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ERCC3_BOVIN
ID   ERCC3_BOVIN             Reviewed;         782 AA.
AC   Q1RMT1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 114.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) 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; BC114729; AAI14730.1; -; mRNA.
DR   RefSeq; NP_001039453.1; NM_001045988.1.
DR   AlphaFoldDB; Q1RMT1; -.
DR   SMR; Q1RMT1; -.
DR   STRING; 9913.ENSBTAP00000027687; -.
DR   PaxDb; Q1RMT1; -.
DR   PRIDE; Q1RMT1; -.
DR   Ensembl; ENSBTAT00000027687; ENSBTAP00000027687; ENSBTAG00000020777.
DR   GeneID; 507984; -.
DR   KEGG; bta:507984; -.
DR   CTD; 2071; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020777; -.
DR   VGNC; VGNC:28570; ERCC3.
DR   eggNOG; KOG1123; Eukaryota.
DR   GeneTree; ENSGT00390000002204; -.
DR   HOGENOM; CLU_008213_0_0_1; -.
DR   InParanoid; Q1RMT1; -.
DR   OMA; PTHIHEY; -.
DR   OrthoDB; 100698at2759; -.
DR   TreeFam; TF101233; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000020777; Expressed in oocyte and 105 other tissues.
DR   ExpressionAtlas; Q1RMT1; baseline.
DR   GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IEA:Ensembl.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; ISS:UniProtKB.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; IBA:GO_Central.
DR   GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
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:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
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:0048568; P:embryonic organ development; IBA:GO_Central.
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:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
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; IBA:GO_Central.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
DR   GO; GO:0009650; P:UV protection; IEA:Ensembl.
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_0000323741"
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   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   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;  89193 MW;  378068130D97117B CRC64;
     MGKRDRADRE KKKSKKRHYE DEEDEEDDAP GNDTQEAVPS AAGKQVDESG TKVDEYGAKD
     YRLQMPLKDD HTSRPLWVAP DGHIFLEAFS PVYKYAQDFL VAIAEPVCRP THVHEYKLTA
     YSLYAAVSVG LQTSDITDYL RKLSKTGVPE GIIQFIKLCT VSYGKVKLVL KHNRYFVESS
     HPDVIQHLLQ DPVIRECRLR NSEGEATELI TETFTSKSAI AKSVEGSGGP STSRVTDPQG
     KSDIPTDLFD FYEQMDKDEE EEEETQTVSF EVKQEMIEEL QKRCIHLEYP LLAEYDFRND
     SVNPDINIDL KPTAVLRPYQ EKSLRKMFGN GRARSGVIVL PCGAGKSLVG VTAACTVRKR
     CLVLGNSAVS VEQWKAQFKM WSTIDDSQIC RFTSDAKDKP IGCSIAISTY SMLGHTTKRS
     WEAERVMEWL KTQEWGLMIL DEVHTIPAKM FRRVLTIVQA HCKLGLTATL VREDDKIVDL
     NFLIGPKLYE ANWMELQNSG YIAKVQCAEV WCPMSPEFYR EYVAIKTKKR ILLYTMNPNK
     FRACQFLIKF HERRNDKIIV FADNVFALKE YAIRLNKPYI YGPTSQGERM QILQNFKHNP
     KINTIFISKV GDTSFDLPEA NVLIQISSHG GSRRQEAQRL GRVLRAKKGM VAEEYNAFFY
     SLVSQDTQEM AYSTKRQRFL VDQGYSFKVI TKLAGMEEED LAFSTKEEQQ QLLQKVLAAT
     DLDAEEEVVA GEFGSKSSQV SRRFGTMSSM SGADDTVYME YHSSRSKTST KHVHPLFKRF
     RK
 
 
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