TDA7_YEAS6
ID TDA7_YEAS6 Reviewed; 636 AA.
AC B5VQN1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Topoisomerase I damage affected protein 7;
GN Name=TDA7; ORFNames=AWRI1631_141530;
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631;
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
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; ABSV01001977; EDZ69767.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VQN1; -.
DR Proteomes; UP000008988; 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_0000410748"
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
