TFB1_SCHPO
ID TFB1_SCHPO Reviewed; 533 AA.
AC O13745;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=General transcription and DNA repair factor IIH subunit tfb1;
DE Short=TFIIH subunit tfb1;
DE AltName: Full=RNA polymerase II transcription factor B 73 kDa subunit;
DE AltName: Full=RNA polymerase II transcription factor B p73 subunit;
DE AltName: Full=RNA polymerase II transcription factor B subunit 1;
GN Name=tfb1; ORFNames=SPAC16E8.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBUNIT.
RX PubMed=14534314; DOI=10.1074/jbc.m306750200;
RA Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O.,
RA Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.;
RT "Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent
RT transcription in vitro.";
RL J. Biol. Chem. 278:51301-51306(2003).
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:0000250|UniProtKB:P32776}.
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/ptr8, XPD/rad15, ssl1, tfb1, tfb2, tfb4 and tfb5, which is active
CC in NER. The core complex associates with the 3-subunit CTD-kinase
CC module TFIIK composed of mcs2/cyclin H, mcs6/cdk7 and pmh1/tfb3 to form
CC the 10-subunit holoenzyme (holo-TFIIH) active in transcription.
CC {ECO:0000269|PubMed:14534314}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFB1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11039.2; -; Genomic_DNA.
DR PIR; T37791; T37791.
DR RefSeq; NP_594223.2; NM_001019646.2.
DR AlphaFoldDB; O13745; -.
DR SMR; O13745; -.
DR BioGRID; 278802; 4.
DR IntAct; O13745; 1.
DR STRING; 4896.SPAC16E8.11c.1; -.
DR iPTMnet; O13745; -.
DR MaxQB; O13745; -.
DR PaxDb; O13745; -.
DR PRIDE; O13745; -.
DR EnsemblFungi; SPAC16E8.11c.1; SPAC16E8.11c.1:pep; SPAC16E8.11c.
DR GeneID; 2542336; -.
DR KEGG; spo:SPAC16E8.11c; -.
DR PomBase; SPAC16E8.11c; tfb1.
DR VEuPathDB; FungiDB:SPAC16E8.11c; -.
DR eggNOG; KOG2074; Eukaryota.
DR HOGENOM; CLU_019188_0_0_1; -.
DR InParanoid; O13745; -.
DR OMA; IYNENVP; -.
DR Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SPO-72086; mRNA Capping.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:O13745; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; ISO:PomBase.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:PomBase.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISO:PomBase.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:PomBase.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; ISO:PomBase.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:PomBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR005607; BSD_dom.
DR InterPro; IPR035925; BSD_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR027079; Tfb1/GTF2H1.
DR InterPro; IPR013876; TFIIH_BTF_p62_N.
DR PANTHER; PTHR12856; PTHR12856; 1.
DR Pfam; PF03909; BSD; 2.
DR Pfam; PF08567; PH_TFIIH; 1.
DR SMART; SM00751; BSD; 2.
DR SUPFAM; SSF140383; SSF140383; 1.
DR PROSITE; PS50858; BSD; 2.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..533
FT /note="General transcription and DNA repair factor IIH
FT subunit tfb1"
FT /id="PRO_0000119260"
FT DOMAIN 116..169
FT /note="BSD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00036"
FT DOMAIN 190..241
FT /note="BSD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00036"
FT REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 60600 MW; A042EFFA0B4B469D CRC64;
MGDRVEALAI FRKKQGVLSI DSRLKWTGEG KTTPSVDIAF DAISNLQTTP ASNPKVMIRV
FIVVKEGEDP TSLVFHFTGT PNARENCDMI TNELRNAIQR QREGSQSKPQ GANVDRVNST
NLEKDIDLQE SLLTNNPDLL QTFKEAVMKG HLSNEQFWST RLHLLRAHAV ERSQQRGPYN
VLSTIKPKTV DNQMKVSLTG QQIHDMFEQH PLLRKVYDKH VPPLAEGEFW SRFFLSKLCK
KLRGDRITPM DPSDDIMDKY LKDNEEVTKV SDEPIASHLF DLEGNDQNAN VIAELRPDIT
MRIDKEALPF MKNINQLSER LLEKSLGNSK RFNNENEETY LKESGFHDLE EEASDSKVVL
KIKGQDQLLE NNFVPSKNQV GLEPLPSLEA LQHLYQEDSI SLNHIEHDSD SLAEAAMQLT
QSMREKHEFE THGTASNLPI DIKNEIVLCH TVTIEFLHQF WNALLNTTFP DKKAMAPLQN
ALLNSKKRVE AIASQAQEQN VDPKLVYELV SCTLTSIDTS ISEYQRRMSY PPA
