ID   TDA11_YEASO             Reviewed;         478 AA.
AC   E7NIP9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Topoisomerase I damage affected protein 11;
GN   Name=TDA11; ORFNames=FOSTERSO_2176;
OS   Saccharomyces cerevisiae (strain FostersO) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FostersO;
RX   PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "Whole-genome comparison reveals novel genetic elements that characterize
RT   the genome of industrial strains of Saccharomyces cerevisiae.";
RL   PLoS Genet. 7:E1001287-E1001287(2011).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TDA11 family. {ECO:0000305}.
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DR   EMBL; AEEZ01000050; EGA62015.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7NIP9; -.
DR   SMR; E7NIP9; -.
DR   EnsemblFungi; EGA62015; EGA62015; FOSTERSO_2176.
DR   HOGENOM; CLU_046807_0_0_1; -.
DR   OMA; WSFVSDV; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR031388; Tda11.
DR   Pfam; PF17084; TDA11; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Phosphoprotein.
FT   CHAIN           1..478
FT                   /note="Topoisomerase I damage affected protein 11"
FT                   /id="PRO_0000410768"
FT   REGION          32..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          182..219
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        255..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         239
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P38854"
FT   MOD_RES         247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38854"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38854"
SQ   SEQUENCE   478 AA;  53335 MW;  D84990B6FFE4E283 CRC64;
     MNKFDEFIES NEKDLDVDTS TRNSIISMSP VRKTGRKIRS ASSNGYRLEH HRTSSAGSMH
     SQRLMTPTRL NDQDHPLQAK PDARRVVTRH SSVSVPNAMS KRRSLIQPMV VPTTPESQNN
     LPFGGSVSHS EGSYGIPLES TTVLSSEQAM ASGLRRSRNG SSQSVNSMIA TTIPTNGVDV
     SALLQSLATK ELELLECKQK IEDLKKQTQH EEQNYTRRAC ELHELKEQVS KHLDPSLNTP
     VKNRAFSPVY QNIPLESRTE NAGNSSLPSS VSKPKNMGHQ STNQSRSVSP QDIQERRQRD
     DSSDSSKQSL WSKPLALFNQ FDKIIQHEIE RTLNWDDSLS GTPEVQEGTP TSNSESSAQQ
     YDNEAPGARQ KSPSQGSVSR SLWSFVSDVK AGLLGIEEEN DNDVITDNRC DPVYKSDRQH
     EQKKSTHKIT NRGQAEDSGD DSSLNMRKFK TTTKFQKDNA GNNSLTDESG HRTREKKK