ID A0A178ADX7_9PLEO Unreviewed; 382 AA.
AC A0A178ADX7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00039846};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN ORFNames=IQ06DRAFT_56409 {ECO:0000313|EMBL:OAK95896.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK95896.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK95896.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK95896.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in the folding of proteins containing disulfide
CC bonds, may be involved in glycosylation, prolyl hydroxylation and
CC triglyceride transfer. {ECO:0000256|ARBA:ARBA00002692}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347}.
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DR EMBL; KV441721; OAK95896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178ADX7; -.
DR STRING; 765868.A0A178ADX7; -.
DR InParanoid; A0A178ADX7; -.
DR OrthoDB; 2436898at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
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; 1.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 27..122
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF00085"
FT REGION 344..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 43393 MW; FAEBCB70D7464C06 CRC64;
MRISIFLAGY TSAFVAAEVL REPPGEAEFR SILDLNEKVL VSFTSRSLDS LAPFNDIFRK
TVKNASIPFV TLDCDQAVSL CASYDINSYP TIRYYDRIQN GETVFTRYRG PRTSKGLLSF
VNKRELPILT HLERADMDFR RIDDIVFIAM LDPADKHHLN IFTTIAQRHH LDYVFGYTTD
LTIPEKEKIQ APSVICYRNN DGDNIILGGA FTEKDAENFV FASRASIMRE FKEKFVEDFM
QRDKLTVYVF TRTPEVSRTM RHRLLEVAMS LRHVVTFAMV DVGRYPDMPR NFGTEMSGEV
VLVVHAPFND DLFFWKKGKK VEKEGVEEML ITVLKGNAKQ GQVFGEGAED VEDGTREGGD
GEAEMQVGDD VEAGGQECHD EL
//
