TF3A_YEAST
ID TF3A_YEAST Reviewed; 429 AA.
AC P39933; D6W4I6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Transcription factor IIIA;
DE Short=TFIIIA;
DE AltName: Full=Putative zinc finger protein 1;
GN Name=PZF1; Synonyms=TFC2, TFIIIA; OrderedLocusNames=YPR186C;
GN ORFNames=P9677.9;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1737784; DOI=10.1016/s0021-9258(19)50728-1;
RA Archambault J., Milne C.A., Schappert K.T., Baum B., Friesen J.D.,
RA Segall J.;
RT "The deduced sequence of the transcription factor TFIIIA from Saccharomyces
RT cerevisiae reveals extensive divergence from Xenopus TFIIIA.";
RL J. Biol. Chem. 267:3282-3288(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1570325; DOI=10.1073/pnas.89.9.3999;
RA Woychik N.A., Young R.A.;
RT "Genes encoding transcription factor IIIA and the RNA polymerase common
RT subunit RPB6 are divergently transcribed in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3999-4003(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Interacts with the internal control region (ICR) of
CC approximately 50 bases within the 5S RNA genes, is required for correct
CC transcription of these genes by RNA polymerase III. Also binds the
CC transcribed 5S RNA's.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M80611; AAB08014.1; -; Genomic_DNA.
DR EMBL; M90638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U25841; AAB64615.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11602.1; -; Genomic_DNA.
DR PIR; S20050; S20050.
DR RefSeq; NP_015512.1; NM_001184283.1.
DR AlphaFoldDB; P39933; -.
DR SMR; P39933; -.
DR BioGRID; 36358; 98.
DR MINT; P39933; -.
DR STRING; 4932.YPR186C; -.
DR iPTMnet; P39933; -.
DR MaxQB; P39933; -.
DR PaxDb; P39933; -.
DR PRIDE; P39933; -.
DR EnsemblFungi; YPR186C_mRNA; YPR186C; YPR186C.
DR GeneID; 856316; -.
DR KEGG; sce:YPR186C; -.
DR SGD; S000006390; PZF1.
DR VEuPathDB; FungiDB:YPR186C; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000176804; -.
DR HOGENOM; CLU_044102_0_0_1; -.
DR InParanoid; P39933; -.
DR OMA; ITHTKSF; -.
DR BioCyc; YEAST:G3O-34309-MON; -.
DR PRO; PR:P39933; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P39933; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001010; F:RNA polymerase II sequence-specific DNA-binding transcription factor recruiting activity; IDA:SGD.
DR GO; GO:0001002; F:RNA polymerase III type 1 promoter sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..429
FT /note="Transcription factor IIIA"
FT /id="PRO_0000047086"
FT ZN_FING 49..74
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 80..102
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 108..130
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 134..159
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 163..186
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 194..219
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 222..244
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 253..277
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..389
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 50027 MW; 209B1EDEA20422D9 CRC64;
MGGEVLNNEG MPLAELKQET IPISRSESSE SLNSLTSTRS SSSNRPKTYF CDYDGCDKAF
TRPSILTEHQ LSVHQGLRAF QCDKCAKSFV KKSHLERHLY THSDTKPFQC SYCGKGVTTR
QQLKRHEVTH TKSFICPEEG CNLRFYKHPQ LRAHILSVHL HKLTCPHCNK SFQRPYRLRN
HISKHHDPEV ENPYQCTFAG CCKEFRIWSQ LQSHIKNDHP KLKCPICSKP CVGENGLQMH
MIIHDDSLVT KNWKCHICPD MSFSRKHDLL THYGSIHTEE DIPLELKYKI SDIQQLVQDH
GVQLGNSKHS NEQDEEKISN RLRKRRKLTE NNNVEFLQNE VDLEKRLESG ENGLNLLLNT
VGRKYRCFYN NCSRTFKTKE KYEKHIDKHK VHELKLKILQ EKEENKTLVD QNHKEPFIIQ
KETQSAGDK
