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Database: UniProt
Entry: Q7ZVV1
LinkDB: Q7ZVV1
Original site: Q7ZVV1 
ID   ERCC3_DANRE             Reviewed;         782 AA.
AC   Q7ZVV1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-OCT-2019, 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   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, component of the
CC       general transcription and DNA repair factor IIH (TFIIH) core
CC       complex, which is involved in general and transcription-coupled
CC       nucleotide excision repair (NER) of damaged DNA and, when
CC       complexed to CAK, in RNA transcription by RNA polymerase II. In
CC       NER, TFIIH acts by opening DNA around the lesion to allow the
CC       excision of the damaged oligonucleotide and its replacement by a
CC       new DNA fragment. The ATPase activity of XPB/ERCC3, but not its
CC       helicase activity, is required for DNA opening. In transcription,
CC       TFIIH has an essential role in transcription initiation. When the
CC       pre-initiation complex (PIC) has been established, TFIIH is
CC       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
CC       tail (CTD) of the largest subunit of RNA polymerase II by the
CC       kinase module 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,
CC       which is active in NER. The core complex associates with the 3-
CC       subunit CDK-activating kinase (CAK) module composed of CCNH/cyclin
CC       H, CDK7 and MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH)
CC       active in transcription. Interacts with PUF60. Interacts with
CC       ATF7IP. Interacts with Epstein-Barr virus EBNA2.
CC       {ECO:0000250|UniProtKB:P19447}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000305}.
DR   EMBL; BC045400; AAH45400.1; -; mRNA.
DR   RefSeq; NP_963876.1; NM_201582.1.
DR   SMR; Q7ZVV1; -.
DR   STRING; 7955.ENSDARP00000105166; -.
DR   PaxDb; Q7ZVV1; -.
DR   PRIDE; Q7ZVV1; -.
DR   GeneID; 324323; -.
DR   KEGG; dre:324323; -.
DR   CTD; 2071; -.
DR   ZFIN; ZDB-GENE-030131-3043; ercc3.
DR   eggNOG; KOG0159; Eukaryota.
DR   eggNOG; KOG1123; Eukaryota.
DR   eggNOG; COG1061; LUCA.
DR   HOGENOM; HOG000160172; -.
DR   InParanoid; Q7ZVV1; -.
DR   KO; K10843; -.
DR   OrthoDB; 100698at2759; -.
DR   PhylomeDB; Q7ZVV1; -.
DR   Reactome; R-DRE-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-DRE-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-DRE-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-DRE-5696400; Dual Incision in GG-NER.
DR   Reactome; R-DRE-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-DRE-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-DRE-6782135; Dual incision in TC-NER.
DR   Reactome; R-DRE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-DRE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR   Reactome; R-DRE-72086; mRNA Capping.
DR   Reactome; R-DRE-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-DRE-73772; RNA Polymerase I Promoter Escape.
DR   Reactome; R-DRE-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-DRE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-DRE-73863; RNA Polymerase I Transcription Termination.
DR   Reactome; R-DRE-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-DRE-75955; RNA Polymerase II Transcription Elongation.
DR   Reactome; R-DRE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   Reactome; R-DRE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR   PRO; PR:Q7ZVV1; -.
DR   Proteomes; UP000000437; Unplaced.
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:transcriptional 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
DR   GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:GOC.
DR   GO; GO:0009411; P:response to UV; 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   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
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; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    782       General transcription and DNA repair
FT                                factor IIH helicase subunit XPB.
FT                                /FTId=PRO_0000323744.
FT   DOMAIN      326    487       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      541    701       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     339    346       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         6     17       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       440    443       DEVH box.
FT   COMPBIAS     19     26       Asp/Glu-rich (acidic).
FT   COMPBIAS    257    263       Asp/Glu-rich (acidic).
FT   COMPBIAS    696    699       Asp/Glu-rich (acidic).
FT   COMPBIAS    720    726       Asp/Glu-rich (acidic).
SQ   SEQUENCE   782 AA;  89288 MW;  5CAA94DA15CA7A15 CRC64;
     MGRKDKSDRE KKSKKRYYED EEEDEEVIGG ESQEAVPAAA GKQVDESSTK LDEYGAKDYR
     LQMLLKNDHS SRPLWVAPDG HIFLEAFSPV YKYAQDFLVA ISEPVCRPTH AHEYKLTAYS
     LYAAVSVGLQ TSDIIEYLQK LSKTSVPDGI VQFIKLCTVS YGKVKLVLKH NRYFVESAFP
     DVIQRLLQDT VIRDCRLRSA EGEETELITE TISSKSAISK SQQDNGGPSS SQPADGQRSG
     TQVPEDIFSY YEQMDKEEEE EEETQTVSFE IRQEMIEELQ KRCIQLEYPL LAEYDFRNDT
     VNPDINMDLK PTAVLRPYQE KSLRKMFGNG RARSGVIVLP CGAGKSLVGV TAACTVRKRC
     LVLGNSSVSV EQWKAQFKMW STIDDSQICR FTSDAKDKPI GCSVAISTYS MLGHTTKRSW
     EAERVMEWMK SQEWGLIILD EVHTIPAKMF RRVLTIVQAH CKLGLTATLV REDDKIVDLN
     FLIGPKLYEA NWMELQNNGY IAKVQCAEVW CPMSPEFYRE YVAIKTKKRI LLYTMNPNKF
     RACQFLIRFH ERRNDKIIVF ADNVFALKEY AIRLNKPYIY GPTSQGERMQ ILQNFKHNPK
     INTIFISKVG DTSFDLPEAN VLIQISSHGG SRRQEAQRLG RVLRAKKGMV AEEYNAYFYS
     LVSQDTQEMA YSTKRQRFLV DQGYSFKVIT KLAGMEEEDL MFSTRDEQQQ LLQKVLAASD
     LDAEEEVVMG EVGGKPQFSR RAGTMSSMSG ADDALYMEYQ MPRGSKASVG KNIHPLFKRF
     RK
//
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