RECQ1_CAEEL
ID RECQ1_CAEEL Reviewed; 631 AA.
AC Q9TXJ8; Q5DX50;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Putative ATP-dependent DNA helicase Q1 {ECO:0000250|UniProtKB:P46063};
DE EC=3.6.4.12;
GN ORFNames=K02F3.12;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP CONCEPTUAL TRANSLATION.
RX PubMed=10049920; DOI=10.1093/genetics/151.3.1027;
RA Kusano K., Berres M.E., Engels W.R.;
RT "Evolution of the RECQ family of helicases: a Drosophila homolog, Dmblm, is
RT similar to the human Bloom syndrome gene.";
RL Genetics 151:1027-1039(1999).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=Q9TXJ8-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=Q9TXJ8-2; Sequence=VSP_039081;
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000255}.
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DR EMBL; FO080195; CCD61879.1; -; Genomic_DNA.
DR EMBL; FO080195; CCD61880.1; -; Genomic_DNA.
DR RefSeq; NP_001022656.1; NM_001027485.2. [Q9TXJ8-1]
DR RefSeq; NP_001022657.1; NM_001027486.3. [Q9TXJ8-2]
DR AlphaFoldDB; Q9TXJ8; -.
DR SMR; Q9TXJ8; -.
DR BioGRID; 40515; 5.
DR STRING; 6239.K02F3.12a; -.
DR EPD; Q9TXJ8; -.
DR PaxDb; Q9TXJ8; -.
DR PeptideAtlas; Q9TXJ8; -.
DR EnsemblMetazoa; K02F3.12a.1; K02F3.12a.1; WBGene00019334. [Q9TXJ8-1]
DR EnsemblMetazoa; K02F3.12b.1; K02F3.12b.1; WBGene00019334. [Q9TXJ8-2]
DR GeneID; 175246; -.
DR KEGG; cel:CELE_K02F3.12; -.
DR UCSC; K02F3.12a; c. elegans.
DR CTD; 175246; -.
DR WormBase; K02F3.12a; CE33668; WBGene00019334; -. [Q9TXJ8-1]
DR WormBase; K02F3.12b; CE38084; WBGene00019334; -. [Q9TXJ8-2]
DR eggNOG; KOG0353; Eukaryota.
DR GeneTree; ENSGT00940000157013; -.
DR InParanoid; Q9TXJ8; -.
DR OMA; FKLSTMV; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q9TXJ8; -.
DR PRO; PR:Q9TXJ8; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019334; Expressed in germ line (C elegans) and 4 other tissues.
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; IPR001763; Rhodanese-like_dom.
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 Alternative initiation; ATP-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..631
FT /note="Putative ATP-dependent DNA helicase Q1"
FT /id="PRO_0000393940"
FT DOMAIN 118..293
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 318..466
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 610..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 237..240
FT /note="DEVH box"
FT /evidence="ECO:0000255"
FT COMPBIAS 610..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_039081"
SQ SEQUENCE 631 AA; 71096 MW; 6A6680785B4AEBB2 CRC64;
MATFIFSRGN IFFYVNKITI PDLMSDVLLS KLSTELADLD GEIGQIDQQI SQLRRKKSEL
TQKRQAIERK IELKTNEDSD VVTDRWDRDG FPWSDEATKI LKEQFHLEKF RPLQRAAINA
VMSKEDAVVI LSTGGGKSLC YQLPALLANG LALVVSPLIS LVEDQILQLR SLGIDSSSLN
ANTSKEEAKR VEDAITNKDS KFRLLYVTPE KLAKSKKMMN KLEKSLSVGF LKLIAIDEVH
CCSQWGHDFR TDYSFLNVLK RQFKGVPILG LTATATSNVL DDVKDMLGIQ AALTFRAGFN
RSNLKYKVVQ KPGSEDECTE EIAKTIKRDF AGQTGIIYCL SRNDCEKVAK ALKSHGIKAK
HYHAYMEPVD RSGAHQGWIS GKIQVIVATV AFGMGIDKPN VRFVIHHSLP KSIENYYQES
GRAGRDGQPA TCILYYRLAD IFKQSSMVQQ ERTGIQNLYN MVRYAADSST CRRVKLAEHF
EEAWEPSWCQ KQCDTCENGN GFVGTSSKES TDVSEAAKTT VRIIEEHLNS AKDGSGRITG
NKLVELLTKK LKGSRNREFC EKLIVNLLLE GYLQEDFHYT VYSVISYVVI GSKWRVYNGK
DAIKMRHVEE SKSRKRKASS SVEEEDVMVL D
