ERCC5_XENLA
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 03-AUG-2022, entry version 104.
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}.
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DR EMBL; X69977; CAA49597.1; -; mRNA.
DR PIR; S35994; S35994.
DR AlphaFoldDB; P14629; -.
DR SMR; P14629; -.
DR PRIDE; P14629; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
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 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; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00600; rad2; 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 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 736..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1159
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
