WRN_CAEEL
ID WRN_CAEEL Reviewed; 1056 AA.
AC Q19546;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=ATP-dependent helicase wrn-1 {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q14191};
DE AltName: Full=Werner syndrome protein homolog {ECO:0000305};
GN Name=wrn-1; ORFNames=F18C5.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 REPEATS.
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: Essential for the formation of DNA replication focal centers;
CC stably associates with foci elements generating binding sites for RP-A.
CC Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity. May
CC be involved in the control of genomic stability (By similarity).
CC {ECO:0000250}.
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:Q14191}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; FO080970; CCD68193.1; -; Genomic_DNA.
DR PIR; T16087; T16087.
DR RefSeq; NP_495324.2; NM_062923.5.
DR AlphaFoldDB; Q19546; -.
DR SMR; Q19546; -.
DR BioGRID; 39420; 14.
DR IntAct; Q19546; 4.
DR MINT; Q19546; -.
DR STRING; 6239.F18C5.2; -.
DR EPD; Q19546; -.
DR PaxDb; Q19546; -.
DR PeptideAtlas; Q19546; -.
DR EnsemblMetazoa; F18C5.2.1; F18C5.2.1; WBGene00006944.
DR GeneID; 174081; -.
DR KEGG; cel:CELE_F18C5.2; -.
DR UCSC; F18C5.2; c. elegans.
DR CTD; 174081; -.
DR WormBase; F18C5.2; CE31791; WBGene00006944; wrn-1.
DR eggNOG; KOG0351; Eukaryota.
DR GeneTree; ENSGT00940000159168; -.
DR HOGENOM; CLU_001103_14_3_1; -.
DR InParanoid; Q19546; -.
DR OMA; NCVIMAT; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q19546; -.
DR BRENDA; 3.6.4.12; 1045.
DR Reactome; R-CEL-5693607; Processing of DNA double-strand break ends.
DR PRO; PR:Q19546; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006944; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005694; C:chromosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:WormBase.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006259; P:DNA metabolic process; IDA:WormBase.
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 GO; GO:0044806; P:G-quadruplex DNA unwinding; IBA:GO_Central.
DR GO; GO:0010259; P:multicellular organism aging; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:WormBase.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.80; -; 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; IPR029491; Helicase_HTH.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF14493; HTH_40; 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF47819; SSF47819; 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.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..1056
FT /note="ATP-dependent helicase wrn-1"
FT /id="PRO_0000205048"
FT REPEAT 17..26
FT /note="1"
FT /evidence="ECO:0000269|PubMed:10049920"
FT REPEAT 28..37
FT /note="2"
FT /evidence="ECO:0000269|PubMed:10049920"
FT DOMAIN 236..406
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 427..583
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 806..886
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328,
FT ECO:0000305"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 17..37
FT /note="2 X 10 AA repeats of N-[ED]-E-L-P-E-T-E-P-E"
FT REGION 749..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 348..351
FT /note="DEAH box"
FT COMPBIAS 20..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1056 AA; 118523 MW; 99C23E70D06DAA0B CRC64;
MISDDDDLPS TRPGSVNEEL PETEPEDNDE LPETEPESDS DKPTVTSNKT ENQVADEDYD
SFDDFVPSQT HTASKIPVKN KRAKKCTVES DSSSSDDSDQ GDDCEFIPAC DETQEVPKIK
RGYTLRTRAS VKNKCDDSWD DGIDEEDVSK RSEDTLNDSF VDPEFMDSVL DNQLTIKGKK
QFLDDGEFFT DRNVPQIDEA TKMKWASMTS PPQEALNALN EFFGHKGFRE KQWDVVRNVL
GGKDQFVLMS TGYGKSVCYQ LPSLLLNSMT VVVSPLISLM NDQVTTLVSK GIDAVKLDGH
STQIEWDQVA NNMHRIRFIY MSPEMVTSQK GLELLTSCRK HISLLAIDEA HCVSQWGHDF
RNSYRHLAEI RNRSDLCNIP MIALTATATV RVRDDVIANL RLRKPLITTT SFDRKNLYIS
VHSSKDMAED LGLFMKTDEV KGRHFGGPTI IYCQTKQMVD DVNCVLRRIG VRSAHYHAGL
TKNQREKAHT DFMRDKITTI VATVAFGMGI DKPDVRNVIH YGCPNNIESY YQEIGRAGRD
GSPSICRVFW APKDLNTIKF KLRNSQQKEE VVENLTMMLR QLELVLTTVG CRRYQLLKHF
DPSYAKPPTM QADCCDRCTE MLNGNQDSSS SIVDVTTESK WLFQVINEMY NGKTGIGKPI
EFLRGSSKED WRIKTTSQQK LFGIGKHIPD KWWKALAASL RIAGYLGEVR LMQMKFGSCI
TLSELGERWL LTGKEMKIDA TPILLQGKKE KAAPSTVPGA SRSQSTKSST EIPTKILGAN
KIREYEPANE NEQLMNLKKQ EVTGLPEKID QLRSRLDDIR VGIANMHEVA PFQIVSNTVL
DCFANLRPTS ASNLEMIDGM SAQQKSRYGK RFVDCVVQFS KETGIATNVN ANDMIPPELI
SKMQKVLSDA VRRVYTEHLI SRSTAKEVAT ARGISEGTVY SYLAMAVEKG LPLHLDKLNV
SRKNIAMALN AVRVHLGSNV AVLTPWVEAM GVVPDFNQLK LIRAILIYEY GLDTSENQEK
PDIQSMPSTS NPSTIKTVPS TPSSSLRAPP LKKFKL
