ERCC3_CHICK
ID ERCC3_CHICK Reviewed; 788 AA.
AC Q5ZKK7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=RCJMB04_10e8;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 Epstein-Barr virus EBNA2. {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; AJ720077; CAG31736.1; -; mRNA.
DR AlphaFoldDB; Q5ZKK7; -.
DR SMR; Q5ZKK7; -.
DR STRING; 9031.ENSGALP00000018752; -.
DR PaxDb; Q5ZKK7; -.
DR VEuPathDB; HostDB:geneid_424226; -.
DR eggNOG; KOG1123; Eukaryota.
DR InParanoid; Q5ZKK7; -.
DR OrthoDB; 100698at2759; -.
DR PhylomeDB; Q5ZKK7; -.
DR Reactome; R-GGA-353303; Nucleotide Excision Repair.
DR PRO; PR:Q5ZKK7; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IBA:GO_Central.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
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 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; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..788
FT /note="General transcription and DNA repair factor IIH
FT helicase subunit XPB"
FT /id="PRO_0000323743"
FT DOMAIN 324..485
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 539..699
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..15
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 438..441
FT /note="DEVH box"
FT BINDING 337..344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 788 AA; 89680 MW; D1863405609CDA88 CRC64;
MGRKERDKKK SKKRHYEDEE EEEDDAPGKE SQEAVPSAAG KQVEDSGAKL DEYGAKDYRL
QMPLKADNAS RPLWVAPDGH IFLEAFSPVY KYAQDFLVAI AEPVCRPTHI HEYKLTAYSL
YAAVSVGLQT SDITEYLQKL SKTGVPEGII QFIKLCTVSY GKVKLVLKRN RYFVESTHPD
VIQQLLQDHV IKDCRLRNAE GEETELITET FTSKSAISKS SESGFGPSTS QEADVQNKPD
VPADLYEFYE QMDKDEEEEE ETQTVSFEVK QEMIEELQKR CIHLDYPLLA EYDFRNDSVN
PDINIDLKPT AVLRPYQEKS LRKMFGNGRA RSGVIVLPCG AGKSLVGVTA ACTVRKRCLV
LGNSAVSVEQ WKAQFKMWST IDDSQICRFT SDAKDKPIDC SIAISTYSML GHTTKRSWEA
ERVMEWLKSR EWGLMILDEV HTIPAKMFRR VLTIVQAHCK LELTATLVRE DDKIVDLNFL
IGPKLYEANW MELQNSGYIA KVQCAEVWCP MSPEFYREYV AIKTKKRILL YTMNPNKFRA
CQFLIKFHER RNDKIIVFAD NVFALKEYAI RLGKPYIYGP TAQGERMQIL QNFKHNPKIN
TIFISKVGDT SFDLPEANVL IQISSHGGSR RQEAQRLGRV LRAKKGMVAE EYNAFFYSLV
SQDTQEMAYS TKRQRFLVDQ GYSFKVITKL AGMEEEELSF SSKEEQQQLL QKVLQASDLD
AEEEVVAGEY GSKSVQMSRR TGTMSSMSGA DDAVYMEYHS SRSKASSNKH IHPLLSASGN
DVLHVCVL
