TDA9_YEAST
ID TDA9_YEAST Reviewed; 1251 AA.
AC Q04545; D6W0K2; Q03621;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable transcription factor TDA9;
DE AltName: Full=Topoisomerase I damage affected protein 9;
GN Name=TDA9; OrderedLocusNames=YML081W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP DNA-BINDING, AND PREDICTION OF FUNCTION.
RX PubMed=19111667; DOI=10.1016/j.molcel.2008.11.020;
RA Badis G., Chan E.T., van Bakel H., Pena-Castillo L., Tillo D., Tsui K.,
RA Carlson C.D., Gossett A.J., Hasinoff M.J., Warren C.L., Gebbia M.,
RA Talukder S., Yang A., Mnaimneh S., Terterov D., Coburn D., Li Yeo A.,
RA Yeo Z.X., Clarke N.D., Lieb J.D., Ansari A.Z., Nislow C., Hughes T.R.;
RT "A library of yeast transcription factor motifs reveals a widespread
RT function for Rsc3 in targeting nucleosome exclusion at promoters.";
RL Mol. Cell 32:878-887(2008).
RN [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=21173034; DOI=10.1101/gr.109033.110;
RA Reid R.J., Gonzalez-Barrera S., Sunjevaric I., Alvaro D., Ciccone S.,
RA Wagner M., Rothstein R.;
RT "Selective ploidy ablation, a high-throughput plasmid transfer protocol,
RT identifies new genes affecting topoisomerase I-induced DNA damage.";
RL Genome Res. 21:477-486(2011).
CC -!- FUNCTION: DNA-binding protein that acts probably as a transcription
CC factor.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Leads to cell death when overexpressing the
CC camptothecin mimetic TOP1-T(722)A mutant.
CC {ECO:0000269|PubMed:21173034}.
CC -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RSF2/TDA9 family. {ECO:0000305}.
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DR EMBL; Z46660; CAA86657.1; -; Genomic_DNA.
DR EMBL; Z46373; CAA86497.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09816.1; -; Genomic_DNA.
DR PIR; S49645; S49645.
DR RefSeq; NP_013630.1; NM_001182440.1.
DR AlphaFoldDB; Q04545; -.
DR BioGRID; 35060; 56.
DR IntAct; Q04545; 2.
DR STRING; 4932.YML081W; -.
DR iPTMnet; Q04545; -.
DR MaxQB; Q04545; -.
DR PaxDb; Q04545; -.
DR PRIDE; Q04545; -.
DR EnsemblFungi; YML081W_mRNA; YML081W; YML081W.
DR GeneID; 854894; -.
DR KEGG; sce:YML081W; -.
DR SGD; S000004546; TDA9.
DR VEuPathDB; FungiDB:YML081W; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000176773; -.
DR HOGENOM; CLU_003977_1_0_1; -.
DR InParanoid; Q04545; -.
DR OMA; NFDYFIM; -.
DR BioCyc; YEAST:G3O-32672-MON; -.
DR PRO; PR:Q04545; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04545; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0019413; P:acetate biosynthetic process; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1251
FT /note="Probable transcription factor TDA9"
FT /id="PRO_0000046864"
FT ZN_FING 61..83
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 89..112
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 160..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1251 AA; 141465 MW; 612F064177D6FF3B CRC64;
MSSEEFKGLP IKRDISSTIY ADRPPALSAP PCVGATGNDK IQVLPIPKKS RTIKTDKPRP
FLCHICTRGF VRQEHLKRHQ RAHTNEKPFL CVFCGRCFAR RDLVLRHQHK LHSALVSKES
INSKDKTEID AINDKNIIQI QGNKQTILPT PSNPLAKTAV QLKKAAKEKK NGKQGKLDLS
PSYGANNHST DVSPSVGNSS TPAVIEETDS SSHFPLPDTN IPTKSKRHAS FSASSAFTYS
SDNFQKLHQQ AKSDFDELQE SIPHQVGFST PQLTAQQLIE NAIESGVVDL ETLDLPPFLS
LDGLPPASSS AAVAASEQID ICPSSATDTI SGANSTPNQA ATAPPFQLPI ARESSSLFLA
NTPYLSDFLT MGSSYGGSGG FAKSITADPS LDYFNYKNHS HPDSRHNNSS SGINYSNNKN
NNESIEKSQN NSNVINETID HTDIHAHHAD AHDDSFIESE EWLSKFIMDS QIDNDLKLNI
NHFNDIGFNN LHPQNPTTHS EPRNMHNENR DMHRSASKFQ SVSENISPRE QMSLFKTKQN
KAISKFLSDE KIPSTASPSS SASPVQFDKK NVDINEFLLD ESVSNLFTTR QIDLFKKNVN
LYSPLFQNQK DAVSSTSLTP SLTTQTATTQ SGPGWTDSSQ KLTFFTEQLR NLIIKENNLK
SNLFPTVDEL NHYVDLYQVE FHKYFPFIHL YSIIPSSENY PLVISISMIG ALYGFHSTHA
LLLSKIARTR VRMFLENTRS NHDKTPIWLM QSLVLLTFTS IFSNDMNAFR TVNTQIMILV
QLIKISKLNY PLENFIKPPI ESDHVLEYQD NPAVLNQFKA QYNTREQINR NFKYFILAQS
RIRICHIVLL ISNLFKSLVD FDCCFHSIDL KCGVPCYNEV LFFCENSRTW NENLTRFNIV
LDSKFSLIEV SNGESNYEKC LMYLSNGNPY LYKNAKISFK TLLSLLISIH EKINIERDAL
KDSYESDFHA KNVQWRMHSR PLVATMLKHW ELLYIKNGGI LALSDENLPI INTNPSFRLI
IPLYFFAKLR KCLDIAPTLR CIWNQDWNSM NSSLEKVCYE RESLREATEY AVSVITFWID
TVSVMKGKST QTPIFTITCI FVSILVIAGY MRRLEDFAQN KNSDCMIGSL KSTDRILWLK
AFKTLKRIES HLSEREYKLQ TFAEFLRVPD NGSLDIESLD SSLIENTLNS HDVTNQALDI
ITRTRLSSRT LYCGARILGD TPVWPVSLLF AHALQSRAIY NINHRKSVNS V
