ID A0A1G3Q805_9SPIR Unreviewed; 1279 AA.
AC A0A1G3Q805;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=A2096_14115 {ECO:0000313|EMBL:OHD62837.1};
OS Spirochaetes bacterium GWF1_41_5.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802188 {ECO:0000313|EMBL:OHD62837.1, ECO:0000313|Proteomes:UP000176667};
RN [1] {ECO:0000313|EMBL:OHD62837.1, ECO:0000313|Proteomes:UP000176667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHD62837.1}.
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DR EMBL; MIBC01000097; OHD62837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3Q805; -.
DR Proteomes; UP000176667; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd22352; RecB_C-like; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.3170.10; Recbcd, chain B, domain 2; 1.
DR HAMAP; MF_01485; RecB; 1.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR004586; RecB.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-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}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 7..493
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 563..834
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1279 AA; 144911 MW; D54230EF59B072E5 CRC64;
MRKPDNKERP AFDMAAPDLL CGAAVITASA GTGKTYCLER LYVRMLLGLG TADSGAPGPE
RILAVTFTEK AALEMKERIR SLIYSYLEEP EKLHELFPRI TPGQKKQYLQ HLESTRHKFD
QAAIYTIHGF CRRLLAEYPA ESGTQGAYET GDTSELLSRA VHETLRLYFT SSPPASKDIC
IINWLREHFY IKSFNEPANI MNIEKVFCRV IASSLPHEET YDFFPSCALF NNTSAESLLK
KTAEKISILH HLLEQTGAEN IRAYLADSGV NPVKDLCGII EKFKNDFSPE NLKNLQPDAL
PKIQNNLYYL LAGRSNDSSG FTDGVKILAG LFSGRAASFF RAVYNALLSI YEYRVLEIFF
AENVNIPAEL AVIFSGINSR FTRLKQEKKI TGFDDLLLQV YRAFSAADSR LLALVQEKYC
AVLIDEFQDT DAVQWKIFRL LCGHRKNFPL FLIGDPKQSI YHFRGGNLPT FFSALETVPD
TRHYELKDNY RSHPDLVAKF NILFKNIFCV WNTCHTAPLP ETIMPQGGKF LGLLKNNLEK
STLHNLLSAY RGTEKIPADF YYQQVNAGKN SRWAGFTENA GKIILYDLSG SGSETLSAEK
VRRHSRKYVA AEIFRLLSSG LKKNNGEKLC PGDIAVLCDK NEQCRQTVKD LCDLGLKAVF
TRQGSVWKTD EAFEIKLFFE GLVKFRHPGC LKGALTSSLL GINEQTVCEL EEQGLLDRWG
AQFEKWENMI TEKKVYKVIL EALYKTCDPE IPHDFFRRSL SASRGSRTCA NMLHLAELLH
EAVYRENLDS QEILAFINKK ISAENGVFSE EESEVRLDSD LEAVEVLTLH AAKGLEWPVV
FIMSSDAPKS PAVLDSFYYE NKRLFTLSGR IAGSSRKNRE IPVSSELGSI LKKFSREEKF
RLFYVGFTRA QSLLYIPFIP QGARSTCYLH DFYRELLGYG DDDALNHPGP LLDRYKDVFQ
TVACTAELPE PEDDKKKSQA GTAFRAAEPP PEKLRLKCLP VESYSSLSRG LIFSKTDGKA
GDESGENQPQ HPAVNRFNFA AGPQTGNLFH SLFEKIDYSL LCGHNPDSFM ADSGIDRKFQ
AAAKLQYSAL KYQAYASLIK DIFFETLKVP LGSDEKKFTL ADIPSCRRRH EFQFLLPLAE
SALCLDIKDR SRKLLKTPEG YLYGIIDLVF MHNDKYYIAD WKSNCLGDDS GSYHEQNIIA
AMQEHDYFLQ YYLYTLGLYV FLSASLPGFD YDRDFGGVYY FFIRGMSKEY PGRGVFFDRP
AKNMIEELCS ALLRKKPGN
//
