ERCC3_MACFA
ID ERCC3_MACFA Reviewed; 782 AA.
AC Q60HG1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=General transcription and DNA repair factor IIH helicase subunit XPB;
DE Short=TFIIH subunit XPB;
DE EC=3.6.4.12;
DE AltName: Full=DNA excision repair protein ERCC-3;
GN Name=ERCC3; ORFNames=QnpA-11695;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the general
CC transcription and DNA repair factor IIH (TFIIH) core complex, which is
CC involved in general and transcription-coupled nucleotide excision
CC repair (NER) of damaged DNA and, when complexed to CAK, in RNA
CC transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA
CC around the lesion to allow the excision of the damaged oligonucleotide
CC and its replacement by a new DNA fragment. The ATPase activity of
CC XPB/ERCC3, but not its helicase activity, is required for DNA opening.
CC In transcription, TFIIH has an essential role in transcription
CC initiation. When the pre-initiation complex (PIC) has been established,
CC TFIIH is required for promoter opening and promoter escape. The ATP-
CC dependent helicase activity of XPB/ERCC3 is required for promoter
CC opening and promoter escape. Phosphorylation of the C-terminal tail
CC (CTD) of the largest subunit of RNA polymerase II by the kinase module
CC CAK controls the initiation of transcription.
CC {ECO:0000250|UniProtKB:P19447}.
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 -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which
CC is active in NER. The core complex associates with the 3-subunit CDK-
CC activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and
CC MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in
CC transcription. Interacts with PUF60. Interacts with ATF7IP. Interacts
CC with KAT2A; leading to KAT2A recruitment to promoters and acetylation
CC of histones. {ECO:0000250|UniProtKB:P19447}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000305}.
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DR EMBL; AB125166; BAD51954.1; -; mRNA.
DR RefSeq; NP_001274561.1; NM_001287632.1.
DR AlphaFoldDB; Q60HG1; -.
DR SMR; Q60HG1; -.
DR STRING; 9541.XP_005572937.1; -.
DR Ensembl; ENSMFAT00000008024; ENSMFAP00000033796; ENSMFAG00000003370.
DR GeneID; 102138496; -.
DR CTD; 2071; -.
DR VEuPathDB; HostDB:ENSMFAG00000003370; -.
DR eggNOG; KOG1123; Eukaryota.
DR GeneTree; ENSGT00390000002204; -.
DR OMA; PTHIHEY; -.
DR OrthoDB; 100698at2759; -.
DR Proteomes; UP000233100; Chromosome 12.
DR Bgee; ENSMFAG00000003370; Expressed in pituitary gland and 13 other tissues.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; ISS:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
DR GO; GO:0035315; P:hair cell differentiation; ISS:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR032438; ERCC3_RAD25_C.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001161; XPB/Ssl2.
DR InterPro; IPR032830; XPB/Ssl2_N.
DR Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF13625; Helicase_C_3; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00603; rad25; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..782
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000101988"
FT DOMAIN 327..488
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 542..702
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..18
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 441..444
FT /note="DEVH box"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 340..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19447"
SQ SEQUENCE 782 AA; 89232 MW; 35FA1F625D0FEF88 CRC64;
MGKRDRADRD KKKSRKRHYE DEEDDEEDAP GNDPQEAVPS AAGKQVDESG TKVDEYGAKD
YRLQMPLKDD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL VAIAEPVCRP THVHEYKLTA
YSLYAAVSVG LQTSDITEYL RKLSKTGVPD GIMQFIKLCT VSYGKVKLVL KHNRYFVESS
HPDVIQHLLQ DPVIRECRLR NSEGEATELI TETFTSKSAI SKTAEGSGGP STSRVTDPQG
KSDIPMDLFD FYEQMDKDEE EEEETQTVSF EVKQEMIEEL QKRCIHLEYP LLAEYDFRND
SVNPDINIDL KPTAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG VTAACTVRKR
CLVLGNSAVS VEQWKAQFKM WSTIDDSQIC RFTSDAKDKP IGCSVAISTY SMLGHTTKRS
WEAERVMEWL KTQEWGLMIL DEVHTIPAKM FRRVLTIVQA HCKLGLTATL VREDDKIVDL
NFLIGPKLYE ANWMELQNNG YIAKVQCAEV WCPMSPEFYR EYVAIKTKKR ILLYTMNPNK
FRACQFLIKF HERRNDKIIV FADNVFALKE YAIRLNKPYI YGPTSQGERM QILQNFKHNP
KINTIFISKV GDTSFDLPEA NVLIQISSHG GSRRQEAQRL GRVLRAKKGM VAEEYNAFFY
SLVSQDTQEM AYSTKRQRFL VDQGYSFKVI TKLAGMEEED LAFSTKEEQQ QLLQKVLAAT
DLDAEEEVVA GEFGSRSSQA SRRFGTMSSM SGADDTVYME YHSSRSKAPS KHVHPLFKRF
RK
