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Database: UniProt
Entry: Q6E6J3
LinkDB: Q6E6J3
Original site: Q6E6J3 
ID   RAD25_ANTLO             Reviewed;         687 AA.
AC   Q6E6J3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   31-JUL-2019, entry version 73.
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 repair helicase RAD25;
DE   AltName: Full=RNA polymerase II transcription factor B subunit SSL2;
DE            Short=TFB subunit SSL2;
DE   AltName: Full=Suppressor of stem-loop mutation 2;
GN   Name=SSL2; Synonyms=RAD25;
OS   Antonospora locustae (Microsporidian parasite) (Nosema locustae).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Antonospora.
OX   NCBI_TaxID=278021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15186746; DOI=10.1016/j.cub.2004.04.041;
RA   Slamovits C.H., Fast N.M., Law J.S., Keeling P.J.;
RT   "Genome compaction and stability in microsporidian intracellular
RT   parasites.";
RL   Curr. Biol. 14:891-896(2004).
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 TFIIK, 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/SSL2, 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/SSL2 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 TFIIK controls the initiation of transcription.
CC       {ECO:0000250|UniProtKB:Q00578}.
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/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is
CC       active in NER. The core complex associates with the 3-subunit CTD-
CC       kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the
CC       10-subunit holoenzyme (holo-TFIIH) active in transcription.
CC       {ECO:0000250|UniProtKB:Q00578}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00578}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000305}.
DR   EMBL; AY548884; AAT12293.1; -; Genomic_DNA.
DR   SMR; Q6E6J3; -.
DR   PRIDE; Q6E6J3; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
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   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN         1    687       General transcription and DNA repair
FT                                factor IIH helicase subunit XPB.
FT                                /FTId=PRO_0000388442.
FT   DOMAIN      239    401       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      455    609       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     252    259       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       354    357       DEAH box.
SQ   SEQUENCE   687 AA;  78771 MW;  E2624BDC3A8769C0 CRC64;
     MTRCGWHTCT RVRPRMGETL LPRKASQHEF EPEEIRMKQE HTECPLLVSH NGIIILETFT
     ANAKQATDFL IAIAEPVSRP AHVHEYRITP YSLYAAVSVG LTTEDILSTL DRFAKNTVPD
     TIVRFVRECT LSYGKTRLVF KGGRFLVEAA TREVFDVLTG DAEISRLRAA GTVRDADARY
     VFEVRVDCIE QVRRRCIEID YPMIEEYDFR DDVALRSLDM DLRDTVSIRT YQEVSLNKMF
     GNRRARSGVI VLPCGAGKTL VGITAMCTIK KPCIVLCTSG VSVEQWRQQV LAFSTVSADA
     VSRFTSERKE MFEADAGILI TTYTMLAFSG RRSAEAQRVM EWLRGTEWGL MILDEVHVVP
     AAMFRKVVSA VSHHCKLGLT ATLVREDDKI EDLNFLIGPK LYEADWQDLS MQGHIARVEC
     VEVWCDMTAE FYREYLGQDP RRRRVLSIMN PAKFQTCEFL IRKHEALGEK IIVFSDNVLA
     LRTYALKLGK PFIYGPTGQT ERMRILRQFQ TNPAINTLFL SKVGDTSIDL PEASCLIQIS
     SHFGSRRQEA QRLGRILRAK RRNDPGFRVY FYTLVSKDTE EMYYSRKRQQ FLVDQGYTFR
     TVTALEGFRD TDVRVFRGKA EQRELLATVL LASEEDLESE ESEDGDEAAA DRRHLRTRGG
     AEDTVPASRT RTERHLLFRK MHKRHRR
//
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