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ERCC3_DANRE
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   03-AUG-2022, entry version 125.
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   Danionidae; Danioninae; 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 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; BC045400; AAH45400.1; -; mRNA.
DR   RefSeq; NP_963876.1; NM_201582.1.
DR   AlphaFoldDB; Q7ZVV1; -.
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   InParanoid; Q7ZVV1; -.
DR   OrthoDB; 100698at2759; -.
DR   PhylomeDB; Q7ZVV1; -.
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; Genome assembly.
DR   Proteomes; UP000814640; 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: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; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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: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   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..782
FT                   /note="General transcription and DNA repair factor IIH
FT                   helicase subunit XPB"
FT                   /id="PRO_0000323744"
FT   DOMAIN          326..487
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          541..701
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           6..17
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           440..443
FT                   /note="DEVH box"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         339..346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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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