TOA1_SCHPO
ID TOA1_SCHPO Reviewed; 369 AA.
AC Q9USU9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Transcription initiation factor IIA large subunit {ECO:0000250|UniProtKB:P32773, ECO:0000312|EMBL:CAB57938.1};
DE Short=TFIIA large subunit {ECO:0000250|UniProtKB:P32773};
GN Name=toa1 {ECO:0000250|UniProtKB:P32773}; ORFNames=SPBC28F2.09;
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] {ECO:0000312|EMBL:CAB57938.1}
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] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP 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: TFIIA is a component of the transcription machinery of RNA
CC polymerase II and plays an important role in transcriptional
CC activation. TFIIA in a complex with tbp mediates transcriptional
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: TFIIA is a heterodimer of the large subunit and the small
CC subunit gamma. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFIIA subunit 1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB57938.1; -; Genomic_DNA.
DR PIR; T40052; T40052.
DR RefSeq; NP_595670.1; NM_001021565.2.
DR AlphaFoldDB; Q9USU9; -.
DR SMR; Q9USU9; -.
DR BioGRID; 277158; 2.
DR STRING; 4896.SPBC28F2.09.1; -.
DR iPTMnet; Q9USU9; -.
DR MaxQB; Q9USU9; -.
DR PaxDb; Q9USU9; -.
DR PRIDE; Q9USU9; -.
DR EnsemblFungi; SPBC28F2.09.1; SPBC28F2.09.1:pep; SPBC28F2.09.
DR GeneID; 2540632; -.
DR KEGG; spo:SPBC28F2.09; -.
DR PomBase; SPBC28F2.09; toa1.
DR VEuPathDB; FungiDB:SPBC28F2.09; -.
DR eggNOG; KOG2652; Eukaryota.
DR HOGENOM; CLU_030027_4_1_1; -.
DR InParanoid; Q9USU9; -.
DR OMA; EVCDASQ; -.
DR PhylomeDB; Q9USU9; -.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6807505; RNA polymerase II transcribes snRNA genes.
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-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q9USU9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005672; C:transcription factor TFIIA complex; ISO:PomBase.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:PomBase.
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; 2.30.18.10; -; 1.
DR InterPro; IPR004855; TFIIA_asu/bsu.
DR InterPro; IPR009088; TFIIA_b-brl.
DR PANTHER; PTHR12694; PTHR12694; 1.
DR Pfam; PF03153; TFIIA; 2.
DR SMART; SM01371; TFIIA; 1.
DR SUPFAM; SSF50784; SSF50784; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription.
FT CHAIN 1..369
FT /note="Transcription initiation factor IIA large subunit"
FT /id="PRO_0000364025"
FT REGION 113..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..318
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 369 AA; 39975 MW; FFEEEC67B78AB6A4 CRC64;
MSNSIVGEVY HHVILDVIAN SRSDFEENGV DDATLRELQN LWQSKLVATD VATFPWAQAP
VGTFPIGQLF DPVSGLRTDS LDVTAPAVAN SPILNNIAAI RAVQQMDTFA QQHGNSNYYS
PPTPSLPQSA TNISFDSSAI PNVQSNPNNT APFPSYSSNS LQLPTNQTAD SPIINDHSTA
NVTSTGQEHA PDSSSTNSFG GLLLPNQNSP KKSELGETES SNTTPANSRN DVPQTDGAIH
DLDDAGSPSN FESNRFAIAQ KADAEIYEVL KKNRILQIDG TIEDNEDEKK PPVDTPSDEA
INSDLDDPDS DEAPETEEGS DIGQAIVLCL YDKVNHHKNK WKCVFRDGVV GVNGKDYLFF
KANGEFEWI
