ID ERCC5_XENLA Reviewed; 1196 AA. AC P14629; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 04-NOV-2026, entry version 118. DE RecName: Full=DNA excision repair protein ERCC-5 homolog {ECO:0000305}; DE EC=3.1.-.- {ECO:0000250|UniProtKB:P28715}; DE AltName: Full=DNA repair protein complementing XP-G cells homolog; DE AltName: Full=Xeroderma pigmentosum group G-complementing protein homolog; GN Name=ercc5; Synonyms=xpg, xpgc; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8483504; DOI=10.1038/363182a0; RA Scherly D., Nouspikel T., Corlet J., Ucla C., Bairoch A., Clarkson S.G.; RT "Complementation of the DNA repair defect in Xeroderma pigmentosum group G RT cells by a human cDNA related to yeast RAD2."; RL Nature 363:182-185(1993). CC -!- FUNCTION: Single-stranded structure-specific DNA endonuclease involved CC in DNA excision repair. Makes the 3'incision in DNA nucleotide excision CC repair (NER). Binds and bends DNA repair bubble substrate and breaks CC base stacking at the single-strand/double-strand DNA junction of the CC DNA bubble. Plays a role in base excision repair (BER) by promoting the CC binding of DNA glycosylase to its substrate and increasing DNA CC glycosylase catalytic activity that removes oxidized pyrimidines from CC DNA. Involved in transcription-coupled nucleotide excision repair (TCR) CC which allows RNA polymerase II-blocking lesions to be rapidly removed CC from the transcribed strand of active genes. Required for DNA CC replication fork maintenance and preservation of genomic stability. CC Involved in homologous recombination repair (HRR) induced by DNA CC replication stress. During HRR, binds to the replication fork with high CC specificity and stabilizes it. {ECO:0000250|UniProtKB:P28715}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P28715}; CC Note=Binds 2 magnesium ions per subunit. They probably participate in CC the reaction catalyzed by the enzyme. May bind an additional third CC magnesium ion after substrate binding. {ECO:0000250}; CC -!- SUBUNIT: Monomer. Homodimer. {ECO:0000250|UniProtKB:P28715}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28715}. CC Chromosome {ECO:0000250|UniProtKB:P28715}. CC -!- DOMAIN: Both nuclear localization signals 1 and 2 act as a monopartite CC signal which binds to the high affinity site on importin-alpha. CC {ECO:0000250|UniProtKB:P28715}. CC -!- DOMAIN: Both the spacer region (also known as the recognition (R) CC domain) and C-terminal domain are required for stable binding to the CC DNA repair bubble. However, both domains are dispensable for incision CC of DNA bubble structures. {ECO:0000250|UniProtKB:P28715}. CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG 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; X69977; CAA49597.1; -; mRNA. DR PIR; S35994; S35994. DR AlphaFoldDB; P14629; -. DR SMR; P14629; -. DR AGR; Xenbase:XB-GENE-960384; -. DR Xenbase; XB-GENE-960384; ercc5.L. DR OMA; AAEMRMM; -. DR Proteomes; UP000186698; Unplaced. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro. DR GO; GO:0000014; F:single-stranded DNA endonuclease activity; IBA:GO_Central. DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central. DR GO; GO:0009411; P:response to UV; IEA:UniProtKB-ARBA. DR CDD; cd09904; H3TH_XPG; 1. DR CDD; cd09868; PIN_XPG_RAD2; 2. DR FunFam; 3.40.50.1010:FF:000023; DNA repair protein complementing XP-G cells; 1. DR FunFam; 1.10.150.20:FF:000037; DNA repair protein complementing XP-G cells homolog; 1. DR FunFam; 3.40.50.1010:FF:000022; DNA repair protein complementing XP-G cells homolog; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.40.50.1010; 5'-nuclease; 2. DR InterPro; IPR036279; 5-3_exonuclease_C_sf. DR InterPro; IPR008918; HhH2. DR InterPro; IPR029060; PIN-like_dom_sf. DR InterPro; IPR006086; XPG-I_dom. DR InterPro; IPR006084; XPG/Rad2. DR InterPro; IPR001044; XPG/Rad2_eukaryotes. DR InterPro; IPR019974; XPG_CS. DR InterPro; IPR006085; XPG_DNA_repair_N. DR NCBIfam; TIGR00600; rad2; 1. DR PANTHER; PTHR16171:SF11; DNA EXCISION REPAIR PROTEIN ERCC-5; 1. DR PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1. DR Pfam; PF00867; XPG_I; 1. DR Pfam; PF00752; XPG_N; 1. DR PRINTS; PR00853; XPGRADSUPER. DR PRINTS; PR00066; XRODRMPGMNTG. DR SMART; SM00279; HhH2; 1. DR SMART; SM00484; XPGI; 1. DR SMART; SM00485; XPGN; 1. DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1. DR SUPFAM; SSF88723; PIN domain-like; 1. DR PROSITE; PS52064; UBM; 1. DR PROSITE; PS00841; XPG_1; 1. DR PROSITE; PS00842; XPG_2; 1. PE 2: Evidence at transcript level; KW Chromosome; DNA damage; DNA repair; DNA-binding; Endonuclease; Hydrolase; KW Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome. FT CHAIN 1..1196 FT /note="DNA excision repair protein ERCC-5 homolog" FT /id="PRO_0000154033" FT DOMAIN 184..219 FT /note="UBM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01409" FT REGION 1..78 FT /note="N-domain" FT /evidence="ECO:0000250|UniProtKB:P28715" FT REGION 31..67 FT /note="DNA-binding; may bind to the undamaged single-strand FT DNA of the DNA repair bubble" FT /evidence="ECO:0000250|UniProtKB:P28715" FT REGION 79..818 FT /note="Spacer region" FT /evidence="ECO:0000250|UniProtKB:P28715" FT REGION 152..176 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 302..321 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 629..661 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 722..758 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 819..914 FT /note="I-domain" FT /evidence="ECO:0000250|UniProtKB:P28715" FT REGION 853..869 FT /note="DNA-binding; may bind to the undamaged single-strand FT DNA of the DNA repair bubble" FT /evidence="ECO:0000250|UniProtKB:P28715" FT REGION 881..913 FT /note="DNA-binding; H2TH (helix-2turn-helix) motif which FT binds double-stranded DNA" FT /evidence="ECO:0000250|UniProtKB:P28715" FT REGION 945..951 FT /note="DNA-binding; may bind double-stranded DNA" FT /evidence="ECO:0000250|UniProtKB:P28715" FT REGION 1075..1196 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1079..1095 FT /note="Nuclear localization signal 1" FT /evidence="ECO:0000250|UniProtKB:P28715" FT MOTIF 1179..1196 FT /note="Nuclear localization signal 2" FT /evidence="ECO:0000250|UniProtKB:P28715" FT COMPBIAS 154..168 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 311..321 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 722..731 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 734..755 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1119..1130 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1142..1158 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 30 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P39748" FT BINDING 77 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P39748" FT BINDING 822 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P39748" FT BINDING 824 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P39748" FT BINDING 843 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P39748" FT BINDING 845 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P39748" FT BINDING 894 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P39748" SQ SEQUENCE 1196 AA; 134207 MW; 1F1CE1891A3C0623 CRC64; MGVQGLWKLL ECSGRPINPG TLEGKILAVD ISIWLNQAVK GARDRQGNAI QNAHLLTLFH RLCKLLFFRI RPIFVFDGEA PLLKRQTLAK RRQRTDKASN DARKTNEKLL RTFLKRQAIK AALSGNKQSN EELPSFSQVP RKETEDLYIL PPLEDNENNS SEEEEEREWE ERMNQKQRLQ EDFFANPSSV DIESEEFKSL PPEVKHEILT DMKDFTKRRR TLFEAMPEDS SDFSQYQLKG LLKKNDLNKC IDNVRKELNQ QYSGEVQAQF ESEGGFLKEV ETRRLVSEDD SHYILIKGIQ SKQEEKKVDS PPQSITFNSS QTPKTYLDLK LASAHKTKPL QTSSAEAAPP SPRTLFAIQE AMAESWDHEK HEKPSVSGCE AEGNVSPRTL QAIYQVLAED EAGESNKIKV VLQSDEERKP KTKVLVISSS DEEDDCLNYQ DGTKTTLGAS LIKSISPSSM QCQESTADSL PNYTRSKPVS QIEEPMADHN LQGDNCNVPN AKDKLIVPPS LGNVDKPIIL SNTIPVNSEF RIPLLPVNMS MRETVIIPNN TGSLGSSRYI SLERDATKQG FSDNPVGDLV RSPDEPALNA SSALSDRKTS ATQSLLCNNI ECTEQSMVQG CSNTLDVTQT TQPSGGSEVN KPAEYNPQDK KVFGSNDSSA MYVPMTPESI IVSDEEFVNE KEDSDSDDSF IEVDSEFSTS NSQHVVFKEP GDTRETATNF QAVEEGNSGS QDIPLEHDSG EPHEQSNSEE SKDLDDVSNE WQDISVEELE SLENNLYVQQ TSLQAQQQQQ ERIAATVTGQ MCLESQELLQ LFGIPYIVAP MEAEAQCAIL DLTDQTSGTI TDDSDIWLFG ARHVYKNFFS QNKHVEYYQY ADIHNQLGLD RSKLINLAYL LGSDYTEGIP TVGYVSAMEI LNEFPGQGLE PLVKFKEWWS EAQKDKKMRP NPNDTKVKKK LRLLDLQQSF PNPAVASAYL KPVVDESKSA FSWGRPDLEQ IREFCESRFG WYRLKTDEVL LPVLKQLNAQ QTQLRIDSFF RLEQHEAAGL KSQRLRRAVT CMKRKERDVE AEEVEAAVAV MERECTNQRK GQKTNTKSQG TKRRKPTECS QEDQDPGGGF IGIELKTLSS KAYSSDGSSS DAEDLPSGLI DKQSQSGIVG RQKASNKVES SSSSDDEDRT VMVTAKPVFQ GKKTKSKTMK ETVKRK //