ID A8ZXL9_DESOH Unreviewed; 1132 AA.
AC A8ZXL9;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Dole_1171 {ECO:0000313|EMBL:ABW66977.1};
OS Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus
OS oleovorans).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW66977.1, ECO:0000313|Proteomes:UP000008561};
RN [1] {ECO:0000313|EMBL:ABW66977.1, ECO:0000313|Proteomes:UP000008561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3
RC {ECO:0000313|Proteomes:UP000008561};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-2007) 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 -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; CP000859; ABW66977.1; -; Genomic_DNA.
DR RefSeq; WP_012174595.1; NC_009943.1.
DR AlphaFoldDB; A8ZXL9; -.
DR STRING; 96561.Dole_1171; -.
DR KEGG; dol:Dole_1171; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG1379; Bacteria.
DR HOGENOM; CLU_005571_0_0_7; -.
DR OMA; EEGKYHA; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000008561; Chromosome.
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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd19067; PfuEndoQ-like; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 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; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF59; DNA HELICASE; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF89550; PHP domain-like; 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|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:ABW66977.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000008561}.
FT DOMAIN 471..748
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 749..1034
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 492..499
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1132 AA; 122708 MW; B2E0691494D1BBAD CRC64;
MRYIADLHIH SAYSRATSSD LDFEHLYIWA QIKGITVLAT GDYTHPAWFA QISEKLVPAE
PGLFRLKDDL AKVCDAEVPA ACRRPVRFVL STEISNIYKK AGAVRKNHNL VFMPGLKAAA
RFNAKLGAIG NIQSDGRPIL GMDARNLLET ALEVSSDAFF VPAHVWTPWF SLFGSRSGFD
AIEACFEDLT DQVFALETGL SSDPPMNWRV SGIDGRTLIS NSDAHSPANL GREANLFDTE
LSYGAMIDAM KTGDPDRFLG TYEFFPEEGK YHLDGHRDCG IRLHPAQTRQ HQGLCPVCGK
PLTLGVLYRV EELADRDEGS LPAKSHPFYS IIPLPEIISE LVGVGPKSKK VVQAYRSVLE
RLGPEFDILY RLPAEEIVQS GLPLLDVAVS RMREGKVTRS AGYDGAYGRV TLFSDGEIER
LKGEQHLFAV PNAPAPAKQV PLVAAPRQAS LFEAPDVVPA PVVAEPENIT AGLSTAQLAA
VNHGAGPMVI VAGPGSGKTR TITCRMAHLI QARQVPAGAV LAITFTNRAA REMADRLAAM
LGGNTDLPFV STFHGFCLGL LREQGGFDAV VLDEYDRRIL AKTVLKRAAA GKADGLPGPD
RLLDMIASAK QAMLGPGDDL SGVARETAPD LLATLYGDYQ ALLAENSGCD YEDLICRAVD
LLEGHKDVRQ TAQQRFVYIF VDEYQDVNHA QYRLIQALAP AGGNICVIGD PDQAIYGFRG
ASAAYFQTFE TDYPGAARFF LEKNYRSTQT IVSAAYHVIT GQDDDPGRVR VYSDIAGVPV
VTVARLASER AEAVFAGRTI ERMVGGLGFH SVDFGKAGYE APAGLGFADF AVLCRTRRQT
EVFADVLESA GIPCHVVSKQ RIYAARGVGE AISLLRLAEG QATFIDLEKA GGVLYGATAA
KKQAVISAWA KERNLPAAEV LAATERFPVP GLSQAAQRRL AGAARTVAEL KARTGHLPVA
GRLRFLIENM EPLATLVNGS KKNREAFDAA VEAARPAGTD ATAFFDTVAL AADADAVMPG
VDRVRLMTLH AAKGLEFAVV FVAGCEEDLV PFSGYGDRAT DIDEERRLFY VAMTRAKERL
FLTWAKNRTL YGKRKACTLS RFVADIEGDL KEQAEVETGR PPKDGHVQME LF
//