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SFC4_SCHPO
ID   SFC4_SCHPO              Reviewed;        1006 AA.
AC   O74458;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Transcription factor tau subunit sfc4;
DE   AltName: Full=TFIIIC subunit sfc4;
DE   AltName: Full=Transcription factor C subunit 4;
GN   Name=sfc4 {ECO:0000312|EMBL:CAA20753.1};
GN   Synonyms=tfc4 {ECO:0000250|UniProtKB:P33339}; ORFNames=SPCC16C4.14c;
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:CAA20753.1}
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   FUNCTION, IDENTIFICATION IN TFIIIC, AND INTERACTION WITH SFC1; SFC3 AND
RP   SFC6.
RX   PubMed=10906331; DOI=10.1074/jbc.m004635200;
RA   Huang Y., Hamada M., Maraia R.J.;
RT   "Isolation and cloning of four subunits of a fission yeast TFIIIC complex
RT   that includes an ortholog of the human regulatory protein TFIIICbeta.";
RL   J. Biol. Chem. 275:31480-31487(2000).
RN   [3] {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).
CC   -!- FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by binding to
CC       intragenic promoter elements. Upstream of the transcription start site,
CC       TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is
CC       sufficient for RNA polymerase III recruitment and function. Part of the
CC       tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and
CC       similar genes. Sfc4 is the TFIIIB assembling subunit of TFIIIC.
CC       {ECO:0000250|UniProtKB:P33339, ECO:0000269|PubMed:10906331}.
CC   -!- SUBUNIT: Component of the TFIIIC complex including sfc1, sfc3, sfc4,
CC       sfc6 and sfc7. The subunits are organized in two globular domains, tauA
CC       and tauB, connected by a proteolysis-sensitive and flexible linker.
CC       Interacts with sfc1, sfc3 and sfc6. {ECO:0000269|PubMed:10906331}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P33339}.
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DR   EMBL; CU329672; CAA20753.1; -; Genomic_DNA.
DR   PIR; T41104; T41104.
DR   RefSeq; NP_587924.1; NM_001022915.2.
DR   AlphaFoldDB; O74458; -.
DR   SMR; O74458; -.
DR   BioGRID; 275758; 15.
DR   IntAct; O74458; 1.
DR   STRING; 4896.SPCC16C4.14c.1; -.
DR   iPTMnet; O74458; -.
DR   MaxQB; O74458; -.
DR   PaxDb; O74458; -.
DR   PRIDE; O74458; -.
DR   EnsemblFungi; SPCC16C4.14c.1; SPCC16C4.14c.1:pep; SPCC16C4.14c.
DR   GeneID; 2539187; -.
DR   KEGG; spo:SPCC16C4.14c; -.
DR   PomBase; SPCC16C4.14c; sfc4.
DR   VEuPathDB; FungiDB:SPCC16C4.14c; -.
DR   eggNOG; KOG2076; Eukaryota.
DR   HOGENOM; CLU_002391_0_1_1; -.
DR   InParanoid; O74458; -.
DR   OMA; CLIAWMA; -.
DR   PhylomeDB; O74458; -.
DR   Reactome; R-SPO-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR   Reactome; R-SPO-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR   PRO; PR:O74458; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:PomBase.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:PomBase.
DR   GO; GO:0006383; P:transcription by RNA polymerase III; IBA:GO_Central.
DR   GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:PomBase.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR039340; Tfc4/TFIIIC-102/Sfc4.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR23082; PTHR23082; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF48452; SSF48452; 3.
DR   PROSITE; PS50005; TPR; 8.
DR   PROSITE; PS50293; TPR_REGION; 4.
PE   1: Evidence at protein level;
KW   Coiled coil; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; TPR repeat; Transcription; Transcription regulation.
FT   CHAIN           1..1006
FT                   /note="Transcription factor tau subunit sfc4"
FT                   /id="PRO_0000307795"
FT   REPEAT          133..166
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          205..238
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          277..310
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          396..429
FT                   /note="TPR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          431..464
FT                   /note="TPR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          466..499
FT                   /note="TPR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          841..874
FT                   /note="TPR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          924..957
FT                   /note="TPR 8"
FT                   /evidence="ECO:0000255"
FT   REGION          64..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          506..554
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        77..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1006 AA;  116401 MW;  7000AC42E602E2B2 CRC64;
     MIQNGGNSYV DSNMNETQND TTDNFDAEMQ DLNGYISEIV DEARNVSEVD AKFLGDTSAL
     QAEGLWSDEE SDYEGSDDES NFSKTASRTE DDIANEEWEE NLKAVAGFRK VRKGHKGRGR
     VSRADMLPSV EVQQMLSLAN HLFAQEGNFD EAQKLAEEIV RIDNNVIAAW KMLGECHRQR
     GNGRVNIEKC LIAWMAAAHL KPKDHELWFT CAKLSESLEF WDQADYCYNR AVSAKPPNKS
     ELKKYIWNRS VLNKEHGSLK KAAEGFKFLL QSSPYNASIL KNLAEIYIKI HAPREILKQF
     EIAWKYFYQY PAPPIGNDIF DLPTLNLYAE LLLLDHQWSN LIRLINRGVR WFRGRKSESF
     WDEFDDDREW DVDERRREFP NASEEHTNKE AYLLPHLFRT KLGIARLKTG ELPEAELHFS
     VIKNLPPDYA WGMLYDIAKA YMDIERLDLA LEYFVLICNH EPAQNIGLWY NMGVCYLELK
     EYEHAQQCME AILIVDNSNT NALIKLAEIN ELQDNRDAAL EIVTNIFEQR RNINELEREQ
     SQNEDHEKNV GSQLFVGNQK VPQDKWEKRA RISRSKEEAR QFTIWKTEET QRRFHKLDIL
     RQSLKKEENV SESLNEWLAI ASELIDEFVS IKAFFPSEKK ARARAGLLTR RTRYASLNDQ
     LTSMINRLND SLTRTKYGDL DLDTILRTGY FRNVSIDAWY QLFVEFSLRL TKVGSVQQAY
     DVLTTAMGAI LFDQDTIKRQ NLRWCMLACS MYARDPQGAL TPLRWVFTTF QFRQDTYRLF
     SAVLSQGYEC SRAFVDSANQ KFLLRLIKLM DQLMSNSLVS GAATLVKNDD GLATVPTSYD
     PVLVLLYGHI MARNRSWIPA INYYSRAFAI NPDCPITNLS LGLAYLHRAM QRLSDNRHYQ
     ILQGFTFLYR YYDLRVNEGL GEKQEALYNL GKAYHFIGLE HYAVKYYEAV LGLSPMSQGD
     KMTSSESTVS TTYDFGFEAA YNLRLIYICS GNIKLAFQIS SKYLIF
 
 
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