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T2EA_SCHPO
ID   T2EA_SCHPO              Reviewed;         434 AA.
AC   Q9P3W1; Q5R229; Q9C1W1; Q9P7Z0;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 3.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Transcription initiation factor IIE subunit alpha;
DE            Short=TFIIE-alpha;
GN   Name=tfa1; ORFNames=SPAC458.07, SPAPYUG7.01;
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 [GENOMIC DNA / MRNA], AND SUBUNIT.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11041002;
RA   Shpakovski G.V., Baranova G.M.;
RT   "Chromosomal localization of the rpb9+ and tfa1+ genes encoding components
RT   of the mRNA synthesis machinery of Schizosaccharomyces pombe.";
RL   Bioorg. Khim. 26:623-630(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=15743411; DOI=10.1111/j.1365-2443.2005.00833.x;
RA   Hayashi K., Watanabe T., Tanaka A., Furumoto T., Sato-Tsuchiya C.,
RA   Kimura M., Yokoi M., Ishihama A., Hanaoka F., Ohkuma Y.;
RT   "Studies of Schizosaccharomyces pombe TFIIE indicate conformational and
RT   functional changes in RNA polymerase II at transcription initiation.";
RL   Genes Cells 10:207-224(2005).
RN   [3]
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   [4]
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   [5]
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).
CC   -!- FUNCTION: Recruits TFIIH to the initiation complex and stimulates the
CC       RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase
CC       activities of TFIIH. Both TFIIH and TFIIE are required for promoter
CC       clearance by RNA polymerase (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: TFIIE is a tetramer of two alpha (tfa1) and two beta (tfa2)
CC       subunits. {ECO:0000269|PubMed:11041002}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the TFIIE alpha subunit family. {ECO:0000305}.
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DR   EMBL; AF237419; AAL55662.1; -; Genomic_DNA.
DR   EMBL; AJ310560; CAC32853.1; -; mRNA.
DR   EMBL; AB176672; BAD74158.1; -; mRNA.
DR   EMBL; CU329670; CAB93849.3; -; Genomic_DNA.
DR   PIR; T50301; T50301.
DR   RefSeq; NP_594701.3; NM_001020129.2.
DR   AlphaFoldDB; Q9P3W1; -.
DR   SMR; Q9P3W1; -.
DR   BioGRID; 280041; 4.
DR   IntAct; Q9P3W1; 1.
DR   STRING; 4896.SPAC458.07.1; -.
DR   iPTMnet; Q9P3W1; -.
DR   MaxQB; Q9P3W1; -.
DR   PaxDb; Q9P3W1; -.
DR   PRIDE; Q9P3W1; -.
DR   EnsemblFungi; SPAC458.07.1; SPAC458.07.1:pep; SPAC458.07.
DR   GeneID; 2543627; -.
DR   KEGG; spo:SPAC458.07; -.
DR   PomBase; SPAC458.07; tfa1.
DR   VEuPathDB; FungiDB:SPAC458.07; -.
DR   eggNOG; KOG2593; Eukaryota.
DR   HOGENOM; CLU_035744_2_1_1; -.
DR   InParanoid; Q9P3W1; -.
DR   OMA; EYYSHMY; -.
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   PRO; PR:Q9P3W1; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005673; C:transcription factor TFIIE complex; IDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; TAS:PomBase.
DR   GO; GO:0001113; P:transcription open complex formation at RNA polymerase II promoter; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR039997; TFE.
DR   InterPro; IPR017919; TFIIE/TFIIEa_HTH.
DR   InterPro; IPR002853; TFIIE_asu.
DR   InterPro; IPR024550; TFIIEa/SarR/Rpc3_HTH_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13097; PTHR13097; 1.
DR   Pfam; PF02002; TFIIE_alpha; 1.
DR   SMART; SM00531; TFIIE; 1.
DR   PROSITE; PS51344; HTH_TFE_IIE; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..434
FT                   /note="Transcription initiation factor IIE subunit alpha"
FT                   /id="PRO_0000211224"
FT   DOMAIN          8..99
FT                   /note="HTH TFE/IIEalpha-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00676"
FT   ZN_FING         124..151
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          217..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..434
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   434 AA;  49117 MW;  F8D4108A7254F249 CRC64;
     MSNAPEIVQR LIKMIMRAFY ETRHIIFMDA ILRHSALTDE QTALLMGIPI KECRFIAGKL
     REDRLLAIQS RTEMKEGQQR QYHTTYFYID FCSTIDSIKW RMHQLVKTVE DRMRNDFDSK
     GYVCPFCNKK FSSLDVLSLV TNEGTFACNV CGTELKDDEE SAEMMSSQKR LGKLMGQVNG
     IIDALKRVDE IVVPQNNFQS ALEHAVPVSL DTQNLSQQNL SKSNSDVRLS TSSPSITVDF
     SADKETDEKR ERNCDKQVKA AQNILPEWHA TSTISGSITR AGAKDAALHS FRTETVNEVQ
     DTKTDITSEK SALDAYYATL RAKQKEESEF MDSENVDDEE DDDFLDVTTA TSLQNKSTDY
     GSVKRKTENL NSDSDIQNKR TKSIEENNSL PPIVSTNGIT DGDTEMQESK KNVIINGFNE
     DDEDDEDEAD FEDV
 
 
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