TDA7_YEASO
ID TDA7_YEASO Reviewed; 636 AA.
AC E7NM81;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 29-SEP-2021, entry version 32.
DE RecName: Full=Topoisomerase I damage affected protein 7;
GN Name=TDA7; ORFNames=FOSTERSO_3962;
OS Saccharomyces cerevisiae (strain FostersO) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=764101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FostersO;
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: 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; AEEZ01000083; EGA60795.1; -; Genomic_DNA.
DR EnsemblFungi; EGA60795; EGA60795; FOSTERSO_3962.
DR HOGENOM; CLU_029057_0_0_1; -.
DR OMA; FYQHWLD; -.
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_0000410752"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..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; 67395 MW; 8611C408C03B37F8 CRC64;
MNSNSTIGRT TLGESDTISL SFSEPSSSLN SRSTDVVFAS TSTLVPQQGS LTSLPPVSST
ATPTYYSTSL TYDETLHTSI DVSSTSTLVS STDSSSSSEQ DTYSSQYDPA TSSYSIITPS
MSIFSSTSPM SSSSSITSEW SSLTSTTPTL SXSATSLSSS WSSLSSPSSL LVSSSLSLSL
SSSYSDTKLF SFDSRSSIFS PSTPTVISPS YTYLSSISAT SFQISTTSEL SXSWFSTISS
PSTTSNKDTT FPSSSRNTST SFYSSSLSST NDFSTISKSS KLSPSASSST VSISTISVPT
SSSVSSSSSK VPSNRPSSSS SSDDTTSAYS STYTFQSLQS TTSSSIPPXT QTPSTSTIST
SPIPTSSQVF NTXAISSSED SKTIYYFYTQ TYDITDSSTT FVTGLPTTIA VAKSEVTSFS
APSSTITADM SFYQHWLDGS LDNNKNQGTS KTNTGTIVGS VVGSVGGILI CVLVVWFMLV
RKRKAKRHFK ENDSFCHEIG RRTGFPTTAQ AKEASLQAQD SGSQQRNTET ASANNPFSNE
FNFKARGNPP PVPPPRNVTA XNGSFQNMRS NFMDQENRFS YGSSFTYSSL GSSTQGGFST
LSSNSIRLGX GLDNDISHDE RNTVQNNSQG FLREII