ID   TDA7_YEAS8              Reviewed;         632 AA.
AC   C8ZG52;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Topoisomerase I damage affected protein 7;
GN   Name=TDA7; ORFNames=EC1118_1N9_1728g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TDA7 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FN393086; CAY82425.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8ZG52; -.
DR   EnsemblFungi; CAY82425; CAY82425; EC1118_1N9_1728g.
DR   HOGENOM; CLU_029057_0_0_1; -.
DR   Proteomes; UP000000286; Chromosome XIV, Scaffold EC1118_1N9.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
PE   3: Inferred from homology;
KW   Glycoprotein; Isopeptide bond; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Ubl conjugation; Vacuole.
FT   CHAIN           1..632
FT                   /note="Topoisomerase I damage affected protein 7"
FT                   /id="PRO_0000410750"
FT   TRANSMEM        453..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         624
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53882"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        558
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        622
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        508
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P53882"
SQ   SEQUENCE   632 AA;  66926 MW;  2B6F107B6EF54E9E CRC64;
     MNSNSTIGRT TLGESDTISL SFSEPSSSLN SRSTDVVFAS TSTLVPQQGS LTSLPPVSST
     ATPTYYSTSL TYDETLHTSI DVSSTSTLVS STDSSSSSEQ DTYSSQYDPA TSSYSIITPS
     MSIFSSTSPM SSSSSITSEW SSLTSTTPTL SSSATSLSSS WSSLSSPSSL LVSSSLSSSS
     YSDTKLFSFD SRSSIFSPST PTVISPSYTY LSSISATSFQ ISTTSELSSS WFSTISPSTT
     SNKDTTFPSS SRNTSTSFYS SSLSSTNDFS TISKSSKLSP SASSSTVSIS TISVPTSSSV
     SSSSSKVPSN RPSSSSSSDD TTSAYSSTYT FQSLQSTTSS SIPPTTQTPS TSTISTSPIP
     TSSQVFNTAA ISSSEDSKTI YYFYTQTYDI TDSSTTFVTG LPTTIAVAKS EVTSFSAPSS
     TITADMSFYQ HWLDGSLDNN KNQGPSKTNT GTIVGSVVGS VGGILICVLV VWFMLVRKRK
     AKRHFKENDS FCHEIGRRTG FPTTAQAKEA SLQAQDSGSQ QRNTETASAN NPFSNEFNFK
     ARGNPPPVPP PRNVTATNGS FQNMRSNFMD QENRFSYGSS FTYSSLGSST QGGFSTLSSN
     SIRLGRGLDN DISHDERNTV QNNSQGFLRE II