ID A0A233HJ40_9VIBR Unreviewed; 724 AA.
AC A0A233HJ40;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN ORFNames=B9J89_14510 {ECO:0000313|EMBL:OXX61356.1};
OS Vibrio sp. V15_P4S5T153.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1938669 {ECO:0000313|EMBL:OXX61356.1, ECO:0000313|Proteomes:UP000215241};
RN [1] {ECO:0000313|EMBL:OXX61356.1, ECO:0000313|Proteomes:UP000215241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V15_P4S5T153 {ECO:0000313|EMBL:OXX61356.1,
RC ECO:0000313|Proteomes:UP000215241};
RA Vazquez-Rosas-Landa M.;
RT "High clonality and local adaptation shapes Vibrionaceae linages within an
RT endangered oasis.";
RL Submitted (FEB-2017) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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:OXX61356.1}.
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DR EMBL; NDIJ01000017; OXX61356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A233HJ40; -.
DR Proteomes; UP000215241; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR005753; DNA_helicase_ATP-dep_UvrD.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR01075; uvrD; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
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}.
FT DOMAIN 9..287
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 288..565
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 724 AA; 82630 MW; DCCC4FE93FD83165 CRC64;
MMDPSLLLDG LNDKQREAVA APLENLLVLA GAGSGKTRVL VHRIAWLISV ENASPFSVMS
VTFTNKAAAE MRGRIEELMM GSASGMWNGT FHGICHRILR AHYLDARLPE DFQILDSEDQ
LRLLRRLIKA QNLDEKQWPT RQVCWWINGK KDEGLRPKHI DAYRDPVTQT YLQLYSAYQE
ACDRAGLVDF AEILLRCHEM LRDKQHIREH YQARFKHILV DEFQDTNNIQ YAWLRMMAGR
DCHLMIVGDD DQSIYGWRGA KIENLEKFTQ EFPSVNTIRL EQNYRSTKTI LQASNALIAN
NTERMGKELW TDGSEGEPIS IYSAYNDLDE ARFTVNKIKE WRDKGGALED CAMLYRNNAQ
SRVLEEALIQ AGLPYRIYGG MRFFERQEIK DALSYLRLMS NRNDDSAFER VVNTPPRGLG
DKTLETIRFA ARDRGCTLWQ ASLVLLEEKV LTGRAASALS RFIELVNALE DDSAEMPLHS
QTDHVIKTSG LFEMYQLEKG EKSKARIENL EELVTATRQF EKPEEADEMS MLTAFLTHAA
LEAGEGQADE FDDAVQLMTL HSAKGLEFPL VFMVGVEEGM FPSQMSAEEA GRLEEERRLC
YVGMTRAMQK LYITYAEIRR LYGQDKYHKP SRFIRELPEN CLDEVRMKAQ VSRPSSAGRF
SQTAVKENFN ETGFSLGARV KHPIFGEGTI INFEGSGPQS RVQVAFNGEG IKWLVTAYAK
LEKL
//
