ID   TAF5_SCHPO              Reviewed;         643 AA.
AC   O13282;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Transcription initiation factor TFIID subunit 5;
DE   AltName: Full=Transcription initiation factor TFIID 72 kDa subunit;
DE            Short=TAFII-72;
GN   Name=taf5; Synonyms=taf72; ORFNames=SPCC5E4.03c;
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].
RX   PubMed=9224658; DOI=10.1046/j.1365-2443.1997.1180316.x;
RA   Yamamoto T., Poon D., Weil P.A., Horikoshi M.;
RT   "Molecular genetic elucidation of the tripartite structure of the
RT   Schizosaccharomyces pombe 72 kDa TFIID subunit which contains a WD40
RT   structural motif.";
RL   Genes Cells 2:245-254(1997).
RN   [2]
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   [3]
RP   FUNCTION, AND INTERACTION WITH GCN5.
RX   PubMed=11279037; DOI=10.1074/jbc.m100248200;
RA   Mitsuzawa H., Seino H., Yamao F., Ishihama A.;
RT   "Two WD repeat-containing TATA-binding protein-associated factors in
RT   fission yeast that suppress defects in the anaphase-promoting complex.";
RL   J. Biol. Chem. 276:17117-17124(2001).
RN   [4]
RP   INTERACTION WITH TAF6 AND GCN5.
RX   PubMed=11972332; DOI=10.1093/nar/30.9.1952;
RA   Mitsuzawa H., Ishihama A.;
RT   "Identification of histone H4-like TAF in Schizosaccharomyces pombe as a
RT   protein that interacts with WD repeat-containing TAF.";
RL   Nucleic Acids Res. 30:1952-1958(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, 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: TAFs are components of the transcription factor IID (TFIID)
CC       complex that are essential for mediating regulation of RNA polymerase
CC       transcription. Regulates the genes involved in ubiquitin-dependent
CC       proteolysis during the progression of M-phase of mitosis.
CC       {ECO:0000269|PubMed:11279037}.
CC   -!- SUBUNIT: Component of the TFIID and SAGA complexes. TFIID is composed
CC       of TATA binding protein (TBP) and a number of TBP-associated factors
CC       (TAFs) whose MWs range from 25-150 kDa (By similarity). Interacts with
CC       gcn5. Interacts (via C-terminal WD repeat-containing region) with taf6.
CC       {ECO:0000250, ECO:0000269|PubMed:11279037,
CC       ECO:0000269|PubMed:11972332}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat TAF5 family. {ECO:0000305}.
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DR   EMBL; AB001372; BAA22162.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAA21958.1; -; Genomic_DNA.
DR   PIR; T41454; T41454.
DR   RefSeq; NP_587902.1; NM_001022894.2.
DR   AlphaFoldDB; O13282; -.
DR   SMR; O13282; -.
DR   BioGRID; 275919; 20.
DR   IntAct; O13282; 7.
DR   MINT; O13282; -.
DR   STRING; 4896.SPCC5E4.03c.1; -.
DR   iPTMnet; O13282; -.
DR   MaxQB; O13282; -.
DR   PaxDb; O13282; -.
DR   PRIDE; O13282; -.
DR   EnsemblFungi; SPCC5E4.03c.1; SPCC5E4.03c.1:pep; SPCC5E4.03c.
DR   GeneID; 2539353; -.
DR   KEGG; spo:SPCC5E4.03c; -.
DR   PomBase; SPCC5E4.03c; taf5.
DR   VEuPathDB; FungiDB:SPCC5E4.03c; -.
DR   eggNOG; KOG0263; Eukaryota.
DR   HOGENOM; CLU_005884_0_2_1; -.
DR   InParanoid; O13282; -.
DR   OMA; RCAFAPE; -.
DR   PhylomeDB; O13282; -.
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:O13282; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IDA:PomBase.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; TAS:PomBase.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:GOC.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR   CDD; cd08044; TAF5_NTD2; 1.
DR   Gene3D; 1.25.40.500; -; 1.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR037783; Taf5.
DR   InterPro; IPR007582; TFIID_NTD2.
DR   InterPro; IPR037264; TFIID_NTD2_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR19879; PTHR19879; 1.
DR   Pfam; PF08513; LisH; 1.
DR   Pfam; PF04494; TFIID_NTD2; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF160897; SSF160897; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; WD repeat.
FT   CHAIN           1..643
FT                   /note="Transcription initiation factor TFIID subunit 5"
FT                   /id="PRO_0000051259"
FT   DOMAIN          8..40
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REPEAT          322..361
FT                   /note="WD 1"
FT   REPEAT          377..416
FT                   /note="WD 2"
FT   REPEAT          419..458
FT                   /note="WD 3"
FT   REPEAT          461..500
FT                   /note="WD 4"
FT   REPEAT          503..542
FT                   /note="WD 5"
FT   REPEAT          545..584
FT                   /note="WD 6"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   643 AA;  72380 MW;  859434527430F3B1 CRC64;
     MSATNGPQPQ DLNRIVLDYL AKKGYSRTEA MLRLEASGSG VSVEEKLKSI EETPDAYTHT
     YTILRDWVDS SLELYKAELH RILFPIFVHS YLNLLSQDHY EAAKQFYELF KDDHTDLHDF
     DVKNLKSLSL PSHVAEDRTA QQYRQNKYQL HFSRITFDLL LHFLFENVSN GGSIIIKLIN
     QHIDIHIVPG RPTVLENAKV INEQEGITGQ SFERGDAQLQ PVKLQQMPMD KEMEKIVEMD
     LEEEDMMHQN DPNNQSPKLL KEFRKLHEPN AEDAPSRDYI PLPPHKGVDI LSEVEAVKDW
     SKRLHLGPRA SLPSVCMYTF HHTNNNMNCA EFSPDSTMIA CGFQESYIRL WSIKADKKSL
     PKSTSVEDSD GSVRLLSHSG PVYGTTFSPD NKYLLSCSED ASARLWSVDT KTALVAYKGH
     TGPVWDVAFG PFGHYFATAS HDQTAQLWSC DHIYPLRVFA GHLSDVDCVT FHPNSAYVLT
     GSSDKTCRLW DVHRGHSVRV FNGHTQPVTA VAIAPDGHTM ASADSEGLIH LWDIGTGRRI
     KTMRGHRGNI YSLSFSREST VLVSGGSDCT VRAWDVFKTN YNNPVSSSLT GSVVTPFSAK
     TSTFNEVNWS TSPDQMVALY TKQTPIFNVS FTRRNLCLAI SVS