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 12-OCT-2022, entry version 158. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 //