRLQETPQPPRRIAIPTGDHGAHHPMILAAIRNAVLPAMDAATAEDREILWCPDEISAREVRAG
>NZ_AP022569.1|WP_163777112.1|3204070_3204544_-|4'-phosphopantetheinyl-transferase-superfamily-protein
MPRARAVNPPKPAPPSVFPSEIDGRRVRVGCDIVAMEDVEGSLAAFGDRYLRKIFTPSEIDDCRGRNRVHSLAARFAAKEAVIKAFAEPEMPFPWREMEVTRDGPLPRLRLSGALAERARGQGWLSSSLSLSHADCHAMAVLLVVCGPVVSSANGPR
>NZ_AP022569.1|WP_163781849.1|3204543_3204789_-|acyl-carrier-protein
MLDQIRDVLSAHGRMAIDPREVDDQADLYELGLTSHASVDVMLALEDAFDIEFPEEVLKKSTFASIHNIAQVVEGLVKAPA
>NZ_AP022569.1|WP_163777114.1|3204826_3205738_-|phytanoyl-CoA-dioxygenase-family-protein
MPTAVRTVGSDCAPADVAEVLKEDGCVVIADLASAETMDQIRAEIAPYLAVTCGGNTDFLGEVTQRTGALIARSPSARPLIAHRTIIDTLDLVLGDHASTFQIDLTQLVTIGPGEPAQMIHRDQWAFDRYRFPMGFEAEVGTMWAVTDFTEEMGATRMVVGSHRWEDDPDDVDFELSAPAIMTKGSVLMYTGSIFHGGGANTTEVSRIGMNVGYSLGWLRQEENQYLACPPEIARTLPEGLLRLMGYQRGSYSIGYVDDMREPLDWLYDSPAYISDFYGYRRVARKRLRATGTYVPPAAPDTN
>NZ_AP022569.1|WP_163777116.1|3205830_3206760_+|TIGR03621-family-F420-dependent-LLM-class-oxidoreductase
MPSTLPFRFGVLAEVTPTMSAWRDQARMAESLGYSTLYISDHLDAQFGPLVAATVAAEATSTLHVGFGVLNNDLRNPVVVAKEIATLGLAAEERVEVGFGAGWLRSDYEQAGIAYDKPAVRVDRLAESLAVMKTLWSEGKSTYTGTYYTVQDARCDPRPALPPRVIVGGGSKRILTVAAEHADTVGVNTSLASGVKGGDLASQASFEHFDRCLSWVRDGAGDRFNAIELQIVAFATRVVASQRAAARTATMLGFPGEDALELPIVLIGTEDELCERLLKRRERWGFTNIVIGAEAMESFAPVVARLAGS

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Crispr_ID: NZ_AP022569_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP022569_5

5196112-5196257

Orphan

Consensus_repeat	Method
TTCGGCAACGGCGGTGACGGGGG	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_AP022569_5

>merge|NZ_AP022569|5|5196112-5196257|CRISPRCasFinder
TTCGGAGACGGCGGCAACGGCTGGGACAGCGACCAGCCCGACGTCGGCGGCGGCAACGGCGGCGACGCGCTCGGTTTCTTCGGCAACGGCGGTGACGGGGGATCGGGCGGCGCGGGAGCGGCCGGCGGTGACGGCGGTGGCGGCGG

>NZ_AP022569|5|5|5196112-5196257|CRISPRCasFinder
TTCGGAGACGGCGGCAACGGCTG	GGACAGCGACCAGCCCGACGTCGGC
GGCGGCAACGGCGGCGACGCGCT	CGGTTTCTTCGGCAACGGCGGTGACGGGGGATCGGGCGGCGCGGGAGCGGCC
GGCGGTGACGGCGGTGGCGGCGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP022569.1\|WP_163782300.1\|5187562_5187880_+\|DUF3349-domain-containing-protein	unknown	unknown	gnl\|CDD\|371747
NZ_AP022569.1\|WP_163780929.1\|5197828_5198797_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|369777
NZ_AP022569.1\|WP_163782298.1\|5185860_5186823_+\|class-1b-ribonucleoside-diphosphate-reductase-subunit-beta	unknown	unknown	gnl\|CDD\|275027
NZ_AP022569.1\|WP_163780922.1\|5190298_5192044_+\|cytochrome-c-oxidase-subunit-I	unknown	unknown	gnl\|CDD\|238832
NZ_AP022569.1\|WP_163780937.1\|5203069_5204452_-\|PQQ-binding-like-beta-propeller-repeat-protein	unknown	unknown	gnl\|CDD\|224437
NZ_AP022569.1\|WP_163780939.1\|5204450_5205188_+\|acetyltransferase	unknown	unknown	gnl\|CDD\|100053
NZ_AP022569.1\|WP_163782304.1\|5193320_5194178_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224044
NZ_AP022569.1\|WP_163780918.1\|5187868_5188909_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	unknown	unknown	gnl\|CDD\|176186
NZ_AP022569.1\|WP_163782306.1\|5198730_5199963_+\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|380115
NZ_AP022569.1\|WP_163780916.1\|5186838_5187384_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP022569.1\|WP_163780920.1\|5189038_5190127_-\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|238566
NZ_AP022569.1\|WP_163780931.1\|5200911_5201763_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP022569.1\|WP_163782302.1\|5192075_5193305_+\|phosphoserine-phosphatase-SerB	unknown	unknown	gnl\|CDD\|319803
NZ_AP022569.1\|WP_163780943.1\|5206541_5207024_-\|tryptophan-rich-sensory-protein	unknown	unknown	gnl\|CDD\|320706
NZ_AP022569.1\|WP_163780941.1\|5205184_5206525_-\|deoxyribodipyrimidine-photo-lyase	unknown	unknown	gnl\|CDD\|223492
NZ_AP022569.1\|WP_163780945.1\|5207117_5207630_+\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224759
NZ_AP022569.1\|WP_163780933.1\|5201938_5202649_+\|DUF3298-domain-containing-protein	unknown	unknown	gnl\|CDD\|378702
NZ_AP022569.1\|WP_163780935.1\|5202645_5203032_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP022569.1\|WP_163780925.1\|5194992_5195682_+\|enoyl-CoA-hydratase	unknown	unknown	gnl\|CDD\|235632
NZ_AP022569.1\|WP_163780924.1\|5194177_5195005_+\|NUDIX-hydrolase	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP022569.1\|WP_163782300.1\|5187562_5187880_+\|DUF3349-domain-containing-protein	gnl\|CDD\|371747	pfam11829, DUF3349, Protein of unknown function (DUF3349). This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 99 to 124 amino acids in length.	8.3964e-34
NZ_AP022569.1\|WP_163780929.1\|5197828_5198797_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	8.43686e-28
NZ_AP022569.1\|WP_163782298.1\|5185860_5186823_+\|class-1b-ribonucleoside-diphosphate-reductase-subunit-beta	gnl\|CDD\|275027	TIGR04171, ribonucleotide-diphosphate_reductase_subunit_beta, ribonucleoside-diphosphate reductase, class 1b, beta subunit. Members of this family are NrdF, the beta subunit of class 1b ribonucleotide reductase. This form uses a dimanganese moiety associated with a tyrosine radical to reduce the cellular requirement for iron. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism].	0
NZ_AP022569.1\|WP_163780922.1\|5190298_5192044_+\|cytochrome-c-oxidase-subunit-I	gnl\|CDD\|238832	cd01662, Ubiquinol_Oxidase_I, Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.	0
NZ_AP022569.1\|WP_163780937.1\|5203069_5204452_-\|PQQ-binding-like-beta-propeller-repeat-protein	gnl\|CDD\|224437	COG1520, COG1520, FOG: WD40-like repeat [Function unknown].	4.74503e-23
NZ_AP022569.1\|WP_163780939.1\|5204450_5205188_+\|acetyltransferase	gnl\|CDD\|100053	cd04647, LbH_MAT_like, Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.	9.53247e-37
NZ_AP022569.1\|WP_163782304.1\|5193320_5194178_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224044	COG1119, ModF, ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion transport and metabolism].	3.48352e-113
NZ_AP022569.1\|WP_163780918.1\|5187868_5188909_-\|alcohol-dehydrogenase-catalytic-domain-containing-protein	gnl\|CDD\|176186	cd05283, CAD1, Cinnamyl alcohol dehydrogenases (CAD). Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.	0
NZ_AP022569.1\|WP_163782306.1\|5198730_5199963_+\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|380115	pfam18096, Thump_like, THUMP domain-like. This is a domain of unknown function found in bacteria.	5.96233e-17
NZ_AP022569.1\|WP_163780920.1\|5189038_5190127_-\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|238566	cd01146, FhuD, Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.	7.98596e-49
NZ_AP022569.1\|WP_163782302.1\|5192075_5193305_+\|phosphoserine-phosphatase-SerB	gnl\|CDD\|319803	cd07500, HAD_PSP, phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p. This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. 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.	3.78857e-89
NZ_AP022569.1\|WP_163780943.1\|5206541_5207024_-\|tryptophan-rich-sensory-protein	gnl\|CDD\|320706	cd15904, TSPO_MBR, Translocator protein (TSPO)/peripheral-type benzodiazepine receptor (MBR) family. This family contains tryptophan-rich translocator protein (TSPO), an integral membrane protein that is highly conserved from bacteria to mammals. In eukaryotes, it is mainly found in the outer mitochondrial membranes of steroid-synthesizing cells of the nervous system where it transports cholesterol into mitochondria. It is known to be highly expressed in metastatic cancer, steriodogenic tissues, as well as inflammatory and neurological diseases such as Alzheimer's and Parkinson's. TSPO is also known as the peripheral benzodiazepine receptor (MBR) and its ligands include benzodiazepine drugs, implicated in regulating apoptosis. In human, a single polymorphism A147T is associated with psychiatric disorders; the mutation causes structural changes in a region implicated in cholesterol binding. TSPO is homologous to bacterial tryptophan-rich sensory proteins, and their tryptophan residues are believed to be functionally important. In bacteria, TSPO acts as a negative regulator of expression of specific photosynthesis genes in response to oxygen/light; it catalyzes a photooxidative degradation of Proto porphyrine (PpIX). R. sphaeroides TSPO (RsTSPO) is involved in porphyrin transport, similar to human, while Arabidopsis translocator protein (AtTSPO) is regulated at multiple levels in response to salt stress and perturbations in tetrapyrrole metabolism.	2.34723e-35
NZ_AP022569.1\|WP_163780941.1\|5205184_5206525_-\|deoxyribodipyrimidine-photo-lyase	gnl\|CDD\|223492	COG0415, PhrB, Deoxyribodipyrimidine photolyase [DNA replication, recombination, and repair].	2.8802e-141
NZ_AP022569.1\|WP_163780933.1\|5201938_5202649_+\|DUF3298-domain-containing-protein	gnl\|CDD\|378702	pfam11738, DUF3298, Protein of unknown function (DUF3298). This family of bacterial protein C-terminal regions is highly conserved but the function is not known. Several members are annotated as being endo-1,4-beta-xylanase-like, but this could not be confirmed, and the structure can be defined as a heat-shock cognate 70kd protein 44kd ATPase.	2.16901e-13
NZ_AP022569.1\|WP_163780925.1\|5194992_5195682_+\|enoyl-CoA-hydratase	gnl\|CDD\|235632	PRK05869, PRK05869, enoyl-CoA hydratase; Validated.	1.83966e-106
NZ_AP022569.1\|WP_163780945.1\|5207117_5207630_+\|MarR-family-transcriptional-regulator	gnl\|CDD\|224759	COG1846, MarR, Transcriptional regulators [Transcription].	5.33589e-14

>NZ_AP022569.1|WP_163780925.1|5194992_5195682_+|enoyl-CoA-hydratase
MAALTEFVSVHLSADRPGIGTLVLSRPPTNALTRQVYREIAHAAAEVGGRDDIATVILFGGHEIFSAGDDMAQLRTLAAPEAESWLAVHREAVDAVAAIPKPTVAAITGYALGAGLGLALAADWRVSGDNVRYGATEILAGLVADGDGIARLARTVGTSRAKELLYSGRFFDAKEALALGLINEMVAPDDVYDAAAAWAGRFVDGPRDALAAAKAGVDAAFELPAADTT
>NZ_AP022569.1|WP_163780924.1|5194177_5195005_+|NUDIX-hydrolase
MTDEPLVPLPVRPAATVMLVREDAQGAEGLEVFLMRRHAGMEFAAGTVVFPGGGVDDRDRNADIAWAGPPPSWWAERFGTDVELAEALVCAAARETFEECGVLFAGPADDPNGIVSDASVYRESRLALADRTLSFADFLRRENLVLRADLLRPWANWVTPEAERTRRYDTYFFVGALPEGQRADGDNTESDRAQWATPQAAVAEFEAGRCFLLPPTWTQLDSLNGRTVADVLAVERQIVTVQPNLEIDGDNWIFEFFDSDRYHRARKAGGLGWRH
>NZ_AP022569.1|WP_163782304.1|5193320_5194178_+|ATP-binding-cassette-domain-containing-protein
MRHDGRVADQTSEAVDPDLLIDFTDVSLRRDGHTLVGPVTWSVELDERWVIIGANGAGKTSLLRIAAAAEHPSSGVAYVLGERLGRVDMSELRSRVGLSSSALAQRIPGNEVVRDLVVSAGYAVLGRWRERYEDVDYHRAVDMLESLGAEHLADRTYETLSEGERKRILIARALMTDPELLLLDEPAAGLDLGGREELVSRLADLAADPDAPALVLVTHHVEEIPPGFSHCMLLAEGEVVAAGLLSDVLTSDNLSATFGQSIVVDVMDGRYFARRTRTRAAHRRR
>NZ_AP022569.1|WP_163782302.1|5192075_5193305_+|phosphoserine-phosphatase-SerB
MPHKVSALITVTGHDKPGVTSALFGVLSGYKVELLNVEQVVIRGRLTLGVLVSAPAEVAGGKAFHDDVEAAIHGVGLDVTIERSDDLPIIREPSTHTIMVLGLPITAEAFGAVAREVAALGVNIDLIRGVSDYPVTGLELRVSVPPGVGGQLQEVLTQVAADAGVDVALEDYSIARRAKRLIVFDVDSTLIQQEVIEMLAARAGAEEAVAAITEAAMRGELDFAESLHQRVGTLAGLPAEVLDEVAEDVTLTPGARTTLRTLRRLGYHVGVVSGGFRQVIEPLAHELMLDFVAANELEVVDGKLTGRVVGAVVDRAGKAKALRDFAHQVGVPMAQTVAVGDGANDIDMLSAAGLGIAFNAKPALREVADASLSHPYLDTVLFLLGVTRGEIEAADALDGVVRRVDIEPD
>NZ_AP022569.1|WP_163780922.1|5190298_5192044_+|cytochrome-c-oxidase-subunit-I
MTAEAPPLGELEASRPYPARTGPKGNLIYRLITTTDHKLIGIMYCVTCFVFFFIGGLLALLMRAELAAPGLQFLSNEQYNQLFTMHGTIMLLFYATPIVFGFANLVLPLQIGAPDVAFPRLNAFSFWLFLFGAMIGMAGFITPGGAADFGWTAYTPLTDAIHSPGAGGDLWIVGLIVAGLGTILGAVNMITTVVCMRAPGMTMFRMPIFTWNILVTSILVLLAFPLLTAALFGLAADRHLGAHIYDSANGGVLLWQHVFWFFGHPEVYIVALPFFGIVSEIFPVFSRKPIFGYTTLVYATLSIAALSVAVWAHHMFATGAVLLPFFSFMTYLIAVPTGIKFFNWVGTMWKGQLTFETPMLFSLGFMVTFLLGGLTGVLLASPPLDFHVTDSYFVVAHFHYVLFGTIVFATFAGTYFWFPKMTGRLLDERLGKLHFWLTFIGFHTTFLIQHWLGDIGMPRRYADYLPTDGFQPYNVVSTIGAFILGVSMLPFVWNVFKSWRYGEVVTVDDPWGYGNSLEWATSCPPPRHNFTELPRIRSERPAFELHYPHMVERIRAEAHVGRAHGPTDGDVTRADDVNVRS
>NZ_AP022569.1|WP_163780920.1|5189038_5190127_-|ABC-transporter-substrate-binding-protein
MLLRGTRPAITAVAAAALATALCSGCTSGSPPHGTAASVITSTTQIAGAGVLGNQRRPDESCAPEPAAPDAGPHVAHNAAGVQPDTVQVPDDPQRIVVLSGDQLDALCALGLQSRIVGAALPDGSPDQPSYLGTIVHKLPGVGTRRSPDLAAIKAAKPDLILGSQALTPTLYSALAGIAPTVFTGAPGAAWQDNLRGVGEATARGDAVGGLVDGFTAKAHDDGATHDAAHYQASIVQFTENSVRVYGSDNFPASVLATVGVDRPAAQRFTDKPYIAVASSDADLAHADFSAADADLVYVSFDSAAAKDRASSLFDSDPWRRLSAVRDNRVFVVNNEIWQTGCGLIAARGIIDDLRWINAPIN
>NZ_AP022569.1|WP_163780918.1|5187868_5188909_-|alcohol-dehydrogenase-catalytic-domain-containing-protein
MSTVSAYAASDKTGHLTKTTIERREPGPHDVAIDIKFVGICHSDIHTVKAEWGTPNYPLVPGHEIAGVVTAVGAEVSKHKVGDHVGVGCMVNSCGHCSSCTAGLEQYCKNGATFTYNATDKDGTITQGGYSQAVVVDENFVVQIPDSLPLDKAAPLLCAGITLFSPLRHWQAGADTRLAIIGLGGLGHMGVKLGAAMGADVTVLSQSLKKMEDGLRLGAKHYYATADRDTFKKLRSSFDLILNTVSANLNLGAYLNLLDVDGTLVELGIPEHPMEVPAFPLALARRSLSGSNIGGIAETQEMLNFCAEHDVTPEIEVIAADYVNEAYERVLASDVRYRFVIDTSTI
>NZ_AP022569.1|WP_163782300.1|5187562_5187880_+|DUF3349-domain-containing-protein
MIQWLQVGYPDGVPGPDRVALLALLRSTPLSEDEITEVVDAIDEERDHEPIDRDVIADFISDMTHYDAGPENISRVAARLAAAGWPLTGITLGDAETTASHSSNG
>NZ_AP022569.1|WP_163780916.1|5186838_5187384_+|hypothetical-protein
MRLRLILQPAWLRFTVWAAFLAAWWALFTSLQAGNELESTVLSAIVFGGALGAYLTVATQGMHRAALVAVSGLNQSERSEAINAVLRGPPPADPDVRASAARLGRAYLRNKSPIQLRCTQIWSWITIAALIAAGIAGAVAFSDDRLSFVVLVVLAAAVLPLSLIDARRVQRNVEQLARAQA
>NZ_AP022569.1|WP_163782298.1|5185860_5186823_+|class-1b-ribonucleoside-diphosphate-reductase-subunit-beta
MKLIDRVSAINWNRVQDEKDAEVWERVTGNFWLPEKVPVSNDLPSWGTLTEVEKQLTMRVFTGLTLLDTIQSTVGAISMIPDALTPHEEAVLTNFAFMESVHAKSYSSIFSTLCSTAQIDDAFRWSEENVNLQRKAQILVDYYRGDEPLKRKVTSTLLESFLFYSGFYLPMYWSSRAKLTNTADLIRLIIRDEAVHGYYIGYKFQRGLALATEAERADIKDYTYELLFELYDNEVEYTQDLYDEVGLTEDVKKFMRYNANKALMNLGYEALFPRDETDVNPAILSALSPNADENHDFFSGSGSSYVIGKAVNTEDEDWDF
>NZ_AP022569.1|WP_163780929.1|5197828_5198797_+|methyltransferase-domain-containing-protein
MTSTDPAPQPHATAEQVEAARLDSKLAQVLYHDWEAESYDEKWSISYDQRCIDYARSCFDGIVPDDEFQRLPYDRALELGCGSGFFLLNLIQSGVARRGSVTDLSPGMVKVATRNGQALGLDIDGRVADAEHIPYDDDTFDLVVGHAVLHHIPDVELSLREVMRVLRPGGRFVFAGEPTTVGNQYARRLADLTWNLTIRAVKLPGLGGWRRPQAEIDENSRAAALEWIVDLHTFSPADLEKMATRAGAVDVDTATVEFTAAMLGWPVRTFESTVPPGKLGWGWSRFAFGSWKTLSWVDANIWRHVVPKGWFYNVMITGVKPS
>NZ_AP022569.1|WP_163782306.1|5198730_5199963_+|class-I-SAM-dependent-methyltransferase
MASRGAERLVLQRDDHRGQAVLKFSLEDVAYLTSDEGSVALAAVEARPLTDRVSEIASLRTQFGDRTPVLVETVLLRRRAIAKLTELPGSAGWLLTDDALQQASAAMVALHRARRLQGNMIHDVTCSIGTELAALRAESVSAVGSDIDPVRLAMARHNLRDNTLLCRADALRPVTRGAVVLADPARRSGARRRFDPRAYQPALDALIDAYRDREIVVKCAPGIDFDAVARLGFDGEIEVTSYRGSVREACLWSAGLAEPGVRRRASILDRGEHFTDAEPDDCPVRAPGRWIVDPDGAVVRAGLVRHFAARYGLWQLDPHIAYLSGDELPSGLRGFEVLDQLGFDERRLRQALGALDCGSLEILVRGVDVDPDALRRRLGLRGSRSLALVVTRLGSGTAARGTAFVCRPSR
>NZ_AP022569.1|WP_163780931.1|5200911_5201763_+|hypothetical-protein
MKRTVAVARLGLIALGLGIGGAFAAIPGTASADSSDWLAAVDGFLSGVAVPAASDASSGLNLAISFDGATLYQDGTAYAYTGDNGDIAIANGAGAHAYAFGTNNYASVDGTDSTAVAGGYDQATAGTSADNTAFAFGNNDTAFAGTTDAANPGSFNYSIIFGNGDGAYSGGTEAGAGSYDGAYVEGNNLATAYAQGGNHLLDLVKFYGDGAGSGTAAATDLLGSDPSGALADGNAFWTDLFSGDTAGALTAGHEFWADMLTAFDGGSLAADAGNLWTDVASLF
>NZ_AP022569.1|WP_163780933.1|5201938_5202649_+|DUF3298-domain-containing-protein
MRMMMSAALIAAGALLGWSGGAVAAADSACTSLGGELQDEQTCHVRISTASYTLQMMFPTDYPDQALTDFLSQNRDGFVNVAQTSPSQTSGAREVPYQMEVTSEQYHSGQAPAGTRSVVLKVFEDLGGPRPSTFYKSFNWDVAGQKSITFDTLFAPNTKPLDAIYPIVQREVGKQTGIGAAILPGSGLDASHYQNFAITDDELIFYFAPGELLPSLAGASQVHVPRTAVPPLAVKT
>NZ_AP022569.1|WP_163780935.1|5202645_5203032_-|hypothetical-protein
MANDPAAQSSPAQQSDGASRRQIGDVLATVVLVIVHFGLYGATFVVLGLLVMGTDSCGYQKCGDPAWLDRAMHLGAWAGGVLLLADVALTLFRVVRKRVAWVVPLIGCIAQVALAFGAGAMESLAGPV
>NZ_AP022569.1|WP_163780937.1|5203069_5204452_-|PQQ-binding-like-beta-propeller-repeat-protein
MAGKPSAAPSGTAKRAISLGNAAAGYPRSVRRWSSLVSAIVLTVALASCGNTDSWVDTVPAQGWPAQYGDAANSSYSPTAGSGRLALRWTRSVKGSLAASVSLSSRNWLAANAQTPGGCSLMEWENDDNGRQRWCTRLYQGGGTSGPLFDGFDNLYVGQPGAILSFPVTQWIRWRRPVMGMPTTPRVLGHGQLLVATHLGQVQVFDGHRGVVVGNSVDLVNDVDPSDFTRGLSDCATAQAGCPVAAAPAFSAATGMIVLSLWEPEAPAAVLVGLKYHPGQTPLLTREWTSSAVGDGVLASPVLSSDGSTVYVNGRDQRLWALNAADGKAKWSVPLKFLAQTPPSVTPGGLIVSGGGPDTRLVAFKDAGNHAQEIWRRNDVSPLSTSSLAGQGVGYAVVTGGPGQGERGMTLLAFEPGSGHTLNSYRLPEATGFPVGVSIGRDRRVVAATSDGQVYSFAPN
>NZ_AP022569.1|WP_163780939.1|5204450_5205188_+|acetyltransferase
MTSMWGAPIHRRWRGSNLRDPRQARFLTLASLRWVLRNRAYTPWYLVRYWRLLKFKLANPHIITRGMVFIGKGVEIHATPELAQLEIGRWVHIGDKNTIRAHEGSLRFGDKVVLGRDNVINCYLDIELGDSVLMADWCYICDFDHRMDDINVPIKDQGIVKSPVRIGPDTWVGVKATVLRGTIIGRGCVLGSHAVVRGDVPDFSIAVGAPAKVVKNRQLAWETSAAQRAELAAALADIERKKAAR
>NZ_AP022569.1|WP_163780941.1|5205184_5206525_-|deoxyribodipyrimidine-photo-lyase
MPALLWFRRDLRLRDLPPLLRAAADSDDVLACFVLDPRLEASSGDRRMQFLCDSLRHLRDDLDGRLLVTRGRPEERIPAIAKEIEAPSVHISEDFAPYGRRRDDRVRSALGDVPLVATGSPYLVSPGRVTKDNGEPYKVFTPFFGRWREMGWRSAAKSGPKAAQWVDPKQLGKRAMQVEIPDPGVELDLSAGEAAAKRQWKKFVDTALEDYGDDRNRPDHDGTSRMSAHLKFGTIHPRTMAADLDQRRAGPRAYLRELAFRDFYASVLHDWPDSSWCNWNRDFDAIEIDTGKKAEQRFEAWKAGKTGFPIVDAGMRQLRDSGFMHNRVRMIAASFLVKDLHLPWQWGARWFLDQLVDGDMASNQHGWQWAAGCGTDAAPYFRVFNPTTQAEKFDPAGDYVRRWVDELTDVDDVRLTKGARPSEYPEPIVDHGAERSEALRRYQDMN
>NZ_AP022569.1|WP_163780943.1|5206541_5207024_-|tryptophan-rich-sensory-protein
MNKQTLAATSLAVGATAGLGSVASQPRITQWYSRLRKPAYVPPNGVFPIAWTSLYTDIAITSATAIDRLRSTGRRDEARRYIVALAANLILNAGWSWVFFKYNKLGASAVGAVVLAASSADLTRRTAAADPRAGAALLPYPLWCAFATAMSVHIWVLNRR
>NZ_AP022569.1|WP_163780945.1|5207117_5207630_+|MarR-family-transcriptional-regulator
MGSDEAAGGRAALESQISADLRVLTAESEQIGRVFAAAHDVRPTDFRALLHVMVAETAGTPITSGELRQRMGLSGAAITYLVDRMMASGHIIRESDPADRRKVILRYSDAGSATAKSFFAPLGAYTHDAMADLPDTDLASASRVFSALIEAMRRYQDHLVSSKSPVQRPN

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_AP022569_2	2.1\|2690743\|25\|NZ_AP022569\|CRISPRCasFinder	2690743-2690767	25	NZ_AP022569.1	2165543-2165567	1	0.96
NZ_AP022569_2	2.1\|2690743\|25\|NZ_AP022569\|CRISPRCasFinder	2690743-2690767	25	NZ_AP022569.1	1455264-1455288	2	0.92
NZ_AP022569_2	2.1\|2690743\|25\|NZ_AP022569\|CRISPRCasFinder	2690743-2690767	25	NZ_AP022569.1	3669267-3669291	2	0.92

1. spacer 2.1|2690743|25|NZ_AP022569|CRISPRCasFinder matches to position: 2165543-2165567, mismatch: 1, identity: 0.96

cgaagcgatgctgaggagcggcgcc	CRISPR spacer
cgaaccgatgctgaggagcggcgcc	Protospacer
**** ********************

2. spacer 2.1|2690743|25|NZ_AP022569|CRISPRCasFinder matches to position: 1455264-1455288, mismatch: 2, identity: 0.92

cgaagcgatgctgaggagcggcgcc	CRISPR spacer
cgaagcgatggggaggagcggcgcc	Protospacer
**********  *************

3. spacer 2.1|2690743|25|NZ_AP022569|CRISPRCasFinder matches to position: 3669267-3669291, mismatch: 2, identity: 0.92

cgaagcgatgctgaggagcggcgcc	CRISPR spacer
cgcagcgatgcggaggagcggcgcc	Protospacer
** ******** *************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK814759	Gordonia phage Reyja, complete genome	6235-6259	3	0.88
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	NZ_CP049031	Fluviibacterium aquatile strain SC52 plasmid pSC52_3, complete sequence	90801-90825	3	0.88
NZ_AP022569_2	2.1\|2690743\|25\|NZ_AP022569\|CRISPRCasFinder	2690743-2690767	25	NZ_CP043499	Rhizobium grahamii strain BG7 plasmid unnamed, complete sequence	603073-603097	4	0.84
NZ_AP022569_2	2.1\|2690743\|25\|NZ_AP022569\|CRISPRCasFinder	2690743-2690767	25	NZ_CP027670	Simplicispira suum strain SC1-8 plasmid unnamed1, complete sequence	100682-100706	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	NZ_CP021355	Rhodococcus sp. S2-17 plasmid pRB98, complete sequence	408045-408069	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	NZ_CP037915	Sphingomonas sp. AAP5 plasmid p150, complete sequence	80924-80948	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	NZ_CP043441	Cupriavidus campinensis strain MJ1 plasmid unnamed1, complete sequence	1799622-1799646	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511042	Pseudomonas phage CF126, partial genome	50005-50029	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511040	Pseudomonas phage CF63, partial genome	35220-35244	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511051	Pseudomonas phage BR181, partial genome	33928-33952	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511041	Pseudomonas phage CF69, partial genome	50033-50057	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MF490237	Pseudomonas phage vB_PaeP_E220, complete genome	44874-44898	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511049	Pseudomonas phage BR326, partial genome	33928-33952	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511045	Pseudomonas phage BR208, partial genome	33928-33952	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511044	Pseudomonas phage BR197, partial genome	50033-50057	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511050	Pseudomonas phage BR150, partial genome	49961-49985	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511048	Pseudomonas phage BR320, partial genome	49961-49985	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511046	Pseudomonas phage BR313, partial genome	33928-33952	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	KM389216	UNVERIFIED: Pseudomonas phage F_ET605sp/Pa1651 clone contig00001 genomic sequence	38306-38330	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511047	Pseudomonas phage BR319, partial genome	50137-50161	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511043	Pseudomonas phage BR228, partial genome	46082-46106	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	KM389247	UNVERIFIED: Pseudomonas phage JBD90 clone contig00001 genomic sequence	19890-19914	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MK511039	Pseudomonas phage CF24, partial genome	50033-50057	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	NZ_CP013104	Paraburkholderia caribensis strain MWAP64 plasmid 1, complete sequence	631623-631647	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	NC_006552	Pseudomonas phage F116, complete genome	28928-28952	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	MT118301	Pseudomonas phage Epa33, complete genome	26937-26961	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	AY625898	Pseudomonas aeruginosa phage F116, complete genome	28928-28952	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	NC_042342	Pseudomonas virus H66, complete genome	28677-28701	4	0.84
NZ_AP022569_5	5.1\|5196135\|25\|NZ_AP022569\|CRISPRCasFinder	5196135-5196159	25	LT603684	Pseudomonas phage phiC725A genome assembly	28251-28275	4	0.84
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NC_013855	Azospirillum sp. B510 plasmid pAB510a, complete sequence	347623-347655	5	0.848
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP029452	Sinorhizobium fredii CCBAU 25509 plasmid pSF25509b, complete sequence	1650942-1650974	6	0.818
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP023071	Sinorhizobium fredii CCBAU 83666 plasmid pSF83666b, complete sequence	1627405-1627437	6	0.818
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP034351	Streptomyces sp. W1SF4 plasmid p1, complete sequence	13539-13571	7	0.788
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP025552	Streptomyces rimosus strain WT5260 plasmid unnamed, complete sequence	46108-46140	7	0.788
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP054615	Azospirillum oryzae strain KACC 14407 plasmid unnamed1, complete sequence	154686-154718	7	0.788
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP039640	Azospirillum sp. TSH100 plasmid p1, complete sequence	157094-157126	7	0.788
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP029232	Sinorhizobium fredii CCBAU 45436 plasmid pSF45436b, complete sequence	375704-375736	7	0.788
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NC_014310	Ralstonia solanacearum PSI07 plasmid mpPSI07, complete sequence	1718788-1718820	8	0.758
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP022760	Ralstonia solanacearum strain T98 plasmid unnamed, complete sequence	1630979-1631011	8	0.758
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP022789	Ralstonia solanacearum strain SL3175 plasmid unnamed, complete sequence	1630980-1631012	8	0.758
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	NZ_CP020695	Sulfitobacter sp. D7 plasmid p1SUD7, complete sequence	13711-13743	9	0.727
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	MH910038	Mycobacterium phage LeMond, complete genome	2377-2409	9	0.727
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	MH910039	Mycobacterium phage Oscar, complete genome	2378-2410	9	0.727
NZ_AP022569_1	1.1\|581738\|33\|NZ_AP022569\|CRISPRCasFinder	581738-581770	33	MK376955	Mycobacterium phage KiSi, complete genome	2377-2409	9	0.727

1. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK814759 (Gordonia phage Reyja, complete genome) position: , mismatch: 3, identity: 0.88

ggacagcgaccagcccgacgtcggc	CRISPR spacer
tgacggcgaccagcccgacgccggc	Protospacer
 ***.***************.****

2. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to NZ_CP049031 (Fluviibacterium aquatile strain SC52 plasmid pSC52_3, complete sequence) position: , mismatch: 3, identity: 0.88

ggacagcgaccagcccgacgtcggc	CRISPR spacer
gaacaccgaccagcccgacttcggc	Protospacer
*.*** ************* *****

3. spacer 2.1|2690743|25|NZ_AP022569|CRISPRCasFinder matches to NZ_CP043499 (Rhizobium grahamii strain BG7 plasmid unnamed, complete sequence) position: , mismatch: 4, identity: 0.84

cgaagcgatgctgaggagcggcgcc	CRISPR spacer
gcaagcgatgccgaggagcgacgcc	Protospacer
  *********.********.****

4. spacer 2.1|2690743|25|NZ_AP022569|CRISPRCasFinder matches to NZ_CP027670 (Simplicispira suum strain SC1-8 plasmid unnamed1, complete sequence) position: , mismatch: 4, identity: 0.84

cgaagcgatgctgaggagcggcgcc	CRISPR spacer
cgaagccatgctgagcagcggcgat	Protospacer
****** ******** ******* .

5. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to NZ_CP021355 (Rhodococcus sp. S2-17 plasmid pRB98, complete sequence) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
cgacagcgaccagcgcgacgtccgg	Protospacer
 ************* ******* *

6. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to NZ_CP037915 (Sphingomonas sp. AAP5 plasmid p150, complete sequence) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcaaccagtccgacgtcgtt	Protospacer
*******.*****.********* .

7. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to NZ_CP043441 (Cupriavidus campinensis strain MJ1 plasmid unnamed1, complete sequence) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
gagcgacgaccagcccgacgtcggc	Protospacer
*..*..*******************

8. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511042 (Pseudomonas phage CF126, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

9. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511040 (Pseudomonas phage CF63, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

10. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511051 (Pseudomonas phage BR181, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

11. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511041 (Pseudomonas phage CF69, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

12. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MF490237 (Pseudomonas phage vB_PaeP_E220, complete genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

13. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511049 (Pseudomonas phage BR326, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

14. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511045 (Pseudomonas phage BR208, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

15. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511044 (Pseudomonas phage BR197, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

16. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511050 (Pseudomonas phage BR150, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

17. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511048 (Pseudomonas phage BR320, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

18. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511046 (Pseudomonas phage BR313, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

19. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to KM389216 (UNVERIFIED: Pseudomonas phage F_ET605sp/Pa1651 clone contig00001 genomic sequence) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

20. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511047 (Pseudomonas phage BR319, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

21. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511043 (Pseudomonas phage BR228, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

22. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to KM389247 (UNVERIFIED: Pseudomonas phage JBD90 clone contig00001 genomic sequence) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

23. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MK511039 (Pseudomonas phage CF24, partial genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

24. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to NZ_CP013104 (Paraburkholderia caribensis strain MWAP64 plasmid 1, complete sequence) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
agtcagcgaccagcccgacgtctgg	Protospacer
.* ******************* *

25. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to NC_006552 (Pseudomonas phage F116, complete genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

26. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to MT118301 (Pseudomonas phage Epa33, complete genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

27. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to AY625898 (Pseudomonas aeruginosa phage F116, complete genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

28. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to NC_042342 (Pseudomonas virus H66, complete genome) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

29. spacer 5.1|5196135|25|NZ_AP022569|CRISPRCasFinder matches to LT603684 (Pseudomonas phage phiC725A genome assembly) position: , mismatch: 4, identity: 0.84

ggacagcgaccagcccgacgtcggc	CRISPR spacer
ggacagcgacgagcccaacgtcgca	Protospacer
********** *****.******

30. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NC_013855 (Azospirillum sp. B510 plasmid pAB510a, complete sequence) position: , mismatch: 5, identity: 0.848

gccgcctgccccgccgccgggcgcagcgggtgc-	CRISPR spacer
gccgcctgcgccgccgccgggcgaag-gcgtgag	Protospacer
********* ************* ** * ***

31. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP029452 (Sinorhizobium fredii CCBAU 25509 plasmid pSF25509b, complete sequence) position: , mismatch: 6, identity: 0.818

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
ccagcctgccccgccgccggccgcagcatgagc	Protospacer
 * ***************** ******. * **

32. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP023071 (Sinorhizobium fredii CCBAU 83666 plasmid pSF83666b, complete sequence) position: , mismatch: 6, identity: 0.818

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
ccagcctgccccgccgccggccgcagcatgagc	Protospacer
 * ***************** ******. * **

33. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP034351 (Streptomyces sp. W1SF4 plasmid p1, complete sequence) position: , mismatch: 7, identity: 0.788

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
gccgccaggcccgccgccgggcgcacgagaggc	Protospacer
****** * ****************  .*. **

34. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP025552 (Streptomyces rimosus strain WT5260 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.788

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
acttccctccccggcgcagggcgcagcgggtgc	Protospacer
.*. **. ***** *** ***************

35. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP054615 (Azospirillum oryzae strain KACC 14407 plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.788

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
gtcacctgcaccggcgccgggcgcagcgccagc	Protospacer
*.*.***** *** **************   **

36. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP039640 (Azospirillum sp. TSH100 plasmid p1, complete sequence) position: , mismatch: 7, identity: 0.788

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
gtcacctgcaccggcgccgggcgcagcgccagc	Protospacer
*.*.***** *** **************   **

37. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP029232 (Sinorhizobium fredii CCBAU 45436 plasmid pSF45436b, complete sequence) position: , mismatch: 7, identity: 0.788

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
ccagcctgccccgccgccagccgcagcatgagc	Protospacer
 * ***************.* ******. * **

38. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NC_014310 (Ralstonia solanacearum PSI07 plasmid mpPSI07, complete sequence) position: , mismatch: 8, identity: 0.758

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
atcgcatgccccgccgccaggcgcagcgcttca	Protospacer
..*** ************.*********  *

39. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP022760 (Ralstonia solanacearum strain T98 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.758

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
atcgcatgccccgccgccaggcgcagcgcttca	Protospacer
..*** ************.*********  *

40. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP022789 (Ralstonia solanacearum strain SL3175 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.758

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
atcgcatgccccgccgccaggcgcagcgcttca	Protospacer
..*** ************.*********  *

41. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to NZ_CP020695 (Sulfitobacter sp. D7 plasmid p1SUD7, complete sequence) position: , mismatch: 9, identity: 0.727

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
cccgcctgccgcgccgccgcgcgcaggtcatcg	Protospacer
 ********* ******** ******   .*

42. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to MH910038 (Mycobacterium phage LeMond, complete genome) position: , mismatch: 9, identity: 0.727

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
ggcttgagccccgccgccgggccgagcgggtcg	Protospacer
* * .  ***************  *******

43. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to MH910039 (Mycobacterium phage Oscar, complete genome) position: , mismatch: 9, identity: 0.727

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
ggcttgagccccgccgccgggccgagcgggtcg	Protospacer
* * .  ***************  *******

44. spacer 1.1|581738|33|NZ_AP022569|CRISPRCasFinder matches to MK376955 (Mycobacterium phage KiSi, complete genome) position: , mismatch: 9, identity: 0.727

gccgcctgccccgccgccgggcgcagcgggtgc	CRISPR spacer
ggcttgagccccgccgccgggccgagcgggtcg	Protospacer
* * .  ***************  *******

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

354079 : 364664

Indivirus(28.57%)

tRNA

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_163774766.1\|354079_355375_+	protein translocase subunit SecF	A0A1B1IVP7	uncultured_Mediterranean_phage	9.7e-22	28.4
WP_163774769.1\|355379_357041_+	hypothetical protein	NA	NA	NA	NA
WP_163774771.1\|357022_357571_+	adenine phosphoribosyltransferase	A0A1V0SKE5	Klosneuvirus	7.8e-13	33.6
WP_163774773.1\|357618_359979_+	RelA/SpoT family protein	A0A2I2L310	Orpheovirus	6.7e-13	38.6
WP_163781189.1\|359999_360977_+	NAD-dependent epimerase/dehydratase family protein	A0A1D8EQC0	Escherichia_phage	6.7e-07	22.8
WP_163774775.1\|360959_361754_-	peptidylprolyl isomerase	A0A1V0SCU1	Indivirus	8.3e-08	30.8
WP_163774777.1\|361753_362629_-	peptidylprolyl isomerase	A0A1V0SCU1	Indivirus	1.2e-07	34.5
WP_163774779.1\|362742_363405_+	MBL fold metallo-hydrolase	NA	NA	NA	NA
WP_163774781.1\|363401_364664_+\|tRNA	histidine--tRNA ligase	A0A2K9L0H9	Tupanvirus	5.8e-11	23.3

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_AP022569

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection