RECQ1_CAEBR
ID RECQ1_CAEBR Reviewed; 618 AA.
AC A8WK63;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Putative ATP-dependent DNA helicase Q1 {ECO:0000250|UniProtKB:P46063};
DE EC=3.6.4.12;
GN ORFNames=CBG24191;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP20856.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: DNA helicase that may play a role in the repair of DNA that
CC is damaged by ultraviolet light or other mutagens. Exhibits a
CC magnesium-dependent ATP-dependent DNA-helicase activity that unwinds
CC single- and double-stranded DNA in a 3'-5' direction (By similarity).
CC {ECO:0000250|UniProtKB:P46063}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46063}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000255}.
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DR EMBL; HE601517; CAP20856.1; -; Genomic_DNA.
DR RefSeq; XP_002640754.1; XM_002640708.1.
DR AlphaFoldDB; A8WK63; -.
DR SMR; A8WK63; -.
DR STRING; 6238.CBG24191; -.
DR EnsemblMetazoa; CBG24191.1; CBG24191.1; WBGene00042359.
DR GeneID; 8582748; -.
DR KEGG; cbr:CBG_24191; -.
DR CTD; 8582748; -.
DR WormBase; CBG24191; CBP13372; WBGene00042359; -.
DR eggNOG; KOG0353; Eukaryota.
DR HOGENOM; CLU_001103_12_5_1; -.
DR InParanoid; A8WK63; -.
DR OMA; FKLSTMV; -.
DR OrthoDB; 445763at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..618
FT /note="Putative ATP-dependent DNA helicase Q1"
FT /id="PRO_0000393939"
FT DOMAIN 95..270
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 295..443
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 586..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 214..217
FT /note="DEVH box"
FT /evidence="ECO:0000255"
FT COMPBIAS 586..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 618 AA; 69563 MW; 053851EE4DDD49CE CRC64;
MSNVLLSKLS SELADLDGQV SQIDQQISQL RRKKAELIQK KQALERKIEM KTNEDSDVVL
DRWDQDSFPW SDEANQILKN KFRLEKFRPL QSAAINAVMS KEDAIVILST GGGKSLCYQL
PALLAKGLTL VISPLVSLVE DQIMQLQKLG IDAASLNANT PKDEAKRVEQ AITKGSTELR
LLYVTPEKLA KSKRMMNQLE KSLGVGYLKL IAIDEVHCCS QWGHDFRTDY SFLNVLKRQF
KGVPILGLTA TATSNVLDDV KKMLGIPVAI VFRAGFNRAN LNYKVLTKPG SEDECVEKIV
RTIKRKFSGK TGIIYCLSRN DCEKLAKSLK ANGIRAKHYH AYMEPVDRSA AHQKWVSGEI
QVIVATVAFG MGIDKPDVRF VIHHSLPKSI ENYYQESGRA GRDGLPATCI LYYRMSDIFK
QSSMIQQEQT GIANLYNMVR YASDTVTCRR VKLAEHFEEA WEPSWCQKQC DVCEKSSNSP
GTATEDVSKE AVVVINIIEE NLSSAKDGSG RITGNKLLDL LSKKLKGRRT KDFCEKLIVH
LLLESYLQED FHYTVYSVIS YVVVGLKWRV YNRKDEIPMT LDNTKKGRAE ENNRKRKAAV
TSSDEEVDVG DDDDVITL
