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Database: UniProt
Entry: E9D2A9_COCPS
LinkDB: E9D2A9_COCPS
Original site: E9D2A9_COCPS 
ID   E9D2A9_COCPS            Unreviewed;       395 AA.
AC   E9D2A9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=General transcription and DNA repair factor IIH subunit TFB4 {ECO:0000256|ARBA:ARBA00021280, ECO:0000256|RuleBase:RU368090};
DE            Short=TFIIH subunit TFB4 {ECO:0000256|RuleBase:RU368090};
DE   AltName: Full=RNA polymerase II transcription factor B subunit 4 {ECO:0000256|ARBA:ARBA00033341, ECO:0000256|RuleBase:RU368090};
GN   ORFNames=CPSG_03707 {ECO:0000313|EMBL:EFW19323.1};
OS   Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=443226 {ECO:0000313|Proteomes:UP000002497};
RN   [1] {ECO:0000313|Proteomes:UP000002497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
RN   [2] {ECO:0000313|Proteomes:UP000002497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA   Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA   Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Coccidioides posadasii strain Silveira.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the general transcription and DNA repair factor
CC       IIH (TFIIH) core complex, which is involved in general and
CC       transcription-coupled nucleotide excision repair (NER) of damaged DNA
CC       and, when complexed to TFIIK, in RNA transcription by RNA polymerase
CC       II. In NER, TFIIH acts by opening DNA around the lesion to allow the
CC       excision of the damaged oligonucleotide and its replacement by a new
CC       DNA fragment. In transcription, TFIIH has an essential role in
CC       transcription initiation. When the pre-initiation complex (PIC) has
CC       been established, TFIIH is required for promoter opening and promoter
CC       escape. Phosphorylation of the C-terminal tail (CTD) of the largest
CC       subunit of RNA polymerase II by the kinase module TFIIK controls the
CC       initiation of transcription. {ECO:0000256|ARBA:ARBA00002817,
CC       ECO:0000256|RuleBase:RU368090}.
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 active in
CC       NER. The core complex associates with the 3-subunit CTD-kinase module
CC       TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit
CC       holoenzyme (holo-TFIIH) active in transcription.
CC       {ECO:0000256|RuleBase:RU368090}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU368090}.
CC   -!- SIMILARITY: Belongs to the TFB4 family. {ECO:0000256|ARBA:ARBA00005273,
CC       ECO:0000256|RuleBase:RU368090}.
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DR   EMBL; GL636490; EFW19323.1; -; Genomic_DNA.
DR   STRING; 443226.E9D2A9; -.
DR   VEuPathDB; FungiDB:CPSG_03707; -.
DR   VEuPathDB; FungiDB:D8B26_007561; -.
DR   eggNOG; KOG2487; Eukaryota.
DR   HOGENOM; CLU_040211_0_0_1; -.
DR   OMA; CFCHRKV; -.
DR   Proteomes; UP000002497; Unassembled WGS sequence.
DR   GO; GO:0000439; C:transcription factor TFIIH core complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005675; C:transcription factor TFIIH holo complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR004600; TFIIH_Tfb4/GTF2H3.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR12831:SF0; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 3; 1.
DR   PANTHER; PTHR12831; TRANSCRIPTION INITIATION FACTOR IIH TFIIH , POLYPEPTIDE 3-RELATED; 1.
DR   Pfam; PF03850; Tfb4; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|RuleBase:RU368090};
KW   DNA repair {ECO:0000256|RuleBase:RU368090};
KW   Metal-binding {ECO:0000256|RuleBase:RU368090};
KW   Nucleus {ECO:0000256|RuleBase:RU368090};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002497};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU368090};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU368090}; Zinc {ECO:0000256|RuleBase:RU368090};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU368090}.
SQ   SEQUENCE   395 AA;  41974 MW;  E30DFBDFA83B2D49 CRC64;
     MNPVDSSDHF EADTAASLLT IVLDTNPHAW ALLEDTLPLS TAVANLLVFV NAHLACNYAN
     KVAVVASHSQ EARWLYPTPT TASSNTNQDE PADTDGDVAM SSTTGESPAS NKYRPFRIVE
     EQLTRNLKAL LATTSPASVS SATSTMMAGA LTLALSHINR ETIAYAETHG TSRLDSDPSN
     PTPTATGLPP PPGSHPDPTS QSSRSSPTGL QSRILIISVS SATGSAHQYI PIMNSIFACQ
     RLHIPIDICK LSGDAVFLQQ ACDATRGIYV PVDHPRGFLQ YLMVAFLPDQ RSRRHLILPT
     RVDVDFRAAC FCHRKVVDVG FVCSICLSIF CEPPEGADCL TCGTHLELGD YGAKPVVIAK
     KKKRKKGATK ALVANGGSSG GATPISNPTS TPTLP
//
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