ID RTEL1_RAT Reviewed; 1274 AA. AC Q5RJZ1; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 02-MAR-2010, entry version 33. DE RecName: Full=Regulator of telomere elongation helicase 1; DE EC=3.6.1.-; GN Name=Rtel1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-1274 (ISOFORM 2). RC TISSUE=Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: ATP-dependent DNA helicase required to suppress CC inappropriate homologous recombination, thereby playing a central CC role DNA repair and in the maintenance of genomic stability. CC Antagonizes homologous recombination by promoting the disassembly CC of D loop recombination intermediates. Also required to regulate CC telomere length; probably due to its anti-recombinase function (By CC similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5RJZ1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5RJZ1-2; Sequence=VSP_036956, VSP_036957; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SEQUENCE CAUTION: CC Sequence=EDL88727.1; Type=Erroneous gene model prediction; 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; CH474066; EDL88727.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC086436; AAH86436.1; -; mRNA. DR IPI; IPI00781945; -. DR IPI; IPI00782143; -. DR RefSeq; XP_001057789.1; -. DR RefSeq; XP_342603.3; -. DR UniGene; Rn.98315; -. DR STRING; Q5RJZ1; -. DR Ensembl; ENSRNOT00000055030; ENSRNOP00000051909; ENSRNOG00000027513; Rattus norvegicus. DR GeneID; 362288; -. DR KEGG; rno:362288; -. DR CTD; 362288; -. DR RGD; 1306721; Rtel1. DR eggNOG; roNOG11890; -. DR ArrayExpress; Q5RJZ1; -. DR Genevestigator; Q5RJZ1; -. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0010569; P:regulation of double-strand break repair vi...; ISS:UniProtKB. DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB. DR InterPro; IPR013020; DNA_helicase_DNA-repair_Rad3. DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3. DR InterPro; IPR006554; Helicase-like_DEXD_c2. DR InterPro; IPR006555; Helicase_ATP-dep_c2. DR InterPro; IPR006935; Restrct_endonuc_I_R/III_Res. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00488; DEXDc2; 1. DR SMART; SM00491; HELICc2; 1. DR TIGRFAMs; TIGR00604; rad3; 1. DR PROSITE; PS00690; DEAH_ATP_HELICASE; FALSE_NEG. DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; DNA damage; DNA repair; KW DNA-binding; Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; KW Nucleotide-binding; Nucleus. FT CHAIN 1 1274 Regulator of telomere elongation helicase FT 1. FT /FTId=PRO_0000370613. FT DOMAIN 7 296 Helicase ATP-binding. FT NP_BIND 42 49 ATP (By similarity). FT MOTIF 151 167 Nuclear localization signal (Potential). FT MOTIF 250 253 DEAH box. FT MOTIF 871 877 Nuclear localization signal (Potential). FT METAL 145 145 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 163 163 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 172 172 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 207 207 Iron-sulfur (4Fe-4S) (By similarity). FT VAR_SEQ 995 998 SKQG -> R (in isoform 2). FT /FTId=VSP_036956. FT VAR_SEQ 1112 1139 RFGMFIRRHHKPRFVQTCADLMGLPTIG -> S (in FT isoform 2). FT /FTId=VSP_036957. SQ SEQUENCE 1274 AA; 141779 MW; CF7D27F451824347 CRC64; MPRVVLNGVT VDFPFQPYPC QQEYMTKVLE CLQKKVNGIL ESPTGTGKTL CLLCTTLAWR EHLRDAVSSL KIAERVQGEL FASRTLSSWR SAADANGDSI DCYTDIPKII YASRTHSQLT QVIGELRNTS YRPKVCVLGS REQLCIHPEV KKQESNHMQI SLCRKKVASR SCHFYNNVEE KSLEQELATP ILDIEDLVKN GSKHKVCPYY LSRNLKQQAD IIFMPYNYLL DAKSRKAHNI DLKGTVVIFD EAHNVEKICE ESASFDLTPR DVASGLEVIN QVLEEQARVA QHGELQQEFI IDTSSSGLNM ELEDIAKLKM ILLHLEEAID AVQLPGDDRG VTKPGSYIFE LFAEAQITFQ TKGCILESLD QIIQHLTGRT GVFTNTAGLQ KLMDIIQIVF SVDPLEGSPG SQVGLGSSHF YKVHIHPETS HRRAAQRSDA WSTTASRKQG KVLSYWCFSP SHSMRELVQQ GVRTLILTSG TLAPLSSFAL EMQIPFPVCL ENPHIIDKNQ LWVGVIPRGP DGVQLSSAYD KRFSEECLSS LGKALGNIAR VVPHGLLVFF PSYPVMEKSL EFWQAQGMSK KVEALKPLFV EPRNKGSFSE VIDAYYQQVA SPGSNGATFL AVCRGKASEG LDFSDMNGRG VIVTGLPYPP RMDPRVILKM QFLDEMKGRS RVGGQCLSGQ EWYQQQASRA VNQAIGRVIR HRHDYGAIFL CDHRFAYADA RAHLPSWVRP YLKVYDNFGR VIRDVAQFFR VAQKAMPLPV PQAVTSSVSE GEAAVKEATL SSHSLSTRKA MSLDVHVPSL RRRPVGLPTA GDSESSVCVE YEQQTFSAQK RPMGLLAALE YNEQKAGASE EQALSSSTPS LRCEKRLSVE QRGGKKKVRL VNHPEEPVAG TQAGRAKMFM VAVKQALSQA NFDTFTQALQ HYKSSDDFEA LVASLTCLFA EDPKKHTLLK GFYQFVRPHH KQQFEDICFQ LTGQRCSYQP GNSLPFGEQA QSTASKQGRR ELESKLTLSE GADRQLDPGE HLNQGWPHLS THLTSKGDTS NCPKVGCVGE KPGQPAVNDY LSDVHKALGS ASCNQLTAAL RAYKQDDDLD KVLAVVAALT TAKPEHLSLL QRFGMFIRRH HKPRFVQTCA DLMGLPTIGK GLELPCPRDE STTVPSELTH EDMKPGPSTS KKPEKTQSKI SSFLRQRPDQ SARSDDTIMQ LPPRLPPEHT TSQWNFVCPA CATEDTVLFQ CPSCDFCRCR ACWQRQLQAS RLCPACGAVN RKQSIAQVIW PKPQ //