ID A0A0N8W6S1_9EURY Unreviewed; 1021 AA.
AC A0A0N8W6S1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=APR53_00065 {ECO:0000313|EMBL:KQC04283.1};
OS Methanoculleus sp. SDB.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1735326 {ECO:0000313|EMBL:KQC04283.1, ECO:0000313|Proteomes:UP000051748};
RN [1] {ECO:0000313|EMBL:KQC04283.1, ECO:0000313|Proteomes:UP000051748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC04283.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-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 -!- 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:KQC04283.1}.
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DR EMBL; LKUD01000053; KQC04283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8W6S1; -.
DR STRING; 1735326.APR53_00065; -.
DR Proteomes; UP000051748; 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:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 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}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 1..299
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 300..588
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 21..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1021 AA; 115929 MW; 5101FCE977437EF1 CRC64;
MQLNQRQQEA VTTTGIQCIL AGPGSGKTRV ITEKIIHLIE QGVAPSEILA LTFSDKAARE
MAERLEKSLG AAGSDIAVYT FHSFCLQVLE DNVLDSGISF SSGIVSRTNQ LVWALRNIDE
FGFEHIEVGN NAPRVLESVI DGISRLRDEL ITPADLDAYL RRKDCCGEGD RDGRERLFHG
RLRDLLRVYE AYERFKREGM LLDFDDMIHE TVRLFERKPY ILALYKQRYR YILVDEFQDT
NYAQLALIKQ LAGDQLCVVG DDDQTIYRFR GAYFGNFDDF RQTYPDLRET LLDENYRNSR
TILAAALQLM AHAPGREDKP LETANPAGEA ITVAECENEN AEAHYVLSEI RRLLETELFD
RGERRKRQVR CGDFAILCRR RAEGVKFYQL LKSHGFPCEF SGEIAFFSMP EVRDMMAWLR
AVKNPLAAGI SLNRIMKAGG VPEAVVQTIN ATAREAAWGV GHSDGVFEAM QAAEGVAPEY
RHGVRELAQS VERLIEKKER ETLSGIVYEV MMRAGAVYRE ALDNDDGRHR LVLNRFYELS
RDYESITKDA RVDDFLEYLS LLSDMDVEMS EPADTDAVQI LTLHKSKGKE FPVVFLVDLS
ERKFPLRYQE KPFSVPRDLA RGLVPEEDEK TLHLQEERRL CYVGMTRAQD RLYLTRAKMY
GDNKHESRPS VFLEELEYAH NPLITVIDVP AEAQDIPFRA QNELEVAKNA LQAQAIRAVV
GMRLGTALQR MMDLEKIRLL EEGEDISAFD RNVFLAVPEA PFTLPGGGDT CAVGPDHVFS
ASALQTYQSC PLQYRFRHVL FIPSEPKSYF GLGTVVHTVI EKLSADELKG IAPTRERARA
MLDRFWSPRA YQSRKHEAED RTKAEILLDS YLGWHLMNDN SLAGIEEKFL FTYHGRTMKG
YIDRIERTPD GGIVVIDFKT GSKPGSLTRT SAKENIQLNL YCLAVRDRYG KLPRRASFLF
LNGNKCVDYF PDDESIELFG RKLSGMIGAI CAGEFPATPS YSACRFCDYT PLCDEQEKET
G
//
