ID Q9KQK8_VIBCH Unreviewed; 646 AA.
AC Q9KQK8;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=ATP-dependent helicase, DinG family {ECO:0000313|EMBL:AAF95138.1};
GN OrderedLocusNames=VC_1990 {ECO:0000313|EMBL:AAF95138.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF95138.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF95138.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC {ECO:0000256|ARBA:ARBA00038058}.
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DR EMBL; AE003852; AAF95138.1; -; Genomic_DNA.
DR PIR; E82133; E82133.
DR RefSeq; NP_231624.1; NC_002505.1.
DR RefSeq; WP_001881716.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KQK8; -.
DR STRING; 243277.VC_1990; -.
DR DNASU; 2613494; -.
DR EnsemblBacteria; AAF95138; AAF95138; VC_1990.
DR KEGG; vch:VC_1990; -.
DR PATRIC; fig|243277.26.peg.1901; -.
DR eggNOG; COG1199; Bacteria.
DR HOGENOM; CLU_012117_2_0_6; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:AAF95138.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000584}.
FT DOMAIN 11..275
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 646 AA; 71685 MW; 622039169F9476D8 CRC64;
MIEKTFSQQG ALGQAIPGFQ PRQAQVDMAK AVASAIANQS QLVVEAGTGT GKTFAYLVPA
LLSGKKVIIS TGSKNLQEQL FHRDLPLMVS ALGFFGQVAL LKGRANYLCL DRLSRQMVES
HTPESDPTLL TQLVKVRSWA SSTQSGDLGE CDDLAEDSPI IPTITSTNDN CLGKECASYQ
DCFVSKARRR AMDADVVVVN HHLFLADLAI KETGFGELIP EAEVFIFDEA HQLPDIASQY
FGQSVSSRQV QDLAKDIELG YRTEAKDMRQ LQKVSDKLVQ AAMDLRIVLG EPGYRGNWRE
VLKVPTVARE VERLNEALQF ALDVLKLALG RSQLLDTAFE RATLILGRIR RVCDVSVTGY
SYWYDTTPRH FSLHITPLSV ADKFREQIAL KEGAWIFTSA TLAVNEDFSH FTERLGLTPS
AQFSLVSPFD YQQQAVLCVP RYLPEPNSSG LAEKLVRMLA PVIEHNQGRC FFLCTSHSMM
RDLGERFRER LTLPVLMQGE TSKQKTLAEF MELGNALLVA TGAFWEGIDV RGDTLSCVII
DKLPFTAPDD PLLKARIEDC RLRGGDPFAQ VQLPEAVITL KQGVGRLIRD KNDKGALIIC
DNRLVTRDYG GVFLASLPPI PRTRDLDVVT TFLQQLAITE INQRDS
//
