SFC6_SCHPO
ID SFC6_SCHPO Reviewed; 582 AA.
AC O60174;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Transcription factor tau subunit sfc6;
DE AltName: Full=TFIIIC subunit sfc6;
DE AltName: Full=Transcription factor C subunit 6;
GN Name=sfc6 {ECO:0000312|EMBL:CAA18865.1};
GN Synonyms=tfc6 {ECO:0000250|UniProtKB:Q06339}; ORFNames=SPBC21H7.05;
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN TFIIIC, AND
RP INTERACTION WITH SFC1; SFC3 AND SFC4.
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 [2] {ECO:0000312|EMBL:CAA18865.1}
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 [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=16751097; DOI=10.1016/j.cell.2006.04.028;
RA Noma K., Cam H.P., Maraia R.J., Grewal S.I.S.;
RT "A role for TFIIIC transcription factor complex in genome organization.";
RL Cell 125:859-872(2006).
RN [4] {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 tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and
CC similar genes. Cooperates with sfc3 in DNA binding. Localizes to
CC chromatin insulator sequence without recruiting RNA polymerase III and
CC plays a role in nuclear organization. {ECO:0000250|UniProtKB:Q06339,
CC ECO:0000269|PubMed:10906331, ECO:0000269|PubMed:16751097}.
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 sfc4. {ECO:0000250|UniProtKB:Q06339,
CC ECO:0000269|PubMed:10906331}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAA18865.1; -; Genomic_DNA.
DR PIR; T39931; T39931.
DR RefSeq; NP_595930.1; NM_001021838.2.
DR AlphaFoldDB; O60174; -.
DR SMR; O60174; -.
DR BioGRID; 276952; 5.
DR IntAct; O60174; 1.
DR STRING; 4896.SPBC21H7.05.1; -.
DR iPTMnet; O60174; -.
DR MaxQB; O60174; -.
DR PaxDb; O60174; -.
DR EnsemblFungi; SPBC21H7.05.1; SPBC21H7.05.1:pep; SPBC21H7.05.
DR GeneID; 2540424; -.
DR KEGG; spo:SPBC21H7.05; -.
DR PomBase; SPBC21H7.05; sfc6.
DR VEuPathDB; FungiDB:SPBC21H7.05; -.
DR eggNOG; ENOG502S1WJ; Eukaryota.
DR HOGENOM; CLU_459389_0_0_1; -.
DR InParanoid; O60174; -.
DR OMA; HKRDICY; -.
DR PhylomeDB; O60174; -.
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:O60174; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
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:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:PomBase.
DR GO; GO:0071443; F:tDNA binding; 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; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..582
FT /note="Transcription factor tau subunit sfc6"
FT /id="PRO_0000307796"
FT REPEAT 221..262
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 268..314
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 326..369
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 66203 MW; E90C1A43F951AE1D CRC64;
MGPKSKEYEN PSSYKNDEDN DDDGDFVLEN VMSEEDIEIE TPSRNRKRVS TTRRTPSKPI
RSQPLTPSSS KGAGNEPKSQ NSSTTRGSAK KQSSKGLEEK LINSYGTHVE SLNKGRRLIE
IWKYYETAPG QSSFEGQTSS DSKLQTLLNL DGQQLLSYSE NPFYLFEVKN LSISFHFESP
QQVEPCQPVN PFKENPQKSG FVVNTGIPLS SVSWLPTNKE TQFLAVGGML KFSETTESVF
MRTSGRNQIQ LWKLENKTNF KSEFILYHDW GSVLQLEWCP TISVEDSILG FLAVVCSDGK
LRVLRVPRSP VKFHVFVEQA DFTFGFNDSL ISCCTWVSPE HGDIHQILVG CSNGYLALWD
ILSSQECPLF YIPYHDSYIH NVVQCLDDFP WLFLTTAFDC YTRIFDIRDP IIDNRPLSHK
RDICYTITWN NMLQSIISCS ESQSVVIESL RGTSTQLLDE RNGSIISLSN SKFHPFVACA
ASDGIVTIVN PFRLLGFSHK QKANVHRIFQ LEYSEKQDSY RMLDGFRPRL PKAKKLDMYI
YPWQIQVNKV EWNGNKGYAG WLASGMACGI LRVEDLSAVE RR
