ID   A0A0B8P1B7_9VIBR        Unreviewed;       960 AA.
AC   A0A0B8P1B7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=JCM19231_3239 {ECO:0000313|EMBL:GAM57123.1};
OS   Vibrio ishigakensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1481914 {ECO:0000313|EMBL:GAM57123.1, ECO:0000313|Proteomes:UP000031671};
RN   [1] {ECO:0000313|EMBL:GAM57123.1, ECO:0000313|Proteomes:UP000031671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RA   Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RT   "Vibrio sp. C1 JCM 19231 whole genome shotgun sequence.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAM57123.1, ECO:0000313|Proteomes:UP000031671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19231 {ECO:0000313|Proteomes:UP000031671};
RG   NBRP consortium;
RA   Sawabe T., Meirelles P., Feng G., Sayaka M., Hattori M., Ohkuma M.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAM57123.1}.
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DR   EMBL; BBRZ01000045; GAM57123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B8P1B7; -.
DR   Proteomes; UP000031671; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 3.40.91.30; -; 1.
DR   Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF63; DNA HELICASE IV; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   Pfam; PF01396; zf-C4_Topoisom; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000031671}.
FT   DOMAIN          184..646
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   BINDING         205..212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   960 AA;  108319 MW;  EEB896D88C8AC600 CRC64;
     MSVVSISVNL WGKLTNSFDT VTFEDGTINL YRKGRRIDTI DTDNFQSFTV SSTSWLGGSI
     TLPKSTCLNG LNPKQVSSFT EAINTAIEKR VASRTLSDIK DFELNAVNSF PRDSESKHLA
     QICESIHLLT TQRPSLLSSF GDSDRNLVRL IADFYPLDIA SLRAFHEGNQ LQQREEFYDA
     VESNPLTQEQ RLAVIRNNDR NMVLAAAGTG KTSVMVAKIL DLVDRKIASP SQILTMAYNK
     SAATELDERL SEKAQKSNVH LEERPQISTF HALGRKILQE SGIDTRLSQL TQDSDKLDIW
     VSRWLQTYLL KHFDKLPTLI EMIAPPIDPM SYRSAAAFQR YQRDNTFSTI KGEKVKGFQE
     LLIANYLFIK GVEYEYEPQY PVKQRVSAGV DYRPDFYLPQ ADVYLEHFGI SRDGSTRIDI
     DSVKYNSDIE WKRQFHESNG TKLVETYHYN WVEGTLNNRL DSLISELEIP AHPKNKDEIL
     KHINESDYIS DGAKILRKCL SAIRSEGLSP ATIFQRLTHN DIIDAKSTTD LLTQLHDDYI
     EELRSNESID FDDMINLATE VVASDEFTPS WSQILIDEFQ DISASRMKLI TTIIEMSKTK
     PALTVVGDDW QSIYRFSGGK LELTTRFADL IGSYSETKLQ KTFRYNNSIA KTAGLFVMEN
     PEQYQKQIQT HTVVDTPQVY LLDDKKNGKD ALETKIYEVV SKIRSHDSQG SIAIIGRYNY
     LLSEANIALG KRNARDGVKF WTFHKSKGLE ADYCILIGFS QGKQGFPSDT LENTVVEALL
     PSIDSFPDSE ERRLFYVGVT RAKKKAYIIA DPSSPSKFVT ELLNPKFGVG IHSESFKQAY
     RTTFKCKHCE EGFLKRIEGQ YGDFYTCSTG NGCAVKNVRS CSKCGSPSSD TRSYSVCHNP
     ACGHKSKVCP ACGRPMVKRT GKKGIFWGCS GYSLSHDQCT YTEKLSASDT ETGSSRKKRA
//