T2FA_SCHPO
ID T2FA_SCHPO Reviewed; 540 AA.
AC O94416;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Transcription initiation factor IIF subunit alpha;
DE Short=TFIIF-alpha;
DE AltName: Full=TFIIF large subunit;
GN Name=tfg1; ORFNames=SPCC1620.09c;
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 INTERACTION WITH TFG3.
RX PubMed=15616156; DOI=10.1093/nar/gkh1000;
RA Kimura M., Ishihama A.;
RT "Tfg3, a subunit of the general transcription factor TFIIF in
RT Schizosaccharomyces pombe, functions under stress conditions.";
RL Nucleic Acids Res. 32:6706-6715(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; SER-261 AND SER-399, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: TFIIF is a general transcription initiation factor that binds
CC to RNA polymerase II and helps to recruit it to the initiation complex
CC in collaboration with TFIIB. It promotes transcription elongation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the fcp1/TFIIF/polII complex via interaction of
CC tfg3 with both tfg1/TFIIF-alpha and tfg2/TFIIF-beta subunits.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFIIF alpha subunit family. {ECO:0000305}.
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DR EMBL; CU329672; CAA22493.2; -; Genomic_DNA.
DR PIR; T41039; T41039.
DR RefSeq; NP_588467.2; NM_001023458.3.
DR AlphaFoldDB; O94416; -.
DR SMR; O94416; -.
DR IntAct; O94416; 2.
DR STRING; 4896.SPCC1620.09c.1; -.
DR iPTMnet; O94416; -.
DR MaxQB; O94416; -.
DR PaxDb; O94416; -.
DR PRIDE; O94416; -.
DR GeneID; 2539294; -.
DR KEGG; spo:SPCC1620.09c; -.
DR PomBase; SPCC1620.09c; tfg1.
DR eggNOG; KOG2393; Eukaryota.
DR HOGENOM; CLU_020322_0_0_1; -.
DR InParanoid; O94416; -.
DR PhylomeDB; O94416; -.
DR Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SPO-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SPO-72086; mRNA Capping.
DR Reactome; R-SPO-72165; mRNA Splicing - Minor Pathway.
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 Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:O94416; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005674; C:transcription factor TFIIF complex; ISS:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISS:PomBase.
DR GO; GO:0001096; F:TFIIF-class transcription factor complex binding; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:PomBase.
DR InterPro; IPR008851; TFIIF-alpha.
DR InterPro; IPR011039; TFIIF_interaction.
DR PANTHER; PTHR13011; PTHR13011; 1.
DR Pfam; PF05793; TFIIF_alpha; 1.
DR SUPFAM; SSF50916; SSF50916; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..540
FT /note="Transcription initiation factor IIF subunit alpha"
FT /id="PRO_0000238604"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 280..382
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 540 AA; 61612 MW; D2E94C9192819D2F CRC64;
MDSQETKVFE NVKQENPDEK KPKVEEPDSQ NNASTQSQQK FLDFQLSWCP ESERKTTKYH
LLKFHSNKAI DPSKSFVPPI KMQRRDPNAP SSSNGEQNAE QGSSSNVNIA SIAPYGGAQN
MKQNAFKRKT RQVVKVDPQA RRLQEEELSP WIMEDFEGKN TWVSTMEGGQ SSAYVLFMFS
ENGFKVIPTD RFYRFNQRNN FQTLSIDEAE AKMNKKTPIP RWFMKKESEE NLAEAGSASP
MYKLKTVPNA RPVTGPRASG SDDELDYDEE FADDEEAPIM EGNEEDNKKL KDKIKKEMLT
ANLFGEADQD VDLEEENDRQ MSREGKKLQR YLKLLEKNLA YESDEEDEDP YASSHDASSE
EEVLQEEEEL QKREEKLKSR FSANASKTNT PRPLERTPSS VSPVKASSQL QSPNTSIQIR
PQEQLINKPG YIILRLSSEK LSRFANDFPR MVPSMGSTET SVGDQVEVVG DTTNVPIDDS
NLITEAEVMK ALRAGPISIK DLVHLFQRKI RADNRNRLGI QKIIRKVARF ENKLLVLKNY
