CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Target MGE spacer number	Prophage number
NZ_CP042179	Burkholderia sp. KBS0801 chromosome 3, complete sequence	1 crisprs	Cas14u_CAS-V,csa3,c2c9_V-U4,cas14j	1	0
NZ_CP042178	Burkholderia sp. KBS0801 chromosome 2, complete sequence	1 crisprs	Cas14u_CAS-V,DEDDh,csa3,DinG,cas3,c2c9_V-U4	0	0
NZ_CP042177	Burkholderia sp. KBS0801 chromosome 1, complete sequence	5 crisprs	cas3,DEDDh,csa3,c2c9_V-U4,DinG,RT	0	3

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP042179_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP042179_1

962601-962677

Orphan

Consensus_repeat	Method
GACACACGTCCGGCATCGGCCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP042179_1

>merge|NZ_CP042179|1|962601-962677|CRISPRCasFinder
GACACACGTCCGGCATCGGCCGCGGCGGTCACATCGGCGGTCGCGGAAACCCAAGACATACGTCCGGCATCGGCCGC

>NZ_CP042179|1|1|962601-962677|CRISPRCasFinder
GACACACGTCCGGCATCGGCCGC	GGCGGTCACATCGGCGGTCGCGGAAACCCAA
GACATACGTCCGGCATCGGCCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP042179.1\|WP_138850693.1\|966232_968002_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042179.1\|WP_138850695.1\|969190_970342_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|240227
NZ_CP042179.1\|WP_138850888.1\|956347_957496_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378468
NZ_CP042179.1\|WP_138850692.1\|964347_964908_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380090
NZ_CP042179.1\|WP_138850691.1\|964127_964439_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237871
NZ_CP042179.1\|WP_138850891.1\|965314_965674_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|312947
NZ_CP042179.1\|WP_138850688.1\|950903_952688_-\|secretion-system-protein-E	unknown	unknown	gnl\|CDD\|225363
NZ_CP042179.1\|WP_012372038.1\|952692_953283_-\|type-IV-pilus-biogenesis-protein-PilP	unknown	unknown	gnl\|CDD\|274394
NZ_CP042179.1\|WP_012372042.1\|958294_959728_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197666
NZ_CP042179.1\|WP_138850697.1\|972635_974033_-\|sodium:sulfate-symporter	unknown	unknown	gnl\|CDD\|273267
NZ_CP042179.1\|WP_006750733.1\|970494_970983_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|312947
NZ_CP042179.1\|WP_138850889.1\|960579_961113_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042179.1\|WP_138850690.1\|957556_958207_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042179.1\|WP_138850687.1\|949837_950914_-\|type-II-secretion-system-protein-F	unknown	unknown	gnl\|CDD\|224376
NZ_CP042179.1\|WP_138850696.1\|971641_972613_-\|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|99782
NZ_CP042179.1\|WP_012372043.1\|959902_960370_+\|lytic-transglycosylase-domain-containing-protein	unknown	unknown	gnl\|CDD\|381603
NZ_CP042179.1\|WP_138850694.1\|968170_969025_+\|formyl-transferase	unknown	unknown	gnl\|CDD\|223301
NZ_CP042179.1\|WP_138850689.1\|954614_956348_-\|PilN-family-type-IVB-pilus-formation-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274177
NZ_CP042179.1\|WP_012372048.1\|965693_965999_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042179.1\|WP_126223945.1\|953272_954589_-\|type-4b-pilus-protein-PilO2	unknown	unknown	gnl\|CDD\|369114

Protein	Function_ID	Function_description	E-value
NZ_CP042179.1\|WP_138850695.1\|969190_970342_-\|hypothetical-protein	gnl\|CDD\|240227	PTZ00009, PTZ00009, heat shock 70 kDa protein; Provisional.	1.65125e-05
NZ_CP042179.1\|WP_138850888.1\|956347_957496_-\|hypothetical-protein	gnl\|CDD\|378468	pfam10671, TcpQ, Toxin co-regulated pilus biosynthesis protein Q. The toxin-coregulated pilus (TCP) of Vibrio cholerae and the soluble TcpF protein that is secreted via the TCP biogenesis apparatus are essential for intestinal colonisation in the disease of cholera. TcpQ is part of an outer membrane complex of the TCP biogenesis apparatus, comprised of TcpC and TcpQ, and the TcpQ is required for proper localization of TcpC to the outer membrane. The domain is found in other Proteobacterial species apart from Vibrio.	7.9831e-22
NZ_CP042179.1\|WP_138850692.1\|964347_964908_+\|hypothetical-protein	gnl\|CDD\|380090	pfam18013, Phage_lysozyme2, Phage tail lysozyme. This domain has a lysozyme like fold. It is found in the tail protein of various phages probably giving them the ability to degrade the host cell wall peptidoglycan layer.	1.76935e-28
NZ_CP042179.1\|WP_138850691.1\|964127_964439_-\|hypothetical-protein	gnl\|CDD\|237871	PRK14965, PRK14965, DNA polymerase III subunits gamma and tau; Provisional.	1.59618e-06
NZ_CP042179.1\|WP_138850891.1\|965314_965674_-\|hypothetical-protein	gnl\|CDD\|312947	pfam09613, HrpB1_HrpK, Bacterial type III secretion protein (HrpB1_HrpK). This family of proteins is encoded by genes found within type III secretion operons in a limited range of species including Xanthomonas, Ralstonia and Burkholderia.	1.10191e-09
NZ_CP042179.1\|WP_138850688.1\|950903_952688_-\|secretion-system-protein-E	gnl\|CDD\|225363	COG2804, PulE, Type II secretory pathway, ATPase PulE/Tfp pilus assembly pathway, ATPase PilB [Cell motility and secretion / Intracellular trafficking and secretion].	4.25938e-76
NZ_CP042179.1\|WP_012372038.1\|952692_953283_-\|type-IV-pilus-biogenesis-protein-PilP	gnl\|CDD\|274394	TIGR03021, pilP_fam, type IV pilus biogenesis protein PilP. Members of this protein family are found in type IV pilus biogenesis loci and include proteins designated PilP. [Cell envelope, Surface structures].	3.34116e-10
NZ_CP042179.1\|WP_012372042.1\|958294_959728_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|197666	smart00342, HTH_ARAC, helix_turn_helix, arabinose operon control protein.	7.66388e-16
NZ_CP042179.1\|WP_138850697.1\|972635_974033_-\|sodium:sulfate-symporter	gnl\|CDD\|273267	TIGR00785, Uncharacterized_transporter_HI_0020, anion transporter. The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally characterized proteins of the DASS family transport (1) organic di- and tricarboxylates of the Krebs Cycle as well as dicarboxylate amino acid, (2) inorganic sulfate and (3) phosphate. The animal NaDC-1 cotransport 3 Na+ with each dicarboxylate. Protonated tricarboxylates are also cotransported with 3Na+. [Transport and binding proteins, Anions, Transport and binding proteins, Cations and iron carrying compounds].	5.84019e-16
NZ_CP042179.1\|WP_006750733.1\|970494_970983_-\|hypothetical-protein	gnl\|CDD\|312947	pfam09613, HrpB1_HrpK, Bacterial type III secretion protein (HrpB1_HrpK). This family of proteins is encoded by genes found within type III secretion operons in a limited range of species including Xanthomonas, Ralstonia and Burkholderia.	3.54946e-21
NZ_CP042179.1\|WP_138850689.1\|954614_956348_-\|PilN-family-type-IVB-pilus-formation-outer-membrane-protein	gnl\|CDD\|274177	TIGR02520, putative_Type_IV_pilus_protein, type IVB pilus formation outer membrane protein, R64 PilN family. Several related protein families encode outer membrane pore proteins for type II secretion, type III secretion, and type IV pilus formation. This protein family appears to encode a secretin for pilus formation, although it is quite different from PilQ. Members include the PilN lipoprotein of the plasmid R64 thin pilus, a type IV pilus. Scoring between the trusted and noise cutoffs are examples of bundle-forming pilus B (bfpB). [Cell envelope, Surface structures, Protein fate, Protein and peptide secretion and trafficking].	1.70527e-142
NZ_CP042179.1\|WP_012372043.1\|959902_960370_+\|lytic-transglycosylase-domain-containing-protein	gnl\|CDD\|381603	cd13400, LT_IagB-like, Escherichia coli invasion protein IagB and similar proteins. Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.	1.23866e-54
NZ_CP042179.1\|WP_138850687.1\|949837_950914_-\|type-II-secretion-system-protein-F	gnl\|CDD\|224376	COG1459, PulF, Type II secretory pathway, component PulF [Cell motility and secretion / Intracellular trafficking and secretion].	7.51989e-22
NZ_CP042179.1\|WP_138850696.1\|971641_972613_-\|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein	gnl\|CDD\|99782	cd06185, PDR_like, Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.	9.32178e-83
NZ_CP042179.1\|WP_138850694.1\|968170_969025_+\|formyl-transferase	gnl\|CDD\|223301	COG0223, Fmt, Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis].	1.38083e-29
NZ_CP042179.1\|WP_126223945.1\|953272_954589_-\|type-4b-pilus-protein-PilO2	gnl\|CDD\|369114	pfam06864, PAP_PilO, Pilin accessory protein (PilO). This family consists of several enterobacterial PilO proteins. The function of PilO is unknown although it has been suggested that it is a cytoplasmic protein in the absence of other Pil proteins, but PilO protein is translocated to the outer membrane in the presence of other Pil proteins. Alternatively, PilO protein may form a complex with other Pil protein(s). PilO has been predicted to function as a component of the pilin transport apparatus and thin-pilus basal body. This family does not seem to be related to pfam04350.	5.18872e-48

>NZ_CP042179.1|WP_138850889.1|960579_961113_-|hypothetical-protein
MKNLGIQTGLVRSRIAEFEKGTKNGATDGAQKQAPARSKGQLDGLSSFKGADGAPPPPPPPPRNFASLPGRTGNVGAQFLSSALHAGSHFLPPGVASTAMHAAGDMMRPSALGAGNPVTQMAAMQNDFMQQQSEMTRLNNANTLAAAVNQQSQELTSALASVGNKGASNISNAAKGQ
>NZ_CP042179.1|WP_012372043.1|959902_960370_+|lytic-transglycosylase-domain-containing-protein
MMRLFTPKPALALALAVLSARPAEVRAQTPDCFAAAAAYQHVSPVVLRAIAWQESHGNANALHRNRNGSTDYGMMQINSIHLPLLSRYGVSADDLMNPCLSVYVAAWHLHKMMVKYGNNWAAIGAYHSETPAERDRYARSVQSIVERMKLADDGQ
>NZ_CP042179.1|WP_012372042.1|958294_959728_+|helix-turn-helix-transcriptional-regulator
MFSTIYFAAASALAFDDTPADVASKMLQGQFLDAVRHAARHADTDTAQAQPGYAQLQVCADLELMLGRHEEAEETYRRAQKAIRAQRDGLRIASCRNTGWQAFFRNQFNVALSCFKRVGEEKAATPHQRLDSLVGATLVSFHLGLIQAACHRLGELAALAATHGDRRWSYLVEALRRDLFAQHELHGAERLADHIYWRSAIGEFEPSEAPVPGSQPAGTVLPLLAERLSHLNRLVSLADGRTSAGETLKQYVSWSRQAGLNDYHRSLCLEITLAAIAGHATPLAEAMLDASGAANSQGSQHARWYLDYLYCRAKIMQQQMRTQEFAQFYGRYALASIQHVRADMSMPAAAADHMQASRTAQRSDDVSARLPAKYRRAYRYLMDNLDQKDLSVREVASHVGVTERAMQAAFKNHLGLSPSELIRRQRMERIRDDLLDDGAPATRVLDVANKWGVRHRSTLINGYRRVFQEAPSETMGR
>NZ_CP042179.1|WP_138850690.1|957556_958207_+|hypothetical-protein
MDREFYFFCCHVLFTLLEPLHLPEQTEQRQADPSLCSGNANNCPKRSSTEWRPEFESKYARKQYRLVRIATAQWVFTAKYTAPLSKKIPLENHPFSASMDDTGTGARMSPSRHKPRPAWRCGSRRIFLDVSARIAEWPPAEICQIQTCAMATFAGEPPIGCRAPRQQRTAAAKSNKKSSKKATQASRSCVKAHRGTALSGKCRCQTEGNKPSQTRA
>NZ_CP042179.1|WP_138850888.1|956347_957496_-|hypothetical-protein
MPPAIRALLCGVWFACTVAHASDQQVIVDGGQRLGGVVRTGGHDVPLLRALEQIMPTSYSINVPNAGAWADASVSWRAGSSVVHALGEVLSVDPALQARVDTDMHLLTVTAHARRANVDAPQPSSPAAGAASRMNSAATNASSTLPAGAAAMAPAAGPAIAPAQTLAQARVSTWIPATPASARTPAAALAVPPVPAPAPAPAPVTSPAPAAGPAMPASVPAPALAMPPAPAAGPAMPASVPVLVSAPPRAQVPAPAKRDAIEPPLLAATQPASGPASPAPSSAPAATPAFVPAAAPERTEWQMRLSDGSVRNALARWASEAGWQFIWDVPTDFQVDATATIHGTLAEALRQVTNALAGSQVPIQVVLYQRNHVMRVVPKGAS
>NZ_CP042179.1|WP_138850689.1|954614_956348_-|PilN-family-type-IVB-pilus-formation-outer-membrane-protein
MSVLRRPFVILAACLSLLAGCTGLLDKIERNSQSDTARAGQLLGKLSNGDNRAVPGSDDVIVKDELWLSGKTIKIATKSTLPKLFDEPASFDGTVDSLRMFADRISRLAHLPAKVAPGTSEAAARATQTAVDTGGAGAYPGVPPLPAGLLQGPAPSTSAATVAARVPSVSSPVRIAYSRGTLRGLLDTASARFGVYWKYEDGAIVFFYTATRVYQVVAIPGDSKLDTNVVSGASNSGGASGNSAGAAGGSGAGGAGIGGGGGGTSGSPSVSSDNTANITMNAQLSVYNGLQTAIKAMLSPAGSVITSPATGSIAVTDTPDVLERVGEFMEQQNRVLARQVLINVTVLSVTLSAADSYGINWHAVYQALGTQFGITTAFTSMIQNPSELSASVITPSSRASSTTAVIDALSTQGTVHRKTSASITTLNDQPVPVQVAEQQGYLAQISTTNTVNIGSQTSLTPGTITTGFNLTVLPHILDDGTIMMQFYSNISSLVNLVPFGPANQQIQLPTVDTRNFLQRIAVKSGQTLVISGYEGITDQDNRQGVGHPSNYAMGGFNASGTREVIVILLSPIAINGA
>NZ_CP042179.1|WP_126223945.1|953272_954589_-|type-4b-pilus-protein-PilO2
MATQVIQIGRQRFICGLFWQSLSRRHALRAEAVELAARLNFDAMVLRIDRTFAGAGFASTREGAQLGLPSLGALVSKTIAAEGAFYDGRQQPAPNWLGAFHLPDGRWAYFAVRDGAFLPNGDRIGSSEEVFERLHSDYSLGGWNVVIGDPQLEVQGFHNFYARRIEDMIPRRGGKPHLPRWLNLSRVSRRAPRREVLLAAVAIVVAAAVVAGIVAYRRHRMEVERQQAFERMRAELALHPPKPAAPPEAAHPWAGEPRPDAFVRACVDHFTHIAPGGWELDDYVCRASNVSYSWSRDGSNVAMLMAAEPRATIDGNGEHASYVEPLALPAGGDEVIDGVRGVRLRMLSAFQLLGIGLTFTLQPASAPQRSLASQTLDRLHPGGGPPPAPSWQTWRMSAQLGGVRPDSLIRYLDEPGVRVETLSYKSGQWTLDGVLYEK
>NZ_CP042179.1|WP_012372038.1|952692_953283_-|type-IV-pilus-biogenesis-protein-PilP
MRNDDALTVLVLACCWAWPLAASGAASAAAATAAAPAEAAPRMNVVPTPAAVQAANELMRLQEETMILKAQLKKLDAQAQVAERQEALHRMGSTVSSYSDVSLVATQGLGKKLSATVATSDGAEFDVGPGDALPNGMRVAAIRPGAIVLASQDGRRTTLTVSASARQQPARSNVASTGSPGVPPVPTLPALPMPAR
>NZ_CP042179.1|WP_138850688.1|950903_952688_-|secretion-system-protein-E
MSSSPTPPGKTRTSVTPLILSRAVKPVETDPSLTQGQPAAPAGPALAPVARPREPVLSAVAAAAAASVQPAQAASQSQPQGQALPLAAVARPLSDSGEFAASDEERKFLCLLDDGTLLVAEGHEMNPFVLSYCARLERLNCRYATRLVTLDAIRRSYQGQRRDGSAERIDHTRMQVLAKNLIARACDERASDIHIRVNRFSTEILFRIHNELVRISEQTREYGERLLATLYAAMSSVSDNTYKPNERQDAAIGDRDKLPDRLFGVRIATAPTSVGSVMVLRLLYNDAGEATALTELGFTVAQANAFELLAQQPHGMNIISGPTGSGKSTTLQRVLTKQLREMAGSIHVITVEDPVEYPIEGAVQTPVVNAPTEEARSLAFAAAIANAMRLDPDTIMIGEVRDRASAQSALRAAMTGHQVWTTVHANGALAIVDRLVDLGLPIAMVTDESLVTGLISQRLAKLLCPHCSRPLAEAMAQLDMGLVARVRRAVGARFDAVRVAGPGCPHCKNGTVGRTVVAEVVRTDATFCELLRAGRKPDAQAYWLSELAGQTVAQHALEKVAAGLIDPRMAERVVGPFMQGSGGRPQPLGSGYGT
>NZ_CP042179.1|WP_138850687.1|949837_950914_-|type-II-secretion-system-protein-F
MALELNRRWARLQFTTQPRLRLYRKIAKMLANGLPLLKILEELELRASHEGRKPNEPLALTLADWRSVVQNGGMLAEAMAWWVPHTEQMIVMAGEQSGRLEAALLNVCTVVQYSRRIRTAIVGGLTYPCVIVAMTIGYVYLFGKLVIPRFASIVSPERWHGVAKSLYELSRFVQGGMIYCLVVLAILVAALFYSMPRWSGNVRVWLDRYPPYSIYRLITGCGFLVAFSSLQAAGFTVERSLARLATDAKPWLRQRIDDMLFGVKSGLNVGEAMKNAGYRFPSEEIVDDLCVYAEYKGFAEALHAIASEWMTDGVETIEAQMRVVNGAAIVVLALVLSWLISGFFGIQQEIAALARSLH
>NZ_CP042179.1|WP_138850691.1|964127_964439_-|hypothetical-protein
MLPWLPPPPLPPPPMPGDAPPPPWPPPPPLTPAGAPPPPPAYAGGAAYEGVPPPMPPTPPASPEFWLEGSRICLISSMSNSSSCASCDSFVPPMPPTSSMPFR
>NZ_CP042179.1|WP_138850692.1|964347_964908_+|hypothetical-protein
MSGGGGGHGGGGASPGIGGGGSGGGGSHGNTLPTVSGGDAAHAIAQDLKSRYGLTDAQVAGVLGNLQQESGLQGNVNQGGAKGAPSGNFADDNANGWGLAQWGGTRKQGEINYAKEHGLDPGSLEANIGFMNQELDTTYSKTITDIKQTTTAEQAALVWDKDYEQATDPQMENRNKYAEQFLAQGF
>NZ_CP042179.1|WP_138850891.1|965314_965674_-|hypothetical-protein
MMELLTELPADAPAMAQAIIEHIEANELDEAEALLARMHDVYPETREVHVFAVTIALVRGRPHEAWQIVNGLPDDRAPELKAICLKVLDDPSWHGYATAHEDSADPYVRLAMRRLLERD
>NZ_CP042179.1|WP_012372048.1|965693_965999_-|hypothetical-protein
MSFIGNIVKSVVGDVTKAAGGVLHGVGNALHGAATFGKGLLSGNPKEALAGAGAIATGGLEALEGGTALAENLTPEGAATALALAGGKEAVRTLTSGTGAA
>NZ_CP042179.1|WP_138850693.1|966232_968002_+|hypothetical-protein
MTGPHSAVHLVSRSENIMAPPPKIEFHSHAIESASLTRTTSDPGPSTGAKPAPVPTRRASAGVLIEELGSLGKRPCAEGLPAAPAAPAAPRPAAAIAPQKPGVDDIGAFVPGAGGKGRRFADFAHAMGVNRKGMTLTAFAAKRPAKDGLNGVSTATHGQFGYDAAPATDLVNALASGSNAAAAHSIHGRYENKVKAMLAADVERFEHPEKRPPGAPMPNQVENLLLTKNSNGEWQYDKGKLSRIARDDAHPLTQHARDVLTAMSIAENKGKQRNGALYQSVTSAIGLTASGLLIGGSHGALAPLAASGHVTNAVKEALDLKKPFVEGRQNLRNAKAATIQRYVDTVLAPHDYTGQTQDERLRAALQTSRAKIDDLRAMEARPADEGLPADLRSPQAQAGIYASLYDDARRYANSTTSFGKRLISGMHAEDKAKVHKDAERDIVVKHILSMVTKSIGRLDPASLAALAGADMAVDASGSQRAKQALAIVGNHPRASRNQDLIAAHTLLTDSGIPKGEAALLLSQLARARREKPQEAPAPSDTSAASRSAAPLTESERLKQIANIIGQPGLTATAAKTAEDAIKKSLGLRS
>NZ_CP042179.1|WP_138850694.1|968170_969025_+|formyl-transferase
MRFAFAGFDRWRVVFDAFVAAGWEPVALYSIPVDNRLDFNSALVERAEKLRIPVQLSRIDEDDLRWLAERQCDTLIVAGYNRKIPAWQPYLRHAANFHPSPLPDGRGPYPAMRAILEGRREWGVSCHRIDADFDTGEIVDSECFPLDADEWHETLQLKLQMAAHRLATRVARDFDRLWNERRPQGAGSYWPRLADAERTIDFAQPVAEVMRIVRACGNVESIAPLFGTTVHVRRATAWQEAHTYAPGQIGHQYRRWVVVAAQDGFVALLEWSPLNASLRQQMEG
>NZ_CP042179.1|WP_138850695.1|969190_970342_-|hypothetical-protein
MNLNVPSMNTYPTDPASYLQRLTNGASTGSTQDVLKDLIGLISQLLKQMQAGQNGQAGGMPGGAGGAGGMPGGMPGGTPGGMSGGGAGAMPGGVGATPGGMGGAGAMPGGSGGMTVQNAAGVLASYMGQHGLSASDPNTMYKLSTNADGGTPPTVQQAAQTMLANPGAYQQIETHDVAGTDGKSAVSNFQWAAQGGLGAAGNATGGAGGAGGVAGQSGTTGGLPGTGGFPANTSTLPTTGGLPTTGATAGFTPGTGDLLKDGKPLQMADEGKALANFNAQDGADFQAMESALSHGDGNAAAKTLANAVKSGKLSQSDAAAIGAQLQQTANAHGGGKISHDASKALSDALGGANVLTPGKTRAAVAFENITGIHTGTIAGVSTK
>NZ_CP042179.1|WP_006750733.1|970494_970983_-|hypothetical-protein
MTYTGCRDEIAGGLTKVLWTASQLDDEADFEDLLEAIRVLRPKWPGAGTVAAWRYVRRQAWGDARRVLEDDDTEAKRSGLHAALMAVCLFGLEDPLWHSYALSAAEQRESIEGATIGARLLERAAKLDASVQAPASTDAPASTHGVPADNSGFSASMTWVRA
>NZ_CP042179.1|WP_138850696.1|971641_972613_-|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein
MIENDLLAARVIARERVACDVISLRLVSDAPGLALPAFEAGAHIDLHLRDGLTRKYSLCNDPVERGVYEIAIKREPASSGGSAHVHDAIRVGDVLRIGAPLNYFPLAPDDSPAVLLAAGIGVTPLLAMAHSLVRAGRSLAFHYFVRSADAAAYGATLASRLADVATMHTGLTPDATRDAITTIVGAMDSRSHLYFCGPAPFMAAVDAIARPALGDARLHHEYFSAPTAEPADGEADAFRIELARSQRALLVPPGQSITDVLYEHGIAVATSCEAGVCGACRTTVLEGTPDHRDAFLSAAEKARNDCMMPCVSRCRGERLVLDL
>NZ_CP042179.1|WP_138850697.1|972635_974033_-|sodium:sulfate-symporter
MSGGALGGPGRGAGMLTGGRVTAALLAAGLASVAALGARGTLSAGDARIVAIVFTCIVLWATGAVASLWVSLLFFFLAATCTAVPTAEIFSGFGSSAFWLVFSGAAIGFALKESGLSERIGIALARRIGGSYLKALLAFAILSFLLSLVMPSTFGRIAILVPIAIGYCDVVKLGAHANGRRGILLLVIVGSYELAAAVLPANLPNVIMAGILEQSHGMHLRFSEYLLLFFPAGVIVRGAVLVLASWWLFADTVGEVEIPAARVALGRREWHAIVLLAITLALWFTDAVHRIAPGWVGLGFALVYFGTSPPAQLERFTATLKMDLLWFIAAIIGLTALVNHLDMRVPDTLALDALRDSPMLVYFALTALSIVVCFAVTSNAEPALYVPIVSRLLAHGLHLKAGLLAQVMGYATTVLPYQSPPIVFGNALAQLDRGAVLRYCIATALLGVVFVIPVNALWWRLIGLM

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Click the colored protein region to show detailed information

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_CP042179_1	1.1\|962624\|31\|NZ_CP042179\|CRISPRCasFinder	962624-962654	31	NZ_CP034087	Methylocystis rosea strain GW6 plasmid pGW6_1, complete sequence	48052-48082	7	0.774
NZ_CP042179_1	1.1\|962624\|31\|NZ_CP042179\|CRISPRCasFinder	962624-962654	31	NZ_CP007130	Gemmatirosa kalamazoonesis strain KBS708 plasmid 2, complete sequence	856894-856924	8	0.742
NZ_CP042179_1	1.1\|962624\|31\|NZ_CP042179\|CRISPRCasFinder	962624-962654	31	NZ_CP043499	Rhizobium grahamii strain BG7 plasmid unnamed, complete sequence	512907-512937	9	0.71
NZ_CP042179_1	1.1\|962624\|31\|NZ_CP042179\|CRISPRCasFinder	962624-962654	31	CP016641	Mycobacterium sp. djl-10 plasmid djl-10_1, complete sequence	2693-2723	9	0.71

1. spacer 1.1|962624|31|NZ_CP042179|CRISPRCasFinder matches to NZ_CP034087 (Methylocystis rosea strain GW6 plasmid pGW6_1, complete sequence) position: , mismatch: 7, identity: 0.774

ggcggtcacatcggcggtcgcggaaacccaa	CRISPR spacer
ggcggtcacagcggcggtcgcgggcggacag	Protospacer
********** ************. .  **.

2. spacer 1.1|962624|31|NZ_CP042179|CRISPRCasFinder matches to NZ_CP007130 (Gemmatirosa kalamazoonesis strain KBS708 plasmid 2, complete sequence) position: , mismatch: 8, identity: 0.742

ggcggtcacatcggcggtcgcggaaacccaa	CRISPR spacer
ggcggtcgcgtcggcggtcgcggcgacgtcg	Protospacer
*******.*.************* .** . .

3. spacer 1.1|962624|31|NZ_CP042179|CRISPRCasFinder matches to NZ_CP043499 (Rhizobium grahamii strain BG7 plasmid unnamed, complete sequence) position: , mismatch: 9, identity: 0.71

ggcggtcacatcggcggtcgcggaaacccaa	CRISPR spacer
ggcggccacgtcggcggtcgcggagctgtcg	Protospacer
*****.***.**************. . . .

4. spacer 1.1|962624|31|NZ_CP042179|CRISPRCasFinder matches to CP016641 (Mycobacterium sp. djl-10 plasmid djl-10_1, complete sequence) position: , mismatch: 9, identity: 0.71

ggcggtcacatcggcggtcgcggaaacccaa	CRISPR spacer
ggcagtcacagcggcggtcgcggcggcgttg	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

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP042178_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP042178_1

2330317-2330403

Orphan

Consensus_repeat	Method
GGGTGCATCGCGACGGCCCGCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP042178_1

>merge|NZ_CP042178|1|2330317-2330403|CRISPRCasFinder
GGGTGCATCGCGACGGCCCGCGCGTCGATCTCGGATGCACCGATGCGTTGACGCGACGATGCGCGGCTGCATCGCGACGGCCCGCGC

>NZ_CP042178|1|1|2330317-2330403|CRISPRCasFinder
GGGTGCATCGCGACGGCCCGCGC	GTCGATCTCGGATGCACCGATGCGTTGACGCGACGATGCGC
GGCTGCATCGCGACGGCCCGCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP042178.1\|WP_138850044.1\|2326209_2327340_-\|porin	unknown	unknown	gnl\|CDD\|238208
NZ_CP042178.1\|WP_138850041.1\|2330410_2331331_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176148
NZ_CP042178.1\|WP_138850042.1\|2329314_2330295_+\|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|99782
NZ_CP042178.1\|WP_011660268.1\|2336995_2337373_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042178.1\|WP_012365407.1\|2332750_2333254_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238357
NZ_CP042178.1\|WP_138850035.1\|2337956_2339081_+\|amidase	unknown	unknown	gnl\|CDD\|223232
NZ_CP042178.1\|WP_138850043.1\|2327751_2329158_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340886
NZ_CP042178.1\|WP_138850039.1\|2333319_2333706_+\|2-hydroxymuconate-tautomerase-family-protein	unknown	unknown	gnl\|CDD\|238274
NZ_CP042178.1\|WP_012365416.1\|2321905_2322916_-\|3-hydroxybutyryl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|181340
NZ_CP042178.1\|WP_138850046.1\|2324168_2325143_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|373110
NZ_CP042178.1\|WP_138850049.1\|2317862_2319011_+\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|223737
NZ_CP042178.1\|WP_138850047.1\|2322912_2324019_-\|glycerol-3-phosphate-dehydrogenase	unknown	unknown	gnl\|CDD\|376763
NZ_CP042178.1\|WP_105786062.1\|2335748_2336942_+\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173848
NZ_CP042178.1\|WP_144594401.1\|2335603_2335807_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042178.1\|WP_012365418.1\|2319007_2320054_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270307
NZ_CP042178.1\|WP_138850036.1\|2337381_2337924_+\|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl\|CDD\|379275
NZ_CP042178.1\|WP_138850040.1\|2331470_2332754_+\|Rieske-2Fe-2S-domain-containing-protein	unknown	unknown	gnl\|CDD\|176888
NZ_CP042178.1\|WP_138850038.1\|2333768_2335322_-\|PAS-domain-S-box-protein	unknown	unknown	gnl\|CDD\|223715
NZ_CP042178.1\|WP_138850045.1\|2325139_2326177_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176148
NZ_CP042178.1\|WP_138850048.1\|2320511_2321879_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340927

Protein	Function_ID	Function_description	E-value
NZ_CP042178.1\|WP_138850044.1\|2326209_2327340_-\|porin	gnl\|CDD\|238208	cd00342, gram_neg_porins, Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus.	1.24471e-63
NZ_CP042178.1\|WP_138850041.1\|2330410_2331331_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176148	cd08459, PBP2_DntR_NahR_LinR_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators that are involved in the catabolism of dinitrotoluene, naphthalene and gamma-hexachlorohexane; contains the type 2 periplasmic binding fold. This CD includes LysR-like bacterial transcriptional regulators, DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. DntR from Burkholderia species controls genes encoding enzymes for oxidative degradation of the nitro-aromatic compound 2,4-dinitrotoluene. The active form of DntR is homotetrameric, consisting of a dimer of dimers. NahR is a salicylate-dependent transcription activator of the nah and sal operons for naphthalene degradation. Salicylic acid is an intermediate of the oxidative degradation of the aromatic ring in soil bacteria. LinR positively regulates expression of the genes (linD and linE) encoding enzymes for gamma-hexachlorocyclohexane (a haloorganic insecticide) degradation. Expression of linD and linE are induced by their substrates, 2,5-dichlorohydroquinone (2,5-DCHQ) and chlorohydroquinone (CHQ). The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	9.51542e-76
NZ_CP042178.1\|WP_138850042.1\|2329314_2330295_+\|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein	gnl\|CDD\|99782	cd06185, PDR_like, Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.	2.29388e-91
NZ_CP042178.1\|WP_012365407.1\|2332750_2333254_+\|hypothetical-protein	gnl\|CDD\|238357	cd00667, ring_hydroxylating_dioxygenases_beta, Ring hydroxylating dioxygenase beta subunit. This subunit has a similar structure to NTF-2, Ketosteroid isomerase and scytalone dehydratase.The degradation of aromatic compounds by aerobic bacteria frequently begins with the dihydroxylation of the substrate by nonheme iron-containing dioxygenases. These enzymes consist of two or three soluble proteins that interact to form an electron-transport chain that transfers electrons from reduced nucleotides (NADH) via flavin and [2Fe-2S] redox centers to a terminal dioxygenase. Aromatic-ring-hydroxylating dioxygenases oxidize aromatic hydrocarbons and related compounds to cis-arene diols. These enzymes utilize a mononuclear non-heme iron center to catalyze the addition of dioxygen to their respective substrates. The active site of these enzymes however is in the alpha sub-unit. No functional role has been attributed to the beta sub-unit except for a structural role.	2.49192e-28
NZ_CP042178.1\|WP_138850035.1\|2337956_2339081_+\|amidase	gnl\|CDD\|223232	COG0154, GatA, Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidases [Translation, ribosomal structure and biogenesis].	3.25585e-83
NZ_CP042178.1\|WP_138850043.1\|2327751_2329158_+\|MFS-transporter	gnl\|CDD\|340886	cd17328, MFS_spinster_like, Protein spinster and spinster homologs of the Major Facilitator Superfamily of transporters. The protein spinster family includes Drosophila protein spinster, its vertebrate homologs, and similar proteins. Humans contain three homologs called protein spinster homologs 1 (SPNS1), 2 (SPNS2), and 3 (SPNS3). Protein spinster and its homologs may be sphingolipid transporters that play central roles in endosomes and/or lysosomes storage. SPNS2 is also called sphingosine 1-phosphate (S1P) transporter and is required for migration of myocardial precursors. S1P is a secreted lipid mediator that plays critical roles in cardiovascular, immunological, and neural development and function. The spinster-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	2.24432e-70
NZ_CP042178.1\|WP_138850039.1\|2333319_2333706_+\|2-hydroxymuconate-tautomerase-family-protein	gnl\|CDD\|238274	cd00491, 4Oxalocrotonate_Tautomerase, 4-Oxalocrotonate Tautomerase: Catalyzes the isomerization of unsaturated ketones. The structure is a homohexamer that is arranged as a trimer of dimers. The hexamer contains six active sites, each formed by residues from three monomers, two from one dimer and the third from a neighboring monomer. Each monomer is a beta-alpha-beta fold with two small beta strands at the C-terminus that fold back on themselves. A pair of monomers form a dimer with two-fold symmetry, consisting of a 4-stranded beta sheet with two helices on one side and two additional small beta strands at each end. The dimers are assembled around a 3-fold axis of rotation to form a hexamer, with the short beta strands from each dimer contacting the neighboring dimers.	1.68628e-13
NZ_CP042178.1\|WP_012365416.1\|2321905_2322916_-\|3-hydroxybutyryl-CoA-dehydrogenase	gnl\|CDD\|181340	PRK08269, PRK08269, 3-hydroxybutyryl-CoA dehydrogenase; Validated.	0
NZ_CP042178.1\|WP_138850046.1\|2324168_2325143_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|373110	pfam14525, AraC_binding_2, AraC-binding-like domain. This domain is related to the AraC ligand binding domain pfam02311.	6.32552e-22
NZ_CP042178.1\|WP_138850049.1\|2317862_2319011_+\|FAD-dependent-oxidoreductase	gnl\|CDD\|223737	COG0665, DadA, Glycine/D-amino acid oxidases (deaminating) [Amino acid transport and metabolism].	2.11686e-62
NZ_CP042178.1\|WP_138850047.1\|2322912_2324019_-\|glycerol-3-phosphate-dehydrogenase	gnl\|CDD\|376763	pfam02317, Octopine_DH, NAD/NADP octopine/nopaline dehydrogenase, alpha-helical domain. This group of enzymes act on the CH-NH substrate bond using NAD(+) or NADP(+) as an acceptor. The Pfam family consists mainly of octopine and nopaline dehydrogenases from Ti plasmids.	3.71087e-39
NZ_CP042178.1\|WP_105786062.1\|2335748_2336942_+\|acyl-CoA-dehydrogenase	gnl\|CDD\|173848	cd01159, NcnH, Naphthocyclinone hydroxylase. Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.	1.82545e-92
NZ_CP042178.1\|WP_012365418.1\|2319007_2320054_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|270307	cd13589, PBP2_polyamine_RpCGA009, The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold. This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	1.20732e-77
NZ_CP042178.1\|WP_138850036.1\|2337381_2337924_+\|nuclear-transport-factor-2-family-protein	gnl\|CDD\|379275	pfam13577, SnoaL_4, SnoaL-like domain. This family contains a large number of proteins that share the SnoaL fold.	5.14697e-15
NZ_CP042178.1\|WP_138850040.1\|2331470_2332754_+\|Rieske-2Fe-2S-domain-containing-protein	gnl\|CDD\|176888	cd08879, RHO_alpha_C_AntDO-like, C-terminal catalytic domain of the oxygenase alpha subunit of Pseudomonas resinovorans strain CA10 anthranilate 1,2-dioxygenase and related aromatic ring hydroxylating dioxygenases. C-terminal catalytic domain of the oxygenase alpha subunit of anthranilate 1,2-dioxygenase (AntDO) and related Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs, also known as aromatic ring hydroxylating dioxygenases). RHOs utilize non-heme Fe(II) to catalyze the addition of hydroxyl groups to the aromatic ring, an initial step in the oxidative degradation of aromatic compounds. RHOs are composed of either two or three protein components, and are comprised of an electron transport chain (ETC) and an oxygenase. The ETC transfers reducing equivalents from the electron donor to the oxygenase component, which in turn transfers electrons to the oxygen molecules. The oxygenase components are oligomers, either (alpha)n or (alpha)n(beta)n. The alpha subunits are the catalytic components and have an N-terminal domain, which binds a Rieske-like 2Fe-2S cluster, and the C-terminal catalytic domain which binds the non-heme Fe(II). The Fe(II) is co-ordinated by conserved His and Asp residues. Oxygenases belonging to this subgroup include the alpha subunits of AntDO, aniline dioxygenase, Acinetobacter calcoaceticus benzoate 1,2-dioxygenase, 2-halobenzoate 1,2-dioxygenase from Pseudomonas cepacia 2CBS, 2,4,5-trichlorophenoxyacetic acid oxygenase from Pseudomonas cepacia AC1100, 2,4-dichlorophenoxyacetic acid oxygenase from Bradyrhizobium sp. strain HW13, p-cumate 2,3-dioxygenase, 2-halobenzoate 1,2-dioxygenase form Pseudomonas cepacia 2CBS, and Pseudomonas putida IacC, which may be involved in the catabolism of the plant hormone indole 3-acetic acid. This subfamily belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket.	1.04981e-89
NZ_CP042178.1\|WP_138850038.1\|2333768_2335322_-\|PAS-domain-S-box-protein	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	4.87877e-31
NZ_CP042178.1\|WP_138850045.1\|2325139_2326177_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176148	cd08459, PBP2_DntR_NahR_LinR_like, The C-terminal substrate binding domain of LysR-type transcriptional regulators that are involved in the catabolism of dinitrotoluene, naphthalene and gamma-hexachlorohexane; contains the type 2 periplasmic binding fold. This CD includes LysR-like bacterial transcriptional regulators, DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. DntR from Burkholderia species controls genes encoding enzymes for oxidative degradation of the nitro-aromatic compound 2,4-dinitrotoluene. The active form of DntR is homotetrameric, consisting of a dimer of dimers. NahR is a salicylate-dependent transcription activator of the nah and sal operons for naphthalene degradation. Salicylic acid is an intermediate of the oxidative degradation of the aromatic ring in soil bacteria. LinR positively regulates expression of the genes (linD and linE) encoding enzymes for gamma-hexachlorocyclohexane (a haloorganic insecticide) degradation. Expression of linD and linE are induced by their substrates, 2,5-dichlorohydroquinone (2,5-DCHQ) and chlorohydroquinone (CHQ). The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	9.54766e-44
NZ_CP042178.1\|WP_138850048.1\|2320511_2321879_+\|MFS-transporter	gnl\|CDD\|340927	cd17369, MFS_ShiA_like, Shikimate transporter and similar proteins of the Major Facilitator Superfamily. This subfamily is composed of Escherichia coli shikimate transporter (ShiA), inner membrane metabolite transport protein YhjE, and other putative metabolite transporters. ShiA is involved in the uptake of shikimate, an aromatic compound involved in siderophore biosynthesis. It has been suggested that YhjE may mediate the uptake of osmoprotectants. The ShiA-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.72065e-167

>NZ_CP042178.1|WP_138850042.1|2329314_2330295_+|2Fe-2S-iron-sulfur-cluster-binding-domain-containing-protein
MQANRHQVRIDALIDAAQDIRCFRVSRVDGQPFDAYEPGAHIDVTAPSGVTRQYSLCGRPDERGSYLFAVKKEARSRGGSRSLHDDVCVGAELSIGAPRNLFRLADNASEHVLIAAGIGITPLLSMAYALEQRGARYRLHYFARSREHAAFVDELSAAPFAAHVTFHYGIEPDALAAELGRCVESIDAHAHVYTCGPGPFMDAVVAAAATRIPEDAIHLERFAAEPAAADAATDAAPAEGFEVRLQRSGQSVRVAPDTSIVDALARIGIEVDTSCGEGVCGTCMVPVLDGEPDHRDHCLSKAERASNTVICCCVSRARSAVLVLDL
>NZ_CP042178.1|WP_138850043.1|2327751_2329158_+|MFS-transporter
MSAPTARAADGKRYTYEWYVVVICMLAYVFSFVDRQVLVLMIEPIKRDLHLTDTQFSLLNGFAFSLFYAVMGLPVAYLADRYARPRIIALGIALWSVATAACGLSQQFVQMFVARMGVGVGEAALSPGAYSMLADYFPKEKLGRAIAVYSLGSFIGGGVAFLIGGYVIALLKHASAFTLPLVGQVHAWQVTFLIVGLPGILVALLFAATVRDPQRKGLAQDRSGAVRRVSMRDSLRFVGTHRATFSCHYLGFSFYAMTLYCLLSWTPAFYIRHFGMTAVEAGYTLGIVLLVANTAGVFCGGWLNDWLLRRGRSDAPMRAGAIGAACMVIPATLFTQLDSLPASLAMLVVAMFFASFPMPTSTAAMQTLAPNQMRAQISALFLLVSNLIALGIGTTVVALFTDRVFGAPAAVGHSMSIVNVVAATLAALLLAAGCRQYRRSLERERGHAAASASAANAPVDGGNAVAAR
>NZ_CP042178.1|WP_138850044.1|2326209_2327340_-|porin
MNHPNGRADRLAVPRATLVAALLTCASLPALAQSSVTLYGRVDTAIEYANAGPNHVTRMGSGNLWASQWGLKGVEDLGGGYAAIFKLEDGFNAASGALSNSSALFGREAWVGITGPFGGVQFGELYTILHTTLVTYSLPGLGAGLAWGNATNNFVGPAFLRVRNSMRYTSPRYAGFMLRAMAARGANGAAGQPATLGDTYGAGLNYARGGLSIDVDYMQQKFSPVAASALGATSPAANGNYTLGAISYDFSVVKIAALYMRHRGGPDVAAAIDSQSAYPHSDTMELSATVPIGRASLLLSIGHYRKVADSDGNADSYGIRFDYPLSKRTVLYTGAAMVRNGAHARFVVNGAAGGGVAVAKPGATASSIVAGILTSF
>NZ_CP042178.1|WP_138850045.1|2325139_2326177_+|LysR-family-transcriptional-regulator
MTHSATSRPPAPARAEASPHDGDSPDGLRVQDLDLNLLKTFRAVYEERHVGRAALRLGVTQPSVSYALGRLRLMFRDALFVRTGTGVEPTPRAQRLAISVDKALAILQDVLDEGSRFTPDSTQRVFRLHMSDFAASAFLPTLLAAFDRRAPGAVIETLHVDECQLNVALESGRIDFALGHFADASSHFQRAALLHERCVLLMPRRTAQRVALPDDFVLDGDAPDTLRFVAVTSHPQSMQLLERHGLMPRVRAALPDFMVVPALLEHGDYALILPETVAITFAARQPCTLYEIAGAGEWAVNAYWHRRFDADPGHRWLRALLLELFDIGRQPPFDAWLAPHPPACA
>NZ_CP042178.1|WP_138850046.1|2324168_2325143_+|helix-turn-helix-domain-containing-protein
MDIALSRHAPNRLGTLHAPDEVERAVAHRLGPHRMAARGRDPFHAELYEVPLHHGALLELCYGRETRIDFGDDADHFLFRLTLSGACELRAGQRVARAGPGELTVSSPALASRLSTSPDCRNLVLRLERGALERKLQDMLHATLTRPLHFDLAAGGSGAGAALVPPTFEYLCRLGAQPGVGTSATTFGADLTAWLMSLLLTHLPHSYSAALARGTPPLPAHVRRACDHVDAHLGEPLALAALAAVAGVAPRTLQHAFRAFLNTTPAAYVRERRLAAVHAALQRGDARSVTDVLIAHGIHGFGHFAKAYARRYGHAPSVTARQAP
>NZ_CP042178.1|WP_138850047.1|2322912_2324019_-|glycerol-3-phosphate-dehydrogenase
MKVCVLGGGHGCHAAAIDLFEKGHDVTWWRRDREPHARLRELGALHVTDYRGERAVPLGDTPGAIRLTDDLAAALHGARLVVVPLPAVSHDALAAQVAPLLEDGQVVFLPPGTFGSFVFARAAADAGNRARVAFAETGTLPYLVRKHGDNKVVISAYATRLPTGVFPANAAGWAFDVLRAGYPSVEPVEDALSGALMNAGPVIHPPLILMNAGPLEHFDAWDIHNEGTQPSIRCVTNALDAERIAVREALGYRAPHFPLADHYATDGDEWMYGRGAHGKLTDSGDWREKIDLRTHRYMLEDTRLGLSFIVSCGRWANVPTPVAQGLLSVASAVTGRDLYAQGRTLDGLGLAALSRDALRALLDAGYAA
>NZ_CP042178.1|WP_012365416.1|2321905_2322916_-|3-hydroxybutyryl-CoA-dehydrogenase
MTAALDVTRVHVLGAGRMGQGIALVFAFAGLDVTLIDFKPRDAHGWRAFEERTRGEILRPLHAQVALGRIDRAQAEAVVARIALVARDGAAHAVRDAGIVFEALPEVLDAKADALRWLGEHVDARATIASTTSTFVVTTLQRHVAHPERMLNAHWLNPALLMPLVEISRSDATDQSVVDALAALLERVGKKPVICGPAPGYIVPRIQALAMNEAARMVEEGVASAADIDTAIRTGFGPRFAVLGLLEFIDWGGCDILYYASTYLAGEIGPRFAPAASVVRNMEAGRDGVRTGAGFHDYAQVDVPAYMQQRLGEFARLLDHLGLAPAFDAARRDSGA
>NZ_CP042178.1|WP_138850048.1|2320511_2321879_+|MFS-transporter
MYPTDTVQSPSAARPLADRQLRRIVIASVAGNAMEWYDFFVYGTAAALVFGHVFFPPGASPLAGSLAAFAAFALGFVARPLGGIVFGHVGDRYGRKASLVWTLLIMGASTFAIGLLPTYAQVGLWAPAALVVLRLLQGVASGGEWGGGVLMISENAPPEQRGYYAAWSQLGVGGGFVLSSAAFLAAQALPDDAFRTWGWRLPFLASIAIFAIGIYIRRHLPESRDYEQAGKRGAHTHLPIVECIRRHPKEILLAMGLRVAENGGAYIFLAFSLVYGKYVGIPNGVMLTGVMIAMIVEMGAMLAWGRLSDRIGRKPVYLIGALSLVACAFPFFWLLDTRATPLVWLALTIGTAVSHGAMIGTLPALVGELFSTEVRYSGVALGHEVASIFAGGMSPLIATALLARYHASWPVSLFLIALGLVTVATLCVMRETRGMPDAGTPAAGMPAASTRGDAA
>NZ_CP042178.1|WP_012365418.1|2319007_2320054_+|ABC-transporter-substrate-binding-protein
MKLFGTIAAAAALCIAGAAAPAFAQTKTIYVGMNGGPMEKAYTSQVLPEFEKANNVKVVVVPGTSSDVLAKLLANRNKPQIHVAFLDDGVMARAVSLGVCQKLDDSPVLKELYPFARMKDDVGAGVQLGMTGIAYNKKLFTEKGWAPPTSWMDFADPKYKGKVVFQSASSSTFGLHGFLAINRLLGGSEQNVEPGFSKWASTVGPNVVEYIPNSAKISEMVQTGEAGLFPLTPTGVGDLQDKGIPVAYANPKEGPVLLLVDLCVVANNPDPQLAQKLAQFLLSAPAQTKAAEAGKQIPTNRLAKMPAAMQQSLGNVDDLVRKVTVVDWAAINARRAQWDTRWNRQIER
>NZ_CP042178.1|WP_138850049.1|2317862_2319011_+|FAD-dependent-oxidoreductase
MSERRHYDVAIVGGGLVGASAALALARRGLRVALFERRDCGAQASGVNYGGVRCQGRPAEQLPLALRARRIWDRLPELIGIDGEFVVSGHLRLARSDADLDALDAYATVAGEHGLPLQVMRGDTFRRRYPWLGRAALGGSLCATDGHANPRVVSPAFARAARAAGADVFEHAAVDDARHDGMRFHVQATGRAYTATWLINSAGAWANTIAARFGEAVPMEPIYPNMWVTEPLPPFITHNLGVYGGGVYARQVARGNCVIGGGRGRGDGEFGQPSVDTTRAVMRDACALLPALRDALLIRTWSGVEGCTPDHNPIIGASRTTPNLLHAFGFSGGGFLLAPGVGEVLAELVTTGETATPLEAFSIGRFAPHAPIAPFRQEETHK
>NZ_CP042178.1|WP_138850041.1|2330410_2331331_-|LysR-family-transcriptional-regulator
MTSVDHLDLNLLRVFQAIVEERSLTKAGERLALSQPAVSYSLGRLRTLFDDPLFVRTRAGMQPTPVALELAGIVGKALDMVRAALRYAERFDPASSTRTFRLSLSDAGEMAYLPAICQALRARAPRVTLSVQPLPVEEIEEALRASRLDFAIGNLPELMPRTRHQVLFEETYVCMTGRRRGLPAGAALSLEQFVRAAHVNVKSVEHSHHALDDALRAQGVGRNIALEVPHFVALPSVLSVTDLYATLPRRLAQILNRGNAFRLYDLPVTLPPAPVTMHWHEHFHEDEGIAWMRALLAEIVEHFDEA
>NZ_CP042178.1|WP_138850040.1|2331470_2332754_+|Rieske-2Fe-2S-domain-containing-protein
MSDIPYQTIDTRALHGLAQPDRIAPAMYHDPALFEAELDRIFYRTWIWVAHDSELPNPGDFITTTIGRQPVIVVRDKTGEINVLQNRCRHRGATVCESHKGNAKGFTCPYHSWSYALDGTLRALPYGDGYEGVCEKGDLPLVKLRVGVYQGLIFASFNDDIEPLEDFLGGAKPWIDLFMKQGAGYPIKANGEHKFKFKGNWKIQLENTTDLYHFPVVHKSWMKSIDDETAAAITSFMTSEHAFCRALGNGHSLAVLMPELIDLDEDDGAPLPERFAPLAATLAERHAPNEVRRIVRSLLGVGFNLNLFPNLALSMAFFRVLRPISANETEIRHVALAMDGGPDEANRERLRIHEHFQGPFGFGSPDDAEAWERVQRGAHAGPDVPILVNRGLNRETTAANGEKTAHATDETGMREAYQQWRKLMEQA
>NZ_CP042178.1|WP_012365407.1|2332750_2333254_+|hypothetical-protein
MMDDRNALFSQQTFARAVEFVWREAEMLDRRDYRAWLDLWDPAGHYVVPIDPDATDFAATLNYVFDDQDMREKRVQRMLSGHSASASDAARTVRTVSRFTLESSSAGIVELKSAQVVVAYKRGVATLFAADVTHKLHVDAEGEMRIAEKIVRLIDSTEALSAIGFLL
>NZ_CP042178.1|WP_138850039.1|2333319_2333706_+|2-hydroxymuconate-tautomerase-family-protein
MPTLEVFLPAGHDDARKAELIARLSGATVDAIGAPIESVRVLLTELPSAHVGLGGRTAADGAPPSLPVIVAILIAGRTDEQKRALIAALSDAGANVLDAPLQATRVIIKDIPNTDFGIGGQTARALGR
>NZ_CP042178.1|WP_138850038.1|2333768_2335322_-|PAS-domain-S-box-protein
MRAAHADAMLDIRPRDAARLHPNPIMSFPDEDDFHRLLDALTTCVLLHDAKTRAIVWANRAACIALGFSVEELLPLKAQDMTRPEPKYRREIAVSAWDRALVDGPQVYEWCYRSRTGVDMLSEATATYVPLRGRDVVMVQFRDISAEEAVRQQLRRYEARLREFMQDLDEGIAVVTPHGRVQFISESGRRVLGLAQDEALGEVLDYCSAADRDRLVAQLRDAPSACPSEPQRYRIVRRDGSTCWLRILCRQVEIEGDLDGLLVQFRDVSDEVAIEDARRAEARMLEYAGRYNAMGEMASVIAHELSQPLAAVRNFIEGAVRRLNARGAVDDAIWGLRSADRQAEHAALIIKSVREFIVKREPAVALADLREILADVAYFIELRAKEAGVTVSIVQADAPLPIRCERVLIGQVVLNLAFNAIEAFAGCERMPRTLMLGTANVGGHAELRAIDNGPGVAEGAHDRLFDGFSSSKAGGNGIGLSLCKSIVTRHGGRIVASPAEGGGLDCRVTLPLADAQA
>NZ_CP042178.1|WP_144594401.1|2335603_2335807_+|hypothetical-protein
MRIRPVFAASRASRAAVLVATHARSICKQTLAHASSCPRNRTPSPGDRHAQRRPRHRCRVPLAARGP
>NZ_CP042178.1|WP_105786062.1|2335748_2336942_+|acyl-CoA-dehydrogenase
MPNAALAIDAASPSPHAVREAAARVSPLDAVIETVAARRDEFDRLSHVPRDVIALFKEAGIYRAGTPRRFGGDALAPGAFLDMIERIATADGSAAWVASFGSANVYLAALPLATQAELYAGGPDQVFAGGLFPVQPAQAAPGGWRVNGTWKFASGCKGADWLGVGIAVPGAQDAAPNKPRTAVFRAADVEIVENWSVVGMQGTGSHDLRVDDRFVPEAWTFVRGGEATVDEPLYRYPTVAYAAQVLAVVNLGLARAALDVANRMSGGRQTTTGAPRLADRAYFRIELAKAEAQLRSARAFFYDATDSVWQSILAGNPVTPEQVSLLRLAATHIAREGASVVERAYRLGGTAAIYRTHPLQRLLRDAMVVTQHAFLGEGNFDGAGAVFTGVAPFPGYL
>NZ_CP042178.1|WP_011660268.1|2336995_2337373_+|hypothetical-protein
MSDSNPLPLRVLFCCGVSQNFFDLPREKIGEVWQAYGAMLAAVEAMPGVRVLGVMDDDRLVVGQADGAPWTFYIMADVADFDTTVAVCNLYRTTPVGEYNLWRYGKIEARVGRALTVPPAARPAS
>NZ_CP042178.1|WP_138850036.1|2337381_2337924_+|nuclear-transport-factor-2-family-protein
MTGSDPARSIEVLEALGALERRVAMLDAERAVRATITRYMALCDVPEDAGDGPALAALFTADAVWEGIGPQYARKFGRREGTDAIVAMLRRYLPPEPHFAANLHFLTSESIDVGADLATARGRWIMLQASRHVDGTAELIAARLTVDFAPADGGTAWLIRHFRTERVLDGPWPLAAAPRP
>NZ_CP042178.1|WP_138850035.1|2337956_2339081_+|amidase
MTGFIDTFTLGGPGPTIAIKDTIDIAGHPTRAASRALADAPPAARHADVVRLLLDAGWQIAGKANMHELAFGMTGINDTTGTPVNPQDPLRIPGGSSSGSASLVGLGVVDAALGTDTGGSIRGPAACCGVAGLKPTFGRVSRRGVAPADTTLDCVGPFARDVDTLAAVMAAIAPGFDRARAAAPVAGCTIAHVIVDADAAIAAALDTALRASGLRVREAVLDELPAAFAAGLAVINAETSRAFGHLVATGKLGADLDARLRTAATTTPAALEEAEAVRARFTAQVDAALEHADVLVLPTLPALPITLQQARDGVSVIAMSSLIRPFNLSGHPALSLPLPLAGTRLKAGLQIVGRKGADEHVCAVAAHFDAALAA

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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

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

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP042177_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP042177_1

591741-591835

Orphan

Consensus_repeat	Method
CGCGTTGCCCGCGACCGCGCCGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP042177_1

>merge|NZ_CP042177|1|591741-591835|CRISPRCasFinder
CGCGTTGCCCGCGACCGCGCCGACGAGGCCGCCCGCGATGGCCGTCAGGATCGACCCCTTGCCGCCGCCGATCGCGCTGCCCGCGACCGCGCCGA

>NZ_CP042177|1|1|591741-591835|CRISPRCasFinder
CGCGTTGCCCGCGACCGCGCCGA	CGAGGCCGCCCGCGATGGCCGTCAGGATCGACCCCTTGCCGCCGCCGAT
CGCGCTGCCCGCGACCGCGCCGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP042177.1\|WP_138848274.1\|588782_588965_+\|response-regulator-SirA	unknown	unknown	unknown
NZ_CP042177.1\|WP_138848267.1\|599226_599871_-\|UDP-N-acetylmuramate--alanine-ligase	unknown	unknown	unknown
NZ_CP042177.1\|WP_006752252.1\|596021_597389_-\|acetyl-CoA-carboxylase-biotin-carboxylase-subunit	unknown	unknown	gnl\|CDD\|236307
NZ_CP042177.1\|WP_138848269.1\|598017_598470_-\|type-II-3-dehydroquinate-dehydratase	unknown	unknown	gnl\|CDD\|235443
NZ_CP042177.1\|WP_012363046.1\|592071_593010_-\|carbohydrate-kinase-family-protein	unknown	unknown	gnl\|CDD\|238917
NZ_CP042177.1\|WP_138848272.1\|590678_591356_+\|histone-H1	unknown	unknown	gnl\|CDD\|237855
NZ_CP042177.1\|WP_138848270.1\|595116_596019_-\|50S-ribosomal-protein-L11-methyltransferase	unknown	unknown	gnl\|CDD\|234786
NZ_CP042177.1\|WP_138848273.1\|590323_590650_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042177.1\|WP_006758913.1\|593103_593607_-\|thiol-peroxidase	unknown	unknown	gnl\|CDD\|179055
NZ_CP042177.1\|WP_138848268.1\|598664_599219_-\|redoxin-family-protein	unknown	unknown	gnl\|CDD\|239264
NZ_CP042177.1\|WP_012363049.1\|597474_597951_-\|acetyl-CoA-carboxylase-biotin-carboxyl-carrier-protein	unknown	unknown	gnl\|CDD\|235777
NZ_CP042177.1\|WP_138848276.1\|584302_584617_+\|deaminase	unknown	unknown	unknown
NZ_CP042177.1\|WP_138848275.1\|585669_588669_+\|ribonucleoside-diphosphate-reductase-subunit-alpha	unknown	unknown	gnl\|CDD\|235966
NZ_CP042177.1\|WP_138848277.1\|583395_584289_+\|inner-membrane-protein-YpjD	unknown	unknown	gnl\|CDD\|226621
NZ_CP042177.1\|WP_011655924.1\|600094_601480_+\|UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl--meso-diaminopimelate-ligase	unknown	unknown	gnl\|CDD\|130153
NZ_CP042177.1\|WP_011655915.1\|589028_590240_+\|ribonucleotide-diphosphate-reductase-subunit-beta	unknown	unknown	gnl\|CDD\|235968
NZ_CP042177.1\|WP_138848271.1\|593679_595071_-\|DUF3426-domain-containing-protein	unknown	unknown	gnl\|CDD\|378759
NZ_CP042177.1\|WP_011655913.1\|584613_585204_+\|1,6-anhydro-N-acetylmuramyl-L-alanine-amidase-AmpD	unknown	unknown	gnl\|CDD\|236984
NZ_CP042177.1\|WP_082089588.1\|585438_585648_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042177.1\|WP_006752240.1\|581938_583306_-\|signal-recognition-particle-protein	unknown	unknown	gnl\|CDD\|236780

Protein	Function_ID	Function_description	E-value
NZ_CP042177.1\|WP_006752252.1\|596021_597389_-\|acetyl-CoA-carboxylase-biotin-carboxylase-subunit	gnl\|CDD\|236307	PRK08591, PRK08591, acetyl-CoA carboxylase biotin carboxylase subunit; Validated.	0
NZ_CP042177.1\|WP_138848269.1\|598017_598470_-\|type-II-3-dehydroquinate-dehydratase	gnl\|CDD\|235443	PRK05395, PRK05395, type II 3-dehydroquinate dehydratase.	1.44134e-95
NZ_CP042177.1\|WP_012363046.1\|592071_593010_-\|carbohydrate-kinase-family-protein	gnl\|CDD\|238917	cd01942, ribokinase_group_A, Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.	1.22584e-98
NZ_CP042177.1\|WP_138848272.1\|590678_591356_+\|histone-H1	gnl\|CDD\|237855	PRK14900, valS, valyl-tRNA synthetase; Provisional.	2.18146e-12
NZ_CP042177.1\|WP_138848270.1\|595116_596019_-\|50S-ribosomal-protein-L11-methyltransferase	gnl\|CDD\|234786	PRK00517, prmA, 50S ribosomal protein L11 methyltransferase.	1.66384e-121
NZ_CP042177.1\|WP_138848268.1\|598664_599219_-\|redoxin-family-protein	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	2.80739e-41
NZ_CP042177.1\|WP_006758913.1\|593103_593607_-\|thiol-peroxidase	gnl\|CDD\|179055	PRK00522, tpx, thiol peroxidase.	1.09654e-95
NZ_CP042177.1\|WP_012363049.1\|597474_597951_-\|acetyl-CoA-carboxylase-biotin-carboxyl-carrier-protein	gnl\|CDD\|235777	PRK06302, PRK06302, acetyl-CoA carboxylase biotin carboxyl carrier protein.	3.98737e-84
NZ_CP042177.1\|WP_138848275.1\|585669_588669_+\|ribonucleoside-diphosphate-reductase-subunit-alpha	gnl\|CDD\|235966	PRK07207, PRK07207, ribonucleoside-diphosphate reductase subunit alpha.	0
NZ_CP042177.1\|WP_138848277.1\|583395_584289_+\|inner-membrane-protein-YpjD	gnl\|CDD\|226621	COG4137, COG4137, ABC-type uncharacterized transport system, permease component [General function prediction only].	3.28592e-60
NZ_CP042177.1\|WP_011655924.1\|600094_601480_+\|UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl--meso-diaminopimelate-ligase	gnl\|CDD\|130153	TIGR01081, mpl, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase. Alternate name: murein tripeptide ligase [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	0
NZ_CP042177.1\|WP_011655915.1\|589028_590240_+\|ribonucleotide-diphosphate-reductase-subunit-beta	gnl\|CDD\|235968	PRK07209, PRK07209, ribonucleotide-diphosphate reductase subunit beta; Validated.	0
NZ_CP042177.1\|WP_138848271.1\|593679_595071_-\|DUF3426-domain-containing-protein	gnl\|CDD\|378759	pfam11906, DUF3426, Protein of unknown function (DUF3426). This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 262 to 463 amino acids in length.	2.26062e-40
NZ_CP042177.1\|WP_011655913.1\|584613_585204_+\|1,6-anhydro-N-acetylmuramyl-L-alanine-amidase-AmpD	gnl\|CDD\|236984	PRK11789, PRK11789, 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD.	3.50423e-122
NZ_CP042177.1\|WP_006752240.1\|581938_583306_-\|signal-recognition-particle-protein	gnl\|CDD\|236780	PRK10867, PRK10867, signal recognition particle protein; Provisional.	0

>NZ_CP042177.1|WP_138848272.1|590678_591356_+|histone-H1
MATAKKKPAAKKVAAKKTVAKKAAPAKKAAAVKKVAAKKVAVKKVAAKKAAPAKKAAAKKVAAKKVATKKVAAKKVAAKKVAAKKVAVKKVAAKKAAPAKKAAAKKVAAKKVATKKVAAKKAAPAKKAAAKKAAPAKKAAAKKAAPAKKAAAKKAAPAKKAAPAKKAAAPKAAAPAKKAAAPKKAVVKKAAPATTASTASVAPASGVKTALNPAAAWPFPTGSRP
>NZ_CP042177.1|WP_138848273.1|590323_590650_+|hypothetical-protein
MQSMPGALTAQRHDRHFANPSVGWANFPPEKADGRVAVRLIKRLGVAARGAPATDLIWRARPWGHARHTVFISVSARYPRTPMNSPLRSARAEQRPREAGFDEGCSLN
>NZ_CP042177.1|WP_011655915.1|589028_590240_+|ribonucleotide-diphosphate-reductase-subunit-beta
MLNWDDEKTAVTPASGAQQNALRTSAGMAVGLQATAPAAHQVRDIFEGDLAVPPQASAVPAAGSEARVNVADKRIINGQTDVNQLVPFKYKWAWEKYLAGCANHWMPQEINMSRDIALWKDPNGLTEDERRIVKRNLGFFVTADSLAANNIVLGTYRHITAPECRQFLLRQAFEEAIHTHAYQYIVESLGLDEGEIFNAYHEVTSIRAKDEFLIPFIHTLTDPAFKTGTLEADQKLLKSLIVFACIMEGLFFYVGFTQILALGRQNKMTGAAEQYQYILRDESMHCNFGIDLINQIKLENPHLWTAEFRAEIRELFKQAVELEYRYAEDTMPRGVLGLNASMFKSYLRFISNRRCQQIGLDPLYPNEENPFPWMSEMIDLKKERNFFETRVIEYQTGGALSWE
>NZ_CP042177.1|WP_138848274.1|588782_588965_+|response-regulator-SirA
MQAVTSDRNIPDDVAFRSAFDTSSAPRDTCATRVALCMNDDALLKVLYRGRNANRKKDFS
>NZ_CP042177.1|WP_138848275.1|585669_588669_+|ribonucleoside-diphosphate-reductase-subunit-alpha
MQTTDNATSQYESASSRPLGGTEQGAKALAPQATFADYKVIRRNGSVVSFEPSKIAIAVTKAFLAVNGGQGAASARVREQVEQLTHNVVRALVRSRPNGGTFHIEDIQDQVELALMRGGEHNVARAYVLYREKRHLERQHAGEEAAAAGGEASAGINVVDNGVTRPLDMNALRELIVSACAGLGAAVNPEPIVAETVKNLYDGVPMSQVYDSAILAARTMIEKDPAYSQVTARILLHTIRREILGEEVLQAEMATRYTEYFPQFLKRGVDAGLLDDKLLQFDLKRLGEALDANRDLQFGYLGLQTLYDRYFLHVEGTRIEMPQAFFMRVAMGLSLNEIDRETRAIEFYNVLSSFDFMSSTPTLFNSGTHRSQLSSCYLTTVADDLDGIYEALKENALLSKFAGGLGNDWTRVRALGSHIKGTNGKSQGVVPFLKVVNDTAVAVNQGGKRKGAVCAYLESWHLDIEEFLELRKNTGDDRRRTHDMNTANWIPDLFMKRVMEGADWTLFSPSTCPDLHDKFGAEFEAAYTAYEDKVARGEIKLFKKIPAQQLWRKMLGMLFETGHPWITFKDPCNVRSPQQHVGVVHSSNLCTEITLNTSDTEIAVCNLGSVNLVAHLVKQADGSYALDHDKLKRTISVAMRMLDNVIDINYYAVPKARNSNLKHRPVGMGIMGFQDCLHLLRTPYASEAAVEFADRSMEAVCYYAYYASTELAEERGRYSSYRGSLWDRGILPQDTLKLLTEARGGYVEVDTSESLDWTTLRSRIAAHGMRNSNCVAIAPTATISNIIGVSACIEPTFQNLYVKSNLSGEFTVVNEYLVRDLKERGLWDEVMVADLKYFDGMLSRIDRIPADLRAIYATAFEVDPTWLVEAASRRQKWIDQAQSLNIYMGGASGKKLDEVYKLAWLRGLKTTYYLRTMAATHVEKSTVAHGALNAVPTGGAGGSSSGGAQGAAGGFGAAGGDASSGAVNAAAALAPVEADGPVCTMRPGDAGFDECEACQ
>NZ_CP042177.1|WP_082089588.1|585438_585648_-|hypothetical-protein
MVRREPRIKTNAARWSARAVRGERCGGDAGAVDARQPSRSCASSCVPLPRRSSLRLIATPGPPGPGAPP
>NZ_CP042177.1|WP_011655913.1|584613_585204_+|1,6-anhydro-N-acetylmuramyl-L-alanine-amidase-AmpD
MSDAAPLSVDAHGWVREARHAPSPNFEARPAGAVPTLVVVHNISLPPGEFGGDAIESLFLNRLDCDAHPYYQSHLRGVRVSAHFLIRRDGELVQFVSCDERAWHAGSSEFFGRPRCNDFSIGIELEGADDVPFDPAQYATLGVLARTLAARYPIDAVAGHSDVAPGRKTDPGPHFDWQRFAGDAGFSAEYFPFRQH
>NZ_CP042177.1|WP_138848276.1|584302_584617_+|deaminase
MRQILLLILLLFAGSWLARKLRQAQEQAQARTGRGDGADAPGHGGAGAARPNGGTRSLPEPMVRCAECGVHAPKGDAVAAGGEYFCSTDHARRHGARASGHDAR
>NZ_CP042177.1|WP_138848277.1|583395_584289_+|inner-membrane-protein-YpjD
MDIVLYALTAFLYGGLAVAGWRTHRQGATPLVASVPAVPVPASAASGMSAAGRALLFAALVAHGVLLHMTIFPHDAMIFGFAFALSAMFWLGAGIYWIESFFFPLDSLRLLVLPLACGASLLPLVFGGVRVLPYAAAPLFKMHFLIANIAYGLFAIAALHAVLMLMVERRLQSLRSSGRDGSTGWIASWLETLPPLLTLEKLLFRLIGAGFVLLTLTLASGILFSEQVDARALRLDHKTVFAVLSWLMFGGLLVARKTSGWRGRGAARWVLVSFAALLLAYVGSRFVFEVLLHRSVV
>NZ_CP042177.1|WP_006752240.1|581938_583306_-|signal-recognition-particle-protein
MLDNLTQRMARVVKTLRGEARLTEANTQEMLREVRLALLEADVALPVVREFIAKVKEKALGEEVISSLSPGQALVGVVQKELTAVIGGDYEGKAAELNLAVTPPAVILMAGLQGAGKTTTVGKLAKLLREKHKKKVLTVSCDVYRPAAIMQLKTVSEQVGADFFPSTPDQKPVDIAVAAVDWAKRHYHDVLIVDTAGRLGIDEAMMQEIAALHGTLKPAETLFVVDAMLGQDAVNTAKAFNDTLPLTGVVLTKLDGDSRGGAALSVRHITGKPIKFVGVAEKLDGLEVFHPDRMANRILGMGDILALVEEAQRGVDVQAAQKLADKVKKGGDFDLNDFRAQISQMKNMGGLSSLMDKLPAQFQQAAAGADMGQAEKSIRRMEGIISSMTPAERAKPEIIKATRKRRIAAGAGVPVQEVNRMLNQYDQMRTMMKKLKGGNMQKMMRGLKGMMPGMR
>NZ_CP042177.1|WP_012363046.1|592071_593010_-|carbohydrate-kinase-family-protein
MTTLICGSLAYDNIMTFEGRFREHILPDQVHLLNVSFLVPTMRREFGGCAGNIAYALHMLGGDARIMATVGANDADRYLERLDSLGLSKASVRVVPETHTAQAMITTDLDNNQITAFHPGAMMVSHLNRADEVAGVKLGIVAPDGFDGMVQHAEQFAKAGVPFVFDPGQGLPLFDGATLRRIIELATFVAVNDYEGKLVSDKTGWSEQDIASRVQALIITRGEHGSTILHKNGEEQIPVVQAERVVDPTGCGDAFRGGLLYGIENGLDWATTGRLASLMGSIKIAHQGPQTYALTRAEIDARFEAAFGYSLK
>NZ_CP042177.1|WP_006758913.1|593103_593607_-|thiol-peroxidase
MSKVTLGGNPIDLAGTFPAVGSQAPDFKLVGKDLADLSLASFAGKRKVLNIVPSLDTPTCATSTRKFNEAASSLDNTVVVVVSGDLPFAATRFCTTEGLANVVTASTFRGGRAFANAYGVDVTSGPLNGLTARAVVVLDAQDKVIHAQLVDEIKDEPNYDAALAALK
>NZ_CP042177.1|WP_138848271.1|593679_595071_-|DUF3426-domain-containing-protein
MLLATRCPHCETVFRLQQEQLSLHDGLVRCGHCQQVFNASQSLVPDPARQPGPALTEAAPAGPHAAAPQPDAAPPRLFATDAPVEAASDIDYKPEGWDMWAPWLDAGVDPSLQHTVQTVRAKPLVPLALPAMEAGVVRLSGTPAPIASVPAELHAAHTQAAEPDATLHETDASGTSFAAPTAEPDLREPRFVAHTPSAEPAAAEPAEPVGNARFAVPDDEHAPREPRFAFRPAQAESAPESGPDIHADERAPAPTAAASEPAAEPDIQPVVQPAIPFPAALTDDDRPHFAVTRETRETGAPQRRGMLGGFFGGLVAAALVVLLVAQLAWWQRETVMIYWPATQGWFRQACVPLGCRLTPPRAIDGLRLDATDLRQIDGPRTLELKVPLTNRYRVALAYPSLELTLLDDTNHVTVRRVLAPRDYVRPGTPIDAGLPPGTTQTMVVRLDTNGTPASNFRVQIFYP
>NZ_CP042177.1|WP_138848270.1|595116_596019_-|50S-ribosomal-protein-L11-methyltransferase
MSYRELVVELAREHAEALSDALLELGALSVSVEDADADTPDEQPLFGEPGLVPDRTAWQHSRVIALLSPDHEPAVLLAAAVNEIGVAETPKFDVREVEEQDWVRLTQSQFEPIPIGERIWVVPSWHDAPDPDALILELDPGLAFGTGSHPTTRLCMEWLEQSVKPGQSVLDYGCGSGILAILARKCGANPVVGIDIDPQAVESARQNSERNHAEVTYGLPDACPAGEFDIVVANILSNPLKLMASMLASKVKPGGRIALSGVLARQADEVAAVYARYVDISVWREHEGWVCLAGTRRESH
>NZ_CP042177.1|WP_006752252.1|596021_597389_-|acetyl-CoA-carboxylase-biotin-carboxylase-subunit
MFEKILIANRGEIALRIQRACRELGVKTVVVYSEADKEAKYVRLADEAVCIGPAPSNLSYLNMPALISAAEVTDAEAIHPGYGFLSENADFAERVEQSGFTFIGPRPETIRMMGDKVTAKQTMIKTGVPCVPGSEGALPDDPKEIVKIARTIGYPVIIKAAGGGGGRGMRVVHTEAALVNAVNMTREEAGRAFGNPQVYMEKFLENPRHIEIQVLSDAHKNAIWLGERDCSMQRRHQKVIEEAPAPGIPRRLIERIGDRCADACKKMGYLGAGTFEFLYENNEFYFIEMNTRVQVEHPVSEMITGVDIVQEQIRIAAGEKIALRQRDIQFRGHAIECRINAEDPFKFTPSPGRITSWHTPGGPGVRVDSHAYNGYFVPPNYDSMIGKLITYGATRDQAIRRMRIALSEMVVEGIHTNIPLHRELMIDSKFVEGGTSIHYLEHRLAQKQQVAPEEA
>NZ_CP042177.1|WP_012363049.1|597474_597951_-|acetyl-CoA-carboxylase-biotin-carboxyl-carrier-protein
MDLRKLKTLIDLVSESGISELEVTEGEGKVRIVKNAPPVYVQQTAGFAPQVSAPAPSAALPTDGAAAPAAGAAAAAPAVPQGHVVTSPMVGTFYRAPSPGADPFVQVGDTVKEGQTICIIEAMKLLNEIESDKAGVVKEILVENGQAVEYGQPLFVIG
>NZ_CP042177.1|WP_138848269.1|598017_598470_-|type-II-3-dehydroquinate-dehydratase
MTRLLVLHGPNLNLLGTREPEVYGRVTLAQIDQALVARAQEAGAELSSFQSNHEGALVDRIQAAREEQTDFILINPAAYTHTSVAIRDAIAGVGIPFVEIHLSNVHRREAFRHHSYFSDQAEGVICGLGWKGYLYALEYALDKLQGASRG
>NZ_CP042177.1|WP_138848268.1|598664_599219_-|redoxin-family-protein
MMTKRMLALAVVAAAAVAGGLAAGHWFRGGSADDGVAVAAPAAQGNPVDQLWAASLTGVDGKPASLAAFKGQKVVVNFWASWCGPCVEEMPELVALSHQYKQKGVRFIGIGVDSDQNVKNFLQKVKVDYPVFVSGYAGADLARNFGNTAGALPFTVVIDETGKIRETKLGQIQPAELRKALDAL
>NZ_CP042177.1|WP_138848267.1|599226_599871_-|UDP-N-acetylmuramate--alanine-ligase
MSRKPLVDPRRAREEIAQSAARLIAEDGLDYASAKRKAARQLFGDARVAGEWLPDNDLIEEELREYLALFQSDTQPDELRRLRELALDWMRRLAEFNPYVTGAVLHGTANEHSDIHLQIFTDNPKDVAIYLLNQNVQYDVSETRHFAGRADVETLSFLWRPRRDMDAIGIHVALYASDDLRGAVKADARGRVARADATALRALLEASNVPSEPE
>NZ_CP042177.1|WP_011655924.1|600094_601480_+|UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl--meso-diaminopimelate-ligase
MHIHILGICGTFMGGLAVLAREAGHTVTGCDAGVYPPMSTQLEAQGITLIEGYGAEQIDLKPDLFVIGNVVTRGNPLMEAILDRGLPYVSGPQWLGEHVLAGKWVLAVAGTHGKTTTSSMLAWLLEDAGLNPGFLIGGVPLNFGVSARLTDSSFFVIEADEYDTAFFDKRSKFVHYRPRTAVLNNLEFDHADIFPDLAAIETQFHHLVRTVPGVGRLVTNGRSDALERVLARGCWSEVERFGVDGGWQALPAEDGVPVDERFAVYSQSERVGEVAWQVQGDHNRMNALAAIAAARHVGVPPAQAAESLASFRNVKRRMEVRGSIDGVTVYDDFAHHPTAIETTIAGLRARIGRQNSRILAVLEPRSNTMKLGVMKAQLPASLADADLVFGYGAPAGRDVLGWNLADALAPLGDKARAFDDLHLLVKSVVEAARPGDHVLVMSNGGFGGVHQKLLDALGSRA

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Crispr_ID: NZ_CP042177_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP042177_2

1207078-1207179

Orphan

Consensus_repeat	Method
GAAGGACGCGATGGGCCACGACGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP042177_2

>merge|NZ_CP042177|2|1207078-1207179|CRISPRCasFinder
GAAGGACGCGATGGGCCACGACGCGATGGCGAAGGACGGCGCGATGAAGAAGGGCACCATGAAGAAGCATGCGATGAAGAAGGATGCGATGGGCCACGACGC

>NZ_CP042177|2|2|1207078-1207179|CRISPRCasFinder
GAAGGACGCGATGGGCCACGACGC	GATGGCGAAGGACGGCGCGATGAAGAAGGGCACCATGAAGAAGCATGCGATGAA
GAAGGATGCGATGGGCCACGACGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP042177.1\|WP_138848008.1\|1200712_1201993_-\|EAL-domain-containing-protein	unknown	unknown	gnl\|CDD\|238923
NZ_CP042177.1\|WP_012363478.1\|1200256_1200661_+\|aminoacyl-tRNA-hydrolase	unknown	unknown	gnl\|CDD\|181730
NZ_CP042177.1\|WP_041489781.1\|1217619_1218648_-\|extracellular-solute-binding-protein	unknown	unknown	gnl\|CDD\|270267
NZ_CP042177.1\|WP_138848001.1\|1214814_1215846_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|226361
NZ_CP042177.1\|WP_138848498.1\|1190902_1194241_+\|exodeoxyribonuclease-V-subunit-gamma	unknown	unknown	gnl\|CDD\|335690
NZ_CP042177.1\|WP_138848005.1\|1209021_1210959_+\|RICIN-domain-containing-protein	unknown	unknown	gnl\|CDD\|237057
NZ_CP042177.1\|WP_138848003.1\|1212508_1213708_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340882
NZ_CP042177.1\|WP_105787219.1\|1215870_1216767_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|224098
NZ_CP042177.1\|WP_138848007.1\|1202280_1202610_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042177.1\|WP_138848004.1\|1211308_1212487_+\|EamA-family-transporter	unknown	unknown	gnl\|CDD\|183067
NZ_CP042177.1\|WP_006759245.1\|1204090_1204303_-\|glycine-zipper-2TM-domain-containing-protein	unknown	unknown	gnl\|CDD\|182532
NZ_CP042177.1\|WP_012363481.1\|1204540_1206472_-\|phosphomethylpyrimidine-synthase-ThiC	unknown	unknown	gnl\|CDD\|236451
NZ_CP042177.1\|WP_138848009.1\|1197938_1200260_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|236783
NZ_CP042177.1\|WP_011656437.1\|1202563_1203490_-\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|273359
NZ_CP042177.1\|WP_138848000.1\|1216777_1217602_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223629
NZ_CP042177.1\|WP_011656438.1\|1203632_1203881_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378701
NZ_CP042177.1\|WP_012363484.1\|1207981_1208770_+\|molybdopterin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|239026
NZ_CP042177.1\|WP_138848006.1\|1207319_1207952_+\|DUF4405-domain-containing-protein	unknown	unknown	gnl\|CDD\|226602
NZ_CP042177.1\|WP_138848002.1\|1213951_1214776_-\|phosphodiesterase	unknown	unknown	gnl\|CDD\|277347
NZ_CP042177.1\|WP_138848010.1\|1194237_1197942_+\|exodeoxyribonuclease-V-subunit-beta	unknown	unknown	gnl\|CDD\|236784

Protein	Function_ID	Function_description	E-value
NZ_CP042177.1\|WP_138848008.1\|1200712_1201993_-\|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.	2.33627e-55
NZ_CP042177.1\|WP_012363478.1\|1200256_1200661_+\|aminoacyl-tRNA-hydrolase	gnl\|CDD\|181730	PRK09256, PRK09256, aminoacyl-tRNA hydrolase.	5.18109e-68
NZ_CP042177.1\|WP_041489781.1\|1217619_1218648_-\|extracellular-solute-binding-protein	gnl\|CDD\|270267	cd13549, PBP2_Fbp_like_3, Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	8.28446e-164
NZ_CP042177.1\|WP_138848001.1\|1214814_1215846_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|226361	COG3842, PotA, ABC-type spermidine/putrescine transport systems, ATPase components [Amino acid transport and metabolism].	4.47191e-133
NZ_CP042177.1\|WP_138848498.1\|1190902_1194241_+\|exodeoxyribonuclease-V-subunit-gamma	gnl\|CDD\|335690	pfam04257, Exonuc_V_gamma, Exodeoxyribonuclease V, gamma subunit. The Exodeoxyribonuclease V enzyme is a multi-subunit enzyme comprised of the proteins RecB, RecC (this family) and RecD. This enzyme plays an important role in homologous genetic recombination, repair of double strand DNA breaks resistance to UV irradiation and chemical DNA-damage. The enzyme (EC:3.1.11.5) catalyzes ssDNA or dsDNA-dependent ATP hydrolysis, hydrolysis of ssDNA or dsDNA and unwinding of dsDNA. This family consists of two AAA domains.	0
NZ_CP042177.1\|WP_138848005.1\|1209021_1210959_+\|RICIN-domain-containing-protein	gnl\|CDD\|237057	PRK12323, PRK12323, DNA polymerase III subunit gamma/tau.	1.7338e-09
NZ_CP042177.1\|WP_138848003.1\|1212508_1213708_-\|MFS-transporter	gnl\|CDD\|340882	cd17324, MFS_NepI_like, Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily. This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	6.55637e-62
NZ_CP042177.1\|WP_105787219.1\|1215870_1216767_-\|ABC-transporter-permease-subunit	gnl\|CDD\|224098	COG1177, PotC, ABC-type spermidine/putrescine transport system, permease component II [Amino acid transport and metabolism].	2.51701e-46
NZ_CP042177.1\|WP_138848004.1\|1211308_1212487_+\|EamA-family-transporter	gnl\|CDD\|183067	PRK11272, PRK11272, putative DMT superfamily transporter inner membrane protein; Provisional.	9.18498e-58
NZ_CP042177.1\|WP_006759245.1\|1204090_1204303_-\|glycine-zipper-2TM-domain-containing-protein	gnl\|CDD\|182532	PRK10540, PRK10540, osmotically-inducible lipoprotein OsmB.	2.0396e-09
NZ_CP042177.1\|WP_012363481.1\|1204540_1206472_-\|phosphomethylpyrimidine-synthase-ThiC	gnl\|CDD\|236451	PRK09284, PRK09284, thiamine biosynthesis protein ThiC; Provisional.	0
NZ_CP042177.1\|WP_138848009.1\|1197938_1200260_+\|AAA-family-ATPase	gnl\|CDD\|236783	PRK10875, recD, exodeoxyribonuclease V subunit alpha.	2.68745e-73
NZ_CP042177.1\|WP_011656437.1\|1202563_1203490_-\|DMT-family-transporter	gnl\|CDD\|273359	TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter. [Transport and binding proteins, Amino acids, peptides and amines].	8.42615e-14
NZ_CP042177.1\|WP_138848000.1\|1216777_1217602_-\|ABC-transporter-permease-subunit	gnl\|CDD\|223629	COG0555, CysU, ABC-type sulfate transport system, permease component [Posttranslational modification, protein turnover, chaperones].	3.98548e-44
NZ_CP042177.1\|WP_011656438.1\|1203632_1203881_-\|hypothetical-protein	gnl\|CDD\|378701	pfam11737, DUF3300, Protein of unknown function (DUF3300). This hypothetical bacterial gene product has a long hydrophobic segment and is thus likely to be a membrane protein.	0.000296921
NZ_CP042177.1\|WP_012363484.1\|1207981_1208770_+\|molybdopterin-dependent-oxidoreductase	gnl\|CDD\|239026	cd02108, bact_SO_family_Moco, bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This domain is found in a variety of oxidoreductases. Common features of all known members of this family, like sulfite oxidase and nitrite reductase, are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate. The specific function of this subgroup is unknown.	2.81152e-87
NZ_CP042177.1\|WP_138848006.1\|1207319_1207952_+\|DUF4405-domain-containing-protein	gnl\|CDD\|226602	COG4117, COG4117, Thiosulfate reductase cytochrome B subunit (membrane anchoring protein) [Energy production and conversion].	4.41059e-49
NZ_CP042177.1\|WP_138848002.1\|1213951_1214776_-\|phosphodiesterase	gnl\|CDD\|277347	cd07402, MPP_GpdQ, Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain. GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	6.79909e-91
NZ_CP042177.1\|WP_138848010.1\|1194237_1197942_+\|exodeoxyribonuclease-V-subunit-beta	gnl\|CDD\|236784	PRK10876, recB, exonuclease V subunit beta; Provisional.	0

>NZ_CP042177.1|WP_012363481.1|1204540_1206472_-|phosphomethylpyrimidine-synthase-ThiC
MNANPKFLSADAHVDAAAVAPLPNSRKVYVTGSQPDIRVPMREITQADTPTGFGGEKNPPIYVYDTSGPYTDPDAKIDIRAGLPALRQGWIEARGDTEVLDGLSSQYGLERAADPATADLRFPGLHRNPRRAQPGKNVTQMHYARQGIITPEMEYIAIRENQRRAEYIESLKSSGPNGAKLAAMMGRQHPGQAFGAAAFGANALAEITPEFVRDEVARGRAIIPANINHPESEPMIIGRNFLVKINANIGNSAVTSSIGEEVDKMTWAIRWGGDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVNGKAEDLTWEIFRDTLIEQAEQGVDYFTIHAGVRLQYVPLTANRMTGIVSRGGSIMAKWCLAHHKESFLYEHFEEICEIMKAYDVSFSLGDGLRPGSIYDANDEAQLGELKTLGELTQIAWKHDVQVMIEGPGHVPMQLIKENMDLQLDWCKEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGTAMLCYVTPKEHLGLPNKDDVKEGIITYKLAAHAADLAKGHPGAQVRDNALSKARFEFRWEDQFNIGLDPDKAREFHDETLPKDSAKVAHFCSMCGPHFCSMKITQDVREFAAQQGVSETEALKKGMEVKAVEFVKTGAEIYHRQ
>NZ_CP042177.1|WP_006759245.1|1204090_1204303_-|glycine-zipper-2TM-domain-containing-protein
MNSIRRFGVYALLVATVASLSACDSMSRRQRDTAIGAGVGGVAGAAIGGNALSTLGGAAAGGLIGNQVGK
>NZ_CP042177.1|WP_011656438.1|1203632_1203881_-|hypothetical-protein
MNRTLVAAALACATLAGCYYPYGYYPSGYYAAAPVQTAPVYVEPGPAYYYPAPAYAPAWGGYWGPALSLNFGFGGRGGHRHH
>NZ_CP042177.1|WP_011656437.1|1202563_1203490_-|DMT-family-transporter
MSPKNAFLLTVLAALWGASFLFIRIGVAEFGVAPLMALRVGIGALFLTGLALTRFKPADLAARLRRHAWPLFVVGLLNSGAPFCLFAYAELTLSAGVTSVINATTPLWGALVAYVWLKDKLSLPRALGLVIGFAGVLTLVWDQIANAHGSTGASATALAAVAALGATLLYGIAANYTKRKLSGVDPLVNATGSMIGSTVLLLPFAIATWPAAAVSAHAWGAVLALGIACTGIAYFIFFYLIAHVGPARAITVTFVIPVFGLLWGALFLSEHVSVVMLEGCAIVLVGTALATGVIKRIPGVRPRGEEAA
>NZ_CP042177.1|WP_138848007.1|1202280_1202610_+|hypothetical-protein
MRRGSESGGPEGGVPRAVVGLGRKTPCFRAYRWTRGVRRRPRTDNGRVTRNRQPAGRRPPRSPPFSSLRLLSPLTPLTPLTPLTPLTPLRQLRPLRQLPPPADGPRESA
>NZ_CP042177.1|WP_138848008.1|1200712_1201993_-|EAL-domain-containing-protein
MKASRELSLESLLERLTPTPSGWIATYRETTLRSVFQPVLSITHKRVVGYEALLRVVDANGTLVSPVALFDKTRAVADALLLDRLARCLHTANFVAQGIGDGWLFLNVTPRVLDSGLVQREFVEALCRHFALPPNRIVLEVVEQPSRDEAALARTIDMIQHRDFLIAIDDFGTGFSNFDRVWRARPDIVKLDRSLVERATGSGEDRRIMHHLVSMLHQAGAMVLAEGVENDDALQALMDADIDFVQGFQFGQPDGSIAHASAAAPAMLDAAWQRFIAQRHTPGSAEQPGFDAIERLVLAGAAAFSASGNLNDAAQRVFAVPAARRVFVTDEIGEQFLPSIGAPAEDGQAGGTRLSPLFPETHSNWSRRPYFQRAIAAPGRVALMGPHFSLTEGRDCYTAAVAIRAQSRLVVFCVDFVLDSAGTVMR
>NZ_CP042177.1|WP_012363478.1|1200256_1200661_+|aminoacyl-tRNA-hydrolase
MMIRYTLDPAEVEWTAVRAQGAGGQNVNKVSSAIHLRFDIRASSLPPVIKERLLALSDQRITRDGIVVIKSQEYRTQEKNRDAALARLDALIGSVAYTPRARVATRPTRASKERRLEHKSRRSAVKSGRGKVTD
>NZ_CP042177.1|WP_138848009.1|1197938_1200260_+|AAA-family-ATPase
MNASDDTLEFTGGLVARLPEPADFGIALAEGFARRMGDLSRRAGAPAVAARWAARAAFAASRATAGGHVCVSLGALAQRYEEPVDDVRAALAASGVVAFGTLARGDERPLIVDRLDHLYLSRYFDYERRLADALVAQAGVAAPGDALSPERLRDSLARYFGPATGEVDWQRVAAIVALTGRVTIVSGGPGTGKTTTVVGVLACLLDAHPGLRIALAAPTGKAAQRMQEALHARAGDLPPELAARLPDTSYTLHRLLGGGGAAGFRHHRDNPLPYDLIVVDEASMIDVALAAHLLDALAPGARLVLLGDKDQLAAVEAGAVFAELSARPTFTAAARTRIAGALGIDEAAFVAALPVPDGEAAAVAATTQAPAPAPAPASAPVSTSAARRPPARRNVDTRQASLFDDDPQDEAMSAADVAAPPAASLSPAAAAPTDIDSVGASADPAWIEADELAWLDAIELAPFDPADAADAANASLASTAATQADDPAAASPAPAPLADCVVWLERNYRFGLDSPIGRLSLAIRRGDVQAALDALPADDAAAASFHDDAGDTLAASTVERLARRFAAYLDALRTALSEPVPDPLPLFDALNRFRILCATRTGSRGAEHVNALVATHVRQAARVPLAVGAHWFTGRPIMVTRNDYALGLFNGDIGIALPDAHGVLRVWFRRADGTARAVSPAALPPHETAFALTVHKSQGSEFDEAALVLPASFGRVLTRELVYTAVTRARTRVQVIGLRRVLAQAVATRTQRDSGLAARVDEALARRRKEPSR
>NZ_CP042177.1|WP_138848010.1|1194237_1197942_+|exodeoxyribonuclease-V-subunit-beta
MSAASQPQAALELDVFACPLGGVNQIEASAGTGKTWNICALYVRLLLEKDLGADEILVVTFTKAATAELHERIRGRLAQLAHALDTGDDGGDPFVARLLETTLGDAGTLDPETAAKRIRRALRAFDQAAIHTIHAFCQRALQEAPFAAAMPFAFDMQADDAALRFELAADFWRTRVEPMAARWPGFATWLVDSGAGPAALDAQLARRLKKPLAALRWDGVVEPDESAEAAAAECFAEAARLWADERDAIDALLRTAQPALNQRSHKPDALADALAAWSAHFAQGDAAAALPKAALKLTRTALAKATKKGGVTPEHAFFDVADALEAAVAAAEATQRARWLALIADWLDTAPGELAERKRTRRVVSFDDLLANLYHALHAHPWLAETLRARYPAALIDEFQDTDPLQFAIFNRIFAPGGPLFLVGDPKQAIYSFRAADLHTYLAARASASACYTLAVNQRSTPAIVDACNRFFMSNPRAFVLDGLDYYAVRAGTRVRAPFVDATDPGPAGDFRIWSLPGGDGTLLKREAQAQAAQACAAEIARLMRGAREGHARLGDTPLSPGDIAVLVQTHRQGSLVKRVLATWGIGSVELAQASVFSTGDAEQLERVLAAIDAPGDLRRLRSALAADWFGLDAGALWRMEQGDGDASREAADSADAMSWVERFSRYRLLWRERGFAVMWRTFTRELRIAERLMAGADGERRVTDINHLAELTQARASAQPGIAPTLRWLAAQRLDGGGEEAQLRLESDRNLVQIVTVHKSKGLEYAVVFCPFLNDGGLREPPASGLPDAREYHDDAGDAVLHYGCDDEAAEHAARQALREQAAERARLVYVALTRAVYRCYLVAGPYLSSRSTREARRSVLNWLVAGAGQSFDAWLDEPPDEAVLDSAWQALAGGPVSVAPLPVPARRERLAAGHDATQTLAARHATRVLRDAWRMASFSSLTSSMAREEAGVAVVPDDELRPDHDALAAVAPDGAFVAADTVASEPPDDDILRFPRGAAAGECLHRLFELSRFTEPDSWYQAALGALHDRPVEAEPELATRLPAMMARLVDDVVRTELVPGMRLADLDPTRRLDEMGFLFPAPSLELGALRRLLVAHGYPDVALDSGMLAGFIKGFIDMILEHDGRFWIVDWKSNHLGNTPDAYGPRALDVAMSDHAYHLQALLYTVALHRYLRGRLPDYDYDTHMAGYLYLFVRGVRPDWRSGGEPAGVHARRPARELVDALDRMMEGGRA
>NZ_CP042177.1|WP_138848498.1|1190902_1194241_+|exodeoxyribonuclease-V-subunit-gamma
MLHLFYSNRHETLADALLDDLAAFPARNGPWAPQQVIVPSAALRRRLELDIAARHGVCANVEFTYLAQWLWAQIGRVLTVPARSPFAPDRLVWRCYRLFAQAEGDAPWLASPRLAAYLSASDDAMRYELAQRVAAVLDHYLTYRPEWLAAWQAGESVLAGDAAPRGISDAARDDEHWQAALWRALLAELSDSGTPPAHRFLVEARNLDPETVARADWPESVSVFALPTMPPLHVALLRELSRWIDVRVYALNPCREFWFDIVTAAHAEALDAAGRLDYQQVGHPLLAEWGRQTQAQLHMLHELTESAALGDASRFVGNPAPTWLARVQNAILDLQPEAELGEAPAEHGIEVHVCHSLARQLEVLHDRLLAWFDADATLQPSDVLVAVADLAAAGPLIDAVFGTAGAGGARVPYRITGLPPSQANPVARVLLEWLALPERQVGAPELVEWLRVDAVAARYGIDAAALETVQTWLAAAGARRGLSPTASDDAAVPAPRHTFSDALARLFLGYAMPEGAAPVGAWLPIEAATGSEAELLGRLARFTDDLDGFSRRLASAHTPRAWSELFADTLARFFDSGAAYADALAGVRDALDAMLAAMTEGAPDEALPAAVVRAGLTAALDDPARGGVPWGGVTFSSLTSLRGLPYRVVCLLGMDDGVLPSLARADEFDLMAVLPKLGDRQRRDDERNLFLDLLLAARDRLLIAYTGRSIRDNAPLPPAALVDELLDHLALVTAGADTAPGAVDAARRAFIVEHPLQPFAAEYFRPGSELASYDAERATLASLLAAEAARDATREQPFFAQPLPAEPVEPIAFNEFERFWRHPARALLRARLGIVLSDAQAELLDTEPFALDFAGSDALAERVLPLLIESDEGGVHDHALRIADTSPELPGGATGAVWRDQALGSMMQLASNVRRALADGMERRPFTLAITPAWPDTDQALFGADDAMLSGDALSAPLELHGTLNRVTPAGQIIYRYARPSARDYLSAWLAHLVYCAVEPDGPRRTMWFGSGGAFELTPVATPLERLAPLAALFRAGRRMPLRFFPRSAWARVSDGEAKAASVWINERVVSEADDPAIAIAWRGAHPSLDEPFGTLARIVFEPMLEHLKEIA
>NZ_CP042177.1|WP_138848006.1|1207319_1207952_+|DUF4405-domain-containing-protein
MQTVPATGRAAATPPARPIHPLWVRASHWLNALAAVLMALSGWRIYDASPIYPPFTFPHGITLGGWLGGALQWHFAAMWLLVGNGLFYLTMSLATGRLVRKMLPVTPASVWRDVRAALRGRLSHADLSVYNAVQRAAYLTAIVDLVVLVLSGLAIWKSVQFPLLRELFGGYDNARVVHFWAMSLLVAFFVVHVAMALLVPRSLLAMLRGR
>NZ_CP042177.1|WP_012363484.1|1207981_1208770_+|molybdopterin-dependent-oxidoreductase
MSESENRRGQPRWTLDRKSLELDVRRELEMPSRRLFNRRVLTLGGLTMLTGCTLQDDASVNTFLEKVSRMNDRVQAWLFSPDRLAPTYTEADITRPFPFNAYYGIDDVPHVDESTYRLVLSGRVTGKRVWTLDELRALPHAEQITRHICVEGWSAIGRWGGTPFGAFLARAGADTHAKYVGFKCADDYYESIDMPTALHPQTLLTFDYDGQRLPPEFGFPMKLRMPTKLGYKNPKHIMEIFVTDTFPGGYWVDQGYNWFGGS
>NZ_CP042177.1|WP_138848005.1|1209021_1210959_+|RICIN-domain-containing-protein
MHSEPNAGRQAGCFVRGSPVNPVRDEVSKMNPFVSRRAVAPALLCALVLVLSACGGDDSGAPAIVVQEQQGESGEHVKPAPEIVADGVAVSDEPGAPPDPSYPRPPVAPEPGEPPATIEPPSPRPPAIVEPAPPEPAPEPPAIVEPAPPEPAPEPPAIVEPAPPDPPPALDTSLAIRNLATGEALCLGMSTGNGTYVGFQSCNGSDAQRWRMVRAASPYFNVKNVLAEAQGRDVCLRAAPSGQSPANLAPCGGADYPTTRMWRASIGASGAFTLQNKHWVDTGRRATLQAMDRTLAMLPEIDAPAARWTYDGELPSPRRVVTGARSVLLVSGHFTGQRANPAEPVRKAVFGDGDDFASLAHYLKLASRGKLTLSGTMLTNVDLGAFPAGCQSGAILAQARAAAQARGVDANGFDYLFVDYPRSSECKFAGLAARPGQWILSNGAGTGYWMWTHEFGHGLGAGHPDSLRNCPVADGAVVLGSLCVTGGIDDPTDTVGGGGRRMYPVDYQLFAGWLDDEDVPTLVKPGTYRIAPLWSALPGKQGYRLPRADGSTLLLEFRRPMGAKGTFEDWPDTSPFVNGVTVRIVRYPGNAIQNTLVDATPGSQDGMKDAPLMPGQSLVDTLSGRRITVLSADGSGAVVRIEPAS
>NZ_CP042177.1|WP_138848004.1|1211308_1212487_+|EamA-family-transporter
MTPLDRLLDFLARLPFRIRLPQSRGGRVALALVFIYFVWGSTYSGLHFALQSFPPLLLSGLRNLLGGIGLFIFALRRKPEWPTLLEIRNSAIVGTMLVALSSGTIALGMRTVSSGSAAVMVATVPLFATVIAAVAGRPVTKGEWSAVALGMVGIVVLNSGGAAAANSALGTISVLAGALFWAGGAHLSTRLKLPSDLFLSTSLQIGLGGLMSTLAAWLLGERIEQVAAAPVFAFLYLMVFCTMAAYVAYGYLIRHTSPIIASSCMYVNPIVAVALGALMLGEPVTMATVIATVAILGSVGLSFLFDPARRPAARAAVDVSPAVATGSAAAPAPVPPPDQAAVPDSAPILTPSAIPLAVPTPAAVVDPAAVMDPAQAFTPPPADEPAESRARA
>NZ_CP042177.1|WP_138848003.1|1212508_1213708_-|MFS-transporter
MSAASTDRPTDAASPHYSRSLLLLLATIAGVSVANIYYNQPLLDSFRSAFPHSASWIGAVPTATQLGYAAGMFLLAPLGDRFDRRGLILLQIAGLSIALIVAAAAPSLAVLAAASLAIGVLATIAQQAVPFAAEIAPPAERGHAVGTVMSGLLLGILLARTAAGFVAEYFGWRAVFGASVAALAALAAVIVLRLPRSSPTSTLSYGKLLGSMWHLVVELRGLREASLTGAALFAAFSAFWPVLTLLLAGAPFHLGPQAAGLFGIVGAAGALAAPYAGRFADKRGPRAIISLAIALLAASFVIFALSGTSLVGLVIGVIVLDVGVQAAQISNQSRIYALKPDARSRVNTVYMVCYFIGGALGSSVGVAAWHAFGWIGMCAAGLLFTALAGWFHHRGAQRA
>NZ_CP042177.1|WP_138848002.1|1213951_1214776_-|phosphodiesterase
MLLAQISDLHIKRPGQLAYRRVDTAAALARCIAKLNALLPRPDAVLVTGDLTDFGHDDEYRHLRDLLAPLEIPYYLMVGNHDDRAGLRRAFADRPELQDGEFVQYALDVGAVRVLALDSQVPGASHGDLCDARLAWLAARLDAARDRPVIVALHHPPFVSGIGHMDALRLAPAAAAKLDALLRGYPNVERVLCGHVHRTMFTRFGGTLASAVPAPAHQVAFDLRADAPSAFRLEPPAFAVHVHTPQTGMTSHHVYVDEGDGPYPFYEPSGELVD
>NZ_CP042177.1|WP_138848001.1|1214814_1215846_-|ATP-binding-cassette-domain-containing-protein
MKLDSTPITLTRCAKTFRGTRVLEPLDLSIGAGETLVLLGPSGCGKTTTLRLVAGLDTPDAGGTIAFGGDDVTALPIERRQVGMVFQNYALFPNLTVRGNVGYGLKIRKTEPRALRERVDELLAMMRLDAHADKPVDQLSGGQRQRVALARALAVRPRVLLLDEPLTALDAKLRDVLRREMNALLRELGVTTVYVTHDQAEAMELGDRIVVMGAGRIEQIGTPRDIYYRPANRTVAQFIGTLNRLAGQWRDGALVTTGGAIVTPHAADEWFFRPEDAQLADPAHAPLRGAIGACAFLGERTRLTIEHAAPDALVIDVPGRIELARGTAVGIAIAAEGLIALAA
>NZ_CP042177.1|WP_105787219.1|1215870_1216767_-|ABC-transporter-permease-subunit
MQSLSGSSAPSPAPAPSHANGVARRAPRVTGARAIAALQWSVTLLLCAFLIVPVVMSVLAGLTVNYFRGLSSGLTLRWLEQVWQQYQGSVALSLGVAFATLAIVLAVGVPAGYALARSKSRVARAIEEALVLPVALPGLASALALLVVYGGFTAFRMSLWFIVVGHVVFTLPFMVRAVAAVAAGADLRTLEEGAASLGASFVTRFVTIVLPNLRPGIVAGALAVLTLSIGEFNLTWMLHTPDTKTLPVGLADTYASLRLEVGSAYTIVFLLMTLPLLVAMQWLGVDPSGTRALKRRPR
>NZ_CP042177.1|WP_138848000.1|1216777_1217602_-|ABC-transporter-permease-subunit
MLDLTFPLRWRVALVAPALAVFAAFWLLPMAALVHVSADGAFFTQYATLLGNARYMKSLGETVALSAGVTLATLALSTISGLLLARREFAGKRVLLALLTFPLAFPGVVVGFMVIMLAGRQGLVGMLSAKLTGDKWVFAYSVAGLFVGYLYFSIPRVIVTVIAAASKLDASLEEAARSLGASPWRIFVDIVLPALAPGLIAAGAICFATAMGAFGTAFTLATDLNVLPMTIYTEFTLNANIATAAGLSIVLGIVTWAVLALARRFTGHTATAAA
>NZ_CP042177.1|WP_041489781.1|1217619_1218648_-|extracellular-solute-binding-protein
MSFRLTSLLRVLAAPVACAALVAFAPAAHADESAICYNCPPEWADWAAQIAAIKQKTGIRVPFDNKNSGQAIAQLIAEQKSPVADVVYLGVSSAFQAKDKGVIAPYKPAHWNDIPANLKDPQGYWFAIHSGTLGFFVNKDALDGKPVPRSWADLLKPEYKGMVGYLDPSSAFVGYAGAVAVNQALGGSLDNFKPALDWFRKLKANAPIVPKQTAYARVLSGEIPILLDYDFDAYRAKYKDHANVEFVIPQEGTIAVPYVMSLVKGAPHDANGRKVLDFVLSDEGQKLWANAYLRPVRAQTLGADVAAKFLPASEYARAKPVDFGKMAAGQQAFGLQYLQVMQ

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Crispr_ID: NZ_CP042177_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP042177_3

1825810-1825918

Orphan

Consensus_repeat	Method
GGTTCAAGGAACGGTAAAGGAGGAACA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP042177_3

>merge|NZ_CP042177|3|1825810-1825918|CRISPRCasFinder
GGTTCAAGGAACGGTAAAGGAGGAACAGCCTGCGCGACGATGCGCGAGAACGCCGCGCCCTCCGGCGAACGCAAACGGCGGCGGTTCAAGGAAAGGTAAAGGAGGAACA

>NZ_CP042177|3|3|1825810-1825918|CRISPRCasFinder
GGTTCAAGGAACGGTAAAGGAGGAACA	GCCTGCGCGACGATGCGCGAGAACGCCGCGCCCTCCGGCGAACGCAAACGGCGGC
GGTTCAAGGAAAGGTAAAGGAGGAACA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP042177.1\|WP_138847679.1\|1833967_1834732_-\|TIM-barrel-protein	unknown	unknown	gnl\|CDD\|366542
NZ_CP042177.1\|WP_006755043.1\|1825971_1826436_-\|Lrp/AsnC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224439
NZ_CP042177.1\|WP_138847681.1\|1831502_1832783_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340877
NZ_CP042177.1\|WP_006755038.1\|1822095_1822383_+\|YciI-family-protein	unknown	unknown	gnl\|CDD\|237238
NZ_CP042177.1\|WP_138847684.1\|1823693_1824311_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|379324
NZ_CP042177.1\|WP_138847687.1\|1817620_1818085_-\|RidA-family-protein	unknown	unknown	gnl\|CDD\|100006
NZ_CP042177.1\|WP_012363937.1\|1827467_1827899_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|290790
NZ_CP042177.1\|WP_138847682.1\|1830531_1831497_-\|bifunctional-glyoxylate/hydroxypyruvate-reductase-B	unknown	unknown	gnl\|CDD\|185307
NZ_CP042177.1\|WP_138847685.1\|1819372_1820080_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|237218
NZ_CP042177.1\|WP_138847683.1\|1828322_1829111_-\|YhfC-family-intramembrane-metalloprotease	unknown	unknown	gnl\|CDD\|337619
NZ_CP042177.1\|WP_006755042.1\|1824406_1825507_-\|NAD(P)H-binding-protein	unknown	unknown	gnl\|CDD\|224662
NZ_CP042177.1\|WP_012363939.1\|1829165_1830209_-\|LacI-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380506
NZ_CP042177.1\|WP_138847688.1\|1816928_1817348_-\|Ohr-family-peroxiredoxin	unknown	unknown	gnl\|CDD\|274649
NZ_CP042177.1\|WP_012363934.1\|1823550_1823697_+\|cytochrome-bd-I-oxidase-subunit-CydX	unknown	unknown	gnl\|CDD\|369733
NZ_CP042177.1\|WP_012363936.1\|1826802_1827339_+\|Spy/CpxP-family-protein-refolding-chaperone	unknown	unknown	gnl\|CDD\|369534
NZ_CP042177.1\|WP_006755037.1\|1821173_1821662_-\|YbaK/EbsC-family-protein	unknown	unknown	gnl\|CDD\|239824
NZ_CP042177.1\|WP_138847680.1\|1832946_1833939_-\|sugar-kinase	unknown	unknown	gnl\|CDD\|238571
NZ_CP042177.1\|WP_138847686.1\|1818349_1819282_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_CP042177.1\|WP_011656931.1\|1827947_1828310_-\|DUF3022-domain-containing-protein	unknown	unknown	gnl\|CDD\|378603
NZ_CP042177.1\|WP_012363933.1\|1822392_1823370_-\|magnesium/cobalt-transporter-CorA	unknown	unknown	gnl\|CDD\|213364

Protein	Function_ID	Function_description	E-value
NZ_CP042177.1\|WP_138847679.1\|1833967_1834732_-\|TIM-barrel-protein	gnl\|CDD\|366542	pfam01261, AP_endonuc_2, Xylose isomerase-like TIM barrel. This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.	7.21145e-06
NZ_CP042177.1\|WP_006755043.1\|1825971_1826436_-\|Lrp/AsnC-family-transcriptional-regulator	gnl\|CDD\|224439	COG1522, Lrp, Transcriptional regulators [Transcription].	7.52546e-29
NZ_CP042177.1\|WP_138847681.1\|1831502_1832783_-\|MFS-transporter	gnl\|CDD\|340877	cd17319, MFS_ExuT_GudP_like, Hexuronate transporter, Glucarate transporter, and similar transporters of the Major Facilitator Superfamily. This family is composed of predominantly bacterial transporters for hexuronate (ExuT), glucarate (GudP), galactarate (GarP), and galactonate (DgoT). They mediate the uptake of these compounds into the cell. They belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	2.28652e-85
NZ_CP042177.1\|WP_006755038.1\|1822095_1822383_+\|YciI-family-protein	gnl\|CDD\|237238	PRK12866, PRK12866, YciI-like protein; Reviewed.	2.44704e-59
NZ_CP042177.1\|WP_138847684.1\|1823693_1824311_+\|AAA-family-ATPase	gnl\|CDD\|379324	pfam13671, AAA_33, AAA domain. This family of domains contain only a P-loop motif, that is characteristic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.	5.02361e-20
NZ_CP042177.1\|WP_138847687.1\|1817620_1818085_-\|RidA-family-protein	gnl\|CDD\|100006	cd02199, YjgF_YER057c_UK114_like_1, This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.	3.32908e-60
NZ_CP042177.1\|WP_012363937.1\|1827467_1827899_+\|hypothetical-protein	gnl\|CDD\|290790	pfam14083, PGDYG, PGDYG protein. This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 150 amino acids in length. There is a conserved PGDYG motif.	1.26877e-54
NZ_CP042177.1\|WP_138847682.1\|1830531_1831497_-\|bifunctional-glyoxylate/hydroxypyruvate-reductase-B	gnl\|CDD\|185307	PRK15409, PRK15409, glyoxylate/hydroxypyruvate reductase GhrB.	8.94118e-162
NZ_CP042177.1\|WP_138847685.1\|1819372_1820080_-\|SDR-family-oxidoreductase	gnl\|CDD\|237218	PRK12825, fabG, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional.	2.1225e-56
NZ_CP042177.1\|WP_138847683.1\|1828322_1829111_-\|YhfC-family-intramembrane-metalloprotease	gnl\|CDD\|337619	pfam10086, DUF2324, Putative membrane peptidase family (DUF2324). This domain, found in various hypothetical bacterial proteins, has no known function. This family appears to be related to the prenyl protease 2 family pfam02517, suggesting this family may be peptidases.	7.59802e-52
NZ_CP042177.1\|WP_006755042.1\|1824406_1825507_-\|NAD(P)H-binding-protein	gnl\|CDD\|224662	COG1748, LYS9, Saccharopine dehydrogenase and related proteins [Amino acid transport and metabolism].	3.04077e-85
NZ_CP042177.1\|WP_012363939.1\|1829165_1830209_-\|LacI-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|380506	cd06283, PBP1_RegR_EndR_KdgR-like, ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR. Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.	3.45503e-91
NZ_CP042177.1\|WP_138847688.1\|1816928_1817348_-\|Ohr-family-peroxiredoxin	gnl\|CDD\|274649	TIGR03561, organ_hyd_perox, peroxiredoxin, Ohr subfamily. pfam02566, OsmC-like protein, contains several deeply split clades of homologous proteins. The clade modeled here includes the protein Ohr, or organic hydroperoxide resistance protein. [Cellular processes, Detoxification].	6.49734e-65
NZ_CP042177.1\|WP_012363934.1\|1823550_1823697_+\|cytochrome-bd-I-oxidase-subunit-CydX	gnl\|CDD\|369733	pfam08173, YbgT_YccB, Membrane bound YbgT-like protein. This family contains a set of membrane proteins, typically 33 amino acids long. The family has no known function, but the protein is found in the operon CydAB in E. coli. Members have a consensus motif (MWYFXW) which is rich in aromatic residues. The protein forms a single membrane-spanning helix. This family seems to be restricted to Proteobacteria.	1.08032e-09
NZ_CP042177.1\|WP_012363936.1\|1826802_1827339_+\|Spy/CpxP-family-protein-refolding-chaperone	gnl\|CDD\|369534	pfam07813, LTXXQ, LTXXQ motif family protein. This protein family includes two copies of a five residue motif is found in a number of bacterial proteins bearing similarity to the protein CpxP. This is a periplasmic protein that aids in combating extracytoplasmic protein-mediated toxicity, and may also be involved in the response to alkaline pH. Another member of this family, Spy, is also a periplasmic protein that may be involved in the response to stress. The homology between CpxP and Spy may indicate that these two proteins are functionally related.	8.22789e-06
NZ_CP042177.1\|WP_006755037.1\|1821173_1821662_-\|YbaK/EbsC-family-protein	gnl\|CDD\|239824	cd04332, YbaK_like, YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, ProX, and PrdX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express an INS homolog in trans (e.g. YbaK, ProX, or PrdX).	1.41839e-29
NZ_CP042177.1\|WP_138847680.1\|1832946_1833939_-\|sugar-kinase	gnl\|CDD\|238571	cd01166, KdgK, 2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.	1.13025e-96
NZ_CP042177.1\|WP_138847686.1\|1818349_1819282_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	9.10714e-69
NZ_CP042177.1\|WP_011656931.1\|1827947_1828310_-\|DUF3022-domain-containing-protein	gnl\|CDD\|378603	pfam11226, DUF3022, Protein of unknown function (DUF3022). This family of proteins with unknown function appears to be restricted to Proteobacteria.	1.11302e-49
NZ_CP042177.1\|WP_012363933.1\|1822392_1823370_-\|magnesium/cobalt-transporter-CorA	gnl\|CDD\|213364	cd12830, MtCorA-like, Mycobacterium tuberculosis CorA-like subfamily. This bacterial subfamily belongs to the Thermotoga maritima CorA (TmCorA)-like family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This subfamily includes the Mg2+ transporter Mycobacterium tuberculosis CorA (which also transports Co2+). Thermotoga maritima CorA forms funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport by a related protein, Saccharomyces cerevisiae Alr1p. Natural variants in this signature sequence may be associated with the transport of different divalent cations. The functional diversity of the MIT superfamily may also be due to minor structural differences regulating gating, substrate selection, and transport.	1.58281e-141

>NZ_CP042177.1|WP_006755042.1|1824406_1825507_-|NAD(P)H-binding-protein
MKIAIVGAGLIGHTIAHMLRETGDYEVVAFDRDADALAKLSREGIATQRVDSADANAIREAVKGFDALVNALPYYLAVNVAAAAKAAGVHYFDLTEDVRATHAIRELADGSDRAFMPQCGLAPGFIGIAAHELVNGFSEVRDVKMRVGALPEYPTNALKYNLTWSVDGLINEYCQPCEAIRDGRKQWVQPLEGLEHFSLDGTEYEAFNTSGGLGTLCETLSGKVETLDYKSVRYPGHRELVQFLLEDLRLSSDRDTLKSIMRRAVPSTKQDVVLVFVTVTGVKDGQLVQDVFTRKIFAKDVCGMHMSAIQITTAGAMCAVLDLFREKKLPQSGFIPQEKVSLKAFLSNRFGKLYEGGTMERVHEVA
>NZ_CP042177.1|WP_138847684.1|1823693_1824311_+|AAA-family-ATPase
MTHLVFFCGHAGTGKTTLAKRLIGPLMRVTGEAFCLLDKDTLYGRYSSAAMGALTSDPNDRDSPLYLKHLRDPEYQGLLDTARENLALGIGALVVGPLSREVRDRRILDRAWLGIGPEIALTVVWVHTAEDVAHQRIVARGNPNDAYKLAHWDEYRQRRFVPTGHECDGIVMFDNTAPSDADIDALLYRIVPPAPQATLVPPLPA
>NZ_CP042177.1|WP_012363934.1|1823550_1823697_+|cytochrome-bd-I-oxidase-subunit-CydX
MWYFSWILGIGVALGFGIINVMWLEAEVFPREDKRTDASRAGSGSRYS
>NZ_CP042177.1|WP_012363933.1|1822392_1823370_-|magnesium/cobalt-transporter-CorA
MLINCAAYQDGRKLADIDIDAISDYVSKPECFVWVALKDPTPDEIDLMGEEFALHELALEDARKGHQRPKIEEYGDSLFAVLHTVELDEDGEFNVGELNVFVGPNYVLSIRNHTEQDFRAVRKRCEREPHLLQEGSAFVFYALMDQVVDRYFPILETLGTELEELEDRIFAKASLASSRAIIEDLYSLKRRLVMLYQHTAPLMEPLAKLTGGRIPQVCSGMQHYFRDVYDHLQRIVKTIEGRREMVVTAIQVNLGMISLAENEVTKRLGSFAALFAIPTMIAGIYGMNFANMPELHLKYGFYGCIAVMVAADLALWWRFKRAGWL
>NZ_CP042177.1|WP_006755038.1|1822095_1822383_+|YciI-family-protein
MHYQLIYELVDDYLSRREQYRAEHLALAKAATERGELMLAGALQDPADQAVLVFEGDSPEVAESFARADPYVQNGLVKSWRVRPWRVVVGKHAPH
>NZ_CP042177.1|WP_006755037.1|1821173_1821662_-|YbaK/EbsC-family-protein
MPVSATLQDCLRQKSSRYEVVYHPYSHTSMETAAAAHIPGDRLAKTVLLEDDEGYVAAVLPTSHAVRLSDLWVKTGRHLVLAREMELRELFKDCDLGALPPVCMAYGMKTFLEEQLAQQPEVYFEAGDHEALIHMTQDEFLSLMETAERAHFSHKMQGMWVS
>NZ_CP042177.1|WP_138847685.1|1819372_1820080_-|SDR-family-oxidoreductase
MSTSKVIIVTGASQGIGAETVNAFRAQGHRVVATSRSIGPSDDPDLVTVAGDIGDPAVARRVVDTAIERFGRVDTLVNNAGVFIAKPFTQYTADDYAAITRVNLDGFFHVTQRAIAAMQRHGGGHVVSITTSLVDHANSNVPSALASLTKGGLNAATKSLAIEYAKAGIRVNAVSPGIINSPMHAPDTHATLASLHPVGRMGEMSDIVGAILYLDSAPFVTGEILHVDGGQSAGH
>NZ_CP042177.1|WP_138847686.1|1818349_1819282_+|LysR-family-transcriptional-regulator
MQRKFDDLLLGSIELFCLAAELGSFTLAATAASVTPAAVSRSVARLEERLGVRLFVRTTRQIRLTDSGRRYFEQCRDALSQLVDAEREATGQQATPAGVLRISMPTPYGHYRVLPLLPAFRERYPDVRVETHLSNRNIDFAEEGFDLAIRGRAPADSSLVARKLEDAELVVVATPGYLKRAGVPRAVDDLHAHECIQFELPSSGRPIPWLFNDGTAEIEIATTGGYGTSGDVLAGVTLARSGAGLFQTYRFIVERDLREGTLAEVLSGQGERSRPFMLLYPHARYLSSRVRVFVDFLVEHLEQAPDRRKR
>NZ_CP042177.1|WP_138847687.1|1817620_1818085_-|RidA-family-protein
MTIEQKLAGLGFTLPEPPQPLGSYTAVSEAGNLLFVSGQLPLADGKVAYTGRVGEQLSVDDGRHAAQLAALNVLAQIGKHLGGFDRLHHIVRVEGHVASADGFHGQPAVIDGASNLFAAVLGDKAGHARSAFSQRQLPADAAVILVVIAEIRQA
>NZ_CP042177.1|WP_138847688.1|1816928_1817348_-|Ohr-family-peroxiredoxin
MSKIEKVLYTGKTHTTSGGRDGAARSSDGRLDIQLSSPGSAGTGTNPEQLFAAGWSACFIGAMQLAARAAKVTLPADLAVDTEVDLGMGGNAYFLQARLNVSVPGLDRDVVQHIVATAHQTCPYSKATRGNIDVEIRIV
>NZ_CP042177.1|WP_006755043.1|1825971_1826436_-|Lrp/AsnC-family-transcriptional-regulator
MRPPRLDQLDDLDRQLVALLQADARASVADLARQLDVARTTVVARIARLERTNVIAGYSVRLGQDVLDASIYAYVGIILTPKFGKDVLRRLDRMPEVQLLCAVSGEYDYVAWLRADSPERLNDLLDQIGTLEGVERTTTSIILSRKIDRGTIGG
>NZ_CP042177.1|WP_012363936.1|1826802_1827339_+|Spy/CpxP-family-protein-refolding-chaperone
MKKISLTLAMLAVAAGAFAQTPPQPQTPASAAAASAPSAEQRAARHEARIEQRIKYLHDQLKITSAQESQWKTFADTMRENGETMGHLYRARMENHNVSAVDDMKQYAELAQANADGAKKLADAFAPLYQSFPAEQKALADTTFRSWLHHGGERRGSGKAKKEGKAAAAPAASAPAQP
>NZ_CP042177.1|WP_012363937.1|1827467_1827899_+|hypothetical-protein
MLELKHIDLRTDPQARHVVKDETVTVAFADADGELMSLEGPNRYVAGDALITGSTGDRWVVSRARFDAKYLPADPALAHGTPGAYRNRPAVVLARRMDEPFTIARSENGDTLRGVAGDWVMQYAPGDYGVVQAQRFAQVYRDA
>NZ_CP042177.1|WP_011656931.1|1827947_1828310_-|DUF3022-domain-containing-protein
MDDYLIECQSSEFDALARVICDLFPEQTRFAESSDERGRFLSVHWLAMRFGSTPKRMTLDIRIVPPALARYLALKPMQRARSHAVLHAYTEAMLGSLEERHAAGEAVERDAELELDEDFA
>NZ_CP042177.1|WP_138847683.1|1828322_1829111_-|YhfC-family-intramembrane-metalloprotease
MTVAPVTLAVLIAATLIIALLPFVLFRILRKPLALDRRDTIVGVAVFTLFAMIVERAFHGFVLSQTPAGGWLTQPLAFVAYSAFATAVFEEVGRYLGMRILNRRYGASAGDGRGIGYGIGHAGAEAWFVGVLVWGQWSYLAWLASRGQLETQLADLPGDTVVRLHVMLATLSAQSILLLLLERCAAFVVQLALSVLVWRGVRAGRAGVLPLAIVLHALAVAPALLYQVRVLPAGSLEAVYVVLAAILIAVLVKAGRSPRAAA
>NZ_CP042177.1|WP_012363939.1|1829165_1830209_-|LacI-family-DNA-binding-transcriptional-regulator
MSDSQPSTQRPATISDVAREAGTGKTSVSRYLNGETHVLSADLRQRIETAIARLNYRPNQMARGLKRGRNRLLGMLAADLTNPYTIEVLQGVEAACHALGYMPLICHAANEVEMERRFLQLLTTYRVEGLIVNALGAEEDVLRPLRGAGIPAVLVDRTVEGFEADLIGLDNTDAIEMALAHLVARGFDAIHFVVQPFERVSSRRLREAAFRAALGARGLPVPPTVVLDLNEPAAAAAALADLDARLDDATRRGVRAALFAANAPVALAIARHLRARFGAAWQEKAALLSIDDPEWAELIGITTIRQPTYEIGYKAVEFVHERIDGAAGDVRVAMLPGELIARASTAS
>NZ_CP042177.1|WP_138847682.1|1830531_1831497_-|bifunctional-glyoxylate/hydroxypyruvate-reductase-B
MKPRIVAYKPLPDDVLAYLREHADVVQADGPAALADALGDAHGAIGASLKVTPQMLDRAPKLKAWSTISVGYDNFDVADLTRRGIVLAHTPDVLTESTADTVFSLILASARRVVELAEWVKAGHWHRSIGPDLYGTDVQGKTLGIVGLGRIGGAVARRAVLGFRMQVLYTNRSAHAEAETQYGARRVTLDELLAQSDFVCLQVPLSPETHHLIGAAEFTKMKRGAILINASRGPVVDEAALIDALRVGTIRGAGLDVFEKEPLPADSPLLRMNNVVALPHIGSATHETRHAMARCAAENLVGALAGTLRTNLVNPDALARA
>NZ_CP042177.1|WP_138847681.1|1831502_1832783_-|MFS-transporter
MAANLAVRRWWTIMPIVFITYSLAYLDRANYGFAAAAGINQDLGISKGLSSLIGALFFLGYFFFQIPGAIYAERRSVKKLVFVSLVLWGACAALTGVVADIPSLMVIRFVLGVVEAAVMPAMLIYISNWFTKSERSRANTFLILGNPVTVLWMSIVSGYLVHEFGWRHMFIAEGVPAVIWAVCWWFLVQDKPADSPWLTTQEKRDLDAALAAEQAAIKPVRNYGEAFRSPAVIKLCAQYFCWSIGVYGFVLWLPSIVKNGSELGMVATGWLSALPYLAATIAMLVASWASDKVGSRRGFVWPFLLIGAAAFAASYALGSSHFWISYALLVVAGAAMYAPYGPFFAIVPELLPKNVAGGAMALINSMGALGSFVGSYFVGYLNGATGSPVASYAFMSAALVAAVILTLSVKPQARDAHSLAAPLQGK
>NZ_CP042177.1|WP_138847680.1|1832946_1833939_-|sugar-kinase
MKAALDVVTYGEAMAMFVAAEPCHLAHAAQFTKRIAGADLNVAIGLSRLGFRVGWMSRVGRDSFGTYVLDTLAREGIDASCVTVDPRYPTGFQLKSRNDDGSDPTVEYFRKGSAASHLSCDDYVADYVLAARHLHLTGVAPAISATSCELAFQLAREMRAAGKTISFDPNLRPTLWPSADVMAKTLNALATLADWVLPGLAEGRQLTGHDTPADIAGFYLARGARGVVIKLGPEGAYFRTADGRAGTVAGERVAKVVDTVGAGDGFAVGVVSALLEGRSVEQAVARGNRIGALAIQVIGDSEGLPTRAALDQLENVSNRADRLEETVTAQ
>NZ_CP042177.1|WP_138847679.1|1833967_1834732_-|TIM-barrel-protein
MADIVIVASAFGMDRVRQEGHRAFLATAAASGATGFEVRRELFASDDDATPAALAELGTALSAHGLWSVYSTPATLYTEAGALDADALRDTLVEADALGARFVKFQLGGFAGDAHAAQIVALSRGARARVVVENGQLPIGGALAQFCGLFDALTDAGTPDALGMTFDIGNWQWPGEAPLACAHALAPHVEYIHCKAVAGDGARRFAMAPAPGDPLVTGVLAALPQAVPRGIEFPFDAADLAGDAGRRVAWLAAA

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Crispr_ID: NZ_CP042177_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP042177_4

2426319-2426390

Orphan

Consensus_repeat	Method
CCCATGCAAAGCTGTCGACCGGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP042177_4

>merge|NZ_CP042177|4|2426319-2426390|CRISPRCasFinder
CCCATGCAAAGCTGTCGACCGGAGTTGGCGCTTGAGCACTTACTCCGGGCCCATGCAAAGCTGTCGAGCGGA

>NZ_CP042177|4|4|2426319-2426390|CRISPRCasFinder
CCCATGCAAAGCTGTCGACCGGA	GTTGGCGCTTGAGCACTTACTCCGGG
CCCATGCAAAGCTGTCGAGCGGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP042177.1\|WP_138848473.1\|2421238_2422456_+\|DUF2863-family-protein	unknown	unknown	gnl\|CDD\|371362
NZ_CP042177.1\|WP_012364298.1\|2414782_2415187_-\|Cu(I)-responsive-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133383
NZ_CP042177.1\|WP_006478295.1\|2414420_2414567_-\|DUF3563-domain-containing-protein	unknown	unknown	gnl\|CDD\|288904
NZ_CP042177.1\|WP_138847422.1\|2413077_2413923_+\|23S-rRNA-(adenine(2030)-N(6))-methyltransferase-RlmJ	unknown	unknown	gnl\|CDD\|225509
NZ_CP042177.1\|WP_012364307.1\|2429913_2430705_+\|enoyl-CoA-hydratase	unknown	unknown	gnl\|CDD\|181009
NZ_CP042177.1\|WP_012364302.1\|2424388_2425036_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042177.1\|WP_138847416.1\|2433743_2434940_-\|pimeloyl-CoA-dehydrogenase-large-subunit	unknown	unknown	gnl\|CDD\|132248
NZ_CP042177.1\|WP_138847418.1\|2431621_2432098_-\|MaoC-family-dehydratase	unknown	unknown	gnl\|CDD\|239534
NZ_CP042177.1\|WP_138847421.1\|2427295_2427793_+\|putative-toxin-antitoxin-system-toxin-component,-PIN-family	unknown	unknown	gnl\|CDD\|379205
NZ_CP042177.1\|WP_012364297.1\|2413937_2414273_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042177.1\|WP_138847420.1\|2427824_2428997_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|181642
NZ_CP042177.1\|WP_012364308.1\|2430877_2431570_+\|thiol:disulfide-oxidoreductase	unknown	unknown	gnl\|CDD\|183298
NZ_CP042177.1\|WP_012364301.1\|2423577_2424252_+\|membrane-protein	unknown	unknown	gnl\|CDD\|225775
NZ_CP042177.1\|WP_138847417.1\|2432590_2433724_-\|pimeloyl-CoA-dehydrogenase-small-subunit	unknown	unknown	gnl\|CDD\|132247
NZ_CP042177.1\|WP_138847419.1\|2429045_2429702_-\|glutathione-S-transferase-family-protein	unknown	unknown	gnl\|CDD\|198344
NZ_CP042177.1\|WP_012364300.1\|2422671_2423502_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225107
NZ_CP042177.1\|WP_012364303.1\|2425114_2426269_-\|carboxypeptidase-family-protein	unknown	unknown	gnl\|CDD\|349453
NZ_CP042177.1\|WP_012364310.1\|2432094_2432556_-\|MaoC-family-dehydratase	unknown	unknown	gnl\|CDD\|239538
NZ_CP042177.1\|WP_012364304.1\|2426455_2427238_-\|peroxide-stress-protein-YaaA	unknown	unknown	gnl\|CDD\|234999
NZ_CP042177.1\|WP_012364295.1\|2411994_2412966_+\|NADP-dependent-aryl-alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|381369

Protein	Function_ID	Function_description	E-value
NZ_CP042177.1\|WP_138848473.1\|2421238_2422456_+\|DUF2863-family-protein	gnl\|CDD\|371362	pfam11062, DUF2863, Protein of unknown function (DUF2863). This bacterial family of proteins have no known function.	0
NZ_CP042177.1\|WP_012364298.1\|2414782_2415187_-\|Cu(I)-responsive-transcriptional-regulator	gnl\|CDD\|133383	cd01108, HTH_CueR, Helix-Turn-Helix DNA binding domain of CueR-like transcription regulators. Helix-turn-helix (HTH) transcription regulators CueR and ActP, copper efflux regulators. In Bacillus subtilis, copper induced CueR regulates the copZA operon, preventing copper toxicity. In Rhizobium leguminosarum, ActP controls copper homeostasis; it detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations. These proteins are comprised of two distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain winged HTH motifs that mediate DNA binding, while the C-terminal domains have two conserved cysteines that define a monovalent copper ion binding site. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements.	1.33634e-69
NZ_CP042177.1\|WP_138847422.1\|2413077_2413923_+\|23S-rRNA-(adenine(2030)-N(6))-methyltransferase-RlmJ	gnl\|CDD\|225509	COG2961, ComJ, Protein involved in catabolism of external DNA [General function prediction only].	1.57439e-127
NZ_CP042177.1\|WP_012364307.1\|2429913_2430705_+\|enoyl-CoA-hydratase	gnl\|CDD\|181009	PRK07511, PRK07511, enoyl-CoA hydratase; Provisional.	3.7365e-155
NZ_CP042177.1\|WP_006478295.1\|2414420_2414567_-\|DUF3563-domain-containing-protein	gnl\|CDD\|288904	pfam12086, DUF3563, Protein of unknown function (DUF3563). This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are about 50 amino acids in length. This protein has conserved AYL and DLE sequence motifs.	0.000501132
NZ_CP042177.1\|WP_138847416.1\|2433743_2434940_-\|pimeloyl-CoA-dehydrogenase-large-subunit	gnl\|CDD\|132248	TIGR03204, pimC_large, pimeloyl-CoA dehydrogenase, large subunit. Members of this protein family are the PimC proteins of species such as Rhodopseudomonas palustris and Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Especially relevant is pimeloyl-CoA, basis of the gene symbol, as it is a catabolite of benzoyl-CoA degradation, which occurs in Rhodopseudomonas palustris.	2.29298e-175
NZ_CP042177.1\|WP_138847418.1\|2431621_2432098_-\|MaoC-family-dehydratase	gnl\|CDD\|239534	cd03450, NodN, NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.	1.10824e-70
NZ_CP042177.1\|WP_138847421.1\|2427295_2427793_+\|putative-toxin-antitoxin-system-toxin-component,-PIN-family	gnl\|CDD\|379205	pfam13470, PIN_3, PIN domain. Members of this family of bacterial domains are predicted to be RNases (from similarities to 5'-exonucleases).	3.44575e-26
NZ_CP042177.1\|WP_012364304.1\|2426455_2427238_-\|peroxide-stress-protein-YaaA	gnl\|CDD\|234999	PRK02101, PRK02101, peroxide stress protein YaaA.	9.60735e-143
NZ_CP042177.1\|WP_138847420.1\|2427824_2428997_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|181642	PRK09082, PRK09082, methionine aminotransferase; Validated.	0
NZ_CP042177.1\|WP_012364308.1\|2430877_2431570_+\|thiol:disulfide-oxidoreductase	gnl\|CDD\|183298	PRK11752, PRK11752, putative S-transferase; Provisional.	3.06731e-84
NZ_CP042177.1\|WP_012364301.1\|2423577_2424252_+\|membrane-protein	gnl\|CDD\|225775	COG3235, COG3235, Predicted membrane protein [Function unknown].	2.42257e-17
NZ_CP042177.1\|WP_138847417.1\|2432590_2433724_-\|pimeloyl-CoA-dehydrogenase-small-subunit	gnl\|CDD\|132247	TIGR03203, pimD_small, pimeloyl-CoA dehydrogenase, small subunit. Members of this protein family are the PimD proteins of species such as Rhodopseudomonas palustris, Bradyrhizobium japonicum. The pimFABCDE operon encodes proteins for the metabolism of straight chain dicarboxylates of seven to fourteen carbons. Especially relevant is pimeloyl-CoA, basis of the gene symbol, as it is a catabolite of benzoyl-CoA degradation, which occurs in Rhodopseudomonas palustris.	9.36108e-92
NZ_CP042177.1\|WP_138847419.1\|2429045_2429702_-\|glutathione-S-transferase-family-protein	gnl\|CDD\|198344	cd10424, GST_C_9, C-terminal, alpha helical domain of an unknown subfamily 9 of Glutathione S-transferases. Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 9; composed of uncharacterized proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.	1.30919e-39
NZ_CP042177.1\|WP_012364300.1\|2422671_2423502_+\|response-regulator-transcription-factor	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	3.63275e-34
NZ_CP042177.1\|WP_012364303.1\|2425114_2426269_-\|carboxypeptidase-family-protein	gnl\|CDD\|349453	cd06234, M14_PaCCP-like, Peptidase M14-like domain of ATP/GTP binding proteins and cytosolic carboxypeptidases similar to Pseudomonas aerugnosa CCP (PaCCP). A bacterial subgroup of the Peptidase M14-like domain of Nna-1 (Nervous system Nuclear protein induced by Axotomy), also known as ATP/GTP binding protein (AGTPBP-1) and cytosolic carboxypeptidase (CCP)-like proteins. This subgroup includes PaCCP from Pseudomonas aeruginosa, a carboxypeptidase homologous to M14D subfamily of human CCPs. Structural complexes with well-known inhibitors of metallocarboxypeptidases indicate that PaCCP might only possess C-terminal hydrolase activity against cellular substrates of particular specificity. The Peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Nna1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins (such as alpha-tubulin in eukaryotes) to remove a C-terminal tyrosine. Nna1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain. It has been suggested that this N-terminal domain might act as a folding domain.	7.72586e-152
NZ_CP042177.1\|WP_012364310.1\|2432094_2432556_-\|MaoC-family-dehydratase	gnl\|CDD\|239538	cd03454, YdeM, YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.	3.13463e-68
NZ_CP042177.1\|WP_012364295.1\|2411994_2412966_+\|NADP-dependent-aryl-alcohol-dehydrogenase	gnl\|CDD\|381369	cd19143, AKR_AKR6C1_2, AKR6C family of aldo-keto reductase (AKR). Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.	0

>NZ_CP042177.1|WP_012364303.1|2425114_2426269_-|carboxypeptidase-family-protein
MTLSITSNFDAGAIDVVSCDSPDAIRLRVRGDNRSEFAQWFYYRLTGARGERCVMSFENAAECAYPSGWRNYSAVASYDRVDWFRVPTTFDGKTMTIDHTPEFDSIYYAYFEPYSEERHAAFLGAVQQLPQARVVELGRTVEGRPMSLLTLGTPEVDGAPKKKVWVIARQHPGETMAEWFIEGLVKRLAGWGDWAGDPVARKLYDRATFYIVPNMNPDGSVHGNLRTNAAGANLNREWMEPDAERSPEVLAVRDAIHAIGCDMFFDIHGDEDLPYVFVAGSEMLPSFTEQQRKEQTAFIDAFKVASPDFQTEHGYAASKYKEDALKLASKYIGHQFGCLSLTLEMPFKDNANLPDERVGWNGERSAALGAAMLAAILVHVETFA
>NZ_CP042177.1|WP_012364302.1|2424388_2425036_+|hypothetical-protein
MPHSLLTNNQMDSSPASLRIFRALGKLAACVAGLSLALPAPVLADLLDQRSELINKFVNEMHADPIVADCAAHGSFIASTSSAFDRVDFAPKAFENGNAAITPWNDSFDQGKQRVKVDNIVTVDGLGIHSDGSDPTPLKFRCGYVGQQMLAFSWNDPVPPLKPRVERPSSSTKKFTGKSHRGKVKATSRTGKKAAATKKSSGQKKVVKKKTAKKS
>NZ_CP042177.1|WP_012364301.1|2423577_2424252_+|membrane-protein
MGFLFTPLPLWVGIGGWIGAVALLALALWNRPFVRLQDATLQHVWLALVTAITVLWASNAWLEDGTVMHLLGATLLVTLFDWTLALIAMGAVTGIAAIVFDAPWHGIGLTYLIYGALPVAVSALLQRAVIAWLPHNLTSFITGQGFLSPAIAIVAVAAAAAGVQLALADGVPVVIPAGYLLNTALLALGEAWFTGMATALIAVYRPAWVTTFDVRRYRLGGPRA
>NZ_CP042177.1|WP_012364300.1|2422671_2423502_+|response-regulator-transcription-factor
MRFLVLNSDAERRDGLKALLRQIDRHASINDAPDGFQARRLLRAQRFDLVAINWPDVGRLSELQALCSACSPTPAAVLIDESTPEAIQRFYNYGVAGVIPHSMRPHLIVRALEMVLLGGHYIPPIALSLLPSAAAARHDAHFQTLAGSLPRRPASRLLSPRQAQIMRFVHMGNTNKMIARTLGISEGTVKIHLASIFQQLGAANRAAAVAIYNGWLSPHLEVLLANRERAQKPTIGERGPVPLRMQRKNRPYPLPDANTADLPLAAEPPARFRRER
>NZ_CP042177.1|WP_138848473.1|2421238_2422456_+|DUF2863-family-protein
MRQRIAKRLPPDADKLVGLSLALFASGSRIEDRFWEAKLDALLAKIVRNGNQTTLDAALDHLQQNHPDAYGALADMAETHSESMVIEHDGQPYDALLVAVPVLAWTRYMIPSGPLKGDVADALRTQLQAHVLASGTLVGLAPFLYSIDQLPRHHVETYRLAQQLAHAAIGQHAAKLSFGDLPETSPILADPRFLLAVVAAPAGAPLFRWQEEEHGNRIERGQCLEQWTAQGGPSLSVALPGCEFECLLPDAYYSACRDADERIRPHTVRTAIRYLFDTLGAAPQELRAVVAGFGERRIDEYRVGFTRRASNDVIYGVVWPLYGRENGDVSIDSATLEGEAPMEGPMEEIVSLLKECGVTDVRRHAGRFEPEYCDDCGVPLYADPLGEIVHAEMPEDASPAQPHFH
>NZ_CP042177.1|WP_012364298.1|2414782_2415187_-|Cu(I)-responsive-transcriptional-regulator
MNIGDASRESGVSAKMIRYYEQVGLLAPSKRSEAGYRIYGSDEIHILRFIRQARRLGFLVEDIRKLLMLWQDRSRASAEVKSIALEHVAELDKRIAELSDMRNTLADLAAHCHGDGRPECPILARLADPVGEPD
>NZ_CP042177.1|WP_006478295.1|2414420_2414567_-|DUF3563-domain-containing-protein
MIAYIVEKLSNWFESAERERREAYLATSSDIVQLESRIRSLETNGYSL
>NZ_CP042177.1|WP_012364297.1|2413937_2414273_-|hypothetical-protein
MRLRLDVRHASRARLVLGAAVLVHGIAAGAATSSKPLILDTQRGIQDGQGGLVLQTAPLSSEPIVEPAGMRMPAGQGPNSSVPLFVAPYINVPGWGASRANQPRPAPRLQP
>NZ_CP042177.1|WP_138847422.1|2413077_2413923_+|23S-rRNA-(adenine(2030)-N(6))-methyltransferase-RlmJ
MLSYRHGFHAGNHADVLKHAVVVQLLRYLNKKDKSYWYIDTHAGAGVYSLREGYAAKTGEFDTGIGQLWNDKNLPEALGDYIDEVRALNDDGELHYYPGSPYLAWRAMREQDRMRLFEMHTTEIDVLRHNFRDAGRRAMIYAGDGFEGIKALLPPPPRRALVLIDPSYEDKKDYARTVTCVTECLKRFATGCYAIWYPQVARVESQRFPEQLKRLQPNNWVHLTLTVSNPPADGLGLYGSGMFILNPPYTLAQSMNEALPYLVERLGQDSGARCEIEHRGN
>NZ_CP042177.1|WP_012364295.1|2411994_2412966_+|NADP-dependent-aryl-alcohol-dehydrogenase
MHYRRLGRSGLQISELSLGSWVTYGNQVDQRAARECLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKSLGWPRISYLVSTKFFWGLAEAPNQYHTLNRKYLLNAIDGSLRRLQLDYVDLVYCHRPDPNTPIEETVWAMSDMIVRGKALYWGTSEWSADEIRAAYEIAERHHLHKPVVEQPQYNLFHRTRVEREYARLYDDYGLGLTTWSPLASGLLTGKYRNGVPPGSRAELQGYDWLRDRLTDPTSNDVVERLGGIAAELGCSTAQLAIAWVLANPRVSSVITGASRIEQIGDNMRALDVAAKLTPEVRQRIEEAVGDAYE
>NZ_CP042177.1|WP_012364304.1|2426455_2427238_-|peroxide-stress-protein-YaaA
MIIVLSPAKSLDYDTPAHVPSYTKPAFVDDASELIDGLRKLSPQDIATLMDISDPLARLNFQRYADWSPTFSPANAKQAVLAFNGDVYEGFDAKSLSAADLDYAQQHVRVLSGLYGLLRPLDLLQPYRLEMGTRFANARGKDLYAFWGDRITRALNEQLETRSGAARVLVNCASTEYFKSVKPKLLAAPVVTPVFEDWKGGRYKIISFHAKRARGLMARYIVENRIAEPAALKDFAMEDYVFDAAASNDSTYVYRRRIGE
>NZ_CP042177.1|WP_138847421.1|2427295_2427793_+|putative-toxin-antitoxin-system-toxin-component,-PIN-family
MTRSSAPHAAHRVVLDSNVWIDILVFDDPATRPIRAALERGTLAAVIDGRCLNELELVLDYPQFRERAIDKAEALATVARLTSRVEPLPVDADAPPLPKCKDRDDQKFLELARAAQADWLVSKDRALLKLAKRTARDFGFRIAQPAPFTEACALDAASAIPTTPA
>NZ_CP042177.1|WP_138847420.1|2427824_2428997_+|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MNAPSDMPTNPVFPSRLPNVGTTIFTVMSALAAEKGAVNLGQGFPDFDCDPRIVDAVAAAMRDGHNQYPPMAGVAPLRDAIADKIAQVYGRRYDPATEITVTAGATQALLTAILCAVHPGDEVIVVEPTYDSYLPSIELAGGKPVFVTLEAPDYAIPFDRLAAAITPKTRMIMINTPHNPTGTVWREADMRKLEEIVRGTNVLILSDEVYEHMVYDGARHESVARYPELAERSFIVSSFGKTYHVTGWKIGYVAAPAALMAEFRKVHQFNVFTVNTPTQIGLADYLRDPAPYLTLPDFYQKKRDFFRAGLERTRFKLLPCTGTYFQCVDYSAISDLPEAEFSKWLTSEIGVAAIPVSAFYHEPHESGVVRFCFAKQESTLASALERLARL
>NZ_CP042177.1|WP_138847419.1|2429045_2429702_-|glutathione-S-transferase-family-protein
MLQLCGIPLSNYYNKVKFVLLEHDIPFEEATCTLPVSDPALLADSPLGKIPFLKTEEGALFESQVIIEYLAARYPDKAIFPAGPFAAAKVRELVETLELYLEWTAREVYTEAFFGGKVSDGTKAHVEKRLPRAIDAFKRMTQFSPYVLGDTFGLADIAASVHLPVIGMATKAIFGRDFLLDAGIDWKAHAKLVGERPAAQRVAADRKAYVEATAAARS
>NZ_CP042177.1|WP_012364307.1|2429913_2430705_+|enoyl-CoA-hydratase
MSAELLASRPPESESTLVLTLSNPGARNALHPDMYAAGVEALATAERDPAIRAVVLTGADRFFCAGGNLNRLLENRAKDPSYQADSIDQLGAWITAIRASTKPVIAAVEGAAAGAGFSLALACDLIVAAHDAKFVMSYARVGLTPDGGGSWFLARALPRALAAEILFEGKPVAAERLHALGVVNRLAVPGAALSDALAWADSLAGISPNALTRIKSLLDDAPAQPLETHLGTERDHFVASLHHADAFEGITAFLEKRQPRYKR
>NZ_CP042177.1|WP_012364308.1|2430877_2431570_+|thiol:disulfide-oxidoreductase
MIDVYSWATPNGHKVHIMLEETGLAYRVHPVDIGAGDQFKPEFLKISPNNKIPAIVDADGPGGKPISLFESGAILVYLAEKTGKFLPTDPAGRYATLEWLMFQMGGVGPMLGQAHHFRLYAPEQIEYAVNRYTNEAKRLYNVMEKRLGESEYLAGDTYTIADIATFPWTRSWQNQGIVLDELPNVKRWQEAIAARPAVQRGVEVLASMRKALQDDKAREMLFGATQYAKH
>NZ_CP042177.1|WP_138847418.1|2431621_2432098_-|MaoC-family-dehydratase
MTDVTLPLIASPQALHAQVGAEPLASGWVEIDQRRVDGFADATGDRQWIHVDPERARRESPFGGPIAHGFLTLSLIPALMADAMRFEQKMGVNYGLNRVRFLKPVPVGTRVRALFAVKETAEAARGGVQVTWSVSMQAERPDAPLLVCAAEFITLHYF
>NZ_CP042177.1|WP_012364310.1|2432094_2432556_-|MaoC-family-dehydratase
MGISYEDLEVGSTTEIGRYTFEPDDIKTFAQRYDPQPFHLDEEAGKASPFGGLVASGWHTCSVFMSLLIKKLGPDSTSMGSPGIDSIRWLKPVRAGDTITMLQKIHDKRVSASKPDRGIVSTEWIGINGAGDTVISVHTKVIFGLRHPQGAGA
>NZ_CP042177.1|WP_138847417.1|2432590_2433724_-|pimeloyl-CoA-dehydrogenase-small-subunit
MDFSFTDEQQQFADALRRYLGEQYGFDARQAIVRSDAGVSDAQWSAFAELGLTALPVPEAQGGFGGGPVDMLVAMQELGRALVVEPYWATAVGIEALRLAGSGTGDDAALLEAVALGQKRLAVAFHEPRARYDLYELGTQAREQGGAGRLTGTKSVVQHGAQAHAWIVPARVDGGGIGLFVVERDAAGVKLVDYRTIDGQRAATIELHETPARQLTGGARDAAALEQIADYATFLLCAEAVGALDELNRATVEYTKTREQFGVPIARFQALQHRMVDMLIHAEQARSLTYLAAVRYAGGDADARRKAASAAKARVGTAARFVGQQAVQLHGGMGVTNEVAAAHLFKRLSIIETTLGDTDHHLARITALPDFAQADAA
>NZ_CP042177.1|WP_138847416.1|2433743_2434940_-|pimeloyl-CoA-dehydrogenase-large-subunit
MDLDYSPADDAFRVDVRAWLEANLPHALRAKVLDHKRLDREDFASWHRILGQRGWSAPAWPAEYGGPGWNATQRHIWDEECARIGAPTVLPFGVSMVAPVLMKYGSEAQKRHYLPRILDGTDWWCQGYSEPGSGSDLASLRTRAERHGDYYVVNGQKTWTTLGQYADMMFCLVRTDPAAKKQEGISFLLIDMATPGITVRPIITLDEDHEVNEVFFEDVKVPVENLVGDENRGWTYAKYLLGHERTGIARVGASKRELVFLKRVASHQQKNGKPLLADPVFAAKVAALEVELMALEVTVLRVVSRETSGKGPGPEASMLKIKGTEVQQALTELMFEAIGPLAAPFDVPFLEGKREHSIAGDDDAAPLAAYYFNYRKTSIYGGSNEIQKNIIAQMILGL

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Crispr_ID: NZ_CP042177_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP042177_5

3288973-3289080

Orphan

Consensus_repeat	Method
CTGAACGCGGGCAAGCGCTGACGCGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP042177_5

>merge|NZ_CP042177|5|3288973-3289080|CRISPRCasFinder
CTGAACGCGGGCAAGCGCTGACGCGGAGGCGGCGCGGCTGGCCCCGGATGCCGCGGCGGGCACAGCGCGCACGCAAGGCACCCTGAACGCGGGCAGGCGCTGACGCGG

>NZ_CP042177|5|5|3288973-3289080|CRISPRCasFinder
CTGAACGCGGGCAAGCGCTGACGCGG	AGGCGGCGCGGCTGGCCCCGGATGCCGCGGCGGGCACAGCGCGCACGCAAGGCACC
CTGAACGCGGGCAGGCGCTGACGCGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP042177.1\|WP_012364859.1\|3285690_3286767_-\|porin	unknown	unknown	gnl\|CDD\|238208
NZ_CP042177.1\|WP_138847048.1\|3282297_3283194_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_CP042177.1\|WP_138847042.1\|3295256_3295472_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042177.1\|WP_138847045.1\|3292309_3293590_+\|AGE-family-epimerase/isomerase	unknown	unknown	gnl\|CDD\|225493
NZ_CP042177.1\|WP_138847044.1\|3293586_3294495_+\|carbohydrate-kinase	unknown	unknown	gnl\|CDD\|238572
NZ_CP042177.1\|WP_138847043.1\|3294901_3295096_-\|DUF2905-family-protein	unknown	unknown	gnl\|CDD\|378570
NZ_CP042177.1\|WP_011658110.1\|3297418_3297823_+\|dihydroneopterin-aldolase	unknown	unknown	gnl\|CDD\|214902
NZ_CP042177.1\|WP_006754117.1\|3291293_3292313_+\|LacI-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224525
NZ_CP042177.1\|WP_105834748.1\|3280757_3281660_-\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|273359
NZ_CP042177.1\|WP_006754262.1\|3280307_3280514_+\|DUF1289-domain-containing-protein	unknown	unknown	gnl\|CDD\|377738
NZ_CP042177.1\|WP_138847040.1\|3296596_3297340_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|236389
NZ_CP042177.1\|WP_011658106.1\|3294602_3294824_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042177.1\|WP_138847046.1\|3289277_3291116_+\|EAL-domain-containing-protein	unknown	unknown	gnl\|CDD\|238923
NZ_CP042177.1\|WP_011658093.1\|3278849_3279782_+\|hydroxymethylglutaryl-CoA-lyase	unknown	unknown	gnl\|CDD\|180206
NZ_CP042177.1\|WP_012364860.1\|3287133_3287622_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP042177.1\|WP_138847047.1\|3283473_3284433_+\|nitronate-monooxygenase	unknown	unknown	gnl\|CDD\|224981
NZ_CP042177.1\|WP_138847041.1\|3295392_3296583_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|224481
NZ_CP042177.1\|WP_006754260.1\|3281773_3282265_+\|Lrp/AsnC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224439
NZ_CP042177.1\|WP_011658094.1\|3279804_3280311_+\|YbaK/EbsC-family-protein	unknown	unknown	gnl\|CDD\|239825
NZ_CP042177.1\|WP_012364858.1\|3284556_3285519_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114

Protein	Function_ID	Function_description	E-value
NZ_CP042177.1\|WP_012364859.1\|3285690_3286767_-\|porin	gnl\|CDD\|238208	cd00342, gram_neg_porins, Porins form aqueous channels for the diffusion of small hydrophillic molecules across the outer membrane. Individual 16-strand anti-parallel beta-barrels form a central pore, and trimerizes thru mainly hydrophobic interactions at the interface. Trimers are stabilized by hytrophillic clamping of Loop L2. Loop 3 bends into the pore, creating an elliptical constriction of about 7 x 11A, large enough to allow passage of a glucose molecule without steric hindrance. Removal of the C-terminal residue (usuallly F) destabilizes the trimer and removal of the 16th beta-sheet abolishes trimerization. Unlike typical membrane proteins, porins lack long hydrophobic stretches. Short turns are found at the smooth, periplasmic end, longer irregular loops are found at the rough, extracellular end. C-terminal residue forms salt bridge with N-terminus.	9.90167e-64
NZ_CP042177.1\|WP_138847048.1\|3282297_3283194_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	8.71572e-23
NZ_CP042177.1\|WP_138847040.1\|3296596_3297340_+\|SDR-family-oxidoreductase	gnl\|CDD\|236389	PRK09134, PRK09134, SDR family oxidoreductase.	5.16375e-46
NZ_CP042177.1\|WP_138847045.1\|3292309_3293590_+\|AGE-family-epimerase/isomerase	gnl\|CDD\|225493	COG2942, COG2942, N-acyl-D-glucosamine 2-epimerase [Carbohydrate transport and metabolism].	2.88355e-109
NZ_CP042177.1\|WP_138847044.1\|3293586_3294495_+\|carbohydrate-kinase	gnl\|CDD\|238572	cd01167, bac_FRK, Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.	9.70816e-91
NZ_CP042177.1\|WP_138847043.1\|3294901_3295096_-\|DUF2905-family-protein	gnl\|CDD\|378570	pfam11146, DUF2905, Protein of unknown function (DUF2905). This is a family of bacterial proteins conserved of unknown function.	4.54806e-12
NZ_CP042177.1\|WP_011658110.1\|3297418_3297823_+\|dihydroneopterin-aldolase	gnl\|CDD\|214902	smart00905, FolB, Dihydroneopterin aldolase. Dihydroneopterin aldolase catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate. In the opportunistic pathogen Pneumocystis carinii, dihydroneopterin aldolase function is expressed as the N-terminal portion of the multifunctional folic acid synthesis protein (Fas). This region encompasses two domains, FasA and FasB, which are 27% amino acid identical. FasA and FasB also share significant amino acid sequence similarity with bacterial dihydroneopterin aldolases. This region consists of two tandem sequences each homologous to folB and which form tetramers.	1.77216e-27
NZ_CP042177.1\|WP_006754117.1\|3291293_3292313_+\|LacI-family-transcriptional-regulator	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	4.12527e-78
NZ_CP042177.1\|WP_006754260.1\|3281773_3282265_+\|Lrp/AsnC-family-transcriptional-regulator	gnl\|CDD\|224439	COG1522, Lrp, Transcriptional regulators [Transcription].	8.22481e-33
NZ_CP042177.1\|WP_006754262.1\|3280307_3280514_+\|DUF1289-domain-containing-protein	gnl\|CDD\|377738	pfam06945, DUF1289, Protein of unknown function (DUF1289). This family consists of a number of hypothetical bacterial proteins. The aligned region spans around 56 residues and contains 4 highly conserved cysteine residues towards the N-terminus. The function of this family is unknown. Structural modelling suggests this domain may bind nucleic acids.	9.16639e-16
NZ_CP042177.1\|WP_138847046.1\|3289277_3291116_+\|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.	1.61144e-59
NZ_CP042177.1\|WP_011658093.1\|3278849_3279782_+\|hydroxymethylglutaryl-CoA-lyase	gnl\|CDD\|180206	PRK05692, PRK05692, hydroxymethylglutaryl-CoA lyase; Provisional.	0
NZ_CP042177.1\|WP_138847047.1\|3283473_3284433_+\|nitronate-monooxygenase	gnl\|CDD\|224981	COG2070, COG2070, Dioxygenases related to 2-nitropropane dioxygenase [General function prediction only].	3.90179e-94
NZ_CP042177.1\|WP_138847041.1\|3295392_3296583_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|224481	COG1565, COG1565, Uncharacterized conserved protein [Function unknown].	5.35318e-118
NZ_CP042177.1\|WP_105834748.1\|3280757_3281660_-\|DMT-family-transporter	gnl\|CDD\|273359	TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter. [Transport and binding proteins, Amino acids, peptides and amines].	3.41107e-15
NZ_CP042177.1\|WP_011658094.1\|3279804_3280311_+\|YbaK/EbsC-family-protein	gnl\|CDD\|239825	cd04333, ProX_deacylase, This CD, composed mainly of bacterial single-domain proteins, includes the Thermus thermophilus (Tt) YbaK-like protein, a homolog of the trans-acting Escherichia coli YbaK Cys-tRNA(Pro) deacylase and the Agrobacterium tumefaciens ProX Ala-tRNA(Pro) deacylase and also the cis-acting prolyl-tRNA synthetase-editing domain (ProRS-INS). While ProX and ProRS-INS hydrolyze misacylated Ala-tRNA(Pro), the E. coli YbaK hydrolyzes misacylated Cys-tRNA(Pro). A few CD members are N-terminal, YbaK-ProX-like domains of an uncharacterized protein with a C-terminal, predicted Fe-S protein domain.	4.09956e-59
NZ_CP042177.1\|WP_012364858.1\|3284556_3285519_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	1.52859e-76

>NZ_CP042177.1|WP_012364860.1|3287133_3287622_-|hypothetical-protein
MMTERVKLKVGRWVAGVLGTLLMPFALAQPPHGGHAFGGHGFGGGDMRAYGQSAASAQVWRRALPPGGARAGGVSGYGSRWGLRPTPSYGHYAAQSPYRPISADSRQMPRPPGGGNVPMRAGSIRADVARYNEERGGRPMPPPRSQEEPAAHSPYFSPFYRN
>NZ_CP042177.1|WP_012364859.1|3285690_3286767_-|porin
MKAFARRASRTSVKLIAAATCVAAAAPVHAQSSVSLYGQVDEWVGATKFPGGDRAWNVSGGGMSTSYWGLHGAEDLGNGYKAIFTLESFFRAQNGQFGRFQGDTFFARNAYVGVSSPYGTVTAGRLTTHLFLSTILFNPFYDSYTFSPMVYHVFLGLGTFPTYPSDQGAVGDSGWNNALSYTSPSFGGLNFGAMYALGNTAGDNRSKKWSAQFNYANGPFAATAVYQYVNFNNGPQDLSSLVTGMKSQGIGLVGATYDLKYVKLFGQYMYTKNDQVAGSWHVNTAQGGVSVPLGVGNAMASYAYSRDGGGLDQTRQTWAVGYDYPLSKRTDVYAAYMNDHISGLSSGNTFGAGIRAKF
>NZ_CP042177.1|WP_012364858.1|3284556_3285519_-|LysR-family-transcriptional-regulator
MDTLVSMNVFRYVVEVGSFVGAAERMQMSAAMASKHVMHLEQQLGARLLHRTTRRVAPTEAGREYYERLVQALSELDEAGQAVGAASVVPQGRLRVTSLSAFGLRHVMQAVTDYAGRFPDVVVDMTLSDRVVDLIEEGYDVAVRAAPNGLKSSSLVARQIATAHILLVASPEYLEKHGTPQTIADLAHHNYLRRDSNSTMLDSLVIDAAAASRVNLNGNLIVNHLEGLRAAVLAGAGIALLGTEVVGDDIESGRLVPVLLDSVPPHEAPIYAVYASRRHVSAKVRSFVDFLAARFEGQSLCPSIESHLRVLPITRIKRAG
>NZ_CP042177.1|WP_138847047.1|3283473_3284433_+|nitronate-monooxygenase
MALPAVLQNLTLPVIASPMFIVSYPELVLAQCKAGIVGSFPALNARPAELLDEWLTQIQSELAGHKAKHPDAVIGPIAVNQIVHQSNVRLEHDVRVCVEHKVPIFITSLRAPAREIVDAVHSYGGIVLHDVINLRHAQKALEAGVDGLILVAAGAGGHAGTTSPFALVGEVRRMFDGPIVLSGSIANGGSILAAQAMGADFAYMGTRFIATQEAHAVEDYKHAILNAKSSDIIYTNLFTGVHGNYIRESIEKAGLDPDALPESDKTKMNFGGDKTKAWKDIWGAGQGVGLMDDLPSVGELVERMKREYDDAKARLGIAR
>NZ_CP042177.1|WP_138847048.1|3282297_3283194_-|alpha/beta-fold-hydrolase
MSFDAFASFRVTMQDTDIFGVKGGAGPPLLLLHGHPQTHMIWHRVAATLANHFTVIATDLRGYGASGRPPSDARHAPYSKRAMAADQVAVMRHFGFEQFHVCAHDRGARVAHRLALDHPAAVERMMLLDIAPTLAMYEKTDRAFATAYFHWFFLIQPAPLPETLIEGRTDAYIERVMGNRSAGLAPFAPEALAAYRAALAQPGAVHAMCEDYRASATIDLEHDRADLERGNKVACPLRVLWGERGIVGRCFDPLDEWRRVARDVSGRALACGHYIPEEAPVALVDELLAFFDARDAAA
>NZ_CP042177.1|WP_006754260.1|3281773_3282265_+|Lrp/AsnC-family-transcriptional-regulator
MSKRLSPPAVASLDATDRAILAALAEDARIATSELARQIGLSAPATADRVRRLEAQGVIAGFTVELDPRALGYTLQAIVRVKPLPGQLHLVEEVLRRIPEFVECDKVTGEDCFICRLYLRTIGHLDDILSKVTERAETSTAIVKSTPVPRRLPPLVEDDAARR
>NZ_CP042177.1|WP_105834748.1|3280757_3281660_-|DMT-family-transporter
MASNETRRGAAEMVVAMMMSGTIGWLVMSSQQPLTNVVFFRCLFGAATLAIVCAALGFLRRALFSPRMLALATLGSVAIVANWLLLFAAYSRASISMATAVYNTQPFMLVALGAIVFRERISASTITWLALAFVGLVCVVRVEPAVLAVPGEYLEGVALSLGAAFLYAVSSIVTKHLKGTPPHLLALLQAGLGIVLLAPFAHFGTLPATPAQWLDLVVLGVVNTGVMYVLLYGAIQKLPVAMTGALSFVYPVVAIIVDRVAFGQTLAWTQVLGALLILLAAAGVNLGWRIVPARRASVGN
>NZ_CP042177.1|WP_006754262.1|3280307_3280514_+|DUF1289-domain-containing-protein
MSDVPVVVGTVASPCTDVCRIDPRTDWCAGCLRTRDEIKGWRASDDDARRALLARLDARRRLLARSGA
>NZ_CP042177.1|WP_011658094.1|3279804_3280311_+|YbaK/EbsC-family-protein
MTTPTSFDSLPDSARRVALLLRERGHSKGIVMLAETGKTSAEAAAGLGCSVAQIAKSILFRRESDGLPVLVVASGVNRVDEKKVAAQVGPVGRADAKFVRDHTGYAIGGVCPIGHLVEPVTLIDADLLALDSLWAAAGHPHAVFNLSPQELVSLTGAPVADVALRNDA
>NZ_CP042177.1|WP_011658093.1|3278849_3279782_+|hydroxymethylglutaryl-CoA-lyase
MTFPTAVKIVEVGPRDGLQNEKTFVPTDVKIALVDRLSRAGFRNIEAASFVSPKWVPQMADGADVMAGIERRAGTVYSVLTPNLKGFENALAARADEVVIFGAASEAFSQRNINCSIAESIARFEPVAKAAKDAGVRLRGSVSCTLGCPYQGEVPVASVVDVVERFAALGCDEIDIADTIGVGTPKRTREVLSAVTRVFPRERLSGHFHDTYGQALANIYAALFEGIEIFHASVAGLGGCPYAKGATGNVATEDVLYLMQGLGIDTGIDLAQVVAAGDFISNAIGRANVSRAGRALLAKAQSATDAPSCV
>NZ_CP042177.1|WP_138847046.1|3289277_3291116_+|EAL-domain-containing-protein
MPAPHPDSSVAPTTRLIAERALAAVFQPIVDLGSGTVVGYEGLIRGPRGTDLEPPAALFAQAARDGTTIALEQAAALACLDAFAALGCDGKLFLNFSAGTIVQLVRERERARQLLGRAGVGAERIVIELTEQTAMPDVARIEPAVASLRDAGIQFALDDYGTANASMNLWLRLHPDVVKIDRFFIHDIARDPLKFEAVRAMQHFAHASGAQLIAEGIENASDLIVVRDMGICCVQGFLLGRPNARPSPVVAPAARDAIRTPHIAVFPGATRTARPAGTIAAKMLVPAPALPRDATSNDVLDLFNRMPGLHAVALVERGRPVALVNRRGFIDRFTLPYHREVFGKKPCLQFANDAPLMIDNATSVEQLAMLLASHDQRYLADGFVITEHGRYLGLGTGESLVRAVTEMRIEAARYANPLTFLPGNIPISAHIDRLLERDAGFHACYVDLNQFKPFNDQYGYWQGDEVLKFAATVLAGVCDPQRDFLGHVGGDDFLVLFQRDDWRARATDAIARFNDGAQRFYTQADRLAGGLRGEDRHGNPAFFGFVTMAIGAVGVPAGAHGAMRYGSDEIASVAALAKRRAKQQPGGLAVVDLDAGRAALRERGEPPLAAAG
>NZ_CP042177.1|WP_006754117.1|3291293_3292313_+|LacI-family-transcriptional-regulator
MGTTIRDVARAAEVSIGTVSRALKNQPGLSEATRARIVEIAQRLGYDPAQLRPRIRRLTFLLHRQHNRFPASPFFSHVLHGVEDACRERGIVPTLLTVGPNDDVLRQMRPHAPDAIAVAGFIEPETIEALAATGRPLVLIDLWAPGLRSVNIDNATGAALAMRHLLATGRSRIAFIGGSAAHYSIAQRAIGYRRAFFEAGRLFDPAYEVTIDAGLDPDTGAARAMQQLLDAPGPRPDAVFAYNDAAALAAQRVCIARGVRIPEDIAIVGFDDIPAAAHANPPLTTLAVDKEALGRRGVELLLAEAPERTEISLPVELIVRASSQPAGSPALDTATVTES
>NZ_CP042177.1|WP_138847045.1|3292309_3293590_+|AGE-family-epimerase/isomerase
MNMPPVQSRTATPANHAQAAPFVASFRDPSFLLSHIEDTLRFYATNAFDPTGGFYHYFRDDGSVYNRTSRHLVSSCRFVFNYAMAYRHFGDPRHLEYARHGLRFLRDAHWDDDLQGYDWELDWRDGAKRETLDATRHCYGLAFVLLAAAHATMAGIDEARALIASTFELAEHRFWDAAAGLYADDATPNWHVSSYRGQNANMHMTEALLAAYEATGHVTYLDRAEKLATHVTQRQAALSGGLVWEHYHADWSVDWDYNKEDSSNIFRPWGFQPGHQTEWAKLLLILERHRPLDWLVPRAAELFDAALTHAWDADHGGLCYGFGPDFTICDHNKYFWVQAETFAAAAMLGARTGSERFWDWYDEIWRYSWAHFVDHRYGAWYRILTCDNRKYSDEKSPAGKTDYHTMGACYDVLATLARAARSEPTQ
>NZ_CP042177.1|WP_138847044.1|3293586_3294495_+|carbohydrate-kinase
MSGGTFPAFVSAGDILTDMVRAGDAQWTSVPGGAGWNVARAVARLGVPSALAGAIGEDCFSDVLWRTSDAAGLDLRFLQRVPRAPLLAIVHETRPPAYFFIGDASADLAFDPARLPAGWTEHVRWAHFGCISLVREPLASTLVALAADLHARGVKISFDPNYRNLMTAAYRPTLEKMAGLADLIKVSDEDLRHLFGGDGPDAVDAVRALNPRAAVLVTRGAQAATLYADGDVLEASPPRVEVVDTVGAGDASIGGLLFSLMAAPQRPWREHLAFALAAGAAACRHTGAHAPTLDEVVALLER
>NZ_CP042177.1|WP_011658106.1|3294602_3294824_+|hypothetical-protein
MDTNTFTKGIYTAKAHTQHTANGQYQGYVILARDDGDETENMRYDVHTTSPSEEEAFDEAKALAHRILGEIEL
>NZ_CP042177.1|WP_138847043.1|3294901_3295096_-|DUF2905-family-protein
MLRWLMASFFAVMILTRCWPWLGKLGVGRMPGDVTLTLGGRRYPFPFMSTLVVTLLVSMVARLL
>NZ_CP042177.1|WP_138847042.1|3295256_3295472_+|hypothetical-protein
MPEIARMAASLVACLARPNGAPHSLPYERFRAFACAFHMETGPRPVRARASGRRARMRRACRRSRARRRSP
>NZ_CP042177.1|WP_138847041.1|3295392_3296583_-|class-I-SAM-dependent-methyltransferase
MNPKAHESASLPAPGPDALAQSEMLAAQLRDEIAAAGGWLPFDRFMERALYAPGLGYYSGGARKFGRRADDGSDFVTAPELSPLFAQTLANPVADALAASGTRHVMEFGAGTGKLAAGLLAALDALDVELDEYLIVDLSGELRERQRDTIAATAPALAGKVRWLDALPERFDGVVVGNEVLDAMPVRLFAKSGGAWLERGVTLDARHAFVLGDRPVGAAGLPPVLATLDVDDGYVTETHEAALAFTRTVCTMLARGAVLLVDYGFPAHEYYHPQRDRGTLMCHYRHHAHDDAFLYPGLQDITAHVEFTGIYNAGVGTGADLLGYTSQARFLLNAGITDALAAIDPSDIHQFLPAANAVQKLISEAEMGELFKVIAFSRGIDGTLDAFARGDRSHAL
>NZ_CP042177.1|WP_138847040.1|3296596_3297340_+|SDR-family-oxidoreductase
MTVSADTSTPRIALVAGALDSAADAASLGRALATAFAQRGWDVALQRSAGAPRAAGDALVAEVAARGRRAAVLDADLALEADAGALVAACGAALGRPKCAVFVSACAGTDDAQTVNGAALADALARNVTAPLALARALADATPDAARDDETLRACVIHVLDQALFHPAPARLSHALMQAALNRATAALALALAPKVRVAALVRGHAPHADDIAAAACYLASAPGVTGATLTVDGGEHLVPPAAGPKE
>NZ_CP042177.1|WP_011658110.1|3297418_3297823_+|dihydroneopterin-aldolase
MFSALLHPRLADCRRLYLRDYEVHMKIGAFEHEKRGEQRVVINIDLFVPLALSTPVDDRLHEVVDYDLMKQSVAQCLARGHIHLQETLCDAIAANLLAHDIVRAVRVRTEKPDAYPDCDAVGVEVFRIKDEERA

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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

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

406618 : 448654

Pseudomonas_phage(20.0%)

protease,integrase,transposase,plate

attL 401316:401332|attR 429876:429892

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
401316:401332	attL	NA	NA	NA	NA
WP_012362941.1\|406618_407140_+\|protease	ClpXP protease specificity-enhancing factor	A0A1S5R3H3	Pseudomonas_phage	3.7e-20	48.7
WP_138848339.1\|407409_408627_+\|integrase	tyrosine-type recombinase/integrase	Q7M297	Enterobacteria_phage	3.0e-89	43.0
WP_138848338.1\|409248_412125_-	DUF927 domain-containing protein	A0A1B0VP75	Pseudomonas_phage	8.6e-71	35.6
WP_138848337.1\|412233_412560_-	hypothetical protein	NA	NA	NA	NA
WP_138848336.1\|412569_412917_-	hypothetical protein	NA	NA	NA	NA
WP_004522499.1\|412909_413122_-	hypothetical protein	NA	NA	NA	NA
WP_138848515.1\|413114_413417_-	hypothetical protein	NA	NA	NA	NA
WP_122652590.1\|413409_413586_-	hypothetical protein	NA	NA	NA	NA
WP_138848335.1\|413913_414438_-	hypothetical protein	NA	NA	NA	NA
WP_010111958.1\|414434_414626_-	AlpA family phage regulatory protein	A0A2L0V109	Agrobacterium_phage	4.9e-07	49.1
WP_138848334.1\|415264_416326_-	hypothetical protein	NA	NA	NA	NA
WP_138848333.1\|416327_418244_-	DUF3696 domain-containing protein	Q2P9X8	Enterobacteria_phage	3.4e-15	37.0
WP_138848332.1\|418811_419387_+	helix-turn-helix domain-containing protein	A0A219Y9V9	Aeromonas_phage	9.3e-25	41.2
WP_138848331.1\|419515_420481_+	hypothetical protein	C9E2Q0	Enterococcus_phage	5.7e-11	33.3
WP_138848330.1\|420909_421530_-	hypothetical protein	NA	NA	NA	NA
WP_138848329.1\|422006_423938_+	beta-galactosidase	NA	NA	NA	NA
WP_138848328.1\|424978_425182_+	hypothetical protein	NA	NA	NA	NA
WP_006751250.1\|425264_426065_-	cystine ABC transporter substrate-binding protein	NA	NA	NA	NA
WP_138848327.1\|426377_429551_+	type VI secretion system tip protein VgrG	A0A2H4JCD4	uncultured_Caudovirales_phage	4.6e-57	28.5
WP_138848326.1\|429600_434247_+	sugar-binding protein	A0A2H4JFP5	uncultured_Caudovirales_phage	9.7e-48	51.0
429876:429892	attR	NA	NA	NA	NA
WP_138848325.1\|434234_434678_+	SMI1/KNR4 family protein	NA	NA	NA	NA
WP_138848514.1\|435083_435479_+	hypothetical protein	NA	NA	NA	NA
WP_144594363.1\|435750_435879_+	hypothetical protein	NA	NA	NA	NA
WP_138848324.1\|436048_436432_+	DUF2750 domain-containing protein	NA	NA	NA	NA
WP_138848323.1\|436773_437247_+	hypothetical protein	NA	NA	NA	NA
WP_138848322.1\|437427_437853_+	SMI1/KNR4 family protein	NA	NA	NA	NA
WP_138848513.1\|438033_438225_+	hypothetical protein	NA	NA	NA	NA
WP_138848321.1\|438282_439542_-\|transposase	IS256 family transposase	A0A218MNI5	uncultured_virus	3.9e-44	45.0
WP_138848320.1\|439761_440079_+	hypothetical protein	NA	NA	NA	NA
WP_138847259.1\|440220_441546_+\|transposase	IS4 family transposase	NA	NA	NA	NA
WP_006751242.1\|441612_442395_-	DotU family type IV/VI secretion system protein	NA	NA	NA	NA
WP_012362961.1\|442391_443738_-\|plate	type VI secretion system baseplate subunit TssK	NA	NA	NA	NA
WP_105785629.1\|443842_444451_-	type VI secretion system lipoprotein TssJ	NA	NA	NA	NA
WP_011655822.1\|444827_445466_+	tetratricopeptide repeat protein	NA	NA	NA	NA
WP_006751238.1\|445510_446026_+	type VI secretion system contractile sheath small subunit	NA	NA	NA	NA
WP_006751237.1\|446041_447532_+	type VI secretion system contractile sheath large subunit	NA	NA	NA	NA
WP_006477093.1\|447602_448106_+	type VI secretion system tube protein Hcp	NA	NA	NA	NA
WP_012362963.1\|448168_448654_+\|plate	type VI secretion system baseplate subunit TssE	NA	NA	NA	NA

DBSCAN-SWA_2

842531 : 849713

Enterobacteria_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_012363223.1\|842531_843593_+	dTDP-glucose 4,6-dehydratase	I7HTA3	Enterobacteria_phage	1.7e-85	47.1
WP_138848164.1\|843604_844498_+	glucose-1-phosphate thymidylyltransferase RfbA	A0A291LA53	Escherichia_phage	5.7e-98	59.2
WP_138848163.1\|844482_845034_+	dTDP-4-dehydrorhamnose 3,5-epimerase	I7HJC4	Enterobacteria_phage	4.7e-50	53.6
WP_012363225.1\|845026_845926_+	dTDP-4-dehydrorhamnose reductase	A0A291LA50	Escherichia_phage	2.5e-24	34.7
WP_012363226.1\|846250_847699_+	mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase	A0A1V0SH58	Hokovirus	7.5e-55	28.8
WP_012363227.1\|847698_848493_+	ABC transporter permease	NA	NA	NA	NA
WP_012363228.1\|848492_849713_+	ABC transporter ATP-binding protein	A0A2H4PQG7	Staphylococcus_phage	4.1e-14	27.0

DBSCAN-SWA_3

3408864 : 3442929

Erwinia_phage(25.0%)

protease,plate

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_006760749.1\|3408864_3409401_+\|protease	ATP-dependent protease subunit HslV	NA	NA	NA	NA
WP_138846991.1\|3409411_3410755_+\|protease	ATP-dependent protease ATPase subunit HslU	A0A191ZC11	Erwinia_phage	1.4e-42	29.7
WP_011658200.1\|3410923_3411466_-	response regulator transcription factor	NA	NA	NA	NA
WP_138846990.1\|3411479_3412886_-	HAMP domain-containing histidine kinase	NA	NA	NA	NA
WP_138846989.1\|3413018_3413243_-	hypothetical protein	NA	NA	NA	NA
WP_006754950.1\|3413539_3414439_+	acetylglutamate kinase	NA	NA	NA	NA
WP_012364953.1\|3414435_3415227_+	pyrimidine 5'-nucleotidase	NA	NA	NA	NA
WP_138846988.1\|3415193_3415859_+	nucleoid occlusion factor SlmA	NA	NA	NA	NA
WP_138846987.1\|3415938_3418602_-	type VI secretion system ATPase TssH	A0A2I7SAX5	Vibrio_phage	8.5e-81	33.5
WP_138846986.1\|3419120_3420140_+	TagK domain-containing protein	NA	NA	NA	NA
WP_138846985.1\|3420120_3420981_+	ImpE protein superfamily protein	NA	NA	NA	NA
WP_138846984.1\|3420964_3421486_+\|plate	type VI secretion system baseplate subunit TssE	NA	NA	NA	NA
WP_012364959.1\|3421487_3423368_+\|plate	type VI secretion system baseplate subunit TssF	NA	NA	NA	NA
WP_138846983.1\|3423371_3424433_+\|plate	type VI secretion system baseplate subunit TssG	NA	NA	NA	NA
WP_138846982.1\|3424429_3425488_+	hypothetical protein	NA	NA	NA	NA
WP_138848447.1\|3425529_3426561_+	fimbrial protein	NA	NA	NA	NA
WP_138846981.1\|3426600_3427956_+	hypothetical protein	A0A292GJ55	Xanthomonas_phage	1.0e-106	46.5
WP_138848446.1\|3428069_3431519_-	RHS repeat protein	NA	NA	NA	NA
WP_105785664.1\|3431539_3431806_-	hypothetical protein	NA	NA	NA	NA
WP_144594376.1\|3431890_3434911_-	type VI secretion system tip protein VgrG	A0A077K8Q4	Ralstonia_phage	3.6e-35	26.3
WP_041489873.1\|3435017_3435581_-	hypothetical protein	NA	NA	NA	NA
WP_138846979.1\|3435561_3436347_-	DUF2094 domain-containing protein	NA	NA	NA	NA
WP_138846978.1\|3436355_3440264_-	type VI secretion system membrane subunit TssM	NA	NA	NA	NA
WP_138846977.1\|3440278_3441583_-	type VI secretion system protein TssL	NA	NA	NA	NA
WP_012364971.1\|3441579_3442929_-\|plate	type VI secretion system baseplate subunit TssK	NA	NA	NA	NA

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP042179

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NZ_CP042178

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

3. NZ_CP042177

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection