TDA11_YEAS1
ID TDA11_YEAS1 Reviewed; 504 AA.
AC B3LSS3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Topoisomerase I damage affected protein 11;
GN Name=TDA11; ORFNames=SCRG_04871;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TDA11 family. {ECO:0000305}.
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DR EMBL; CH408053; EDV09204.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LSS3; -.
DR SMR; B3LSS3; -.
DR EnsemblFungi; EDV09204; EDV09204; SCRG_04871.
DR HOGENOM; CLU_046807_0_0_1; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
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..504
FT /note="Topoisomerase I damage affected protein 11"
FT /id="PRO_0000410761"
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..504
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 COMPBIAS 465..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..504
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 504 AA; 56314 MW; AE8B894335D1DB63 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 LNMRKFKTTT KFQKDNAGNN SLTDESGHRT REKKSKRSSN
KLSFIGEPDN DNSSVKNSVE MTDF