ID   TDA11_YEASL             Reviewed;         475 AA.
AC   E7KPK0;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Topoisomerase I damage affected protein 11;
GN   Name=TDA11; ORFNames=QA23_2213;
OS   Saccharomyces cerevisiae (strain Lalvin QA23) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin QA23;
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; ADVV01000041; EGA82562.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7KPK0; -.
DR   SMR; E7KPK0; -.
DR   EnsemblFungi; EGA82562; EGA82562; QA23_2213.
DR   HOGENOM; CLU_046807_0_0_1; -.
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..475
FT                   /note="Topoisomerase I damage affected protein 11"
FT                   /id="PRO_0000410767"
FT   REGION          32..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          179..231
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        252..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         236
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P38854"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38854"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38854"
SQ   SEQUENCE   475 AA;  53096 MW;  A3659CD73388ED0C CRC64;
     MNKFDEFIES NEKDLDVDTS TRNSIISMSP VRKTGRKIRS ASSNGYRLEH HRTSSAGSMH
     SQRLMTPTRL NDQDHPLQAK PDARRVVTRH SSVSVPNAMS KRRSLIQPMV VPTTPESQNN
     LPSVSHSEGS YGIPLESTTV LSSEQAMASG LRRSRNGSSQ SVNSMIATTI PTNGVDVSAL
     LQSLATKELE LLECKQKIED LKKQTQHEEQ NYTRRARELH ELKEQVSKHL DPSLNTPVKN
     RAFSPVYQNI PLESRTENAG NSSLPSSVSK PKNMGHQSTN QSRSVSPQDI QERRQRDDSS
     DSSKQSLWSK PLALFNQFDK IIQHEIERTL NWDDSLSGTP EVQEGTPTSN SESSAQQYDN
     EAPGARQKSP SQGSVSRSLW SFVSDVKAGL LGIEEENDND VITDNRCDPV YKSDRQHEQK
     KSTHKITNRG QAEDSGDDSS LNTRKFKTTT KFQKDNAGNN SLTDESGHRT REKKK