CRISPRimmunity

Please click to download your results

Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_LN890335	Achromobacter xylosoxidans isolate AX_NCIMB_11015_WG chromosome BN2877	4 crisprs	DinG,DEDDh,WYL,csa3,PD-DExK	0	1	4	0

Results visualization

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Crispr_ID: NZ_LN890335_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN890335_1

32301-32410

Orphan

Consensus_repeat	Method
TTTTTTGCCGCCGGGCCGCCCCAAGGCAAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN890335_1

>merge|NZ_LN890335|1|32301-32410|CRISPRCasFinder
TTTTTTGCCGCCGGGCCGCCCCAAGGCAAAAACGTCCCCTCGGGGGCAGCGACCCGCGCAGCGGCGAGCGTGGGGGCTTTTTTTTGCCGCCGGGCCGCCCCAAGGCAAAA

>NZ_LN890335|1|1|32301-32410|CRISPRCasFinder
TTTTTTGCCGCCGGGCCGCCCCAAGGCAAAA	ACGTCCCCTCGGGGGCAGCGACCCGCGCAGCGGCGAGCGTGGGGGCTT
TTTTTTGCCGCCGGGCCGCCCCAAGGCAAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN890335.1\|WP_155864641.1\|30301_32254_+\|phospholipase-C,-phosphocholine-specific	unknown	unknown	gnl\|CDD\|274561
NZ_LN890335.1\|WP_049055498.1\|35822_37352_-\|amidase	unknown	unknown	gnl\|CDD\|223232
NZ_LN890335.1\|WP_054515370.1\|41745_42666_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|182646
NZ_LN890335.1\|WP_020924404.1\|20158_21058_+\|lipid-A-hydroxylase-LpxO	unknown	unknown	gnl\|CDD\|380241
NZ_LN890335.1\|WP_155864643.1\|37540_38920_-\|DNA-recombination-protein-RmuC	unknown	unknown	gnl\|CDD\|224241
NZ_LN890335.1\|WP_155864640.1\|15446_16538_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340831
NZ_LN890335.1\|WP_049058827.1\|39085_39820_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378479
NZ_LN890335.1\|WP_006384053.1\|39856_40582_-\|DNA-3-methyladenine-glycosylase	unknown	unknown	gnl\|CDD\|234840
NZ_LN890335.1\|WP_006384055.1\|40939_41749_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|182574
NZ_LN890335.1\|WP_006384047.1\|32504_33230_-\|phosphate-signaling-complex-protein-PhoU	unknown	unknown	gnl\|CDD\|182974
NZ_LN890335.1\|WP_049050958.1\|22434_24168_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|227319
NZ_LN890335.1\|WP_006384045.1\|29893_30166_+\|oxidative-damage-protection-protein	unknown	unknown	gnl\|CDD\|180059
NZ_LN890335.1\|WP_006384037.1\|14601_15450_-\|polysaccharide-deacetylase-family-protein	unknown	unknown	gnl\|CDD\|213026
NZ_LN890335.1\|WP_006384039.1\|16537_20029_-\|DNA-polymerase-III-subunit-alpha	unknown	unknown	gnl\|CDD\|235554
NZ_LN890335.1\|WP_020924413.1\|40586_40943_-\|Spx/MgsR-family-RNA-polymerase-binding-regulatory-protein	unknown	unknown	gnl\|CDD\|239333
NZ_LN890335.1\|WP_006384044.1\|28416_29775_+\|amino-acid-N-acetyltransferase	unknown	unknown	gnl\|CDD\|235386
NZ_LN890335.1\|WP_006384041.1\|21130_22426_-\|AAA-associated-domain-containing-protein	unknown	unknown	gnl\|CDD\|224041
NZ_LN890335.1\|WP_053499797.1\|24338_28250_-\|ATP-dependent-RNA-helicase-HrpA	unknown	unknown	gnl\|CDD\|273900
NZ_LN890335.1\|WP_155864642.1\|34103_35768_-\|isovaleryl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|183199
NZ_LN890335.1\|WP_054515367.1\|33386_34067_-\|ribose-5-phosphate-isomerase-RpiA	unknown	unknown	gnl\|CDD\|234816

Protein	Function_ID	Function_description	E-value
NZ_LN890335.1\|WP_155864641.1\|30301_32254_+\|phospholipase-C,-phosphocholine-specific	gnl\|CDD\|274561	TIGR03396, PC_PLC, phospholipase C, phosphocholine-specific, Pseudomonas-type. Members of this protein family are bacterial, phosphatidylcholine-hydrolyzing phospholipase C enzymes, with a characteristic domain architecture as found in hemolytyic (PlcH) and nonhemolytic (PlcN) secreted enzymes of Pseudomonas aeruginosa. PlcH hydrolyzes phosphatidylcholine to diacylglycerol and phosphocholine, but unlike PlcN can also hydrolyze sphingomyelin to ceramide ((N-acylsphingosine)) and phosphocholine. Members of this family share the twin-arginine signal sequence for Sec-independent transport across the plasma membrane. PlcH is secreted as a heterodimer with a small chaperone, PlcR, encoded immediately downstream. [Cellular processes, Pathogenesis].	0
NZ_LN890335.1\|WP_049055498.1\|35822_37352_-\|amidase	gnl\|CDD\|223232	COG0154, GatA, Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit and related amidases [Translation, ribosomal structure and biogenesis].	3.38392e-96
NZ_LN890335.1\|WP_054515370.1\|41745_42666_-\|ABC-transporter-permease-subunit	gnl\|CDD\|182646	PRK10683, PRK10683, putrescine transporter subunit: membrane component of ABC superfamily; Provisional.	4.26265e-128
NZ_LN890335.1\|WP_020924404.1\|20158_21058_+\|lipid-A-hydroxylase-LpxO	gnl\|CDD\|380241	NF033391, lipid_A_LpxO, lipid A hydroxylase LpxO. Members of this family are LpxO, an enzyme that modifies one of the lipid chains in lipid A by hydroxylation, with resulting changes in resistance to the host immune response and to the antibiotic colistin. This family, as built, includes LpxO1 from Pseudomonas aeruginosa, but not its paralog LpxO2.	0
NZ_LN890335.1\|WP_155864643.1\|37540_38920_-\|DNA-recombination-protein-RmuC	gnl\|CDD\|224241	COG1322, COG1322, Predicted nuclease of restriction endonuclease-like fold, RmuC family [General function prediction only].	4.08929e-95
NZ_LN890335.1\|WP_155864640.1\|15446_16538_-\|glycosyltransferase	gnl\|CDD\|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	6.96996e-66
NZ_LN890335.1\|WP_049058827.1\|39085_39820_+\|hypothetical-protein	gnl\|CDD\|378479	pfam10707, YrbL-PhoP_reg, PhoP regulatory network protein YrbL. This is a family of proteins that are activated by PhoP. PhoP protein controls the expression of a large number of genes that mediate adaptation to low Mg2+ environments and/or virulence in several bacterial species. YbrL is proposed to be acting in a loop activity with PhoP and PrmA analogous to the multicomponent loop in Salmonella where the PhoP-dependent PmrD protein activates the regulatory protein PmrA, and the activated PmrA then represses transcription from the PmrD promoter which harbours binding sites for both the PhoP and PmrA proteins. Expression of YrbL is induced in low Mg2+ in a PhoP-dependent fashion and repressed by Fe3+ in a PmrA-dependent manner.	1.13519e-89
NZ_LN890335.1\|WP_006384053.1\|39856_40582_-\|DNA-3-methyladenine-glycosylase	gnl\|CDD\|234840	PRK00802, PRK00802, DNA-3-methyladenine glycosylase.	1.06237e-67
NZ_LN890335.1\|WP_006384055.1\|40939_41749_-\|ABC-transporter-permease-subunit	gnl\|CDD\|182574	PRK10592, PRK10592, putrescine transporter subunit: membrane component of ABC superfamily; Provisional.	1.7753e-105
NZ_LN890335.1\|WP_006384047.1\|32504_33230_-\|phosphate-signaling-complex-protein-PhoU	gnl\|CDD\|182974	PRK11115, PRK11115, phosphate signaling complex protein PhoU.	3.54726e-72
NZ_LN890335.1\|WP_049050958.1\|22434_24168_-\|ABC-transporter-permease-subunit	gnl\|CDD\|227319	COG4986, COG4986, ABC-type anion transport system, duplicated permease component [Inorganic ion transport and metabolism].	4.11939e-173
NZ_LN890335.1\|WP_006384045.1\|29893_30166_+\|oxidative-damage-protection-protein	gnl\|CDD\|180059	PRK05408, PRK05408, oxidative damage protection protein; Provisional.	2.71711e-57
NZ_LN890335.1\|WP_006384037.1\|14601_15450_-\|polysaccharide-deacetylase-family-protein	gnl\|CDD\|213026	cd10969, CE4_Ecf1_like_5s, Putative catalytic NodB homology domain of a hypothetical protein Ecf1 from Escherichia coli and similar proteins. This family contains a hypothetical protein Ecf1 from Escherichia coli and its prokaryotic homologs. Although their biochemical properties remain to be determined, members in this family contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.	8.68408e-88
NZ_LN890335.1\|WP_006384039.1\|16537_20029_-\|DNA-polymerase-III-subunit-alpha	gnl\|CDD\|235554	PRK05673, dnaE, DNA polymerase III subunit alpha; Validated.	0
NZ_LN890335.1\|WP_020924413.1\|40586_40943_-\|Spx/MgsR-family-RNA-polymerase-binding-regulatory-protein	gnl\|CDD\|239333	cd03035, ArsC_Yffb, Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein encoded by the yffb gene, related to the thioredoxin-fold arsenic reductases, ArsC. The structure of Yffb and the conservation of the catalytic cysteine suggest that it is likely to function as a glutathione (GSH)-dependent thiol reductase. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from GSH via glutaredoxin, through a single catalytic cysteine.	3.49548e-47
NZ_LN890335.1\|WP_006384044.1\|28416_29775_+\|amino-acid-N-acetyltransferase	gnl\|CDD\|235386	PRK05279, PRK05279, N-acetylglutamate synthase; Validated.	0
NZ_LN890335.1\|WP_006384041.1\|21130_22426_-\|AAA-associated-domain-containing-protein	gnl\|CDD\|224041	COG1116, TauB, ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism].	3.19271e-110
NZ_LN890335.1\|WP_053499797.1\|24338_28250_-\|ATP-dependent-RNA-helicase-HrpA	gnl\|CDD\|273900	TIGR01967, ATP-dependent_RNA_helicase_HrpA, RNA helicase HrpA. This model represents HrpA, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria and a few high-GC Gram-positive bacteria. HrpA is about 1300 amino acids long, while its paralog HrpB, also uncharacterized, is about 800 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. The HrpA/B homolog from Borrelia is 500 amino acids shorter but appears to be derived from HrpA rather than HrpB. [Unknown function, Enzymes of unknown specificity].	0
NZ_LN890335.1\|WP_155864642.1\|34103_35768_-\|isovaleryl-CoA-dehydrogenase	gnl\|CDD\|183199	PRK11561, PRK11561, isovaleryl CoA dehydrogenase; Provisional.	0
NZ_LN890335.1\|WP_054515367.1\|33386_34067_-\|ribose-5-phosphate-isomerase-RpiA	gnl\|CDD\|234816	PRK00702, PRK00702, ribose-5-phosphate isomerase RpiA.	7.9383e-116

>NZ_LN890335.1|WP_155864641.1|30301_32254_+|phospholipase-C,-phosphocholine-specific
MKEDPSSASSSDLPPAIRRALAVAPDRKHGTLHDVRHVVILMQENRSFDHYFGSLPGVRGFADPHPVPTPAGDVLTQADGAERVRPYALQGEYASDTPVGYITPHTWDDAQRAWNDGRMDQWLAAKRRLGMGAYRSAEVPFQTALANAFTLCDAYHCSVQAGTNPNRLFLWTGTNDPLGRAGGPALVNTFDRLGPADQGYGWTTYPERLQAAGIDWRIYQDMADNFHDNPLAGFRQYRRQHEAGGADAPLRDRGLSTHTLDDLAHDVEQNTLPQVSWIIAPAADSEHPEVSSPRQGGAYTERVLEILTRNPAVWSGCVFLVTYDENDCFFDHMPPPAPPARETDGRSGGLSTVELDGEYHDTRHGPSAATPDDPAALHGRGFGMGPRVPMLVVSPWSRGGWVNSQVFDHTSVIRFLEARFGVAEPNISAWRRAVAGDLTSAFDFAGDRATLHADSARHTCALPYALEAVGRMTADGEHYRLTFRNPGTAGAVLHVYDRRALERAPRRYTVGAGARLDDGWRLDAEGAYDLWLLGPDGFHRRFRGDTRDAGLLETQLVPVTSGIRLRLINHGDTHLPVQIESRMGDGWRAMAHVQAGGALELKYAGCEGWYDLDVSAQGLPAFGRRLAGRINAGKSGVPDPRLCQGAELPL
>NZ_LN890335.1|WP_006384045.1|29893_30166_+|oxidative-damage-protection-protein
MARTVNCVKLKREAEGLDFPPYPGELGTRIWQSISKEAWEEWKQVQTRLVNENRLNLADARARKYLQQQMERFLFEDGSVEAQGYVPPSA
>NZ_LN890335.1|WP_006384044.1|28416_29775_+|amino-acid-N-acetyltransferase
MPDLEPDTVSALEAPEFAPAQFVRWFRDVAPYVHAFRGKTFVVAFGGELVQAGALNALVQDLSLLSSLGIRLVLVHGSRPQVNEQLRLKGFTQQFDRGLAPTDAAALECAKEAAGEIRLDIEAAFSQGLPNTPMSHAHIRVISGNFVTARPTGVLDGVDYKHTGQVRKIDVDALKFAIEKGSSVVLLSPLGFSPTGDAFNLAMEDLATSVAVALRAEKLIFLSSGQGVLNDDGSVDTELARVDADALLAGGSLDEETGAYLQYASLAVKRGVARAHLVPFALDGSVLLEIFTHDGVGTMVVEDTLDDLRPATLDDVGAILSLIEPLEADGTLVPRPRSVIERDVENFTVLEHDGVIYGCATLHNFPEDHMAEMACLIVHPEWQGSGEGEILLRHMESRARASGAKRLFVLTTRTSHWFMKRGFVQGGIADLPREKQNNYNRSRNSLVFIKKL
>NZ_LN890335.1|WP_053499797.1|24338_28250_-|ATP-dependent-RNA-helicase-HrpA
MPADGPTRGPRKPRADAAAPAARQAPRPERPIPAVTYPEDLPVSARRQEIARAIAGHQVVIVSGETGSGKTTQLPKICLELGRGRQKMIGHTQPRRLAATSVAKRIAEELNTPMGEVVGYQVRFNDRTGPNASIKLMTDGILLAESQRDPLLRRYDTIIIDEAHERSLNIDFLLGYLKQLLPRRPDLKVIITSATIDAERFARHFAASEDKPAPVIEVSGRLYPVEVRYRPVREEAAEDEAAPARPGRDRERMSGDEERDLIDAIVDAVDECARHGPGDVLVFLPGEREIRESAEALRKRHPAGTEVLPLYARLSQAEQEQIFHPRGNARRIVLATNVAETSLTVPGIRFVVDSGLARVKRYSWRNKVEQLRIEPVSRASANQRAGRCGRVGPGVCIRLYDEADFNARAAFTDPEVLRSSLASVILRMKSLKLDDIEQFPFVEAPPGRAVADGYHLLQELGAIELAAADDGDDASRTGASFVLTQTGHELAKLPVDPRIGRMILAAREHQCLAEMLIIASALSVQDARDRPMQEREAAEAAHAKFADDKSEFISFLKLWRWYGEQVQHKASQRKLVGLLRQNFLSPIRLREWHDVHTQLAALVGEQGWRVNQLEATYEQLHMALLSGLLGNIGFKSDEGGHYQGAREIRFHIHPGSRLVKKAGRWIVAAELVETTRLYARCVARIDPVWLEKVGAHLIRKNWSDPRWEKKAGQVVANERATLYGLTIYSGRRIQYGRVHPREARELFIRQALVPGEIDTRLAFVAHNRKLIAGIEKLEHQTRRPDILVDDELIYAFYDRQLPADISQTATLEKWVNGLDKAEAAKLLLTRDELMRHEAAGVTTDVFPKKVEWQGVSMALDYHFEPGSPRDGVTLAVPLFALNQIDPARCEWLVPGMLKEKVHLLLKSLPQKLRRHCVPLPDYAAGFYDRWFERLGDPQTGLVDALIADMWDQVQVRPAAADFKLETLPAHLFMNFRVVDEHGRMLAAGRNLAQLRAEFGKQAQATFQQLAASDTQVAQALAHENLTAWTFGPLPEIMEIKRRGQSVIGYPALVDRGAHCDLDVFDDPDEARKAHRAGLLKLFRLGLREQVKFLEKNLADLTKISMLYMTLGTQEELRDQIIDCALGQACLAEPWPVNEQQFEARRAEGKGRLGLLAQEVARLAGTILTEYAALQRKLPQAKPHAAAYADLQQQLGALMPKWFIRDTPYPQLSHFPRYLKAAVARIDKLRADPGRDAKLVAEMAPLVTQYQRARSALKGAPDPRLDEFRWLLEELRVALFAQELRTPMPVSVKRLMKSWESLQR
>NZ_LN890335.1|WP_049050958.1|22434_24168_-|ABC-transporter-permease-subunit
MFELFSTRTRPSASSRSSPNRWDWALLPLVLGVLAAMAYGASQMSRPFAVGEELPISLDPIYLPYYLLRTILRMFTALAFSLLFSFVFAAIAAKFRTAEKAMIPMLDILQSVPILGFQAIAIAPFIALFPGNLLGVECAAIFAIFTSQAWNMAFSLYQSMRTVPAELNEAARVFRLSGWQRFWRLELPYATPGLLWNMMMSMSGGWFFLVAAEAISVAGQDIKLPGIGSYIAVAIDAENGRAIAWAIGAMMAGILLYDQLFFRPLLAWADKFRFEESQADVAQQSWLLDWTRRSRWMQALSNMFWARMRRALGWFSVPYDGTSIRARAKAPDPRWTRIWDSLLAAAALLATYKLVVFVHQEVGWSEVLHVVGLGGITLARVMVLIGLASLIWVPIAVWIGLRPRYSQRVQAVAQFLAAFPVNLLFPAVVFVMVAFKLNPNIWLSPLIIFGTQWYILFNVVAGASTIPNELRLAAGNLGLKGWLLWRRVYLPAVFPSFITGAITASGGSWNASIVAEYVSWGNTSLVADGLGSYIKQMTEQGDFHRIALGIGVMSIFVMLLNRFFWRKLYLLAEDRGR
>NZ_LN890335.1|WP_006384041.1|21130_22426_-|AAA-associated-domain-containing-protein
MPSNFLIELHDVGKSFRAADGTARHVLEHVDFTLREGEIVALLGKSGSGKSTLLRIMAGLVNADQGTVTYRGQPVYGPAAGIAMVFQSFALFPWLTAQQNVELGLEAQGVAPAERARRADAVLDLMGLGGFGGALPRELSGGMRQRVGIARALVMNPDVLLMDEAFSALDVLTGETLRDDMLELWDESRISTKGILIVSHNIEEAVMMADRIIVFSSDPGRIRSQVQIGLPRPRNADSPQVRALIDEVYALMTQRPAHDMPTPRQQGLGYRFPHTEVERMEGVLDVLAEAPFNGRADLPKLAEEAEISDDDLLPACEALGLFGLAQIDKGDIYLTPLGQRYVQADQDQKQAIFGRQLLAHVPLAAHIRHSLEQEPAGELPERNFLDSLEEFLKPDEAERVLKIAVEWGRYGEIYGYDYHTGLLSLPERAAG
>NZ_LN890335.1|WP_020924404.1|20158_21058_+|lipid-A-hydroxylase-LpxO
MKWLIPGIWLAAILFAHFRGRVKLPLGRQLLDHSVLLAPVNAFMVLTSRVPSTPYLTTSEIAELKVLDDNWETIRDEALQMAELRRIKAADSHNDIGFNSFFKYGWKRFYLKWYDARHPSAEELCPKTVAILKTLPKVKAAMFAELPPGGKLNAHRDPFAGSLRYHLGLTTPNDDRCHIIVDGESYSWRDGESVVFDETYVHEAYNHTDQNRIILFCDVERPLKWGWAEAFNRWFGRVVMSAASSPNDGGDQTGAINKLTHAHWVIDQKRKAFKAWNRNVYKATKYGLIILVIAGFIAL
>NZ_LN890335.1|WP_006384039.1|16537_20029_-|DNA-polymerase-III-subunit-alpha
MSEAVTTPSPFVHLRVHSEFSVVDGIVRIPDLIKRVAKLGQPAVALTDLSNLFGLIKFYKGARGAGIKPIAGCDVWLSNDDDPAKPFRVLLLVRNHQGYLNLCELLSRAFLTNQGKGRAEIRREWLQGQDGLIVLSGGRGGDVGQALDAGNAVSALALARQWAHMFPGSYYIELQRAGMDGDEAYTQAAMRLAAEAGLPVVATHPVQFLDEYEFQAHEARVCIAEGEILANPRRVRRFSKEQYLLSSEEMARRFADVPSALANTVEIAKRCNLSLVLGKPRLPNFPTPDGVSLDDYLVQLSEEGLEKRMAFLFPDEAERASKREQYYERLRWECKTIIQMGFPGYFLIVQDFINWGKNNGVPVGPGRGSGAGSLVAYALGITDLDPIRYDLLFERFLNPERVSMPDFDIDFCQDNRERVIDYVKEKYGRAAVSQIATFGTLGAKAVVRDAGRVLDMPYMFCDGLSKLIPFNPMDPWTLERTLKDEPAFKDRYEQEEEVRALVDLAKPLEGLTRNIGMHAGGVLIAPGKLTDFCPLYCQPGQENSAVSQFDKDDVEAAGLVKFDFLGLRNLTILDWAVRYVRQFNEDKRDFDVMALSLDDPAAYKILCDANTTAVFQLESRGMKELLKKLRPNTFEDIIAMLALYRPGPLESGMVDDFVNRKHGRAAVDYFHNDLESTLKSTYGVIVYQEQVMLISQIIGGYSLGGADLLRRAMGKKKPEEMAKHRELFEKGAKEKGHDPDLAVKLFDLMEKFAGYGFNKSHSAAYALISYQTAWLKAYHPTEFLAATMSSDMDDTDKVQIFCRDAQDNGVEVLPPDVNFSGYRFEPVADKHTEKGKPPRTMRYGLGAVKGTGQGAVEDILRARKEGGPFQNLFDFCRRVSKHAVNRRTIEALIKAGAFDTIEPNRAAMLASVPTAMEAAEQAARSANQSSLFGDDSSDVVAGELAKVAPWDLHKKLTEEKSALGYYYSGHLFDAWRDEVRQIVPMQLARVEPQRDLQWMCGVLASVRVMMTRRGKMVFAVLDDGTAQVEISVFNELYEKHRNRLREDQLVIVQGKVSNDDYSGGMRIVAEQLYDLQLAREARAKSLRVKLNGGADAARLRQMLNPFRAEPENGIPGVPVDIVYTKNNFLCTVRLGEEWRVRMADTLLENLNAWTKPNGVEVTY
>NZ_LN890335.1|WP_155864640.1|15446_16538_-|glycosyltransferase
MRIVHSEAATSFGGQEGRIFKEMNAMRARGHHLEAICQPTALLAERLSDAGFTVHTLEMDGPVNYVKGVIAIRRILREGRFDVLNTHSRRDTVIAAAAGRLAGTPLIVRTRHLSNKVGSLWSYTRLPHRVTTVSDHVREHLIERGVPADHVATVYSPIVLPPPVEHSTLREELGLAADDVVVGCVAVMRATKGHKDLIDAIAPLMAARPKLHLVFVGGGSPVFEQTQAYVAERGLADRIHLMGMRRDVPNLLAGCDLFALATQQEASGTVYVEAQASGLPVIGTDVGGVSEMFRDGETGILVPPKDPAALTAALERLVDDAALRHRMGEAGRKMVWEEGVFSPARLAETTETVYTRWLAERRG
>NZ_LN890335.1|WP_006384037.1|14601_15450_-|polysaccharide-deacetylase-family-protein
MNAPNVPVLMYHHVTPAGGMIAATPEVFEAQIARLARAGYQSLSTDQFAAYLAGAPAPERSVLITFDDGYLNNWVHAHPVLARHGMRAVLFTITGWIGDGPARPHAGQGLPLPATPDHDACKKLIAAGRGDEAMLRWSEIEAMRAAGTFEFHSHTHTHTRWDKVCGADTEAKRAHIARELSDSRETLIQRLGQASDHLCWPQGYFDADYVAAARQAGFRHLYTTDPFGQNTPGADPGHIYRFAVRNQGGTWLNRRLWLSRDPFWGPRYHAWKAWKKRLRNRG
>NZ_LN890335.1|WP_006384047.1|32504_33230_-|phosphate-signaling-complex-protein-PhoU
MTEHTNKQFDADLESVRSQFLQMGGVVEAMIQEAIDALASGDLTLVEKVREREKEVNRHEVEIDESISRILARHQPTAIDLRMLMAVSKMLTDMERSGDEAEKVATVARRIHESEVRHIPVIELRHMAANVRTMLHQALDAFARLDPILAAAVVRSDKEVDKEWKGALRHLITYMIEDPRTISRAIDMIFIARALERIGDHAKNMSERVIYMVKGADVRHTGVKNTERLARGEEDTPGQDD
>NZ_LN890335.1|WP_054515367.1|33386_34067_-|ribose-5-phosphate-isomerase-RpiA
MLSQQELKQQAADAALELVEQVAGPDVIIGVGTGSTADLFIDGLARFKGRIGGTVASSERSAARLAGHGLKVLDLNDVTSMPIYVDGADEIDANLHMIKGGGGAQTREKIVASVADRFVCIVDESKLVEVMGKFPLPIEVIPMARESVARAMTAMGGQPRLREGFVTDNGNIILDVAGLSITDAPGLEARINNLPGVVTCGLFAIAGADVALLATQNGIRRLDRRA
>NZ_LN890335.1|WP_155864642.1|34103_35768_-|isovaleryl-CoA-dehydrogenase
MPSFVTHTVLNQVPPLEDYSLFETDPALREAAVREGAGAWLGDLGAHGAWLGRAQTLAAGVDANRYPPRLQAYDRTGHRIDHVDFHPAWQLLMSGIVARGLHSRAWAQPVPGAQVARAAAYLMQGQVEAGTLCPTTMTFAAVPLLQREPAGVIDYTGDWLPALYSREFDGADAPLAGKRGALIGMGLTEKQGGSDLRAVTTRAAPLGAIGRGCAYSLVGHKWFFSVPQADAHLVLAQTDEGLGCFLVPRWIPEGPRNAVRIRRLKDKLGNHSNASAEVEFEDAWGVMVGEPGRGLAVLLEMAATTRLDCVLGSAALLRQALVQSLHHACHRQAFGKPLLAQPLMRNVLGDLALESEAAQALALRLARAVDERGDAGARALARVGTPAAKLWVCKRAIAAVAECMEAWGGNGYVEEGPMPRLYRETPVNSIWEGSGNVMALDVLRALQREPEALPALEGEFAPALGQYREFDAALARWRALLADPAQAEFQARRIACGLACLWQAALLIRHAPGPVAQGFVGSRLAGVGGVFGELAGGLDVGTILARAWPAAAAC
>NZ_LN890335.1|WP_049055498.1|35822_37352_-|amidase
MGTADRVDSSSFDAMALGAEIAQGATTAQAAMQQAVERVAARNPSINAACGVQAELGLELARALDDELATLTAEQRLALLRERPFLGVPTLLKDLGTAALGLPSAMGSVLYGQVEWNVDAEIVKRYRRAGLIPFGRSTSAELGLSPTSESPVYGAPTQNPWKAGHSAGGSSGGAGAALASGMVRIAHGSDGGGSIRIPASCCGVLGLKPSRGMMPLGPLKGEGWGGLATEHMMTLSVRDCAAALDISAGADVGAPYAAPARPGESYRDIVARVSADPRSSPRRRIAYINTTYEGEAIHPEVAAAVDEAARLFAGLGHELVVAAPPVGSEEVLSPMLPLIASAAANAIDSFVGARNRRLAADELQPTTLGAREYARAISGAQYVACVDTCHEITRRIGRFLHREGTQGHDLFLSPVLAQLPAPIGRYAMDNADYLAYRLGKKGVIGYSPFAPLANLTGMPAISIPFGLSADGLPIGIQVMGPLGSEAWLLELAAQVEALRPWQRVAPIAR
>NZ_LN890335.1|WP_155864643.1|37540_38920_-|DNA-recombination-protein-RmuC
MSNEVLLWVAAGGAVLACLAALMAWLSRPARDDRLDALLDGLERTERALRADIAEGQRGLRAEFSESTRGLRQELAQSHGELRAALTRDAQAARVESAESLARFAAGFNEQLQGLIQINERRLMEVRETVDQRLQALQNDNSAKLDDMRRTVDEKLHATLEQRLGESFKQVSDRLEAVHKGLGEMQALAAGVGDLKRVLTNVKSRGTWGEVQLARLIEDNMTPEQYASNIKPVPGSDAVVEFAIRLPGRGDGGMPVWLPIDAKFPKEEYERLMDAQEAADAEGVKAAGAALAKAVELQARLIATKYVAPPHTTDFAIMFLPTESLYAEVLRRPGLLDRLHDLRINVAGPSNLAALLNSLQMGFRTLAIEQRSSEVWQVLRAVKTEFGKFGDALAGVKKTLDTASSKIGQTEVRTRAMLRNLKSVEALPEAEALRLLGAEGAADETAAEGDAPAAPASGA
>NZ_LN890335.1|WP_049058827.1|39085_39820_+|hypothetical-protein
MNTADFPTYCPPPVAFESIFGPLNLNDETPVAVGGDRHIFQHPHAPSLLVKVMDMQARAIYLEARPFKRWYKQYQRESAYRVYLNEITEYVTTTTRPSGVWQVPMARILGVAQTTLGLGLLVEKITDEAGNIAPTLADLAPQGTMDAALSAQLDEFIEDLADAHVVLHDLTASNIACGQNAEGRSGLFLIDGFGVLPLVPIYAWSKRINRRRIQRKYAEMRAGMAERARKAAQQAGTGGSGPQG
>NZ_LN890335.1|WP_006384053.1|39856_40582_-|DNA-3-methyladenine-glycosylase
MAGKADKASRGAGKALPDAFFNRDARQLARELLGKVVRHRVDGLWLSARIIETEAYYLEEKGSHASLGYTHKRRALFMDGGVVYMYYARGGDSLNFSAGGPGNAVLIKSGYPWVDALSGPEALARMQALNPDAQGRPRLPARLCAGQTLLCRALGLKVPDWDARRFDPDALYVEDVGESPQALISTARLGIPPGRDEHLEYRYVDPAYAAWCTRNPLRRGQVAGRDYHWVDRQGAPLKQAP
>NZ_LN890335.1|WP_020924413.1|40586_40943_-|Spx/MgsR-family-RNA-polymerase-binding-regulatory-protein
MKQTTLYGLTKCSTCVKAREWLTAHGVDHQFIDYRDHPVPAATLKEWAGQLGGWEKLVNRASMTWRNLPDDRKTASTDAQWTRLIAEFPALVRRPVAVTPDGEVGVGFSEKRYGERFA
>NZ_LN890335.1|WP_006384055.1|40939_41749_-|ABC-transporter-permease-subunit
MNGPNKTLRAVVLGLGYFFLYVPIISLMVFSFNESPAVTSWTGFSFRWYHSLFNDDALLRAAWLSFRIAAMTATAAVIIGTWAGYVLGRMGRFRGFALYVGMLSAPLVIPEVVLGISLLLMFVELRGHLGWPAENGIFTIWVGHVTLCMAFVAVVIQTRIRDLDRSLEEAALDLGATPITVFFKITLPLIAPALASAWLLSFTLSLDDVVLASFLSGPSSSTLPMEVFSRVRLGLKPEINALATLFILAVGTCVILANRMQWRKESEPK
>NZ_LN890335.1|WP_054515370.1|41745_42666_-|ABC-transporter-permease-subunit
MSRFSPRDWLPSGRALAVVPPFAWLVLFLLVPFLLVFKISFAELKFGIPPYTSLAEFKDEAVQFSLHLRGYILLFTDSLYFATYLSSVKIAAITTLACVLIGYPIAYYIARSSPRVRNLLLLGVILPFWTSLLLRVYAWVGILRNDGLLNNFLQWLGIISSPLEIYRTDLAVYIGMVYAYLPFFILPLYATLVKMDLRLLEAAYDLGARPWQAFWQITVPLSRQGVIAGAMLVFIPAVGEYVIPEMLGGANTLMMGRVMWNEFFNNTDWPMASAVTCVMVLLLLVPLALFQYNQVKQQELANGGRK

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NZ_LN890335_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN890335_2

3003513-3003589

Orphan

Consensus_repeat	Method
CCGACGGTGGCCTGGCGGCCGAA	CRISPRCasFinder

1 spacers

csa3,WYL

The CRISPR arrays of NZ_LN890335_2

>merge|NZ_LN890335|2|3003513-3003589|CRISPRCasFinder
CCGACGGTGGCCTGGCGGCCGAATTCGATCGTGCCCCAGGCGTCGCTGGCCAGTCCGATGGTGGCCTGGCGGCCGAA

>NZ_LN890335|2|2|3003513-3003589|CRISPRCasFinder
CCGACGGTGGCCTGGCGGCCGAA	TTCGATCGTGCCCCAGGCGTCGCTGGCCAGT
CCGATGGTGGCCTGGCGGCCGAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN890335.1\|WP_020926507.1\|2996398_2996764_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN890335.1\|WP_155866564.1\|3005620_3006406_-\|SURF1-family-protein	unknown	unknown	gnl\|CDD\|225883
NZ_LN890335.1\|WP_049050728.1\|2996783_2997788_-\|YafY-family-transcriptional-regulator	WYL	COG2378_WYL_CAS-I:CAS-III	gnl\|CDD\|225253
NZ_LN890335.1\|WP_155865482.1\|3012172_3013189_-\|transporter-substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|270410
NZ_LN890335.1\|WP_006387364.1\|3004147_3005329_-\|porin	unknown	unknown	gnl\|CDD\|238208
NZ_LN890335.1\|WP_006384571.1\|2995778_2996222_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN890335.1\|WP_155865483.1\|3013233_3014562_-\|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|99735
NZ_LN890335.1\|WP_020926523.1\|3014721_3015621_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|182228
NZ_LN890335.1\|WP_035183054.1\|2993846_2994497_-\|response-regulator	unknown	unknown	gnl\|CDD\|182771
NZ_LN890335.1\|WP_006387357.1\|2997904_2998513_+\|glutathione-S-transferase-family-protein	unknown	unknown	gnl\|CDD\|223698
NZ_LN890335.1\|WP_155865481.1\|3000728_3001895_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340878
NZ_LN890335.1\|WP_026384122.1\|2999991_3000690_+\|metalloregulator-ArsR/SmtB-family-transcription-factor	csa3	COG0640_csa3_CAS-I-A	gnl\|CDD\|238089
NZ_LN890335.1\|WP_020926512.1\|3001985_3002774_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_LN890335.1\|WP_155865480.1\|2994920_2995718_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN890335.1\|WP_054515905.1\|3007439_3009443_-\|cytochrome-o-ubiquinol-oxidase-subunit-I	unknown	unknown	gnl\|CDD\|131890
NZ_LN890335.1\|WP_035183065.1\|3009514_3010558_-\|ubiquinol-oxidase-subunit-II	unknown	unknown	gnl\|CDD\|182518
NZ_LN890335.1\|WP_045953003.1\|3010782_3012117_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340927
NZ_LN890335.1\|WP_006387367.1\|3006805_3007447_-\|cytochrome-o-ubiquinol-oxidase-subunit-III	unknown	unknown	gnl\|CDD\|131889
NZ_LN890335.1\|WP_006387366.1\|3006410_3006809_-\|cytochrome-o-ubiquinol-oxidase-subunit-IV	unknown	unknown	gnl\|CDD\|225667
NZ_LN890335.1\|WP_110059760.1\|2998526_2999852_-\|chromosome-partitioning-protein-ParB	unknown	unknown	gnl\|CDD\|319249

Protein	Function_ID	Function_description	E-value
NZ_LN890335.1\|WP_049050728.1\|2996783_2997788_-\|YafY-family-transcriptional-regulator	gnl\|CDD\|225253	COG2378, COG2378, Predicted transcriptional regulator [Transcription].	1.11987e-49
NZ_LN890335.1\|WP_155865482.1\|3012172_3013189_-\|transporter-substrate-binding-domain-containing-protein	gnl\|CDD\|270410	cd13692, PBP2_BztA, Substrate bindng domain of ABC glutamate/glutamine/aspartate/asparagine transporter; the type 2 periplasmic binding protein fold. BztA is the periplamic-binding protein component of ABC transporter specific for carboxylic amino acids, glutamine and asparagine. The BZtA domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	4.56551e-120
NZ_LN890335.1\|WP_006387364.1\|3004147_3005329_-\|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.	1.57721e-66
NZ_LN890335.1\|WP_026384122.1\|2999991_3000690_+\|metalloregulator-ArsR/SmtB-family-transcription-factor	gnl\|CDD\|238089	cd00158, RHOD, Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.	1.21657e-21
NZ_LN890335.1\|WP_155865483.1\|3013233_3014562_-\|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|99735	cd00610, OAT_like, Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.	4.29771e-133
NZ_LN890335.1\|WP_035183054.1\|2993846_2994497_-\|response-regulator	gnl\|CDD\|182771	PRK10840, PRK10840, transcriptional regulator RcsB; Provisional.	1.49026e-51
NZ_LN890335.1\|WP_006387357.1\|2997904_2998513_+\|glutathione-S-transferase-family-protein	gnl\|CDD\|223698	COG0625, Gst, Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones].	5.89798e-36
NZ_LN890335.1\|WP_155865481.1\|3000728_3001895_-\|MFS-transporter	gnl\|CDD\|340878	cd17320, MFS_MdfA_MDR_like, Multidrug transporter MdfA and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This family is composed of bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as MdfA (also called chloramphenicol resistance pump Cmr), EmrD, MdtM, MdtL, bicyclomycin resistance protein (also called sulfonamide resistance protein), and the uncharacterized inner membrane transport protein YdhC. EmrD is a proton-dependent secondary transporter, first identified as an efflux pump for uncouplers of oxidative phosphorylation. It expels a range of drug molecules and amphipathic compounds across the inner membrane of E. coli. Similarly, MdfA is a secondary multidrug transporter that exports a broad spectrum of structurally and electrically dissimilar toxic compounds. These MDR transporters are drug/H+ antiporters (DHA) belonging 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.	4.13949e-68
NZ_LN890335.1\|WP_155866564.1\|3005620_3006406_-\|SURF1-family-protein	gnl\|CDD\|225883	COG3346, COG3346, Uncharacterized conserved protein [Function unknown].	3.50385e-77
NZ_LN890335.1\|WP_020926512.1\|3001985_3002774_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	1.30167e-25
NZ_LN890335.1\|WP_020926523.1\|3014721_3015621_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|182228	PRK10082, PRK10082, hypochlorite stress DNA-binding transcriptional regulator HypT.	9.9853e-28
NZ_LN890335.1\|WP_054515905.1\|3007439_3009443_-\|cytochrome-o-ubiquinol-oxidase-subunit-I	gnl\|CDD\|131890	TIGR02843, Cytochrome_bo3_ubiquinol_oxidase_subunit_1, cytochrome o ubiquinol oxidase, subunit I. Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport].	0
NZ_LN890335.1\|WP_035183065.1\|3009514_3010558_-\|ubiquinol-oxidase-subunit-II	gnl\|CDD\|182518	PRK10525, PRK10525, cytochrome o ubiquinol oxidase subunit II; Provisional.	2.35645e-130
NZ_LN890335.1\|WP_045953003.1\|3010782_3012117_+\|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.	2.9501e-86
NZ_LN890335.1\|WP_006387367.1\|3006805_3007447_-\|cytochrome-o-ubiquinol-oxidase-subunit-III	gnl\|CDD\|131889	TIGR02842, Cytochrome_bo3_ubiquinol_oxidase_subunit_3, cytochrome o ubiquinol oxidase, subunit III. Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport].	2.12702e-105
NZ_LN890335.1\|WP_006387366.1\|3006410_3006809_-\|cytochrome-o-ubiquinol-oxidase-subunit-IV	gnl\|CDD\|225667	COG3125, CyoD, Heme/copper-type cytochrome/quinol oxidase, subunit 4 [Energy production and conversion].	1.88727e-38
NZ_LN890335.1\|WP_110059760.1\|2998526_2999852_-\|chromosome-partitioning-protein-ParB	gnl\|CDD\|319249	cd16390, ParB_N_Srx_like, uncharacterized family distantly related to the N-terminal domain of the ParB/Srx superfamily. Uncharacterized proteins distantly related to the N-terminal domain of the ParB superfamily, primarily involved in bacterial and plasmid parABS-related partitioning systems. A small minority of proteins in this family include a C-terminal inorganic pyrophosphatase domain. Also within the ParB superfamily is sulfiredoxin (Srx), which is a reactivator of oxidatively inactivated 2-cys peroxiredoxins. Other families includes a putative regulator in the biosynthetic gene cluster and a family containing a Pyrococcus furiosus nuclease and putative transcriptional regulators SbnI (Staphylococcus aureus siderophore biosynthetic gene cluster ) and EdeB (Brevibacillus brevis antimicrobial peptide edeine biosynthetic cluster). Nuclease activity has also been reported in Arabidopsis Srx.	2.90274e-59

>NZ_LN890335.1|WP_020926512.1|3001985_3002774_+|helix-turn-helix-transcriptional-regulator
MPIYTLPAVEDPDLVACPIVGMAIDTREHASDWHAHQRTQLLYQAEGGVTLYLADRVGQLAPLQAAWLPAGCVHRTAMQGSFAYRSLYFDVRAYPNLPREPAILDVNPLLRELIVRVTQWPSDAALDAPRQRLVGALLDELAAAPTAPLHLPMPRDRRLAPIARELLENPACPLSIDEWGRRVGASGRTLARVFLAETGLSFTRWRAQCRLLMARARLAEGASVTEVAHAVGYASDSAFIAMYRRAYGEPPGRRLRRRDPPP
>NZ_LN890335.1|WP_155865481.1|3000728_3001895_-|MFS-transporter
MSSPSSSSGARALPPPWLVIALLALPQVAETILAPALPDLARHWRLDAAATQPVMGIFFVGFAAGVLLWGHLADTRGRRPAMLAGLALGLAGTLCALAAPAYPWLLAGRFLQALGLAACSVVTQTVLRDCLDGPRLTHYFVTLGTVLAWSPAVGPLTGQALADGHGYGGVLAAIAVVVALLLGSVAWRWRETRPAPTAAVPLAALARRMLADGALRLAVQRVAGLNLLVFSFYAAGPFMTGSLPGLGFGWVGLGVALAGSLGAACNRRLPATASAAIRVRHGLRCVALGAAAQALAMAWRPQPGWLWAAAALPVFIGYGLAIPNLLGPALRRYGHCLGRAGALFGLAYYSLLGLGLAATSWLPFDTPLPLSAAWLAVALWLLAARERD
>NZ_LN890335.1|WP_026384122.1|2999991_3000690_+|metalloregulator-ArsR/SmtB-family-transcription-factor
MTAPSVQPPLAAELAELARTLGNAHRLILLEHIAQGERPVERLAELSGLSVANASQHLQQLRRAGFVVTRREGKHVYYRLGSAPIAGLLNALDAVAQHNRGEMRRLVADSQDRRDGLEAISRDELLSRLGEGSMTLLDVRPADEFAQGHLPGAINIPADELLKRLEELPADHEIVAYCRGPFCVLSSDAVTALRAHGLRARRLDAGFPDWRAEGLAVEAPPARKGRRRPQTP
>NZ_LN890335.1|WP_110059760.1|2998526_2999852_-|chromosome-partitioning-protein-ParB
MSRMPSSDLLRPFTARWRPALRTLALAALPLLLAACNGGGDDDDDEATSPPVAQNPAPPADTRNQAYLAAKAGDVIQVRIEELRPTQAAIGYDQIYYKLGRWQGDFNRATWAADPVKQLDYLNRTVGKKFSDYCEDMGATTSQAFTSIAQLRAARLDQPATFSCTAAMGADPANLKTVVVGWDGNLYLTDGHHTFSSLREIADGGPKLPVWVKVDANYSGVGTAAAFWQRMVDERKAWLRDGQNQPITVDQLPTRLGIANAQEAGGMQEDRYRSLVYFTRDIAYSNGNLPEFAEFLWGDWLRRQVAGGQLPGLDQYAMMAPSTPAQILTVSTLNASLASTGANDGYAAAVRNAALKMSALADSDIVFQDRTAASLGRIQLVAGAPSGSPTKKARDTLEELPRNDVKTDASPEGSPRGAGKLWFAVNYRACGKPAAGTCWGW
>NZ_LN890335.1|WP_006387357.1|2997904_2998513_+|glutathione-S-transferase-family-protein
MSIVFYWHPQSSASPIAAALAELQVPHERVKVDIRAGEQRRPEFLAINPNGKVPTLTVDGAPLFEALAIQLWLGEHWGVERGLWPAAGTPQRLAAMSWCAWSYVSYGAVLWRLFHLGHGDEGQRDPRQAERALADLDSLLAVLEGHLARQPWMLGAEYSLADLVVGSVIGYSAMLGAPIAAHPKVQAWLGKVQARPAMQVDR
>NZ_LN890335.1|WP_049050728.1|2996783_2997788_-|YafY-family-transcriptional-regulator
MLASSNRLLRLLSLLQTRRHWAGGELAQTLEIHPRTLRRDIDRLRELGYPIQASSGVAGGYAFRAGNALPPLLLDDDEALTVAITLRTAATGSVGGAEEAALRALVKLEQVMPARLRHKVDALRTALVPVPRAGPLIDASQLAVLAAACRDQLRVHFDYTDGRGQATSRQVEPQGLAHTGYRWYLVAWDPARADWRTFRLDRIAGPVTPGAHFAPRPPPDGGDLRAYVARSVGQAANGEEARIVLHATRAAMTARIPAAVGEIDALDDDRCLLRCPGQSLDALAYWLMALEVEFDVLAPAALALRLRSAAERVARMLQRRETAPGSVPDGPAGG
>NZ_LN890335.1|WP_020926507.1|2996398_2996764_+|hypothetical-protein
MIAVNASNAANRAGFRTSDAASGDAFRAAFTDAQQRGASALAGGVKGAAPVASAAEREFMDYASMSLQEKMFYAALASLGISKAEYDAMSAADKLKVAEKVSLVLQQLAKAEQARQVEHAG
>NZ_LN890335.1|WP_006384571.1|2995778_2996222_-|hypothetical-protein
MSLDTNPTSLPSASVAPPADVFLQFLVNLVNNGGQLKSIGVTLQMGGMLVSGSIVSGAEYFDRFAETFSDSLSDMDTQARQSVRTSLAELGDVFRLPQPAEPLPNYIHLVDALFFTADGTPIAGQPTLWRGRSSAVDGFILGRLQSE
>NZ_LN890335.1|WP_155865480.1|2994920_2995718_+|hypothetical-protein
MRDAARRWPPREESLFLRFQPVFTAQGQVHEYAVADSITPLRSGSPGLMAQRARLRAAVAFAAGLPAPLDLSFEHALTVPDGTDVARRLCADLDISVSRDHICLGPAAGNTPLQLATRRLTFSVPLFRRLLPQAHVLACHTEFRASLRARLLPASCGGKPVASGVMRVTGLTLRIPRGLGADRALQRRFDTLMECATTAKLQVTIDGIEDMHDFVWLRPRPGLLFRGTVLSAPISAQCLDVWLQADGDAWRSFHACTAQSSWTER
>NZ_LN890335.1|WP_035183054.1|2993846_2994497_-|response-regulator
MQRLRIVIADDHPLVLMGMTDLLNKDLSFDVVATLASPTALVEHMKRDLPQVVITDYSMPGDEIYGDGIRLVKYLIRHFPGARIVVLTMVSNPMIISALYDAGVEAVVFKRDDLGEIVTALHALQLGRKYYPPGFQREGSLAARHKFIGERINSLSPKEFEVLRHFIRGESMMQVADSLKRSVKTVSGQKISAMRKLNVQTDQELVAFCVESGMFQ
>NZ_LN890335.1|WP_006387364.1|3004147_3005329_-|porin
MKKTLLAAAILTTFAGVAQAETSVTLYGIIDTGIGYNKVSGTVPVIDQATGKTQAVDVSGSRIGMINGVQAGSRWGLKGSEDLGDGLRAMFTVESGFDSGDGQSQQNRLFNRQATVGLANDAWGSVEFGRQTTVGGTFLAEIDPFYTSFTQANIGTSFSAANTMRWDNMIMYRSPWTDGFQFALGYSFNVDTTDKNQSGFRTADNARGITAGLRYVNGPLNVSLTYDQINSSNQARVLDADGEQLVSGGKPVEFDHDATPRQYAVAASYDLEVVKLAAAYGRTTDGWFVSQDLPNVKLGSYHYANGFKANSYMLGATIPLGGASNLFGSWQHVSPSNALLTGDDAKMNIWSVGYTYDLSKRTSLYAYGSYGKNYAFIDGLKSTAGGVGVRHLF
>NZ_LN890335.1|WP_155866564.1|3005620_3006406_-|SURF1-family-protein
MAATKDSTHSGDTPRNPRSATTLAVLGVVAVALFAGLCALGTWQVHRLAWKQNLIAQVEQRAHAPATPAPARADWPGLTADNAEYRRVSASGAYQYDKQTLVQAATELGSGYWVMTPLQLADGGGTVLVNRGFVLPEWRKRQAGGQADAGPVKVDGLLRMGEPGNGFLRNNDPAANLWYSRDLPAIASARGLGEVAPYFIDADAAPGAGRDPTQAPVGGLTTLTFPNNHLVYAITWYALAAMIVLGAGIVAREERRLRARR
>NZ_LN890335.1|WP_006387366.1|3006410_3006809_-|cytochrome-o-ubiquinol-oxidase-subunit-IV
MNAHADHAGHGHDHGHHDDDDGAAHGTLKSYVTGFVLAAILTAIPFWLVMDRVFASSRTTALVILAFAVVQIVVHIIYFLHMDTKSESGWNMLALIFTLVLVVITLSGSIWIMYHLNSNMMPMSVHDMRNMP
>NZ_LN890335.1|WP_006387367.1|3006805_3007447_-|cytochrome-o-ubiquinol-oxidase-subunit-III
MSDTLAPTLPGGSAPPAEPVFHVAGEHHPKNGTLLGFWVYLMSDCLIFACLFATYGVLGRNYAAGPSGADLFDLPLVAVNTSLLLLSSITYGFAMLEMRRNRVGATQGWLAVTGLLGLGFLSLELYEFAHLIHQGAGPQRSAFLSSFFTLVGTHGLHVTFGIVWLVTMMVQVRMHGLIPENRRRLMCLSMFWHFLDLIWVGVFTFVYLMGVLP
>NZ_LN890335.1|WP_054515905.1|3007439_3009443_-|cytochrome-o-ubiquinol-oxidase-subunit-I
MTDQPDLTKLIFGRLTWDAIPFHEPILLATFAMVAIGGIALLGAITYYRKWGYLWHEWFTSIDHKKIGIMYMILGLVMLLRGFADAIMMRLQQAVAFGDSTGYLPPHHYDQIFTAHGVIMIFFVAMPLVTGLMNYVVPLQIGARDVAFPFLNNFSFWMTTGGVVLVMMSLFVGEFARTGWLAYPPLSGIAHSPDVGVDYYIWALQIAGVGTLLSGVNLLVTIVKMRAPGMSLMRMPIFTWTALCTNVLIVAAFPVLTAVLALLSMDRYVGTNFFTADFGGNAMMYVNLIWIWGHPEVYILILPAFGIFSEVVATFCRKRLFGYASMVYATVVITVLSYLVWLHHFFTMGSGASVNSFFGITTMIISIPTGAKIFNWLFTMYRGRIRFEVPMLWTLGFMVTFVIGGMTGVLLAVPPADFALHNSLFLIAHFHNVIIGGVLFGLMAGITYWFPKAFGYKLDPFWGKCSFWFWLVGFYFAFMPLYVLGLMGVTRRVNHFEDMSLQIWFQVAAFGAFLIAIGIACFLIQLVVSYRRRESLRDFSGDPWDGRTLEWSTSSPPPNYNFAFTPRIHDQDAWWQMKQHGYQRPQAGFIPIHMPKNTWAGIVLAAISVVMGFALIWHMWPLAVLSFAALIIVSIVHTFNYKREYYVPADEVVRTEDARTHLLAKHV
>NZ_LN890335.1|WP_035183065.1|3009514_3010558_-|ubiquinol-oxidase-subunit-II
MPSFPRLRGLLLFAALPLLSGCNAVLLSPSGDIALQQRNLIIISTGLMLLIIVPVIFLTFLFAWRYRASNRDAHYDPDWNHSTMLELLIWAAPLLIIIALGALTWVSTHQLDPYRPLARLSEGREVPPGTKPLVVEVVALDWKWLFLYPEQGVAAVNEMAAPVDRPIQFKITSSTVMNSFFIPALAGQIYAMPGMQTTLHAVINHPGEYEGLSANYSGAGFSGMRFRFHGLDQQGFDKWIADARASGATLGRDTYLKLEQPSERNPVQRYASVAPGLFDAIVNRCVEPNRMCMKDAMAIDAGGGMGIPGARNIASLDEATRERLGLADAPVRKYVGAMCTSAAELAL
>NZ_LN890335.1|WP_045953003.1|3010782_3012117_+|MFS-transporter
MATTTQYPGHASPLPSPGAAGATGSHAKVAPGEIAVGVVIGRASEYFDFFVFGIACVLVFPRVFFPFEPQLEGTLWAFVIFSFAFIARPIGTAVSMAIQRRWGRGTKLTIALFLLGTATVGMAFLPGYDVIGAHAIVLLAVFRCLQGLAFGGSWDGLPSLLALNAPPKRRGWYAMLGQLGAPIGFMIASALFLFLHVTLTEADFIEWGWRYPFFVAFAINVVALFARLRLVVTEEYTQLMEEGELEPISTGQMVREQGYNLFLGAFAALASYALFHLVTVFPLSWIAVSATQQIPDVLIVQIIGAGLGILGTIASGWIADRIGRRTTLGLLAALIGVFALFTPWLLGGSPKAQDAFILIGFALLGLSYGQASGTVTANFSKRFRYTGAALTTDMAWLVGAAFAPLVALGLSARFGLVAVSIYLLSGTACTLLALRINKALETRD
>NZ_LN890335.1|WP_155865482.1|3012172_3013189_-|transporter-substrate-binding-domain-containing-protein
MPIFRTAAGALALATVTGLAHAGPTLDTVKKRGYVQCGVSTGIQGFSSPDSKGNWQGLDVDMCRAIAATVFNDASKFRLTPLTTQARFTALQSGEVDVLTRNVTPTMARDTTLGLISTGVNYYDSQGVMVSARLGVRKLKELDGATICVQPGTVTELDLADWFRANGLKFKPVVIDKYDEIVRAFSAGRCDAFTSDKSQLAASRTTLEHPDNYVILDENIAKSPLGPMVRQGDDNWFNVVRWTLNAMLEAEEFGVTSANVDSQLKSTNPNVQRILGVTPGMGKNLGLDDKWAYNIVKQVGNYGESYERNLGMASAMKLPRGLNAQWRDGGQMYGWPVR
>NZ_LN890335.1|WP_155865483.1|3013233_3014562_-|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme
MDQTLRAAAREYLIRYGGDTFPNLFKSAKGTVVRDDTGREILDFTSGQMCATIGHNHPAIVDAVRRAGETAFHFFSGMIPESVAQLAATMARDWMPTGMTKSIFVNTGSESNEIALRMAKMHKSGFEILAVGGSWHGVTSGAGSVSYASDRKGYGVPPAGVFVMPEPNSYRPYIAGLDAEQSALACLEIGLKMFDMASAGRPAAIIVEPVISAGGVLVPPKSYMQALRRAADARGMLLIFDEAQTAFGRLGCRTGSEHFGVTPDIISVSKTLGGGLPLAATITTPAIEQDVHEKGFTFYTSHVSDPLPATVGLAVLETLQREQLLERSRRQGDYLRRGLLELQQRHEAIGDVRGLGLLLGVELVQDRDTREPYHALGALTTQRCFELGLSMNIRRRPERGSVWRIAPPLTVSNDEIDRAIAILDQALTESLDQIAKPRALSA
>NZ_LN890335.1|WP_020926523.1|3014721_3015621_+|LysR-family-transcriptional-regulator
MDTRWLQDFITLSELRNFTRAAEARNLSQAAFSRRIQSLENWAGARLIDRSAFPTQLTEAGERFRVAAIELVNQLVEARAGIAAVPARNQLRLATSYALATTHLPGWWRDWSAGQQLSCSLQTGNVHDTVSAFTSGAADLLICFHQVAQPLPLDLSRYDCLTLGRELIRPYAARGLVEREGLDLPGTMDRPVPLLMYSPSVYFARLIDAAIESGPEPLHGVRLFEAEMSDVLGDMAAQGLGVAWLADSALRRLGAADLAPLANRAWDIEVSILAFKDRSDARAAVEAVWRRMAAGAQPA

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NZ_LN890335_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN890335_3

3691203-3691317

Orphan

Consensus_repeat	Method
GGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN890335_3

>merge|NZ_LN890335|3|3691203-3691317|CRISPRCasFinder
GGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGGGCCTTTTTTTGCCGCCGGGCCGCCCCAAGGCAAAAACGCCCCCTCGGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGG

>NZ_LN890335|3|3|3691203-3691317|CRISPRCasFinder
GGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGG	GCCTTTTTTTGCCGCCGGGCCGCCCCAAGGCAAAAACGCCCCCTC
GGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN890335.1\|WP_054518358.1\|3691700_3693248_+\|YifB-family-Mg-chelatase-like-AAA-ATPase	unknown	unknown	gnl\|CDD\|223679
NZ_LN890335.1\|WP_024068407.1\|3690641_3691076_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237030
NZ_LN890335.1\|WP_026385253.1\|3684678_3685656_+\|glutathione-synthase	unknown	unknown	gnl\|CDD\|235371
NZ_LN890335.1\|WP_155865631.1\|3697803_3698142_+\|integration-host-factor-subunit-alpha	unknown	unknown	gnl\|CDD\|178961
NZ_LN890335.1\|WP_006387989.1\|3681990_3683943_+\|threonine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234752
NZ_LN890335.1\|WP_006387999.1\|3694346_3695369_+\|phenylalanine--tRNA-ligase-subunit-alpha	unknown	unknown	gnl\|CDD\|234780
NZ_LN890335.1\|WP_006387995.1\|3688490_3689729_-\|ammonium-transporter	unknown	unknown	gnl\|CDD\|182630
NZ_LN890335.1\|WP_076410237.1\|3683963_3684515_+\|translation-initiation-factor-IF-3	unknown	unknown	gnl\|CDD\|234582
NZ_LN890335.1\|WP_006387992.1\|3685673_3686075_+\|PTS-mannose-transporter-subunit-IIA	unknown	unknown	gnl\|CDD\|225446
NZ_LN890335.1\|WP_006388000.1\|3695382_3697800_+\|phenylalanine--tRNA-ligase-subunit-beta	unknown	unknown	gnl\|CDD\|234804
NZ_LN890335.1\|WP_006218735.1\|3689760_3690099_-\|P-II-family-nitrogen-regulator	unknown	unknown	gnl\|CDD\|366157
NZ_LN890335.1\|WP_006387988.1\|3680733_3681648_+\|dTDP-4-dehydrorhamnose-reductase	unknown	unknown	gnl\|CDD\|367904
NZ_LN890335.1\|WP_162531794.1\|3699771_3699939_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LN890335.1\|WP_006387993.1\|3686185_3686455_+\|HPr-family-phosphocarrier-protein	unknown	unknown	gnl\|CDD\|376329
NZ_LN890335.1\|WP_026385254.1\|3686579_3688274_+\|phosphoenolpyruvate--protein-phosphotransferase	unknown	unknown	gnl\|CDD\|224006
NZ_LN890335.1\|WP_006387997.1\|3693694_3693892_+\|50S-ribosomal-protein-L35	unknown	unknown	gnl\|CDD\|234676
NZ_LN890335.1\|WP_054444174.1\|3698199_3698631_+\|MerR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133393
NZ_LN890335.1\|WP_131727054.1\|3699335_3699650_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LN890335.1\|WP_006387998.1\|3693909_3694269_+\|50S-ribosomal-protein-L20	unknown	unknown	gnl\|CDD\|179959
NZ_LN890335.1\|WP_006384618.1\|3691363_3691615_+\|accessory-factor-UbiK-family-protein	unknown	unknown	gnl\|CDD\|377337

Protein	Function_ID	Function_description	E-value
NZ_LN890335.1\|WP_054518358.1\|3691700_3693248_+\|YifB-family-Mg-chelatase-like-AAA-ATPase	gnl\|CDD\|223679	COG0606, COG0606, Predicted ATPase with chaperone activity [Posttranslational modification, protein turnover, chaperones].	0
NZ_LN890335.1\|WP_024068407.1\|3690641_3691076_+\|hypothetical-protein	gnl\|CDD\|237030	PRK12270, kgd, multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit.	6.44042e-06
NZ_LN890335.1\|WP_026385253.1\|3684678_3685656_+\|glutathione-synthase	gnl\|CDD\|235371	PRK05246, PRK05246, glutathione synthetase; Provisional.	0
NZ_LN890335.1\|WP_155865631.1\|3697803_3698142_+\|integration-host-factor-subunit-alpha	gnl\|CDD\|178961	PRK00285, ihfA, integration host factor subunit alpha; Reviewed.	7.11993e-63
NZ_LN890335.1\|WP_006387989.1\|3681990_3683943_+\|threonine--tRNA-ligase	gnl\|CDD\|234752	PRK00413, thrS, threonyl-tRNA synthetase; Reviewed.	0
NZ_LN890335.1\|WP_006387999.1\|3694346_3695369_+\|phenylalanine--tRNA-ligase-subunit-alpha	gnl\|CDD\|234780	PRK00488, pheS, phenylalanyl-tRNA synthetase subunit alpha; Validated.	0
NZ_LN890335.1\|WP_006387995.1\|3688490_3689729_-\|ammonium-transporter	gnl\|CDD\|182630	PRK10666, PRK10666, ammonium transporter AmtB.	0
NZ_LN890335.1\|WP_076410237.1\|3683963_3684515_+\|translation-initiation-factor-IF-3	gnl\|CDD\|234582	PRK00028, infC, translation initiation factor IF-3; Reviewed.	6.16089e-98
NZ_LN890335.1\|WP_006387992.1\|3685673_3686075_+\|PTS-mannose-transporter-subunit-IIA	gnl\|CDD\|225446	COG2893, ManX, Phosphotransferase system, mannose/fructose-specific component IIA [Carbohydrate transport and metabolism].	5.57584e-23
NZ_LN890335.1\|WP_006388000.1\|3695382_3697800_+\|phenylalanine--tRNA-ligase-subunit-beta	gnl\|CDD\|234804	PRK00629, pheT, phenylalanyl-tRNA synthetase subunit beta; Reviewed.	0
NZ_LN890335.1\|WP_006218735.1\|3689760_3690099_-\|P-II-family-nitrogen-regulator	gnl\|CDD\|366157	pfam00543, P-II, Nitrogen regulatory protein P-II. P-II modulates the activity of glutamine synthetase.	1.56881e-56
NZ_LN890335.1\|WP_006387988.1\|3680733_3681648_+\|dTDP-4-dehydrorhamnose-reductase	gnl\|CDD\|367904	pfam04321, RmlD_sub_bind, RmlD substrate binding domain. L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.	1.2411e-113
NZ_LN890335.1\|WP_006387993.1\|3686185_3686455_+\|HPr-family-phosphocarrier-protein	gnl\|CDD\|376329	pfam00381, PTS-HPr, PTS HPr component phosphorylation site.	1.83273e-32
NZ_LN890335.1\|WP_026385254.1\|3686579_3688274_+\|phosphoenolpyruvate--protein-phosphotransferase	gnl\|CDD\|224006	COG1080, PtsA, Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism].	0
NZ_LN890335.1\|WP_006387997.1\|3693694_3693892_+\|50S-ribosomal-protein-L35	gnl\|CDD\|234676	PRK00172, rpmI, 50S ribosomal protein L35; Reviewed.	5.92937e-23
NZ_LN890335.1\|WP_054444174.1\|3698199_3698631_+\|MerR-family-transcriptional-regulator	gnl\|CDD\|133393	cd04765, HTH_MlrA-like_sg2, Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators. Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.	9.18694e-41
NZ_LN890335.1\|WP_006387998.1\|3693909_3694269_+\|50S-ribosomal-protein-L20	gnl\|CDD\|179959	PRK05185, rplT, 50S ribosomal protein L20; Provisional.	5.46719e-63
NZ_LN890335.1\|WP_006384618.1\|3691363_3691615_+\|accessory-factor-UbiK-family-protein	gnl\|CDD\|377337	pfam04380, BMFP, Membrane fusogenic activity. BMFP consists of two structural domains, a coiled-coil C-terminal domain via which the protein self-associates as a trimer, and an N-terminal domain disordered at neutral pH but adopting an amphipathic alpha-helical structure in the presence of phospholipid vesicles, high ionic strength, acidic pH or SDS. BMFP interacts with phospholipid vesicles though the predicted amphipathic alpha-helix induced in the N-terminal half of the protein and promotes aggregation and fusion of vesicles in vitro.	1.05315e-18

>NZ_LN890335.1|WP_024068407.1|3690641_3691076_+|hypothetical-protein
MMNTQRKTFAVLALAAALAALAGCNKSDEKAAPPAASTTPAPSTTTPGTPPAATTPPATTAPSGSGAPAGATAGLPAECDAYLTQVSACMDKLGASNPAAASFKQQLDAAKTQWATISDKTQLASQCKQSADLFAQSASQMGCK
>NZ_LN890335.1|WP_006218735.1|3689760_3690099_-|P-II-family-nitrogen-regulator
MKLIIAIIKPFKLDEVRVALSGIGVQGLTVTEVKGFGRQKGHTELYRGAEYAVDFLPKLRVEAAVPDHLVDQVIEAIEQAARTGKIGDGKIFAAPLEQVIRIRTGEAGEAAL
>NZ_LN890335.1|WP_006387995.1|3688490_3689729_-|ammonium-transporter
MDKADISWLLVSTLLVLMMAVPGLAMFYGGLVRSKNVLSVLLQVMCTFVLGLVLWFIYGYSLAFTEGNAFFGGLSRAFFSGMFTPADGKYAMSNSLTELLFASFQATFAGITCALIVGSFAERARFSAVLVFTVIWFTFAYIPIAHMVWFASETAPGLLNAKGALDFAGGTVVHINAGVAGLVGAYVVGKRVGYGREAMQPHNLPMTFVGAALLWVGWFGFNAGSALAANENATLAFFNTMIATAGAVLAWLFTEWAIKGKPSMLGAASGAVAGLVGITPAAGLVGPVGALIIGVVAGVVCVWGVNGLKRLLRADDALDVFGVHGVGGIVGALLTGIFNAQALGGPGLAEPGMILGQLWVQLEGVLLTIVWSGVVAWIAYKIANALCGLRVPEDQEREGLDVTSHGESAYHS
>NZ_LN890335.1|WP_026385254.1|3686579_3688274_+|phosphoenolpyruvate--protein-phosphotransferase
MARGYAIGRAVVMGAAALEVAHYRIAPEDVPAESSRLTEALASAQQELRQLADTLPADAPRELGAMLNVHSLLLGDPLLAEQTLALIAERHYNAEWALTTQGQILGQQFDAMEDEYLRERGADVRQVIERVLHVLSGTSAILPDMSHMGGDEALVVVAHDISPADMLRLRGGRFAAFVTDLGGPTSHTAIVARSMGVPAVVAMGNVRELVRDGDMLIIDGAAGAVVVNPSERILQEYRRRQAAYADERAELGLLRDEPSVTLDGIDIVLHANIELPEEAALALASGAHGIGLFRSEFLFMGRPDLPGEEEQYEAYASVVKVMAGRPVTIRTLDIGSDKTLDGEATVATNPALGQRAIRYCLARPEMFATQLRAILRASAHGPVRLLIPMIAHMHEVVATRAAIESARRELDARGQAYAAHMEVGAMVEVPAIAIAIEPFAQALDFLSIGTNDLIQYTLAIDRGDHDVASLYDPLHPAVLRLVAHTINAGERAGKPVAVCGEMAGDSRMTRLLLGLGLTEFSMHPQQLLDVKREVRRAHTNALRVKVASALNRALPVDLDTLDLA
>NZ_LN890335.1|WP_006387993.1|3686185_3686455_+|HPr-family-phosphocarrier-protein
MPNTDIVISNKLGLHARAAAKLTQLASKFSSEIFISRGAQRVNAKSIMGVMMLAAGLGVTVKLEASGSDAEQALSEIETLFDSKFGEQE
>NZ_LN890335.1|WP_006387992.1|3685673_3686075_+|PTS-mannose-transporter-subunit-IIA
MTTGIVIVVHAPLGAAMRECASHVMGNLDGMLAIHDIQPEDLPDDLAPAVLKDILEQDHGGGVLVLTDLIGATPANISKRAVADAQAQGIQCCVLAGLNTPMLLRALTYRNLSLAETREKALAGGVQGVLRVD
>NZ_LN890335.1|WP_026385253.1|3684678_3685656_+|glutathione-synthase
MHVLFVLDPLPLLKAYKDSSVAMMRALVARGHTLSVAMQGDLYIETGTVKAVTTPIELVDGADLHGHDWWRESAPQDLPLADFGAVVMRKDPPFDMEYVYSTHLLEYAQAQGAKVFNGGAAIRNHPEKLAITEISEFTAPTLVTRNMARLKAFHDTHHDVIVKPLDGMGGTGVFRLQPKDPNLNAILETLTDNGARTIMAQRYIPEIVKGDKRILLIGGEPVPYSLARIPLAGETRGNLAAGGRGVAQPLSPRDREIAEAVAPRLAARGLLLVGLDVIGDYVTEVNVTSPTCFVEIAEQTGFDVAGMFVEALEKAVATGAVAAAA
>NZ_LN890335.1|WP_076410237.1|3683963_3684515_+|translation-initiation-factor-IF-3
MATEKANRINGEIRVPEVRLIGLDGEQLGIVKIADAFRLSEQNDVDLVEIAPNAEPPVCRLMDYGKFKYQEQKRQAEARSKQKVIQVKEVKFRPATDEGDYQVKLRNLRRFLEEGDKAKVTLRFRGREMAHQELGMRVLERVRDDLLELAQVEAMPKLEGRQMVMVLAPKKKAAPAGKPESAA
>NZ_LN890335.1|WP_006387989.1|3681990_3683943_+|threonine--tRNA-ligase
MVQITLPDGSQRQYPGPVTVAEVAQSIGAGLAKAALGGRVTFDGADSTLVDTSYRIEGDARLAIVTAKDADGLDMIRHSTAHLLAYAVKELFPDAQVTIGPVIDNGFYYDFSYKRPFTPEDLAAIEKKMAELAKKDEVVTREVWSRDDAVEFFKGIGEKYKAEIIASIPSNEPLSLYREGEFIDLCRGPHVPSTGKLKVFKLMKVAGAYWRGDSKNEMLQRIYGTAWATKEEQEAYLHMLEEAERRDHRKIGRELDLFHFQDEAPGLIFWHPKGWALWQQVEQYMRSVYRDNGYQEVKAPQILDISLWKKTGHWDNYRENMFTTESENRVYGLKPMNCPGHVQIFNAGLHSYRELPLRYGEFGQCHRNEPSGSLHGMMRVRGFTQDDGHIFCTEEQLQDECADFTALLQKVYRDFGFTEVLYKVATRPEKRIGSDEVWDTAEQALMESLRRTGCEFEISPGEGAFYGPKVEYTLKDAIGRHWQCGTIQVDFSMPVRLGAEYVDQNDQRRPPVMLHRAILGSLERFIGMLIENHAGAMPPWLAPVQAVVCCISEPSADYAAEITQSLKKQGFRVESDLRGEKITRKIREHSLQKVPYILVVGDKEKQNGTVAVRGLGGLDLGAIAFDDFVARLSEDVSTRRDVNQPDGSAA
>NZ_LN890335.1|WP_006387988.1|3680733_3681648_+|dTDP-4-dehydrorhamnose-reductase
MPKKILVIGRDGQLGFELRRSLAPLGVVTAVGRADCDLTYPLQIARLVRREKPDVIVNAAAFTAVERAQEDGVRAMRINAEAAGELSALAAERGALIVHYSSDYVFDGAKPGAYDERDTPAPLNVYGRSKLAGEQAVRAMNPAHLVFRTSWVYGVFGNSFLKTMLMALRQPETLRVVSDQRGAPTGAAYIADATALVLARYLARPADEAFPFGLYHLAATGDASWHEYACFIAQQARRAGLAVTLTPADIRAVPSDQYPTTARRPLNSRLDSRLLERTFGIRAPHWEDGVTHALAAIADSRNLA
>NZ_LN890335.1|WP_006384618.1|3691363_3691615_+|accessory-factor-UbiK-family-protein
MNNRTQWMEDIQKNISDLIARSPAADVERNVRAMMTQAFSKLDLVTREEFDVQADLLARTRARVDQLSATVEQLESRLAALDK
>NZ_LN890335.1|WP_054518358.1|3691700_3693248_+|YifB-family-Mg-chelatase-like-AAA-ATPase
MTLAVIASRTLSGLHAHAVRVETHLGPGLPSFNVVGLPDTEVRESRERVRAAILNSGFNFPAGRITVNLSPADIPKESGRFDLPIALGLLLAAGQLAPREEGAQEGGAAAAQAAAPDPLLAGLVLAGELSLTGALVPVSAALVIALSVARESPGATLILPAGSAEQAAWVEGLRVLSARSLADVAAHVAGVCHLPDAIAASWPAAPPAPCLSDVRGQPGARRALEVAAAGGHSLLMVGPPGAGKSMLAARLPGLLPPLARTQALEVAAIAALAGAPDARMGTPPFRAPHHSASPFALVGGGGRPRPGEISLAHHGVLFLDELPEFSRRTLEALREPLETGRVVIARALHTAQFPARFQLVAAMNPCPCGWRGHPRRACQCTPDQVARYAGKVSGPLLDRIDLYVTLPPPDLESLQGPPGEASAPVRARVARCRERQLARQGKSNAGLAGAELERHCPMDPSAQALLLQAMRRLAGSGRALHRALRVARTIADLDGADTLQASHVAQAVQYRRPGV
>NZ_LN890335.1|WP_006387997.1|3693694_3693892_+|50S-ribosomal-protein-L35
MPKMKTKKSAAKRFQVRGSGSIKRGQAFKRHILTKKTTKNKRQLRGSAAVHETNVASVKAMMPFA
>NZ_LN890335.1|WP_006387998.1|3693909_3694269_+|50S-ribosomal-protein-L20
MPRVKRGVTARARHKKVISAAKGYRGRRGNVFRIAKQAVMRAGQYAYRDRRNKKRTFRALWITRINAAVREHGVSYSVFIAGLKKAAIELDRKVLADLAVRDKAGFAAIVQQAKAALAA
>NZ_LN890335.1|WP_006387999.1|3694346_3695369_+|phenylalanine--tRNA-ligase-subunit-alpha
MTQSVDDLVSQAQERFAAATDAAALENAKARFLGKDGALTVLLKGLGKLDPEQKRDMGARINQAKQKVEELLNLRRAALAQAELDARLASETIDVSLPGRGRVPGGIHPVIRTWERVEEIFRSIGFDVADGPEVENDWTNFTALNNPLDHPARSMQDTFYVDMKDADGLPLLLRTHTSPMQVRYARMHKPPIKVIAPGRTYRVDSDATHSPMFHQVEGLWIAEDISFADLKGVYTDFLRCFFESDDLVVRFRPSFFPFTEPSAEIDMMFTSGPNRGRWLEISGSGQVHPQVVRNFGLDPERYIGFAFGSGLERLTMLRYGVNDLRQFYEGDLRFLRQFNE
>NZ_LN890335.1|WP_006388000.1|3695382_3697800_+|phenylalanine--tRNA-ligase-subunit-beta
MQFPESWLRTLVNPPIATDELAHRLTMAGLEVEDTVPAAPAFTGVVVAHIVEIAPHPDADKLRVCQVDDGSGALLQIVCGAPNAAAGLKVPLARVGAELPGGMKIGVAKMRGVQSSGMLCSARELGLSQDHAGLLELPADMAPGQSIREALDLDDTLFTLKMTPNRADCLSILGVAREVAALTGAPLSVPTAKAVPVTLDELRPVRIEAPDLCGRFGGRVIRGVNARAQTPAWMKTRLERAGQRSVSALVDISNYVMLELGRPSHVFDLDKIHGDLSVRWAREGETLELLNGQTVTLDSKVGVVVAGDQVESLAGIMGGEATAVTLDTQNIYLEAAFWWPQSLAGRARRYKFSSEASHRGERGVDFATIPQHIEFITRLIVDICGGQAGPLDDQIVNLPKREPVRMRLARCHRVLGVPVTQAEVAKIFGSLGLEFTLDGDDFVVTPPSYRFDLEIEEDLIEEVARIYGFENIPTVPPLARAKMFSQPEVRRGPHALRRLAAAQDYQEVVNYSFVEAEWERDYAGNDTPVKLVNPIASHLSVMRSSLIAGLVANIRHNANRKQTRVRLFELGRVFARDDAAKDGPLEVAGVRQPLKLAGAAWGPSVEEQWGVPARQVDFYDVKMDVEALFGARGARLRFEAAAHPALHPGRSARITLDGTQVGWLGELHPRWAQQADLAHAPVVFELDVQALSEGELPQVRELSRQPVVVRDLALWVDAPVTVQSMLDTVAATVKADPQLAVVQDVRLFDVWREKPQGDQPVAEKSLAFRFWLQDTEVTLDEARVAACLARIKDALVSAHGARQRA
>NZ_LN890335.1|WP_155865631.1|3697803_3698142_+|integration-host-factor-subunit-alpha
MGNSMLAEPRTLTKAELAELLFERVGLNKREAKDIVDTFFEEIRDALARGDSVKLSGFGNFQVRDKPPRPGRNPKTGETIPIAARRVVTFHASQKLKSVVEQAAPAAPDAEE
>NZ_LN890335.1|WP_054444174.1|3698199_3698631_+|MerR-family-transcriptional-regulator
MTRTESTVTLPPIPAKRYFTIGEVSDLCGVKPHVLRYWEQEFTQLKPVKRRGNRRYYQHHEVLLIRRIRSLLYEQGFTISGARNRLGDARDTPHDQDAAVRLSGAEMQALRNELGNVSTMLGEALGSAAPASSGSAVSANATA
>NZ_LN890335.1|WP_131727054.1|3699335_3699650_+|hypothetical-protein
MLLLVVLTGCASVEDLRTGGTIYEGETSKPVAEYGPCVSERWSKFSAGWTNYYPVPKGIEIVYAPMFVDLLLRAVEQDGVTRIHIGSRAGWRATDFVQAAKDCA
>NZ_LN890335.1|WP_162531794.1|3699771_3699939_-|hypothetical-protein
MGTTYGAYSAYVPEYTDCAVIFYIDKAGTMLRYDMKTKGKISYNACGEYISGFRF

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NZ_LN890335_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LN890335_4

6022518-6022620

Orphan

Consensus_repeat	Method
TTTTCATCGCCGAGCCGCCTCAAGAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LN890335_4

>merge|NZ_LN890335|4|6022518-6022620|CRISPRCasFinder
TTTTCATCGCCGAGCCGCCTCAAGATGAAAAATGCCCCCTCGGGGGGCAGCAAGCCGAAGGCGCGGCGTGGGGGCCCTTTTCATCGCCGAGCCGCCTCAAGAT

>NZ_LN890335|4|4|6022518-6022620|CRISPRCasFinder
TTTTCATCGCCGAGCCGCCTCAAGAT	GAAAAATGCCCCCTCGGGGGGCAGCAAGCCGAAGGCGCGGCGTGGGGGCCC
TTTTCATCGCCGAGCCGCCTCAAGAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LN890335.1\|WP_155866344.1\|6019761_6022467_+\|aconitate-hydratase-AcnA	unknown	unknown	gnl\|CDD\|236445
NZ_LN890335.1\|WP_165596267.1\|6024743_6026243_+\|efflux-transporter-outer-membrane-subunit	unknown	unknown	gnl\|CDD\|273830
NZ_LN890335.1\|WP_155866346.1\|6027375_6028905_+\|DHA2-family-efflux-MFS-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|129794
NZ_LN890335.1\|WP_006387148.1\|6009747_6010515_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|235546
NZ_LN890335.1\|WP_020928784.1\|6018525_6019455_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_LN890335.1\|WP_026383333.1\|6013062_6014037_-\|pirin-family-protein	unknown	unknown	gnl\|CDD\|224655
NZ_LN890335.1\|WP_173361490.1\|6006725_6007172_+\|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|119323
NZ_LN890335.1\|WP_102949912.1\|6023752_6024640_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176149
NZ_LN890335.1\|WP_155866343.1\|6015073_6016033_-\|tripartite-tricarboxylate-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270296
NZ_LN890335.1\|WP_155866651.1\|6016090_6017530_-\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|236215
NZ_LN890335.1\|WP_026383342.1\|6031629_6032832_+\|DUF2863-family-protein	unknown	unknown	gnl\|CDD\|371362
NZ_LN890335.1\|WP_155866653.1\|6026293_6027376_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|185090
NZ_LN890335.1\|WP_024069798.1\|6030611_6031385_-\|dioxygenase	unknown	unknown	gnl\|CDD\|153375
NZ_LN890335.1\|WP_155866652.1\|6017598_6018408_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187627
NZ_LN890335.1\|WP_006387145.1\|6014154_6015063_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|184959
NZ_LN890335.1\|WP_155866342.1\|6010576_6012778_-\|TonB-dependent-siderophore-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_LN890335.1\|WP_155866347.1\|6028940_6029645_+\|siderophore-interacting-protein	unknown	unknown	gnl\|CDD\|99790
NZ_LN890335.1\|WP_155866348.1\|6029680_6030571_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_LN890335.1\|WP_024069800.1\|6032841_6033957_+\|elongation-factor-P-maturation-arginine-rhamnosyltransferase-EarP	unknown	unknown	gnl\|CDD\|378385
NZ_LN890335.1\|WP_155866345.1\|6022637_6023600_-\|DUF4892-domain-containing-protein	unknown	unknown	gnl\|CDD\|143586

Protein	Function_ID	Function_description	E-value
NZ_LN890335.1\|WP_155866344.1\|6019761_6022467_+\|aconitate-hydratase-AcnA	gnl\|CDD\|236445	PRK09277, PRK09277, aconitate hydratase AcnA.	0
NZ_LN890335.1\|WP_165596267.1\|6024743_6026243_+\|efflux-transporter-outer-membrane-subunit	gnl\|CDD\|273830	TIGR01845, Outer_membrane_protein_OprM, efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family. Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins].	8.35824e-67
NZ_LN890335.1\|WP_155866346.1\|6027375_6028905_+\|DHA2-family-efflux-MFS-transporter-permease-subunit	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	3.05323e-126
NZ_LN890335.1\|WP_006387148.1\|6009747_6010515_+\|SDR-family-oxidoreductase	gnl\|CDD\|235546	PRK05653, fabG, 3-oxoacyl-ACP reductase FabG.	4.98682e-91
NZ_LN890335.1\|WP_020928784.1\|6018525_6019455_+\|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.	3.04852e-56
NZ_LN890335.1\|WP_026383333.1\|6013062_6014037_-\|pirin-family-protein	gnl\|CDD\|224655	COG1741, COG1741, Pirin-related protein [General function prediction only].	1.48298e-36
NZ_LN890335.1\|WP_173361490.1\|6006725_6007172_+\|branched-chain-amino-acid-ABC-transporter-permease	gnl\|CDD\|119323	cd06581, TM_PBP1_LivM_like, Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivM forms a heterodimer with another TM, LivH, to generate the transmembrane pore. LivH is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.	1.32314e-27
NZ_LN890335.1\|WP_102949912.1\|6023752_6024640_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176149	cd08460, PBP2_DntR_like_1, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold. This CD includes an uncharacterized LysR-type transcriptional regulator similar to 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. This substrate-binding domain shows significant homology to 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.	3.2876e-69
NZ_LN890335.1\|WP_155866343.1\|6015073_6016033_-\|tripartite-tricarboxylate-transporter-substrate-binding-protein	gnl\|CDD\|270296	cd13578, PBP2_Bug27, Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. Bug27 binds non-carboxylated solute nicotinamide, in contrast to BugD (aspartic acid transporter) and BugE (glutamate transporter) which both bind aliphatic carboxylated ligands. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity.	5.50516e-121
NZ_LN890335.1\|WP_155866651.1\|6016090_6017530_-\|AMP-binding-protein	gnl\|CDD\|236215	PRK08276, PRK08276, long-chain-fatty-acid--CoA ligase; Validated.	0
NZ_LN890335.1\|WP_026383342.1\|6031629_6032832_+\|DUF2863-family-protein	gnl\|CDD\|371362	pfam11062, DUF2863, Protein of unknown function (DUF2863). This bacterial family of proteins have no known function.	0
NZ_LN890335.1\|WP_155866653.1\|6026293_6027376_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|185090	PRK15136, PRK15136, multidrug efflux MFS transporter periplasmic adaptor subunit EmrA.	1.41933e-103
NZ_LN890335.1\|WP_024069798.1\|6030611_6031385_-\|dioxygenase	gnl\|CDD\|153375	cd07363, 45_DOPA_Dioxygenase, The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine. This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.	1.79369e-120
NZ_LN890335.1\|WP_155866652.1\|6017598_6018408_-\|SDR-family-oxidoreductase	gnl\|CDD\|187627	cd05369, TER_DECR_SDR_a, Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR. TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	3.05719e-93
NZ_LN890335.1\|WP_006387145.1\|6014154_6015063_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|184959	PRK14997, PRK14997, LysR family transcriptional regulator; Provisional.	1.1118e-62
NZ_LN890335.1\|WP_155866342.1\|6010576_6012778_-\|TonB-dependent-siderophore-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	4.68357e-108
NZ_LN890335.1\|WP_155866347.1\|6028940_6029645_+\|siderophore-interacting-protein	gnl\|CDD\|99790	cd06193, siderophore_interacting, Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).	3.64097e-39
NZ_LN890335.1\|WP_155866348.1\|6029680_6030571_+\|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.	4.39899e-47
NZ_LN890335.1\|WP_024069800.1\|6032841_6033957_+\|elongation-factor-P-maturation-arginine-rhamnosyltransferase-EarP	gnl\|CDD\|378385	pfam10093, EarP, Elongation-Factor P (EF-P) rhamnosyltransferase EarP. This entry includes family members such as EarP enzymes which are essential for post-translational activation of elongation factor P(EF-P). It was identified as EF-P arginine R32 specific rhamnosyl transferase in Shewanella oneidensis using dTDP-beta-L-rhamnose as donor substrate. This was further confirmed for Pseudomonas aeruginosa, Pseudomonas putida, and Neisseria meningitidis. As for S. oneidensis and P. aeruginosa, EarP enzyme acts as an inverting glycosyltransferase, thus mediating the formation of an alpha-L-rhamnosidic linkage. Structural analysis show that EarP is composed of two opposing domains with Rossmann folds, thus constituting a B pattern-type glycosyltransferase (GT-B) and provide basis for arginine glycosylation by EarP. Mutational analysis of efp and earP genes, resulted in a substantial decrease in the production of rhamnolipids and pyocyanin (important factors for colonization and invasion during infection) of P. aeruginosa. Collectively this indicates that EarP and EF-P are essential for P. aeruginosa pathogenicity.The protein family is also annotated in the CaZy Database as GT104.	4.19896e-175
NZ_LN890335.1\|WP_155866345.1\|6022637_6023600_-\|DUF4892-domain-containing-protein	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	8.42562e-40

>NZ_LN890335.1|WP_155866344.1|6019761_6022467_+|aconitate-hydratase-AcnA
MPHNTLDTLKNFKIGNKSCQYYSLPALGKALGIDVQRLPVSIRIVLESVLRNCDGKKVTEEHVRQLANWQANAKREDEIPFVVARVVLQDFTGVPLLADIAAMRSVADKMGKSPKSIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFKRNQERYQFMKWGMQAFDTFGVVPPGFGIVHQVNLEYLARGVHQGKKNNVYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVAERATIGNMAPEYGATMGFFPVDGRTIDYFRGTGRTEDEIAAFEAYFKAQDMFGVPAAQDINYTKLLTLDLSTVAPSLAGPKRPQDRIEIGNVKSTFIDLFSKPVAENGFNQPAEKLQQTFTTSTGTKVKNGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTPDLNEVITSNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVVAYALAGTVTRDLMTEPVGRGKNGDIWLGDIWPTTEEVEALLKYALDPKAFEANYGQVKSNPGKLWENIKGVTGETYNWPDSTYIAEPPFFEGFGMTPGAMPTVKNARALGVFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHEIMMRGTFANVRIKNLMIPARPDGSRFEGGETLFQPTGEQMSIYDAAMKYVAAGTPTVVFGGEEYGTGSSRDWAAKGTQLLGVKAVITRSFERIHRSNLVGMGVLPLQFKGSDSVQSLGITGEETYDISGLENGIKPMQDVTLTITRKDGSKQDVTLLLRIDTPIEVDYYQHGGILPFVLRQLLAA
>NZ_LN890335.1|WP_020928784.1|6018525_6019455_+|LysR-family-transcriptional-regulator
MTTPPALDLNLIQLFVTIVEAGTLSEAALRQGVTRSHVSRNLQKLERAFGAQLIRRTTRRLELTHEGSVLYDHGARMAREVESARHALQKLGAEPTGHVRLSLPTGLGELDMLRPLLVRFALEHPSLSLRVLFSNRVSDLISSEIDVALRAISVPPQDYVARELGRIKWHLCAAPEYLARMGMPAHPRDLGRFDFLGPPGPRPQATLRLRGKGQPHEVKLATRLQSEYFPFLAQAAREGAGVALLPAYIVRPDLEAGRLLQVLPAYQAEGPGDKLYILTSPTPYPSSAQRALVDFLKRELEPLLRTFLA
>NZ_LN890335.1|WP_155866652.1|6017598_6018408_-|SDR-family-oxidoreductase
MFRADLFLGQRILITGGGTGLGYAMARQLAAGGQVHVHPVDIRDAGAVDAMVARIWDQHGGLDALVNNAAGNFISPTEKLSERGFNAIADTVFRGTFYMTQAVGKRWIGSGASGAVVSIVVTWVWTGSPFVVPSAMSKAGIDAMTKSLAVEWGRRGIRLNAIAPGVIPTEGASARLRPNDSGTDALVKQNPMQRLGQGQDIGELAAFLLAPGNDWINGQTIALDGGDYLANGAYFKQYFDWSDEDWAAARAAIEARTAADKAQRSAGQA
>NZ_LN890335.1|WP_155866651.1|6016090_6017530_-|AMP-binding-protein
MRRGEQVAAGLAAMGIGQGDVVAVLLRNGMPYLEIIQACKRLGCYYCPINWHYTPDEVAYLVRDSGARLLIAEEDLWQAARAALPADLPSRRVGAAAVSEDYASWREAQAPYDGPVVAPRGHMAYTSGTTGRPKGVVRAPFPLDQLAQRLAAVEAVVEQAYGLRPGCRALLPAPVYHSAPSVFAQVALRVCETLVLAPRFDPLEVLRLIERHRIDTVYLVPIMYVRLLKLDPAQRAAFDLSSLRFVASTGAPCAPALKRAMIDWLGPVIHETYASSEAGMVTVIDSHEALARPGSAGRPIGGAQIRIYGDDGALCAPGQIGRIHVRQPAYADFTYRNNPQARSRIERDGLIGLGDLGYLDDDGYLFVCDRESDMVISGGVNIYPAEIEHHLTQYPGVADCAVFGVPDDEFGERLLALVQPAADTTLAPEEVLRWLSTRVARYKVPRELRLRQSLPRDDNGKIAKRRLRDAFWAERDRKV
>NZ_LN890335.1|WP_155866343.1|6015073_6016033_-|tripartite-tricarboxylate-transporter-substrate-binding-protein
MFMRNSGIGRAAAALLLCMAAASPAQAAFPERPVKLVVPYTPGGAADLLSQELAQPVVVENKPGANTMIAATQVARAQPDGYTLFLASNASMVLNPMLYRKISYDAQRDFRVLSVVAELPLVVVANNSVPASTLAQFVDYARARPGKLNYASVGIGNPLQLATELLKSRTGIDVAHVPYNGSAPALSSLMANDTQLMVDVISTSLPLVRENKIKALAVTGAQRLPVLPDVPTVAESGFAGFRAATWFGVAVPRGTPPAEADRLREAVAAVMRQADFRDRFQAQGLVIQAPRGQAEVDAYLAEDRERWNGVIQANHIRLD
>NZ_LN890335.1|WP_006387145.1|6014154_6015063_+|LysR-family-transcriptional-regulator
MHSYIHHLDDLLLFTEVVEKGGFSAAARVLNMQRSKLSRRVAELEARLGLRLLQRNTRRVSLTPMGEQIYVHALAMAREARSAFDLAAAMGDTPSGLLRMTAPSALAVTLLGELVARFCLQHPGVRVLLDTRDQVIDLVGEGYDLAFRAQGASLTDSRLVARELAPVPLILVAAPAMARAAPRHPRDLNALPLLAHATQDSPQSWHFVGPAGEAESIEFRPRCLSSNLAALREMARAGLGVALLPHYLCAGSLAKGDLAQLLPAWRAAPARIYAVMPARRGAPLALRRFLDFAAAEMPALLA
>NZ_LN890335.1|WP_026383333.1|6013062_6014037_-|pirin-family-protein
MTIRLSPPVARPFEPEGDICSYRHFRHSDFPQGMSPLVLVDHFIMTGPAVAPHPHAGISTVTLLLEDTQGGLRIRDSLDNEHEARAGDLHWTVAGRGIVHGHELVGAARLNGLRLYVNLPARLKSMPPSATLVRGWEMPVLQSDAGRVRVVSGRYDGWDAPLATPEPLLILDGWLRPGASRLVPLPAGWNAWLYAAQGELGVRARHETTPPPRPPVEAAPVIPAARFRPAGRAATTGRRAADPDFAVLPPGAALTATADRDGFLQLLAAGAPAHFILVAGAAIDEPVIQRGPFVMTDARALAQAVAAYEAGDFGQLRQESGVPG
>NZ_LN890335.1|WP_155866342.1|6010576_6012778_-|TonB-dependent-siderophore-receptor
MKIRTLACVVAALPYTAIVHAQSAAPAADGSVVSMEAIKVEASADASAGGLAQPYAGGQVARGGRVGVLGTQDIMSTPFSVTSYTNELIQDKQARSVGDVLQNDAGVRVARGFGNFQESYFIRGFILSSDDVAYNGLYSLLPRQYIATELFERVEVLRGASAFLTGAAPSGGGIGGVINLVPKRAPNEPLTRFTTGVSSGGQFSVSTDIARRFGPDDSTGIRLNVANRSGDTGIDDEHSRTSLVSLGLDWRSADTRLSADIGWQENKLKRARPNVTLRGVTSVPDAPDASSNYAQPWSYSNERDVFGTVRAEHDFSDKLTGWAAFGMRRSDEANSLGNVTVTNGSTGDGNFYRFDNTREDSVNTGELGLRAKVRTGPVGHEFVASASFFDLKKKNAYVMDYLNTFPTNIYDPISYDRPAYGSKALFGNDLDDPALQGRTRLSSYAFGDTMSFLDDKVLLTLGIRHQRLSQRDYAYNTGKEQSAYDASRNSPAAGIVFKVAPSVSLYANYIEALVAGDTAPQTANGKPVPNAGQSLQPYVSKQKEIGVKYDGGGLGAGLALFSTDKPRAAYDASNRFTASGKDRHQGIELTVFGEPVNRVRVLGGMTFLDAKQRSTGNSAIDGNRVIGVPRFQANLGAEWDIPGVQGLTVDGRVVYTGASYADDANTLKVPGWTRFDAGLRYMMDVDGHVVTLRARVENIANRNYWSSVGGYPGNGYLVLGGPRTFSLSASMDF
>NZ_LN890335.1|WP_006387148.1|6009747_6010515_+|SDR-family-oxidoreductase
MSARFQDQVIIVTGAVGGIGSAIVEGFLAEGGKVGLIDFNSQGGQAYEKELKKRGHAVSFVHADVSHFDQCQAAYERITRDLGPATILVNNVGISPKTDGRALKVWEMTPGEWDKVVAVNLNSVFYMTHLATPHMVRQRQGRVINMSSVAGKAYCDIVAAHYAATKAALLGLTRHWAAELGEHDVTVNGLAPGRISTPLLKSVPKEINDAVAEVTALRRLGTPEEVADACLFFASDQARFVTGQVLDVAGGWLMT
>NZ_LN890335.1|WP_173361490.1|6006725_6007172_+|branched-chain-amino-acid-ABC-transporter-permease
MFREKINYVIIAFGLFLLVTWVSWTIRKSRIGHYLIAIREREDAALAVGIHTVRVKIIAAVVSAMLTSIIGTFHITYLTFVDPSSAFSLELSIQVAMFALIGGLGTVAGPIAGTFLVLPIAELARGWLSSVGNGMHGLIYGLILVAWC
>NZ_LN890335.1|WP_155866345.1|6022637_6023600_-|DUF4892-domain-containing-protein
MKAHIVKVASLAIVAATLTASPAWAEDVEGSRDHPALTRFEGAEIRAYEHKDYDEALMPDRPVARESEAKGLTLEGKLTRIAYRIDGKKSALEVYRNYQGALQAGGFKTVFECRGDEQCGSDFQSFVLNSGKVSQPGQGDAAFGGKYYVVLAKKEAPTGDIYVFLDVMEDTSNNITPVFQQVIETKPMQTGQVKVLDMAAMQKSLAESGRVAVYGVYFDTDKAEVKAESKAALDEMGKLLNANPKLKVYVVGHTDNQGTLAGNLELSQKRADAVVKALEAGYKIPAARLSARGVASLAPVAANDAEAGRARNRRVELVAQ
>NZ_LN890335.1|WP_102949912.1|6023752_6024640_-|LysR-family-transcriptional-regulator
MNLLVALDALLAEGSVTGAAERLQLSVPAMSRTLERIRRMMGDPLFVRAGRGLVPTPRAEALREPVRALVAQARELLAQDAAFDLKTLRRVFTIRADDGAVSTLGPALLDTLAKEAPRVTVRFISQGKQDVLSLREGAIDLDIGVIEDMGPEIVRQRLFPDRFVAVFRPANPLARHRKLTPERFARARHATVSRRGVLSGPVDIELGKVGLARHISAVTHSFAEALAITRKSDLVATVPDLLTLHLRDDLQMRALPFDTPAVTISQAWHPRFNEDPAHRAIRQMVHRISLAISGR
>NZ_LN890335.1|WP_165596267.1|6024743_6026243_+|efflux-transporter-outer-membrane-subunit
MIHSTRYRPDARPARRMRLRHAPLAAALAALVAVAGCASHDGLRPAGKPLDLAALDAGQDIAAAVRDTADDAAPWWRAWGDDQLDRLIADALRQAPGVRAAQARLGQAEAVFGSVDAKRQPTLDGSATITADRYPGHYTYGAPYADNTGGSGSLLASLRLRLDIWGKWRALADAARLDAEGAALAHADAQLALQQGIAAAYLRLDAAFRLHELARQQRERQRQALELHQTRRQAGLGSDAPVADARGRLARMDAEVERLDREIARQRHALAALAGQAPGYGDALRRPRLALRADPALPAALPARLLGLRPDVLAQRKRLDAADRRIEAAKAEFYPDIDLKAFAGLQSLGLSHLLQGNSLAAGIGPALTLPIFDGGRLRAGLRDRIAGYDLAVADYDATVVRALQEVADGLAGMAQARARRDAARVSLREAGTLARLQAVRASRGLSARQDEIDTDLERLRADSELAAADLDLGLARTALAGALGGRWSPSQSSDNEALK
>NZ_LN890335.1|WP_155866653.1|6026293_6027376_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MLAGGATLLAGAGWAAWTFLAGAATQTTDNAYVNGHVVAITPQVGGAVSAIWADNADRISAGQTLVEVDPADTQIALAGARADLARARRRVQALFASRDQAGAEVARRQAELDRAQADVSARRGIAAQGAITSEEARHAADALNAARAALAVAQAAERAAQAQVDGVTPDTHPDVTLAQARLRAAALDAQRTTIRAPVGGMVAQRSVQLGKHVAIGDKLMAVVPLDQMWIDANFKEIQLAGICPGQPAVVTVDAHGAKVRYSGRVGDVMAGSGSAFALLPSQNATGNWIKVVQRVPVRINLDPKELADHPLRIGLSAEVTVDTARCDPAQAGAARGETTDIYRQQRQAADTLAQAGQGLQ
>NZ_LN890335.1|WP_155866346.1|6027375_6028905_+|DHA2-family-efflux-MFS-transporter-permease-subunit
MSAAPRPIEPMTGLPRVVAAVAISLASFMAVVDITIANVSVPTISGNLGVSPEIGEWAITFFAIANSICIPLTGWLSRRLGQVRLFVLSVAAFTLASVLCGVAQNFESLLAFRVLQGMVSGPIVPLSQALLVAIFPPDKRTLALSMWAMTNMAGPVAGPVLGGWLTDDFSWPWIFLVNAPVGIAVVAVTATMFRGRDTPSTRLPVDLRGLILLAVAIGCLQLTLDRGRTLDWFASPFIVTTALLSALGFVFLVIWELGEAHPIVDLSLFRHRNFAMGTLAVAVGFGLYFAALVLIPLWLQTDMRYTATWAGLATAPMGVFGILLAPLLGRWVQRGDARAFASLAFVAWSLVAWWRASMTTDVGVGLISLACLLQGIGIGLFLTPLVSLSLAGLPPERIAAASGLQTAIRMMAGSLVASLASTYWDERSRYYQNVLVDSATPARPAVQDTLNALAGAGLDEPQSWGVIWNGLKTQADMLALNDFFLWSSLAFALSIALVWLARHPRAAKA
>NZ_LN890335.1|WP_155866347.1|6028940_6029645_+|siderophore-interacting-protein
MQPFSLPRRDVPCIVLRARDVARDMRRLTLGGPELSAWLARPGVDQPGAWVKVFPPGVPGRAYTLRGIDFEASSVEIDFVVHGDAPGTVSEWARRARPGDAVSIAGPREGGFSLLADTRWVWLGADASAWPAASRIIESLPGGIQVLGVRHPAGDDDWPAIASARAPQWAARSLPPGGDEPSAPAPDGPGQVWLAGQAAWVKAWRAHWLQRLRFDPARLSAKGYWKAGEQNYKE
>NZ_LN890335.1|WP_155866348.1|6029680_6030571_+|LysR-family-transcriptional-regulator
MKKELDRMRDMALFVQVAALGSLTRAAESTGVPASTLSRRISEFESQIGVKLLHRSTRRLALTDIGQRYLERITDVVDRARAISGELEEEMGRPTGHLRVCAPVDFNAYFPEAALADYCASHPGVRFELHCSAQLPDLATEPYDICIATTEPPQASRMVRRRIGMAEYQLYAAPAYLRAYGVPAHPAELARHRCVVMPDSESGLALTDGNASAQVALAPLLMLNNQLAVENLLRDGLGIGPLTRGRADALVREGALAPVLPGWTLPPRPILALTASRALPARVRGFIDLLVARVVT
>NZ_LN890335.1|WP_024069798.1|6030611_6031385_-|dioxygenase
MRWPTLFVSHGSPMLAVEPGATGPALAAWSRSLGRKPGAILVVSPHWMGHGLALSTRDRQVAWHDFGGFPPELYTLQYAAPGSPELAARVQALLAEGGIAADRDPRRPLDHGAWVPLRYLYPEVDVPVVQLSLDMGRDAAGQLELGRALAPLRDEDVLIIGSGSLTHNLRDVRMPQDAPPAPYVPAFQAWYADRLAAHDVPALLDWQARAPGAAQAHPHDDHLMPLYVALGAGGARATRLTDEISYGALAMDAYAFD
>NZ_LN890335.1|WP_026383342.1|6031629_6032832_+|DUF2863-family-protein
MARSRSQSAPRLTRDATRLITLAQSLNRSGSRVEDVYWENQLGEAIPKLLKAGQDAPLEAALDHLAQGDVGAYEVLIEQAETLSESMKIDKNGVRYDILLIVAPVVAWTRYAIPTGPVPAGAQQALLAQLHGHVLSSQARSALMPHLVSVDQMPRTFSETWQWLQRLGSQALGAETTKPALNTEVETANMLADTRYIVAAVAVPEFAPVFRWQEQIGEADASRDACLAQWAAQAQPTLAGLLPGCGFEALLPDAYYVSNREADRRVRPLSLRAAISWLEGAVSLDASQLRAVIAGCGESRVDEYRVSFTARNSNDVYYGCVWPLYGREEDLPADEGQPDVVDEIAALLKEYGVSDVRRIPGVLPPEYCEDCGAPYFPNPLGELVHAELPEDAEAAPAKFH
>NZ_LN890335.1|WP_024069800.1|6032841_6033957_+|elongation-factor-P-maturation-arginine-rhamnosyltransferase-EarP
MQADIFCRVVDNYGDIGVCWRLARRLAHGHGWEVRLWVDDLASFARIQPGIDAGLARQAFNGVDIVRWSDAPDPALGARDVVIEAFACDPPEPFLDSMRQRHPAWINLEYLSAEAWVESCHGLPSQRPDGLVKHFYFPGFTPATGGLLREPGLSAERDAFQADTAAQDTFLRGLGVAEAHLSLRHNGARTMSLFCYPDAPVDGLARALAADPRPALLLAPEGVAPGLEAACAMPGGPAVARLPFVAQPDFDRVLWCADLNFVRGEDSFVRAAWAARPLVWQIYPQDENIHLEKLDAWLARYPAPETATALMRAWNQPGAGAATAAALAAALAPPAWQAWARAARDWDAAQAARPDLAENLAGFCAELAKKR

You can click texts colored in the table to view more detailed information

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_LN890335_2	2.1\|3003536\|31\|NZ_LN890335\|CRISPRCasFinder	3003536-3003566	31	NZ_CP016083	Streptomyces sp. SAT1 plasmid unnamed3, complete sequence	370010-370040	6	0.806
NZ_LN890335_2	2.1\|3003536\|31\|NZ_LN890335\|CRISPRCasFinder	3003536-3003566	31	NZ_CP044425	Paracoccus pantotrophus strain DSM 2944 plasmid pPAN2, complete sequence	446142-446172	7	0.774

1. spacer 2.1|3003536|31|NZ_LN890335|CRISPRCasFinder matches to NZ_CP016083 (Streptomyces sp. SAT1 plasmid unnamed3, complete sequence) position: , mismatch: 6, identity: 0.806

ttcgatc---gtgccccaggcgtcgctggccagt	CRISPR spacer
---gatcagggtgtcccaggcgccgctggccagg	Protospacer
   ****   ***.********.**********

2. spacer 2.1|3003536|31|NZ_LN890335|CRISPRCasFinder matches to NZ_CP044425 (Paracoccus pantotrophus strain DSM 2944 plasmid pPAN2, complete sequence) position: , mismatch: 7, identity: 0.774

ttcgatcgtgccccaggcgtcgctggccagt--	CRISPR spacer
ctggatcgtgacccaggcggcgctgg--agccg	Protospacer
.* ******* ******** ******  **.

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

94444 : 138094

Burkholderia_phage(35.29%)

transposase,tRNA,integrase,tail,plate,protease

attL 90234:90253|attR 110869:110888

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
90234:90253	attL	NA	NA	NA	NA
WP_054437210.1\|94444_94975_-	hypothetical protein	A0A2H4JFP9	uncultured_Caudovirales_phage	5.3e-43	57.4
WP_164497481.1\|94964_95456_-	hypothetical protein	A0A0U5LBV3	unidentified_phage	6.3e-14	37.2
WP_155864653.1\|95611_96556_+\|integrase	tyrosine-type recombinase/integrase	A0A2H4JE37	uncultured_Caudovirales_phage	1.9e-19	31.5
WP_155864654.1\|96558_96909_-\|tail	phage tail protein	NA	NA	NA	NA
WP_155864655.1\|97148_98096_-	hypothetical protein	A0A0M3ULD8	Salmonella_phage	1.7e-15	52.9
WP_054496611.1\|98110_98776_-	DUF2612 domain-containing protein	A9YX13	Burkholderia_phage	2.1e-73	60.2
WP_155864656.1\|98777_99959_-\|plate	baseplate J/gp47 family protein	A9YX12	Burkholderia_phage	5.8e-130	62.8
WP_020924456.1\|99955_100309_-	hypothetical protein	A9YX11	Burkholderia_phage	6.1e-35	66.7
WP_054472039.1\|100317_101061_-	hypothetical protein	A9YX06	Burkholderia_phage	1.3e-82	63.1
WP_155864657.1\|101095_102106_-	hypothetical protein	A9YX04	Burkholderia_phage	9.7e-78	52.9
WP_006388474.1\|102125_102425_-	hypothetical protein	NA	NA	NA	NA
WP_155864658.1\|102434_103034_-	hypothetical protein	NA	NA	NA	NA
WP_155864659.1\|103026_104700_-\|tail	phage tail protein	NA	NA	NA	NA
WP_006393814.1\|104692_104851_-	hypothetical protein	NA	NA	NA	NA
WP_024068262.1\|104877_105327_-	hypothetical protein	A0A0N7IRF3	Acinetobacter_phage	1.1e-17	36.5
WP_006388470.1\|105330_105771_-	DUF3277 family protein	A0A0P0IKY2	Acinetobacter_phage	3.1e-36	54.1
WP_155864660.1\|105784_107260_-	DUF3383 family protein	A0A0P0I492	Acinetobacter_phage	5.7e-103	45.2
WP_006388468.1\|107270_107864_-	hypothetical protein	A9YX29	Burkholderia_phage	7.5e-46	46.6
WP_006388467.1\|108355_108613_-	hypothetical protein	NA	NA	NA	NA
WP_006388466.1\|108922_109684_+	S24 family peptidase	NA	NA	NA	NA
WP_054437265.1\|109688_111506_+	DUF4153 domain-containing protein	NA	NA	NA	NA
110869:110888	attR	NA	NA	NA	NA
WP_006388464.1\|111579_111801_-	hypothetical protein	NA	NA	NA	NA
WP_108913895.1\|111969_113091_-	AI-2E family transporter	NA	NA	NA	NA
WP_155864661.1\|113248_113953_-	DUF3053 family protein	NA	NA	NA	NA
WP_006388461.1\|114116_114629_-	GNAT family N-acetyltransferase	NA	NA	NA	NA
WP_026384180.1\|114812_115172_+	hypothetical protein	NA	NA	NA	NA
WP_006388458.1\|115999_116281_+	hypothetical protein	NA	NA	NA	NA
WP_155864662.1\|116390_117083_+	cytochrome b/b6 domain-containing protein	NA	NA	NA	NA
WP_155864663.1\|117195_118562_-\|transposase	IS3 family transposase	A0A1B1P773	Bacillus_phage	2.7e-75	53.4
WP_155864664.1\|118663_119122_-	cytochrome c	NA	NA	NA	NA
WP_006388455.1\|119178_120555_-	adenylosuccinate lyase	A0A2H4UUU6	Bodo_saltans_virus	2.0e-110	47.7
WP_006388454.1\|120716_121328_+	glutathione S-transferase	NA	NA	NA	NA
WP_006388452.1\|122329_123448_-\|tRNA	tRNA 2-thiouridine(34) synthase MnmA	NA	NA	NA	NA
WP_020924474.1\|123460_124381_-	transcriptional regulator GcvA	Q6JIH3	Burkholderia_virus	3.1e-30	31.5
WP_024068252.1\|124572_125562_+	tripartite tricarboxylate transporter substrate binding protein BugE	NA	NA	NA	NA
WP_155864665.1\|125632_126508_+	N-formylglutamate amidohydrolase	NA	NA	NA	NA
WP_024068250.1\|126693_127812_+	Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha	NA	NA	NA	NA
WP_006388447.1\|127816_128134_+	NAD(P) transhydrogenase subunit alpha	NA	NA	NA	NA
WP_006388446.1\|128130_129570_+	NAD(P)(+) transhydrogenase (Re/Si-specific) subunit beta	NA	NA	NA	NA
WP_155864666.1\|129664_130894_-	glycolate oxidase subunit GlcF	NA	NA	NA	NA
WP_054515396.1\|130899_132003_-	glycolate oxidase subunit GlcE	NA	NA	NA	NA
WP_006388443.1\|132015_133515_-	FAD-binding protein	NA	NA	NA	NA
WP_024068245.1\|133782_135192_-	FAD-binding protein	NA	NA	NA	NA
WP_006388441.1\|135290_136364_-	3-deoxy-7-phosphoheptulonate synthase AroG	A0A2I6UFP9	Klebsiella_phage	1.0e-77	47.3
WP_020924482.1\|136633_138094_-\|protease	metalloprotease TldD	NA	NA	NA	NA

DBSCAN-SWA_2

2527229 : 2583567

Burkholderia_virus(29.41%)

transposase,tail

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_155864663.1\|2527229_2528596_-\|transposase	IS3 family transposase	A0A1B1P773	Bacillus_phage	2.7e-75	53.4
WP_155865348.1\|2529286_2530774_-	efflux transporter outer membrane subunit	NA	NA	NA	NA
WP_155865349.1\|2530843_2534059_-	multidrug efflux RND transporter permease subunit	S5VTK5	Leptospira_phage	1.9e-05	23.4
WP_173361433.1\|2534095_2535286_-	efflux RND transporter periplasmic adaptor subunit	NA	NA	NA	NA
WP_020926131.1\|2535681_2536746_+	LysR family transcriptional regulator	NA	NA	NA	NA
WP_006386240.1\|2536924_2538046_+	AI-2E family transporter	NA	NA	NA	NA
WP_006386241.1\|2538158_2538926_+	phytanoyl-CoA dioxygenase family protein	NA	NA	NA	NA
WP_024070553.1\|2539130_2539958_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_047991993.1\|2540009_2540912_-	4-hydroxy-tetrahydrodipicolinate synthase	NA	NA	NA	NA
WP_155865350.1\|2540948_2542724_-	ABC transporter permease subunit	NA	NA	NA	NA
WP_024070550.1\|2542728_2543817_-	ABC transporter ATP-binding protein	G3M9Y6	Bacillus_virus	6.2e-30	40.6
WP_006386246.1\|2543839_2544922_-	ABC transporter substrate-binding protein	NA	NA	NA	NA
WP_049054099.1\|2544961_2546389_-	FAD-binding oxidoreductase	NA	NA	NA	NA
WP_024070549.1\|2546609_2547758_+	alpha-hydroxy-acid oxidizing protein	NA	NA	NA	NA
WP_155865351.1\|2547776_2548583_+	pyrroline-5-carboxylate reductase	NA	NA	NA	NA
WP_054439076.1\|2548597_2550043_-	MFS transporter	NA	NA	NA	NA
WP_026382529.1\|2550221_2551076_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_024070545.1\|2551155_2552052_+	DMT family transporter	NA	NA	NA	NA
WP_080684395.1\|2552540_2553020_+	PadR family transcriptional regulator	NA	NA	NA	NA
WP_006385675.1\|2553046_2553862_+	siderophore-interacting protein	NA	NA	NA	NA
WP_035199499.1\|2553946_2554825_-	LysR family transcriptional regulator	A0A2P0ZL89	Lactobacillus_phage	2.3e-06	21.7
WP_006385677.1\|2554929_2555790_+	isocitrate lyase/phosphoenolpyruvate mutase family protein	NA	NA	NA	NA
WP_155865352.1\|2555833_2558710_-	WG repeat-containing protein	NA	NA	NA	NA
WP_155865353.1\|2558706_2561808_-	WG repeat-containing protein	NA	NA	NA	NA
WP_054516409.1\|2562226_2563639_+	HAMP domain-containing histidine kinase	NA	NA	NA	NA
WP_024070539.1\|2563780_2564974_+	MFS transporter	NA	NA	NA	NA
WP_006385683.1\|2565029_2565410_-	cupin domain-containing protein	NA	NA	NA	NA
WP_006385684.1\|2565555_2565795_+	DUF3596 domain-containing protein	A0A1W6JTA0	Pseudomonas_phage	7.0e-11	55.7
WP_006385685.1\|2565791_2566340_+	ureidoglycolate lyase	NA	NA	NA	NA
WP_076467935.1\|2566527_2567985_+	DUF1254 domain-containing protein	M1IA53	Paramecium_bursaria_Chlorella_virus	6.8e-64	35.4
WP_053497387.1\|2568037_2568733_-	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_049055147.1\|2568957_2569599_+	hypothetical protein	NA	NA	NA	NA
WP_006385689.1\|2569848_2570316_+	hypothetical protein	NA	NA	NA	NA
WP_054497360.1\|2570321_2570795_+\|tail	phage tail protein	A4JX08	Burkholderia_virus	1.8e-26	44.4
WP_006385691.1\|2570794_2571085_+	DUF4035 domain-containing protein	S4TND7	Salmonella_phage	9.1e-13	50.0
WP_054505332.1\|2571142_2572429_+\|tail	phage tail tape measure protein	A0A1W6JP49	Morganella_phage	2.2e-13	30.3
WP_080684394.1\|2572425_2572770_+\|tail	phage tail protein	A0A0S2SYI2	Pseudomonas_phage	4.8e-21	38.4
WP_054499929.1\|2572766_2574728_+\|tail	tail fiber domain-containing protein	A0A0K0KVF1	Prochlorococcus_phage	1.9e-13	36.2
WP_006385695.1\|2574730_2575459_+\|tail	phage minor tail protein L	Q6JIL5	Burkholderia_virus	2.2e-71	58.3
WP_155865354.1\|2575461_2576241_+	Mov34/MPN/PAD-1 family protein	A4JX14	Burkholderia_virus	6.6e-66	49.0
WP_112957455.1\|2576237_2576843_+\|tail	tail assembly protein	Q6JIL3	Burkholderia_virus	6.7e-50	55.2
WP_155865355.1\|2576968_2580472_+	DUF1983 domain-containing protein	Q3HQU5	Burkholderia_phage	2.5e-261	45.9
WP_054439116.1\|2580477_2580849_+	hypothetical protein	NA	NA	NA	NA
WP_149895560.1\|2580829_2581066_+	hypothetical protein	NA	NA	NA	NA
WP_026382513.1\|2581062_2581659_+\|tail	tail assembly protein	Q6JIL3	Burkholderia_virus	3.3e-49	53.5
WP_155865356.1\|2581800_2582730_+	LysR family transcriptional regulator	NA	NA	NA	NA
WP_006385703.1\|2582748_2583567_-	SDR family oxidoreductase	W8CYX9	Bacillus_phage	1.4e-10	49.3

DBSCAN-SWA_3

6284300 : 6311373

Burkholderia_phage(29.17%)

terminase,capsid,plate,tail

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_155866421.1\|6284300_6284828_-	hypothetical protein	A0A0E3M0Y2	Rhodoferax_phage	1.1e-24	39.0
WP_155866422.1\|6284824_6285319_-	hypothetical protein	Q775E1	Bordetella_phage	5.6e-63	70.6
WP_155866423.1\|6285315_6285648_-	hypothetical protein	NA	NA	NA	NA
WP_155866424.1\|6285780_6286167_-\|tail	tail fiber assembly protein	A5X9J5	Aeromonas_virus	6.7e-11	44.6
WP_155866425.1\|6286169_6287210_-	hypothetical protein	NA	NA	NA	NA
WP_155866426.1\|6287210_6287861_-	DUF2612 domain-containing protein	Q6IWQ4	Burkholderia_phage	2.8e-33	38.7
WP_155866427.1\|6287857_6289048_-\|plate	baseplate J/gp47 family protein	Q6IWQ3	Burkholderia_phage	3.1e-67	42.0
WP_155866428.1\|6289040_6289385_-	hypothetical protein	NA	NA	NA	NA
WP_155866429.1\|6289381_6290089_-	hypothetical protein	A1Z003	Burkholderia_virus	4.2e-35	43.6
WP_150101668.1\|6290073_6290898_-	hypothetical protein	Q6IWQ0	Burkholderia_phage	2.0e-41	39.7
WP_155866430.1\|6290890_6291199_-	hypothetical protein	Q6IWP9	Burkholderia_phage	8.5e-09	34.3
WP_155866431.1\|6291195_6291738_-	hypothetical protein	NA	NA	NA	NA
WP_155866432.1\|6291737_6293354_-\|tail	phage tail protein	NA	NA	NA	NA
WP_155866433.1\|6293444_6293900_-	hypothetical protein	Q6IWV4	Burkholderia_phage	1.5e-22	50.4
WP_063570010.1\|6293909_6294359_-	hypothetical protein	A0A2H4P6T4	Pseudomonas_phage	7.5e-30	45.6
WP_155866434.1\|6294417_6295926_-	DUF3383 family protein	A0A088C3U1	Shewanella_sp._phage	5.9e-71	35.2
WP_155866435.1\|6295935_6296463_-	hypothetical protein	NA	NA	NA	NA
WP_155866436.1\|6296459_6296828_-	hypothetical protein	NA	NA	NA	NA
WP_155866437.1\|6296824_6297301_-	hypothetical protein	NA	NA	NA	NA
WP_155866438.1\|6297297_6297726_-	DUF4054 domain-containing protein	A0A088C3T8	Shewanella_sp._phage	5.3e-17	36.2
WP_155866439.1\|6297727_6298078_-	hypothetical protein	Q6IWU7	Burkholderia_phage	4.3e-09	37.5
WP_155866440.1\|6298137_6299220_-	DUF2184 domain-containing protein	Q6IWU6	Burkholderia_phage	5.2e-53	34.6
WP_054449246.1\|6299235_6299718_-	hypothetical protein	A0A2H5BG33	Pseudoalteromonas_phage	8.3e-11	32.8
WP_155866441.1\|6299714_6300980_-	DUF2213 domain-containing protein	A0A088C4R4	Shewanella_sp._phage	1.5e-38	36.2
WP_155866659.1\|6300960_6301830_-\|capsid	minor capsid protein	M4T3R2	Psychrobacter_phage	2.8e-17	29.3
WP_155866442.1\|6301741_6303277_-	DUF1073 domain-containing protein	W5S8I3	Pseudomonas_phage	3.3e-101	47.2
WP_155866660.1\|6303273_6304512_-\|terminase	PBSX family phage terminase large subunit	A0A125RNL7	Pseudomonas_phage	5.0e-201	80.8
WP_155866443.1\|6304498_6304918_-\|terminase	terminase small subunit	E5AGA2	Erwinia_phage	2.9e-36	68.6
WP_155866444.1\|6304968_6305265_-	hypothetical protein	NA	NA	NA	NA
WP_155866445.1\|6305261_6305618_-	hypothetical protein	NA	NA	NA	NA
WP_155866446.1\|6305605_6305815_-	hypothetical protein	NA	NA	NA	NA
WP_150101651.1\|6305951_6306320_-	endonuclease	NA	NA	NA	NA
WP_155866447.1\|6306320_6307709_-	replicative DNA helicase	O80281	Escherichia_phage	1.1e-95	45.7
WP_155866448.1\|6307705_6308551_-	hypothetical protein	A0A2H4J0Z7	uncultured_Caudovirales_phage	7.5e-15	41.6
WP_155866449.1\|6308550_6308973_-	hypothetical protein	NA	NA	NA	NA
WP_155866450.1\|6309005_6309416_-	recombination protein NinB	A0A0H5AUD0	Pseudomonas_phage	7.6e-21	48.6
WP_155866451.1\|6309415_6309730_-	MarR family transcriptional regulator	NA	NA	NA	NA
WP_173361496.1\|6309768_6309933_+	hypothetical protein	NA	NA	NA	NA
WP_173361497.1\|6309935_6310193_-	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_173361498.1\|6310275_6311373_+	helix-turn-helix transcriptional regulator	A0A1B0VRI7	Pseudomonas_phage	1.2e-07	30.2

DBSCAN-SWA_4

6319335 : 6325444

Bordetella_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_155866462.1\|6319335_6319779_+	single-stranded DNA-binding protein	R9TPS8	Aeromonas_phage	2.4e-20	46.9
WP_155866463.1\|6319787_6320291_+	siphovirus Gp157 family protein	A0A2I7RAE0	Vibrio_phage	1.1e-13	28.8
WP_155866464.1\|6320524_6321073_+	hypothetical protein	NA	NA	NA	NA
WP_155866465.1\|6321075_6321309_+	hypothetical protein	NA	NA	NA	NA
WP_173361499.1\|6321312_6321495_+	hypothetical protein	NA	NA	NA	NA
WP_173361500.1\|6321491_6322457_+	Lar family restriction alleviation protein	NA	NA	NA	NA
WP_155866467.1\|6322449_6323115_+	hypothetical protein	H2BDG4	Pseudomonas_virus	6.7e-51	49.4
WP_155866468.1\|6323107_6323323_+	hypothetical protein	NA	NA	NA	NA
WP_155866469.1\|6323322_6323613_+	hypothetical protein	NA	NA	NA	NA
WP_173361501.1\|6323889_6324063_+	hypothetical protein	A0A0K1YAW1	Cronobacter_phage	2.5e-10	57.7
WP_155866470.1\|6324071_6324293_+	excisionase	Q774Z6	Bordetella_phage	1.5e-20	78.1
WP_155866471.1\|6324268_6325444_+	DUF3596 domain-containing protein	Q774Z5	Bordetella_phage	9.7e-146	66.5

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_LN890335

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection