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_CP013351	Pseudoalteromonas issachenkonii strain KCTC 12958 chromosome II, complete sequence	0 crisprs	csa3,cas3,DinG	0	0	0	0
NZ_CP013350	Pseudoalteromonas issachenkonii strain KCTC 12958 chromosome I, complete sequence	2 crisprs	DinG,DEDDh,cas3,cas6f,cas7f,cas5f,csa3	0	1	0	0

Cas Category Instructions

Results visualization

1. NZ_CP013350

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP013350_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP013350_1

447276-447398

Orphan

Consensus_repeat	Method
AACGGACAAATTACTGACTATTTTGAATGCGGCACTAGCTCAGTTG	CRISPRCasFinder

1 spacers

DEDDh

The CRISPR arrays of NZ_CP013350_1

>merge|NZ_CP013350|1|447276-447398|CRISPRCasFinder
AACGGACAAATTACTGACTATTTTGAATGCGGCACTAGCTCAGTTGCCAGAATGTAGGACGCGACCCGTCGCGCACTAACGGACGAATTACTGACTATTTTGAATGCGGCACTAGCTCAGTTG

>NZ_CP013350|1|1|447276-447398|CRISPRCasFinder
AACGGACAAATTACTGACTATTTTGAATGCGGCACTAGCTCAGTTG	CCAGAATGTAGGACGCGACCCGTCGCGCACT
AACGGACGAATTACTGACTATTTTGAATGCGGCACTAGCTCAGTTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP013350.1\|WP_058154109.1\|437852_439805_+\|phosphomethylpyrimidine-synthase-ThiC	unknown	unknown	gnl\|CDD\|236451
NZ_CP013350.1\|WP_016900288.1\|450134_451109_+\|tRNA-dihydrouridine(20/20a)-synthase-DusA	unknown	unknown	gnl\|CDD\|236991
NZ_CP013350.1\|WP_058154111.1\|441920_443447_+\|thiamine-phosphate-synthase	unknown	unknown	gnl\|CDD\|238574
NZ_CP013350.1\|WP_013463959.1\|440917_441112_+\|sulfur-carrier-protein-ThiS	unknown	unknown	gnl\|CDD\|340451
NZ_CP013350.1\|WP_008115498.1\|449432_450053_+\|MarC-family-protein	unknown	unknown	gnl\|CDD\|225006
NZ_CP013350.1\|WP_013463970.1\|452036_452243_+\|PspC-domain-containing-protein	unknown	unknown	gnl\|CDD\|377200
NZ_CP013350.1\|WP_013463972.1\|452658_453168_+\|copper-chaperone-PCu(A)C	unknown	unknown	gnl\|CDD\|377298
NZ_CP013350.1\|WP_013463967.1\|448905_449340_-\|transcriptional-repressor	unknown	unknown	gnl\|CDD\|183251
NZ_CP013350.1\|WP_058154114.1\|451345_452026_+\|phage-shock-protein-A	unknown	unknown	gnl\|CDD\|274372
NZ_CP013350.1\|WP_013463973.1\|453176_454163_+\|DUF2333-family-protein	unknown	unknown	gnl\|CDD\|378387
NZ_CP013350.1\|WP_058154110.1\|439908_440910_+\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|274092
NZ_CP013350.1\|WP_013463966.1\|448374_448842_-\|chemotaxis-protein-CheX	unknown	unknown	gnl\|CDD\|381734
NZ_CP013350.1\|WP_008465084.1\|437125_437503_+\|META-domain-containing-protein	unknown	unknown	gnl\|CDD\|377111
NZ_CP013350.1\|WP_058154112.1\|443439_444207_+\|HesA/MoeB/ThiF-family-protein	unknown	unknown	gnl\|CDD\|238386
NZ_CP013350.1\|WP_016900286.1\|452253_452580_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP013350.1\|WP_028834530.1\|446377_446923_+\|oligoribonuclease	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|235429
NZ_CP013350.1\|WP_013463960.1\|441116_441908_+\|thiazole-synthase	unknown	unknown	gnl\|CDD\|234687
NZ_CP013350.1\|WP_051385867.1\|444315_445143_-\|phosphatidylserine-decarboxylase	unknown	unknown	gnl\|CDD\|234591
NZ_CP013350.1\|WP_013463964.1\|445196_446255_-\|small-ribosomal-subunit-biogenesis-GTPase-RsgA	unknown	unknown	gnl\|CDD\|237039
NZ_CP013350.1\|WP_058154113.1\|447949_448378_-\|YjbQ-family-protein	unknown	unknown	gnl\|CDD\|223509

Protein	Function_ID	Function_description	E-value
NZ_CP013350.1\|WP_058154109.1\|437852_439805_+\|phosphomethylpyrimidine-synthase-ThiC	gnl\|CDD\|236451	PRK09284, PRK09284, thiamine biosynthesis protein ThiC; Provisional.	0
NZ_CP013350.1\|WP_016900288.1\|450134_451109_+\|tRNA-dihydrouridine(20/20a)-synthase-DusA	gnl\|CDD\|236991	PRK11815, PRK11815, tRNA dihydrouridine(20/20a) synthase DusA.	0
NZ_CP013350.1\|WP_058154111.1\|441920_443447_+\|thiamine-phosphate-synthase	gnl\|CDD\|238574	cd01169, HMPP_kinase, 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.	5.44889e-96
NZ_CP013350.1\|WP_013463959.1\|440917_441112_+\|sulfur-carrier-protein-ThiS	gnl\|CDD\|340451	cd00565, Ubl_ThiS, ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS. ThiS, also termed Thiamine biosynthesis protein (ThiaminS), is a sulfur carrier protein involved in thiamin biosynthesis in prokaryotes. It has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub), and is activated in an ATP-dependent manner by sulfurtransferases, similar to the activation mechanism of Ub-activating enzyme E1. ThiS has common evolutionary origin with Ub-related protein modifiers in eukaryotes, a beta-grasp fold as Ub, and is closely related to proteins MoaD and Urm1.	1.10545e-14
NZ_CP013350.1\|WP_008115498.1\|449432_450053_+\|MarC-family-protein	gnl\|CDD\|225006	COG2095, MarC, Multiple antibiotic transporter [Intracellular trafficking and secretion].	3.4272e-37
NZ_CP013350.1\|WP_013463970.1\|452036_452243_+\|PspC-domain-containing-protein	gnl\|CDD\|377200	pfam04024, PspC, PspC domain. This family includes Phage shock protein C (PspC) that is thought to be a transcriptional regulator. The presumed domain is 60 amino acid residues in length.	2.83455e-11
NZ_CP013350.1\|WP_013463972.1\|452658_453168_+\|copper-chaperone-PCu(A)C	gnl\|CDD\|377298	pfam04314, PCuAC, Copper chaperone PCu(A)C. PCu(A)C is a periplasmic copper chaperone. Its role may be to capture and transfer copper to two other copper chaperones, PrrC and Cox11, which in turn deliver Cu(I) to cytochrome c oxidase.	1.5235e-39
NZ_CP013350.1\|WP_013463967.1\|448905_449340_-\|transcriptional-repressor	gnl\|CDD\|183251	PRK11639, PRK11639, zinc uptake transcriptional repressor Zur.	1.72678e-51
NZ_CP013350.1\|WP_058154114.1\|451345_452026_+\|phage-shock-protein-A	gnl\|CDD\|274372	TIGR02977, phage_shock_protein_A, phage shock protein A. Members of this family are the phage shock protein PspA, from the phage shock operon. This is a narrower family than the set of PspA and its homologs, sometimes several in a genome, as described by pfam04012. PspA appears to maintain the protonmotive force under stress conditions that include overexpression of certain phage secretins, heat shock, ethanol, and protein export defects. [Cellular processes, Adaptations to atypical conditions].	1.9842e-53
NZ_CP013350.1\|WP_013463973.1\|453176_454163_+\|DUF2333-family-protein	gnl\|CDD\|378387	pfam10095, DUF2333, Uncharacterized protein conserved in bacteria (DUF2333). Members of this family of hypothetical bacterial proteins have no known function.	0
NZ_CP013350.1\|WP_058154110.1\|439908_440910_+\|FAD-dependent-oxidoreductase	gnl\|CDD\|274092	TIGR02352, Glycine_oxidase, glycine oxidase ThiO. This family consists of the homotetrameric, FAD-dependent glycine oxidase ThiO, from species such as Bacillus subtilis that use glycine in thiamine biosynthesis. In general, members of this family will not be found in species such as E. coli that instead use tyrosine and the ThiH protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine].	8.63501e-68
NZ_CP013350.1\|WP_013463966.1\|448374_448842_-\|chemotaxis-protein-CheX	gnl\|CDD\|381734	cd17906, CheX, chemotaxis phosphatase CheX. This family contains CheX CheY-P phosphatase which is very closely related to CheC chemotaxis phosphatase; both dephosphorylate CheY, although CheC requires binding of CheD to achieve the level of activity of CheX. CheX has been shown to be the most powerful CheY-P phosphatase of the CheC-FliY-CheX (CXY) family. Structural and functional data of CheX and its CheY3 substrate in Borrelia burgdorferi (the causative agent of Lyme disease) bound to the phosphoryl analog BeF3(-) and Mg2+ reveal a unique mode of binding, but a catalytic mechanism which is virtually identical to that used by the structurally unrelated CheZ, providing a striking example of convergent evolution. Thus, CheX is quite divergent from the rest of the CXY family; it forms a dimer and some may function outside chemotaxis. The data also suggest a possible CheX regulatory mechanism through dissociation of the CheX homodimer.	4.36038e-53
NZ_CP013350.1\|WP_008465084.1\|437125_437503_+\|META-domain-containing-protein	gnl\|CDD\|377111	pfam03724, META, META domain. Small domain family found in proteins of of unknown function. Some are secreted and implicated in motility in bacteria. Also occurs in Leishmania spp. as an essential gene. Over-expression in L.amazonensis increases virulence. A pair of cysteine residues show correlated conservation, suggesting that they form a disulphide bond.	2.72307e-27
NZ_CP013350.1\|WP_058154112.1\|443439_444207_+\|HesA/MoeB/ThiF-family-protein	gnl\|CDD\|238386	cd00757, ThiF_MoeB_HesA_family, ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1). .	5.62668e-97
NZ_CP013350.1\|WP_028834530.1\|446377_446923_+\|oligoribonuclease	gnl\|CDD\|235429	PRK05359, PRK05359, oligoribonuclease; Provisional.	8.85093e-131
NZ_CP013350.1\|WP_013463960.1\|441116_441908_+\|thiazole-synthase	gnl\|CDD\|234687	PRK00208, thiG, thiazole synthase; Reviewed.	1.79683e-154
NZ_CP013350.1\|WP_051385867.1\|444315_445143_-\|phosphatidylserine-decarboxylase	gnl\|CDD\|234591	PRK00044, psd, phosphatidylserine decarboxylase; Reviewed.	0
NZ_CP013350.1\|WP_013463964.1\|445196_446255_-\|small-ribosomal-subunit-biogenesis-GTPase-RsgA	gnl\|CDD\|237039	PRK12288, PRK12288, small ribosomal subunit biogenesis GTPase RsgA.	0
NZ_CP013350.1\|WP_058154113.1\|447949_448378_-\|YjbQ-family-protein	gnl\|CDD\|223509	COG0432, COG0432, Uncharacterized conserved protein [Function unknown].	3.93914e-58

>NZ_CP013350.1|WP_028834530.1|446377_446923_+|oligoribonuclease
MTINKSNLIWLDLEMTGLEPETDKILEIATVVTDADLNILAEGPTIAIHQSDELLDGMDEWCTTQHGKSGLTARCKASTFDEAYAVDQTLAFLKQWVPAGASPMCGNSIGQDRRFMNKYMRELEDFFHYRNLDVSTIKELARRWKPDVLAQVNKKGSHLALDDIKDSIMELKVYREKFFNL
>NZ_CP013350.1|WP_013463964.1|445196_446255_-|small-ribosomal-subunit-biogenesis-GTPase-RsgA
MAKQKKLSKGQSRRIKANHQKRLSNADTKPAKVGAQEWQTDNLGQVENAIVISRFGQHADVETQNGDVLRCNIRRTVSNLVCGDEVLFRRAKVSEGDLAGVIEATQERRSQLTRPDFYDGVKVIAANIDQILMVSAVLPEFTPSIIDRYLIACEDMGIEPILVLNKIDLIDEAGLNEIQQILDIYRKLNYQVLLVSNITGEGINELKEVLAGKNNIFVGQSGVGKSTLVNTVLPDAEILTKEVSENSGLGQHTTTVSRLHHLPSGGNLIDSPGIREFGLWHLDVERVTWCFKEFREFIGGCRFRDCKHLNDPGCIIKQAVADGDISKLRFESYHRILETMADGRAGARAPRV
>NZ_CP013350.1|WP_051385867.1|444315_445143_-|phosphatidylserine-decarboxylase
MPKHFISRVVGKLAAAKAGALTTTLIKLFIKQYKIDMSEAKYSDPAHYKSFNEFFTRPLKDGVRPMVEDEEIIIHPVDGAISQLGDIVDGQLIQAKGHDYSLQALLGGSQDDTTPFLGGKFATIYLAPKDYHRIHMPIDGTLSKMIYVPGDLFSVNPLTAQNVPNLFARNERVVAIFETEIGPLAMVLVGATIVASIETIWAGTVTPPAGSDVFSWNYPTKGENAITLKKGEEMGRFKLGSTVVLAWGANKAEILDDQLPEVVTRLGTAFAKIDD
>NZ_CP013350.1|WP_058154112.1|443439_444207_+|HesA/MoeB/ThiF-family-protein
MTDTLQTLNDKETLRYSRHILLDEVGLDGQLMLKRSTVAVVGAGGLGSPALLYLAAAGIGSLILIDDDVVELSNLQRQVLYKVNHLGQNKVRAAGKVLASLNNQINIITHTQKLDDTNSALLLKNADIVLDCSDNFSTRYSVNLYCIANNIRLITGAALATQGQLMGFDFRQSDSPCYGCVFPQSSDAPVINCSNAGVISPLLGIVGSMQAQLTLNMLLGHFKGNVFITFDALSLKQQHFKMTKDLACKECGGYE
>NZ_CP013350.1|WP_058154111.1|441920_443447_+|thiamine-phosphate-synthase
MTNVVWTIAGSDSGGGAGIQADIKAMQSFGVHACTAITALTAQNSLGVEAINAVSTDIIESQLLALEKDMKAKVIKIGMLANVQQIQLISEHISHYKAKWPTPPVIVYDPVAIASSGDLLTEEDTVSAIKECLLPLVDVITPNTHETQLLTGVYLIGPAAIKEAASKLMAWGAKAVVIKGGHWDYPSGYCIDYCTQNGEDYWLGNEKIQVPHSHGTGCSMASVIAACLAKDYPLKDAFILAKAYINQGLKKSVRYGEGIGPVAQTQFPTDLAHYPQVIEPGSWLGDELDFDVPLDFNMAADFAACESKKLGLYGVVDSIEWLEKCLQQGIKTAQLRVKNKTQNELDELIAKAVTLGEQYNAQVFINDYWQLAIKHGAYGVHLGQEDLESANLVAIKEAGLRLGLSTHGFYEMLRAHNYRPSYMAFGAIYPTTTKDMTGQIQGLEKLNKFAPLMQSYPTVAIGGIDLSRATEVANTGVGSVAVVRAISEAPDHVSAIRSLQTAINTKHD
>NZ_CP013350.1|WP_013463960.1|441116_441908_+|thiazole-synthase
MQSKDCLTIYGEPINSRLLIGSALYPSPDIMTQSIKASGAEIVTVSLRRQQNAAAGNDFWQLIKNTGLKILPNTAGCHSVKEAINLAKMCREVFATDWIKLELIGDDYNLQPDPFALLEATKILIDDGFKVLPYCTDDLVLCQRLNGLGCEVLMPWGAPIGTGKGLLNSYNLKTIRERLPNTTLIVDAGLGLPSHACQALELGYDAVLLNSAIAGAGCPVTMSRAFKAAVEAGRFAYNAKAMPEKDVATPSTPTMGMPFWHQQ
>NZ_CP013350.1|WP_013463959.1|440917_441112_+|sulfur-carrier-protein-ThiS
MNITINGEPLNVTSHALLEIVKNVGAMAPYAVAVNGEFIPQSRHSHVVINEGDSIELLSPIQGG
>NZ_CP013350.1|WP_058154110.1|439908_440910_+|FAD-dependent-oxidoreductase
MFYNIAVVGFGLAGRLAALELSKQHRVTVFEADDEHTQNSAGKVAAAMLAPLAESVMCERELALMGVDSITRWPAILEQLNSEVFFQQQGTLVVAHPQDKGDLQSFAQRIKPLLNFSAQAINAQQIEQLEPELAGRFSQGLFLPGEAQIDNQAFYNASFRLLNKRKVKFVFNQRASIFDNKVNNREFDYIIDCRGLGAKQDQPLRGVRGEVARLYAPEVNLTRPVRLMHPRYPIYIAPKPNHEYVIGATEIESQDTGPATVRSTLELLSAAYTVHSGFAEARLLNIQTGLRPAFSDNRPQVKKTSKVISINGLYRHGYMLAPALVAQALSQIE
>NZ_CP013350.1|WP_058154109.1|437852_439805_+|phosphomethylpyrimidine-synthase-ThiC
MSNTTNKSSRRETRAAASDYIYNLTGQPFPSSHKVYVEGSQQGVRVGMREITLSDTFIGGTDENPVYESNEPLRVYDTSGPYTDPNFELDVRKGLDKYREQWIESRGDTEVLESVTSQFAQQRMADDGLDHIRFEHLPKIRRAKAGKNVTQMHYARQGIVTPEMEYVAIRENMGRAQIREELLAAQHKGESFGASIPEFITPEFVRAEIARGRAILPNNINHPETEPMIVGRNFLVKVNANIGNSSVGSSIEEEVEKMVWSTRWGADTVMDLSTGRYIHETREWLVRNSPVPIGTVPIYQALEKVNGVAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVLLRYVPMTAKRVTGIVSRGGSIMAKWCLAHHKENFLYTHFEDICEILKQYDVCFSLGDGLRPGSIADANDEAQFSELRTLGELTKIAWKHDVQVFIEGPGHVPMHMIKANMEEQLKHCDEAPFYTLGPLTTDIAPGYDHITSGIGAAQIAWYGCAMLCYVTPKEHLGLPNKEDVKEGLITYKIAAHAADLAKGHPGAQERDNALSKARFEFRWHDQFNIGLDPVRAREYHDETLPQESGKVAHFCSMCGPKFCSMKITQEVRDYAKDLEARGIDPNNVGDAIEIKMVDVEAEMKAKSEEFKQTGSEIYHKAI
>NZ_CP013350.1|WP_008465084.1|437125_437503_+|META-domain-containing-protein
MLVIGLCVGCASTGTVTTEQLKYTQWQLSKVDGLAIPASFKASMSFIEALQINGFAGCNKFFGEGSLEDSSLSVSKLGMTRKSCGPELDEFEQQFLQALKQGAELNLQDQKLVMQGEQKFVFIPK
>NZ_CP013350.1|WP_058154113.1|447949_448378_-|YjbQ-family-protein
MSWSQTTITLKPRSRGFHLIDNDILTKLPQLSQLKIGLLHLFIQHTSASLTINENADPTVRMDMESHFNQFVPERQPYYRHDYEGDDDMPAHIKTSTLGCELTIPINDGQLALGTWQGIYLGEHRDHGGSRRIIATLQGETF
>NZ_CP013350.1|WP_013463966.1|448374_448842_-|chemotaxis-protein-CheX
MNVEFINPFLSSLMNVLSTMAQTQLKPGKPRIKTDEVACGDVSGLIGMVGPQTRGSFSITFDESLALTIMERMLGERPDSVNEEVTDMVGEITNMVTGGAKNLLGEKGYDFAMATPIVVSGKNHTITHKSDGKKIIMPFTSDAGNANIEVSFDKL
>NZ_CP013350.1|WP_013463967.1|448905_449340_-|transcriptional-repressor
MNIESLVSKAKQVCDNRGARFTPIREKVFRLLASAQGGVGAYDLLEQLKVTETGAKPATIYRALDFLAELGFIHKIESTNAFMLCHHFDHIHPVQLLICDTCGFVKELHSTVISHELNNLAAESGFVVSGQTIEAHGKCDACRA
>NZ_CP013350.1|WP_008115498.1|449432_450053_+|MarC-family-protein
MHELLAIFIFFFAVIDPIGTIPVFIAVTRGDDDKFKRKVIFKAVGVSALVLLFFVVAGEQLLNVIEIPLSAFQIAGGLILLIFALSMTFGESKPEAEIKSVRDSTETAIFPLAIPSIASPGAMLGAVLMTRNEEYTWVEQMITSSMMLAVLVVVLILLLLATHVHKIIGDSGASIISRIMGLILSSVAVTNILNGIAQYFGLQVFA
>NZ_CP013350.1|WP_016900288.1|450134_451109_+|tRNA-dihydrouridine(20/20a)-synthase-DusA
MDKRTLNRRFSVAPMLDWTDRHCRTFHRKMTKHTVLYTEMITTGAILFGRGDYLHFNQHEGPVALQLGGSDPQALAQCAKLAGERGYDEINLNVGCPSDRVQNGRFGACLMAEPELVAECVAAMKSEVSIPVTVKTRIGIDEQDSYEFLCALIEASHKVGCDDFIIHARKAWLKGLSPKENREVPELNYPRVYQLKKDYPQLDLSINGGVKTIEQSLEHLQYIDGVMVGREAYSNPFMLNEVDEKIYGDAANTQSRHDVVRSMYDYIEEEMRLGANFWHVARHMLGIFQGQPGARGFRRHLSENGHGKQADLSVMDKALSYVPE
>NZ_CP013350.1|WP_058154114.1|451345_452026_+|phage-shock-protein-A
MGIFNRVNDVIQANIVAMLDKAEDSEKLLNLMLTEMQEALNECRSTAAALLCEEKSIKRQISNKQQAIANWQLKAEHAVTKKRDDLAKSALAEKHTVEQSIGCLQTQLETLQQSIVKITEDCERLQQKMTQAKAKQAQLAKRENVVEARAKINTQLQSDKVAFALSRFEQIERRVESVESQVEAYELTDTASNTAMQIESLVKNEKIDAELASLKASLNTANKQTA
>NZ_CP013350.1|WP_013463970.1|452036_452243_+|PspC-domain-containing-protein
MNSFNTHRRWYKNTLNKKISGVCSGLAYRLDFPVWSTRLVTVLLFLSFPFAVALGYLIAHCCLEEKAV
>NZ_CP013350.1|WP_016900286.1|452253_452580_+|hypothetical-protein
MKTFAVCLVIVALFLINSGSIIHFDVWQFPLWISDISWTGIELIGALVAIIVVIAIVALVTMGLVGAAMVALAGTILAFLFGSLMIAWPLLFVAGLCWLIADNKKVVS
>NZ_CP013350.1|WP_013463972.1|452658_453168_+|copper-chaperone-PCu(A)C
MIKQCILIASALMVGVFSSSLMAHEGHEHDSVVAQLQVTHAQVREFLPATKASVAYFSIKNHSNVPATLTKATIDGLGRVEIHEHVHADGMMKMQKVESLLIKAHQQLDFKPGSYHLMVFEPQEPLKVGQERKLTLYFEDGNRVFTNAKVVSLASQAEPVKASKDHSHH
>NZ_CP013350.1|WP_013463973.1|453176_454163_+|DUF2333-family-protein
MSQHKGKIITALVLLFVVFYAIAVYWSIEPSRFDVVQNAKQQAQQRSEKLVTGYVTTSTLITVADTLLTKSGGYLSNDVLPPSVIMDNMPAWEYGALEMVRDLALSMRKDFSRSQSQSTEHEALKKAQPQFNISSEAWAWPSAEGEYQKGIDYLMVYRSQIANQHERDSQFYSRADNLRSWLKEAEKRLGSLSQRLSASVGQDKVNTDLAGNSSNTQATYTPLQQQIKTSWWEIDDVFYESRGATWALLHFLQAVEYDFADVLDKKNARVSLQQIIRELEATQETVWSPMILNGNGFGYVANHSLVMANYISRANAALIELSELLAQG

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Crispr_ID: NZ_CP013350_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP013350_2

2350467-2350703

Orphan

Consensus_repeat	Method
AGCGGGTTGCTCTGCATCGAGTAAATCGTCAATATCAAATTCGTCATCTTC	PILER-CR

2 spacers

DEDDh

The CRISPR arrays of NZ_CP013350_2

>merge|NZ_CP013350|2|2350467-2350703|PILER-CR
AGCGGGTTGCTCTGAATCGAGTAAATCGTCAATATCAAATTCGTCATCTTCATCAACTAAGCTGTCAATATCGGTTTCTTCACTCTGTGCAGTAGCGGGTTGCTCTGCATCGAGTAAATCGTCAATATCAAATTCGTCATCTTCATCAACTAAGCTGTCAATATCGGTTTCTTCACTCTCTGCAGTAGCGGGTTGCTCTGCATCGAGTAAATCGTCAATATCAAATTCGTCATCGTC

>NZ_CP013350|2|1|2350467-2350703|PILER-CR
AGCGGGTTGCTCTGAATCGAGTAAATCGTCAATATCAAATTCGTCATCTTC	ATCAACTAAGCTGTCAATATCGGTTTCTTCACTCTGTGCAGT
AGCGGGTTGCTCTGCATCGAGTAAATCGTCAATATCAAATTCGTCATCTTC	ATCAACTAAGCTGTCAATATCGGTTTCTTCACTCTCTGCAGT
AGCGGGTTGCTCTGCATCGAGTAAATCGTCAATATCAAATTCGTCATCGTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP013350.1\|WP_024601782.1\|2358451_2359087_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|379199
NZ_CP013350.1\|WP_058155064.1\|2356150_2358160_+\|bifunctional-tRNA-(5-methylaminomethyl-2-thiouridine)(34)-methyltransferase-MnmD/FAD-dependent-5-carboxymethylaminomethyl-2-thiouridine(34)-oxidoreductase-MnmC	unknown	unknown	gnl\|CDD\|234978
NZ_CP013350.1\|WP_024601787.1\|2343198_2343693_-\|bacteriocin-production-protein	unknown	unknown	gnl\|CDD\|182773
NZ_CP013350.1\|WP_013465470.1\|2354759_2355971_-\|beta-ketoacyl-ACP-synthase-I	unknown	unknown	gnl\|CDD\|181184
NZ_CP013350.1\|WP_013465481.1\|2362369_2363044_-\|ribonuclease-T	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|179951
NZ_CP013350.1\|WP_058155058.1\|2344630_2345896_-\|bifunctional-tetrahydrofolate-synthase/dihydrofolate-synthase	unknown	unknown	gnl\|CDD\|182774
NZ_CP013350.1\|WP_058155066.1\|2359079_2359838_-\|sulfite-exporter-TauE/SafE-family-protein	unknown	unknown	gnl\|CDD\|376667
NZ_CP013350.1\|WP_058155055.1\|2335642_2337580_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP013350.1\|WP_013465463.1\|2343995_2344619_-\|SPOR-domain-containing-protein	unknown	unknown	gnl\|CDD\|225689
NZ_CP013350.1\|WP_058155061.1\|2352467_2353484_-\|aspartate-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|237845
NZ_CP013350.1\|WP_013465461.1\|2341653_2343180_-\|amidophosphoribosyltransferase	unknown	unknown	gnl\|CDD\|236427
NZ_CP013350.1\|WP_016899264.1\|2346973_2347768_-\|tRNA-pseudouridine(38-40)-synthase-TruA	unknown	unknown	gnl\|CDD\|234577
NZ_CP013350.1\|WP_016899267.1\|2339996_2340767_-\|tRNA-(ms[2]io[6]A)-hydroxylase	unknown	unknown	gnl\|CDD\|114868
NZ_CP013350.1\|WP_058155063.1\|2353529_2354651_-\|4-phosphoerythronate-dehydrogenase	unknown	unknown	gnl\|CDD\|240635
NZ_CP013350.1\|WP_008111059.1\|2340966_2341566_+\|YIP1-family-protein	unknown	unknown	gnl\|CDD\|369140
NZ_CP013350.1\|WP_036953707.1\|2363515_2364394_+\|OmpA-family-protein	unknown	unknown	gnl\|CDD\|375819
NZ_CP013350.1\|WP_013465465.1\|2345921_2346797_-\|acetyl-CoA-carboxylase-carboxyltransferase-subunit-beta	unknown	unknown	gnl\|CDD\|235547
NZ_CP013350.1\|WP_058155057.1\|2337572_2339801_-\|EAL-domain-containing-protein	unknown	unknown	gnl\|CDD\|238923
NZ_CP013350.1\|WP_083494660.1\|2364696_2365899_+\|amino-acid-permease	unknown	unknown	gnl\|CDD\|185086
NZ_CP013350.1\|WP_058155067.1\|2360679_2362305_+\|DUF342-domain-containing-protein	unknown	unknown	gnl\|CDD\|377177

Protein	Function_ID	Function_description	E-value
NZ_CP013350.1\|WP_024601782.1\|2358451_2359087_+\|SDR-family-oxidoreductase	gnl\|CDD\|379199	pfam13460, NAD_binding_10, NAD(P)H-binding.	4.17619e-50
NZ_CP013350.1\|WP_058155064.1\|2356150_2358160_+\|bifunctional-tRNA-(5-methylaminomethyl-2-thiouridine)(34)-methyltransferase-MnmD/FAD-dependent-5-carboxymethylaminomethyl-2-thiouridine(34)-oxidoreductase-MnmC	gnl\|CDD\|234978	PRK01747, mnmC, bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC.	0
NZ_CP013350.1\|WP_024601787.1\|2343198_2343693_-\|bacteriocin-production-protein	gnl\|CDD\|182773	PRK10845, PRK10845, colicin V production protein; Provisional.	2.4594e-62
NZ_CP013350.1\|WP_013465470.1\|2354759_2355971_-\|beta-ketoacyl-ACP-synthase-I	gnl\|CDD\|181184	PRK07967, PRK07967, beta-ketoacyl-ACP synthase I.	0
NZ_CP013350.1\|WP_013465481.1\|2362369_2363044_-\|ribonuclease-T	gnl\|CDD\|179951	PRK05168, PRK05168, ribonuclease T; Provisional.	1.24524e-151
NZ_CP013350.1\|WP_058155058.1\|2344630_2345896_-\|bifunctional-tetrahydrofolate-synthase/dihydrofolate-synthase	gnl\|CDD\|182774	PRK10846, PRK10846, bifunctional folylpolyglutamate synthase/ dihydrofolate synthase; Provisional.	1.13222e-148
NZ_CP013350.1\|WP_058155066.1\|2359079_2359838_-\|sulfite-exporter-TauE/SafE-family-protein	gnl\|CDD\|376667	pfam01925, TauE, Sulfite exporter TauE/SafE. This is a family of integral membrane proteins where the alignment appears to contain two duplicated modules of three transmembrane helices. The proteins are involved in the transport of anions across the cytoplasmic membrane during taurine metabolism as an exporter of sulfoacetate. This family used to be known as DUF81.	1.87417e-10
NZ_CP013350.1\|WP_058155055.1\|2335642_2337580_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	4.17779e-27
NZ_CP013350.1\|WP_013465463.1\|2343995_2344619_-\|SPOR-domain-containing-protein	gnl\|CDD\|225689	COG3147, DedD, Uncharacterized protein conserved in bacteria [Function unknown].	4.9412e-27
NZ_CP013350.1\|WP_058155061.1\|2352467_2353484_-\|aspartate-semialdehyde-dehydrogenase	gnl\|CDD\|237845	PRK14874, PRK14874, aspartate-semialdehyde dehydrogenase; Provisional.	0
NZ_CP013350.1\|WP_013465461.1\|2341653_2343180_-\|amidophosphoribosyltransferase	gnl\|CDD\|236427	PRK09246, PRK09246, amidophosphoribosyltransferase; Provisional.	0
NZ_CP013350.1\|WP_016899264.1\|2346973_2347768_-\|tRNA-pseudouridine(38-40)-synthase-TruA	gnl\|CDD\|234577	PRK00021, truA, tRNA pseudouridine(38-40) synthase TruA.	1.28337e-138
NZ_CP013350.1\|WP_016899267.1\|2339996_2340767_-\|tRNA-(ms[2]io[6]A)-hydroxylase	gnl\|CDD\|114868	pfam06175, MiaE, tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE). This family consists of several bacterial tRNA-(MS[2]IO[6]A)-hydroxylase (MiaE) proteins. The modified nucleoside 2-methylthio-N-6-isopentenyl adenosine (ms2i6A) is present at position 37 (3' of the anticodon) of tRNAs that read codons beginning with U except tRNA(I,V Ser) in Escherichia coli. Salmonella typhimurium 2-methylthio-cis-ribozeatin (ms2io6A) is found in tRNA, probably in the corresponding species that have ms2i6A in E. coli. The miaE gene is absent in E. coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.	1.09209e-94
NZ_CP013350.1\|WP_058155063.1\|2353529_2354651_-\|4-phosphoerythronate-dehydrogenase	gnl\|CDD\|240635	cd12158, ErythrP_dh, D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains. D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.	0
NZ_CP013350.1\|WP_008111059.1\|2340966_2341566_+\|YIP1-family-protein	gnl\|CDD\|369140	pfam06930, DUF1282, Protein of unknown function (DUF1282). This family consists of several hypothetical proteins of around 200 residues in length. The function of this family is unknown although a number of family members are thought to be putative membrane proteins.	7.34225e-42
NZ_CP013350.1\|WP_036953707.1\|2363515_2364394_+\|OmpA-family-protein	gnl\|CDD\|375819	pfam18393, MotY_N, MotY N-terminal domain. The bacterial flagellar motor is a rotary motor complex composed of various proteins. MotX and MotY are essential for the Na+-driven flagellar motor motility of Vibrio, Shewanella and Aeromonas species. MotY is main component for T-ring formation and absence of MotY completely disrupt the T-ring formation. This is the N-terminal domain of MotY which is shown to be essential for motility and responsible for the interaction with both MotX and the basal body. Functional analysis suggests that MotY-N connects the basal body to MotX and that the PomA/PomB complex associates with MotX to form the functional stator complex around the rotor. MotY-N alone does not associate strongly with the basal body, but the partial T-ring structure made of the MotY-N/MotX complex is sufficient to allow at least a few PomA/PomB stator complexes to be incorporated into the motor.	3.36341e-70
NZ_CP013350.1\|WP_013465465.1\|2345921_2346797_-\|acetyl-CoA-carboxylase-carboxyltransferase-subunit-beta	gnl\|CDD\|235547	PRK05654, PRK05654, acetyl-CoA carboxylase carboxyltransferase subunit beta.	0
NZ_CP013350.1\|WP_058155057.1\|2337572_2339801_-\|EAL-domain-containing-protein	gnl\|CDD\|238923	cd01948, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.	7.87828e-84
NZ_CP013350.1\|WP_083494660.1\|2364696_2365899_+\|amino-acid-permease	gnl\|CDD\|185086	PRK15132, PRK15132, tyrosine transporter TyrP; Provisional.	1.36542e-153
NZ_CP013350.1\|WP_058155067.1\|2360679_2362305_+\|DUF342-domain-containing-protein	gnl\|CDD\|377177	pfam03961, FapA, Flagellar Assembly Protein A. Members of this family include FapA (flagellar assembly protein A), found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction.	5.43228e-136

>NZ_CP013350.1|WP_016899264.1|2346973_2347768_-|tRNA-pseudouridine(38-40)-synthase-TruA
MRVALGVEYNGARYSGWQRQSHVNSVQQEVEKALSRICNHPVEIVCAGRTDAGVHGTGQVVHFDTHAEREMVAFTLGMNTLLPKDIAIRFAQPVAEDFHARFSATARRYRYVIYNYAFRGAVLNEGVTHFHHPLDEVKMQQACQYLLGEHDFTSFRALHCQANTATRTIHHLSVQRQGAYVIIDIKANAFLHHMVRNITGCLMDIGLHKHEPIWLKELLDVKERAKASATAKAAGLYLVDVDYPDHFNIPRTPLGPLFLADSDI
>NZ_CP013350.1|WP_013465465.1|2345921_2346797_-|acetyl-CoA-carboxylase-carboxyltransferase-subunit-beta
MSWLEKILPKTTKSSGRKEIPEGVWAKCTSCDSILYKAELEKSLNVCPKCDHHMRVSGRKRLEQFLDEGDRHELGAQHEPKDVLKFRDSKKYSDRINAAQKSSGEKDALVAMKGNLKGIPVAAVAFEFSFMGGSMASVVGARFVDAVDQCLEHNMPLICFSASGGARMQEALMSLMQMAKTSAALAKMTEKGLPFISVMTDPTMGGVSASLAMLGDINVAEPKALIGFAGPRVIEQTVRETLPEGFQRSEFLLEHGAIDMIIDRREMRDTLARILAKFMNLPSTEQEHRVA
>NZ_CP013350.1|WP_058155058.1|2344630_2345896_-|bifunctional-tetrahydrofolate-synthase/dihydrofolate-synthase
MTKTIPSQSSSLDDWLCYLESVHPANIEMGLERVARVANNIGLLTSSSKIILIAGTNGKGTTARCLESLLLAQGYRVGTYASPHLIRYNERVRVDGAELDDQYHVDAFNLLEQGRGDTPLTYFEYGTLGALAIFKRLEVDYVLLEVGLGGRFDATNIVTPYASIITTIDLDHKEYLGDTRELVAYDKAGIFRESTPAIIGDLNIPHTMTDYGKEINANMVLSGSDFIFKEHAQSFSWQFKEHNLELPKPAIPCQNVATALTALSVLNLLPSDEVITQCLASLVVEGRFQQLSAEPLVYTDVAHNPESARYLATKLASYKDKGFKIHALAAMLADKDKAGVLKEVSDVVDEWSFASLEGPRGDSAANLNQALLSIPNSNFKQGYNSVEAALDAILPNQSSNTLLIVFGSFFTVAGAIHYFKK
>NZ_CP013350.1|WP_013465463.1|2343995_2344619_-|SPOR-domain-containing-protein
MNSGFINRLVGTSIVVIAAIVFIPNILDGEKVHYKEGFKAIPERSEFKTIDLQESIDQKVANAQPLKEDEVEDIQPDDAAFEQQNSAAQTDITDQPAMVEAVIPDTNQSSTAAIQEPTRPANENLTSMAYVIQLGSFSHAANVKALQAKLKAKGFKTFTKPVKTPNGTLTKVFVGPSLNKQELQSQLPALKELTKLNGKVTQFEVTK
>NZ_CP013350.1|WP_024601787.1|2343198_2343693_-|bacteriocin-production-protein
MIWVDYAILGIIALSTIIGLIRGFVKEAMSLAVWAGAFIISSLFYQYLASFLTSISEPLLRNAAAIAILFFATLLLGGLLNYILGELVQRTGLSGTDRVFGVVFGALRGVLVVSALLFFLDAFTGAPSTHWWGNSILIPEFGFVVEWFFSYLENNSSFLNSVNR
>NZ_CP013350.1|WP_013465461.1|2341653_2343180_-|amidophosphoribosyltransferase
MCGIVGIVGTSPVNQAIYDGLTVLQHRGQDAAGIITIENNTFSLRKANGLVKDVFHTRHMKRLQGNIGIGHVRYPTAGSSSSSEAQPFYVNSPFGIALAHNGNLTNAESLKEQLFSEARRHVNTTSDSEILLNIMAHELSKSDKLKLDPEDIFTAVTEVNNKVSGGYATIAMIIGHGIVAFRDPNGIRPLVFGKRESANGTEYMFASESVALKPDGFEFVRDVAPGEAIYVTENGEFHSLSCADKVSYSPCIFEFVYFARPDSTIDRMSVYAARVNMGTKLGEKVAREWADKDIDVVIPIPETSCDIALEMARVLDLPYRQGFVKNRYIGRTFIMPGQELRKKSVRQKLNAIDREFKGKNVLLVDDSIVRGTTSAQIVEMARESGAKNVYFASAAPEIRFPNVYGIDMPSAAELIAHGREVEDINQSISSDGLIFQSLSDLIAAVSQENPEITKFETSVFDGQYITGDIDQDYLNRIDKLRNDSAKSIRENAMSSGLEIHNQDENESD
>NZ_CP013350.1|WP_008111059.1|2340966_2341566_+|YIP1-family-protein
MILNHLWGLYAHPLEEWQTIDNRHESLTYSLSHILLIALFPSAMGYYSSVYLGWSIGTGNPVFLTHESALMIGAAMYVALIGGVFALAYLAHWMAVTFGAKPTFTQTIELAAYTATPVFMSALAAFWPELWFVVCVGLVALAYSVYLLYTGVPILMHIPQERGFIYASSVVTCGLILLVIILALTAMLWTNGIISPMFT
>NZ_CP013350.1|WP_016899267.1|2339996_2340767_-|tRNA-(ms[2]io[6]A)-hydroxylase
MPHSQLLEPINNFLLCSTPDEWVEQAIKKENLPIILIDHLICELKAAQSAMFLIRKYAVDKESSDALLEWLKPFETLIYKREGNWRDLAAKNKLTKSIIPKSNSPYGQDLIDKMVMLIKEELHHFYQVLEIMDEYGVEYKSITPCRYAKGMLRNVKTFEPNALVDKLIVGAYIEARSCERFAKLAPHVDKRLGDFYISLLRSEARHYQDYLTLAQDIADFDITERVKEFAEIEAQLILSDDEDFKFHSGTPLSKSA
>NZ_CP013350.1|WP_058155057.1|2337572_2339801_-|EAL-domain-containing-protein
MQDKEGLFVFAAEEEQADTDLKTWKILTVEDDLDYQNALVNSLKELKAKDGYKYELLTANSVPEAALALSMHPDIALIFIDVVMEEDDSGLRLVNTIREVIGNAEMRIVLLTGQPGFAPESDIMKMLDIDEYWNKSDLSAEKLQSIVNSNMRTWEYISQIRSAKQGLQLVLDASRSINGKHDMASFSYAVLKEISNILKITEGGGIFCSSNSDPSSECLILSTHGCFSGIKGQPVGPNLPAEMLQDFKQAIRERRHIFSKHHSVFFFETPDQQGADYITIVKSDNPISEQNEYLLKVFSENVSTGFANISLLNRLTELAYTDVSLNLQNRNWLTREIKNMNAQERLKTRLVIFDIYQFDEKAFTFGHEFCNKLMKLVYQSIVDSFTRYDPRIALISNKAFGMLVSVDFDISNAVSYFQNKQKFEIEQVKQYIDVRILELKLNVALNLTPEKVISLAESSLNSSQLNQTKYIQHTEEKTDQITRRYELMAELRTAIGNKSLQVALQPKISLSTLKPAGFEALARWQRADGSFVRPDEFIELAETAGLINELDHVIFEKILETINQLKEQGCNLPVAFNASSYDLVEPSYFEQIKTKIEEYNILPSMLELEVTETQAISNYNLIKEALERFIALGMKVSIDDFGTGYSSLAHINEIPSTSIKIDRYFVSDLEFNDNNQYMIKMILSLANQFNFSVIAEGVENEFEAQWLHQQGCETAQGYYFSKPLFLKDLIVWLKQFEVSKNE
>NZ_CP013350.1|WP_058155055.1|2335642_2337580_-|HAMP-domain-containing-histidine-kinase
MNSLNSLPVGSKKSVLIKSLFSLFITLFIGWLIYEQTYQEKINTIKAKQDEKLVLISGDFSKELSSIKKLTRILAQGPILKSDTPNKPLQSKQRRDEINNYFLNFAAISTNIAQIRWLDTQGQEQYRINAANGIGEIVSPDELQNKQTRYYFQKGMQVSAPDIFATEIDLNIERNQIVIPHQPTIRVTYRTDKENYLLDGLLVVNFNLDYLFDQIKSYNQESTLISILNHDGFWLLNTDAELEWGFMYGKNEQTLALKKPELWQQIIDGNVEYGSHFFNHSLYTYRRFSIFSLRENKGRISNADKELIILISSPNELLITVRNAALRLALICSGLLCLISFGFIYREYKFQNQLLALTHKLHIEKIELDIVNRELDATIKQQQQLQEGLIEAQKLSSLGLLVAGVAHEMNTPIGGAVISVSNADMALNKLNEAMKQGLTKSTLESTTTSIGENLALAKINLNKTAVLVKSFKKMAIDRHNDEFIACDIEKIIEELLLSLNSRLKNSPIKVKTIFLLNKQVISLPGIISQVVENLVVNALNHAFDEKQEGVIEIKVEQATNNRVRLSVSDNGKGVDGEIKADIFEPFYTSARGKGNTGLGLYMVYQWVTQILKGDIKLHSEPQSDTYFKTQFIITLPDLKAKSHYD
>NZ_CP013350.1|WP_058155061.1|2352467_2353484_-|aspartate-semialdehyde-dehydrogenase
MSQKYNVAVLGATGLVGRQIIETLEDRKFPVDQLFLLASSRSAGEDIKFRGETIEVRDVEGFDFSQAHIGLFSAGGSVSEKYAPIAADAGCIVIDNTSHFRNDFEVPLIVPEVNASSLADFRNRNIIANPNCSTIQMMLALKPIYDVYGIDRINVSTYQAVSGAGKEAVDELAKQTANLMNARPMENEIFPKQIAFNVIPQIDSFEDNGYTREEMKMVNETHKILGDTTIAVNPTCVRVPVFFGHSESINIETRMPYDFEHVKQLLSDAPGVELIDDAGDYPTAVSDASGNDTVYIGRLRADISHPHGLNMWVVSDNTRKGAATNSVQIAEELIANYM
>NZ_CP013350.1|WP_058155063.1|2353529_2354651_-|4-phosphoerythronate-dehydrogenase
MKILADQNMPLVEQFFKDMGEVERFDGRQLTPEQLIDVDVLLTRSVTQVNSELLAQANKLSFVGTATIGVDHIDTDLLNAKNIDFTSAPGCNAIAVAEYVISSLFALSQENASPLSGKTIGIVGVGNIGSCLAHKLKALNVNLLLCDPIKHEQGLLTEHVELDELLAQSDIVTFHVPLVKTGTHKTLHMLDKKRLTTLKPGLTLINASRGDVIDNQALLEVMEAGAELDLVLDVWENEPNILTELLEHVRYASVHIAGHTLEGKARGTQMLYQSLCELKGVNAIKSLDDFLPPPAIKKVALGSSFSETDIARLVHLVYDVRRDDGILLRHLADEGFDSLRKNYPTRREFSTVVVEGDSTELAALAQLGFTTAN
>NZ_CP013350.1|WP_013465470.1|2354759_2355971_-|beta-ketoacyl-ACP-synthase-I
MRRAVITGIGVVSSIGNNKEEVLESLRAGKSGIAFNQEFADYKLRSNVSGKIDIDVKEHVDRKAMRFMGDAAAYSYISMAQAIEDAGLSDEQVSNERTGLLVGSGGGSSKWQVEAADILREKGVKRVGPYMVPRTMASTTSACLATPFKIKGVNYSISSACATSAHCIGHAVEQIQLGKQDVIFAGGGEELHWTLAMEFDAMGALSTKYNDTPEKASRTYDANRDGFVISAGGGIVVVEELEHALARGAHIYAEITGYGATSDGYDMVAPSGEGAVRCMRQAMQNVDSIDYLNTHGTSTPVGDVKELGAIQEVFGGNSPMISATKAMTGHALGAAGVHEAIFSLLMLEHGFVAPSINIDELDEQAAGLNIVTEAKDVELNTVMSNSFGFGGTNATLVMSKYKG
>NZ_CP013350.1|WP_058155064.1|2356150_2358160_+|bifunctional-tRNA-(5-methylaminomethyl-2-thiouridine)(34)-methyltransferase-MnmD/FAD-dependent-5-carboxymethylaminomethyl-2-thiouridine(34)-oxidoreductase-MnmC
MIKNAHIHFNDLGTPVANDFDDVYFSNDDGLAESHYVFYQQNSIESRLQNHDREHFVIAETGFGTGLNFLNAWQQFYDHLQCPQVQSQQSNNVQRLHFISFEKYPLSVNDLKQALQAWPSLSHLSAQLVSHYPINLTGCHRLEFANGLVVLDLYFGDVLECINSMSYPQSGLVDAWFLDGFAPSKNPDMWQQSVFNAMVDISRSNATLATFTAAGFVRRGLNEAGFSMQKAKGFGRKREMLVGTLAQANSKQSAPAYFEHHFSPLTNVAVIGGGIASSCILYGLAKRGIPSHLFCQDKQPAMGASHNVQGAIYPHLQAKNSPHSELFAHSFLYAKRLYNQLLNNGFLFDHQWCGVLQHAVKQPLAERHQNLADKQLWPEQLMRNVTADEGDAIAGVKTGYSGVFFEQGGWVNPPQLVSAMLDATQQLNEFESLFNCHIEQLNKQPDGWYLTTQKQTFGPFSDVIICAGEHSDAFAQTKTLPIVGVRGQVSHVQASTQSRKLKTVLCHKGYFTPAYLDHHCMGATFEKNSKSREVTEQDNQTNREQLLSFYNNTEFATSLGDISSAKAAVRCSFIDHLPMAGEWVEQTDYTHAFANLRLGKRYQYQALKKPQQGLHIFTGFGARALCSAPLSAEHLISSLNNEPRPLSERVSQAIHPGRFIVRDLIRNKI
>NZ_CP013350.1|WP_024601782.1|2358451_2359087_+|SDR-family-oxidoreductase
MSKTLIIGASGQIGKMATKLLLENEQNVVALVRDKSKLCDLDSPFLSIVEQDLEGDFSSAINGCDQVIFAAGSGGSTGTDKTVLIDLWAATKAATYSKEHGVKHFIMVSSIGADDPDAIDSDLKPYLVAKHMADEHLIHSGLNYTIVRPGTLTDESASLEVTTERPSDQSKAKISRENVANALLHVATNSFNSNRIFELFDGDKPIKAAIK
>NZ_CP013350.1|WP_058155066.1|2359079_2359838_-|sulfite-exporter-TauE/SafE-family-protein
MDIFTAEHISPLISLLLVLLAGVTSFVSAAFGAGGGLMLLVVMASVMPMAVVVPVHGLVQLGSNANRLLLSIAHLDKSMLLYFTLGGLIGAGLSIQVVSDINLDSMKLFVALFVIYLLWGTTPEFNKDSRLGRLIAGVITAFISTFVGASGPLVASYLHINHYDKLKFTATFSSIMTLQHSLKAVVYAGLGFSFWQWLPLTLAMILSGAIGTWLGIRLLKRLSVARFRVVFKVILTLLAMQLAWQGVSVMLT
>NZ_CP013350.1|WP_058155067.1|2360679_2362305_+|DUF342-domain-containing-protein
MSVFSFDEQTGHISLLSHPNVSGLASTATQLIELISQSEYCECDIIAGNIGKLFAQNNDEETPSLVVAQAIDAKLTINIDEKNMLVEATLITAKGGKLLNMEQAIDVLAQAGIVKGISSHALEQLLAQQLEQPSGSTHCAEVAFGRAPKVGNDAKFVRLCCTAQDRVLSPQAKGGGKVDMRNLGDIITVKPGCELMRRIPATSGVDGFTVFGDVLTAIPGKEHKLQPFDGTKIAPDNPNLLIADCTGVPVALPRGMRVDDVLCFHNIDPSTGHVEFDGSIIVSGDIKDGMRVTATGDITVLGFVESAQLKSNSAITIVKGAIGRKREADEPFTCSIFAKRTVALGYSQYCDIKTEQNLLIERQSLHCDLSAGNLIRVGSAKDPKGKIIGGHILDAMRIETGELGAPAGTKTRVCIAQRWYVLKQKQAQITDFEKVLISKSIELQQARQRINKQVASAQRQQFLNKITTNEEHIANRSASISQQKQLLRKKMAQLLALSRLKVNELMHPGVELKIARESISFSRNYPPHLITHSEGKITQSF
>NZ_CP013350.1|WP_013465481.1|2362369_2363044_-|ribonuclease-T
MANTEQTLFAQRFRGFFPVVIDVETAGFNKETDALLEIAASVLKMDDEGLLSIDHTVHFHVQPFEGANIEQAAIEFNGIEPFSALRGAVPEEEAIKEICKVVRKAQKAAGCQRSVVVAHNAAFDHGFLNAAIERNNIKRTPFHPFVSFDTTSLAGLALGQTVLAKACRAAGIEFDNKQAHSALYDTERTAELYCLIVNRWQQLGGWPLAIDETQQNEDEVSNQD
>NZ_CP013350.1|WP_036953707.1|2363515_2364394_+|OmpA-family-protein
MKCKLLFISLGISSVLYSLNTTAAMRQYTANQDNSNWNLVKTTRLQCQLNHEVPYYGEAVFKASASKNKDLTFNLDMVVRPENYAIAGLKAVPPSWRAGRPARDIADMKLLKKFDGELGNKTAWEMLTELEKGNQPTFYYQDWQNSADKIAVGMSNINFKQAYWAFLQCRDELLPYNFEDISFTIMNYESNSSKLTKSSQQRLDKIAEYLKNDPSIESISIASYTDSYGGRWNNLDLSRKRAKEIKDYMVGLGVDEAKVVTEGFGEKRFVDTNDNILGRDKNRRLVIQIAKM
>NZ_CP013350.1|WP_083494660.1|2364696_2365899_+|amino-acid-permease
MLKNKTIGSMLIVAGTTIGAGMLALPIASAGLGFNTAMVLIIGCWLLMTYTALLMLELHQYAPRDATLNTLAKLWLGKRGQYVANFSMIFLFYALCAAYIAGGGAQLQERINTGFNLSIAPQLGSVILAVVIAGVVTLGTSKVDKLNRVLFSIKIVVLGSLFYMLTPYVHGQHLLEMPVEQGLILSAIPVVFTSFGFHGSIPSIVKYVGLDIKTLRKVMIAGASLPLVIYIFWQVLSQGIMSQAQLLESEGLSGFVASVANIANNTSVSTAVKLFADLALATSFLGVSLGLFDFFADTFKKADTGADRIKTAFITFIPPLGFALFYPQGFIMALGYAAIALVILAVFLPVSMVYKQRQGVEKSGYKVRSGNIGLAIAALCGISIISAQCLQMAGLIPAIG

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP013350_1	1.1\|447322\|31\|NZ_CP013350\|CRISPRCasFinder	447322-447352	31	NC_010802	Burkholderia multivorans ATCC 17616 plasmid pTGL1, complete sequence	43453-43483	9	0.71
NZ_CP013350_1	1.1\|447322\|31\|NZ_CP013350\|CRISPRCasFinder	447322-447352	31	NC_010070	Burkholderia multivorans ATCC 17616 plasmid pBMUL01, complete sequence	70003-70033	9	0.71

1. spacer 1.1|447322|31|NZ_CP013350|CRISPRCasFinder matches to NC_010802 (Burkholderia multivorans ATCC 17616 plasmid pTGL1, complete sequence) position: , mismatch: 9, identity: 0.71

ccagaatgtaggacgcgacccgtcgcgcact	CRISPR spacer
ggaagttgcaggacgcgacacgtcgcgcaga	Protospacer
  *.. **.********** *********

2. spacer 1.1|447322|31|NZ_CP013350|CRISPRCasFinder matches to NC_010070 (Burkholderia multivorans ATCC 17616 plasmid pBMUL01, complete sequence) position: , mismatch: 9, identity: 0.71

ccagaatgtaggacgcgacccgtcgcgcact	CRISPR spacer
ggaagttgcaggacgcgacacgtcgcgcaga	Protospacer
  *.. **.********** *********

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site	Prophage annotation

Anti-CRISPR protein detection

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