ID Q64AB0_9ARCH Unreviewed; 781 AA.
AC Q64AB0;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=RecQ {ECO:0000313|EMBL:AAU83667.1};
GN ORFNames=GZ32E7_30 {ECO:0000313|EMBL:AAU83667.1};
OS uncultured archaeon GZfos32E7.
OC Archaea; environmental samples.
OX NCBI_TaxID=285378 {ECO:0000313|EMBL:AAU83667.1};
RN [1] {ECO:0000313|EMBL:AAU83667.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15353801; DOI=10.1126/science.1100025;
RA Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA Richardson P.M., DeLong E.F.;
RT "Reverse methanogenesis: testing the hypothesis with environmental
RT genomics.";
RL Science 305:1457-1462(2004).
RN [2] {ECO:0000313|EMBL:AAU83667.1}
RP NUCLEOTIDE SEQUENCE.
RA Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL Submitted (AUG-2004) 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=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; AY714855; AAU83667.1; -; Genomic_DNA.
DR AlphaFoldDB; Q64AB0; -.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:AAU83667.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 32..203
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 229..373
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 707..781
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
SQ SEQUENCE 781 AA; 88548 MW; 0E5091E453A40BC3 CRC64;
MSTNSSQAQD PLTILNSVFN HHTFRSRQEE IISNVLAQKN TLAILPTGVG KSICFQIPAL
IFDGLTVVVS PLIALMKDQV DNLKKHGIFE AAYINSMLDQ ATKERIHKLL KESKLKMLYV
APETFVDNKL MSILKTCNIS LIAIDEVHCI SVWGHNFRPD YLRLQRVIAD LHNPPPPVLG
LTATATRTVE EDIQKQLGIE CDVFKDSFDR KNLLFSVIPM KNNNRKELSL KRLLGQLKGS
TIVYVNFTKT AEWLATYLAD SGLSASYYHG QIRDSEERKR IQNDFINGRT RIVVATNAFG
MGIDKEDIRA IIHYNLPKSI ENYYQEVGRA GRDQNISNCI LLYSKGDEIQ LRKLIQRNTP
SAEQIKAVLD LLTQGEGDLI YVNVKRLANE LTLDEVPIRL ILHNLERLGA LKTYFKIFKR
AVVSVQHADF GSLKYRHEAE RIYKNAYFNA SLNRWMDLDM LSSAVQISVP QINNVLRELK
TAGMIELVER DFCTPVKVYP GIKDVDIMDL LQILLRLETN SMKKIDKIVE YVESRECKRK
FILNYFGEDY DGDCNACSIC NPLLSLIGDG FERSTEPQPE LRPATGEEEL LDESATIAFS
ILELVRTLDF HVGRTFLANI LIGSKSKRIL EQNLQESRYY GILKGYTAEV ARTIIDQMIA
KGYLITKQGS SSYPRPQLYL TELAEKALKE QIPIALQLPV KKVEISETGN LSVLEALKAW
RKRIAAENSI PAYCVFHDST LIGIANRLPK TTQELQTIKG IGERKIENYG DEILEIVEAI
E
//
