ID   TDA7_YEAS1              Reviewed;         636 AA.
AC   B3LP27;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Topoisomerase I damage affected protein 7;
GN   Name=TDA7; ORFNames=SCRG_03307;
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: Vacuole membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TDA7 family. {ECO:0000305}.
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DR   EMBL; CH408049; EDV12422.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LP27; -.
DR   EnsemblFungi; EDV12422; EDV12422; SCRG_03307.
DR   HOGENOM; CLU_029057_0_0_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
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..636
FT                   /note="Topoisomerase I damage affected protein 7"
FT                   /id="PRO_0000410746"
FT   TRANSMEM        457..477
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          238..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         628
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53882"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        562
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        626
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        512
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P53882"
SQ   SEQUENCE   636 AA;  67389 MW;  56FED4ADC95CF00E CRC64;
     MNSNSTIGRT TLGESDTISL SFSEPSSSLN SRSTDVVFAS TSTLVPQQGS LTSLPPVSST
     ATPTYYSTSL TYDETLHTSI DVSSTSTLVS STDSSSSSEQ DTYSSQYDPA TSSYSIITPS
     MSIFSSTSPM SSSSSITSEW SSLTSTTPTL SSSATSLSSS WSSLSSPSSL LVSSSLSLSL
     SSSYSDTKLF SFDSRSSIFS PSTPTVISPS YTYLSSISAT SFQISTTSEL SSSWFSTISS
     PSTTSNKDTT FPSSSRNTST SFYSSSLSST NDFSTISKSS KLSPSASSST VSISTISVPT
     SSSVSSSSSK VPSNRPSSSS SSDDTTSAYS STYTFQSLQS TTSSSIPPTT QTPSTSTIST
     SPIPTSSQVF NTVAISSSED SKTIYYFYTQ TYDITDSSTT FVTGLPTTIA VAKSEVTSFS
     APSSTITADM SFYQHWLDGS LDNNKNQGTS KTNTGTIVGS VVGSVGGILI CVLVVWFMLV
     RKRKAKRHFK ENDSFCHEIG RRTGFPTTAQ AKEASLQAQD SGSQQRNTET ASANNPFSNE
     FNFKARGNPP PVPPPRNVTA MNGSFQNMRS NFMDQENRFS YGSSFTYSSL GSSTQGGFST
     LSSNSIRLGR GLDNDISHDE RNTVQNNSQG FLREII