ID   TDA11_YEASA             Reviewed;         446 AA.
AC   E7KDI6;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Topoisomerase I damage affected protein 11;
GN   Name=TDA11; ORFNames=AWRI796_2219;
OS   Saccharomyces cerevisiae (strain AWRI796) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=764097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI796;
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; ADVS01000029; EGA74590.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7KDI6; -.
DR   SMR; E7KDI6; -.
DR   PRIDE; E7KDI6; -.
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..446
FT                   /note="Topoisomerase I damage affected protein 11"
FT                   /id="PRO_0000410766"
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          392..446
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        392..432
FT                   /note="Basic and acidic 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   446 AA;  49747 MW;  A27EFA39F03F675C 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 LNNEEI