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Database: UniProt
Entry: A9CRJ7
LinkDB: A9CRJ7
Original site: A9CRJ7 
ID   RAD25_ENTBH             Reviewed;         609 AA.
AC   A9CRJ7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   31-JUL-2019, entry version 65.
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; ORFNames=EBI_23223;
OS   Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia;
OC   Enterocytozoonidae; Enterocytozoon.
OX   NCBI_TaxID=481877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA   Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M.,
RA   Tzipori S., Keeling P.J.;
RT   "Patterns of genome evolution among the microsporidian parasites
RT   Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT   bieneusi.";
RL   PLoS ONE 2:E1277-E1277(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H348;
RX   PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA   Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA   Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT   "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT   Enterocytozoon bieneusi.";
RL   PLoS Pathog. 5:E1000261-E1000261(2009).
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; ABGB01000001; EDQ31310.1; -; Genomic_DNA.
DR   RefSeq; XP_001827839.1; XM_001827787.1.
DR   EnsemblFungi; EDQ31310; EDQ31310; EBI_23223.
DR   EuPathDB; MicrosporidiaDB:EBI_23223; -.
DR   InParanoid; A9CRJ7; -.
DR   Proteomes; UP000001742; Unassembled WGS sequence.
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; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    609       General transcription and DNA repair
FT                                factor IIH helicase subunit XPB.
FT                                /FTId=PRO_0000388444.
FT   DOMAIN      200    369       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      423    584       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     213    220       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       322    325       DEAH box.
SQ   SEQUENCE   609 AA;  70329 MW;  7CE90AB8B68B2D84 CRC64;
     MKENSEDCPL WINYDGLIIL EMFRENSQQA TNFLIAIAEP ISRPENIHEY QITPYSLFAA
     ASVGLTTDQI TNTLQKFSKN IIPRNVKNLI SDCTLSYGKL KLVRQSQKFF IEVYNDKIFN
     FITSDEILKS FIVNSNIDEL KIEITNVEKI KKRCIEIDYP LIDEYDYTAY ESVNMIKNLH
     IDLKPSCHIR SYQEISLNKM LGNGRARSGI IVLPCGSGKT LVGITAISTI KKSAIILCTS
     AVSVEQWKQS ILLFTTINPY SVSRFTSDCK EWFENYNVEN TSQGGILITT YSMLSFSGKR
     SYDVQRIINK IFAYNWGIMI LDEVHVVPAQ MFRKVVSSVL HQCKLGLTAT LVREDDKIED
     LNFLIGPKLY EANWQDLSDK GHIAKVECSE VWCEMTAEFY REYLIQDTSK KRLLSIMNPV
     KIQMCEYLIQ KHEAQGDKII VFSDSVFALK EYAIKMKKPF IYGPTSQTER MKILKQFQIN
     SKINTLFLSK VGDTSIDLPE ATCLIQISSH FGSRRQEAQR LGRVLRAKKR NNPNFKAYFY
     SLVSKDTEEM HYSAKRQQFL IDQGYSFKTI IGFNDMYYNE TRLYKTKQEQ KELLFNLLSK
     NLSSDETDK
//
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