ID G8BU90_TETPH Unreviewed; 566 AA.
AC G8BU90;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN Name=TPHA0E03790 {ECO:0000313|EMBL:CCE63468.1};
GN OrderedLocusNames=TPHA_0E03790 {ECO:0000313|EMBL:CCE63468.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE63468.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE63468.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
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DR EMBL; HE612860; CCE63468.1; -; Genomic_DNA.
DR RefSeq; XP_003685902.1; XM_003685854.1.
DR AlphaFoldDB; G8BU90; -.
DR STRING; 1071381.G8BU90; -.
DR GeneID; 11531502; -.
DR KEGG; tpf:TPHA_0E03790; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_5_0_1; -.
DR OMA; CRKFAPI; -.
DR OrthoDB; 239925at2759; -.
DR Proteomes; UP000005666; Chromosome 5.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR PANTHER; PTHR18929:SF132; PROTEIN DISULFIDE-ISOMERASE A3; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..566
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003508676"
FT DOMAIN 16..142
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 516..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 63948 MW; EA2395CD7FF67D3E CRC64;
MVSINSLLLV AGLSGNVFGA AAVARDAKAS SSDKIEQLNA TNFDQIVGSK RFFVAEFYAP
WCLHSKNIKE RLAAAADRLL PRDIVFGQID CTENKEVCDK YEIDAYPTLK IFKDSNLTHP
IAWEGSTNVD GLVAYALRKD TVPVTVVDSE SVLQDILRNS GKPVVVKNAN GKFDEQFENI
AKQRMDSITF VSFPREKDAT FSLYINKGKN ANGSPDIKEI SNLENLEYFI NDEQNFVKWI
TQETLPAFGN LTASTHSVYA SLSVPIAYYM YNRDEDATDD IIPFMKELGE TYRGKVNIVG
VDVRQYSKPI ETLGVLPQYP LFAIHDVRKN RRYVLPQLAE EEFKNLEEPV KLSQIHMKQL
LENFTKGEAK PMERSEEVPA KQDSDVYHLV GSTHDKFVFD EKRDILVRYY APWCNISAKI
EPLFNRAAQI FNEDASLKDK LALADINAFD NDVLSVDIEQ FPTLVLFPAG NNTKPVFFEG
GKSIESIMAF VENSSTHKIP GKQMFAAYRQ RVLDEQNKKE SAEKAKKASE EQAKKTSEEQ
AKKTSEEQAK KNDQQQQQQQ AVHDEL
//
