ID   A0A0G4MQD8_9PEZI        Unreviewed;       235 AA.
AC   A0A0G4MQD8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00039846};
DE            EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
DE   Flags: Fragment;
GN   ORFNames=BN1708_016526 {ECO:0000313|EMBL:CRK36476.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK36476.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK36476.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK36476.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) 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; CVQH01024084; CRK36476.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4MQD8; -.
DR   STRING; 100787.A0A0G4MQD8; -.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
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   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT   DOMAIN          99..235
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CRK36476.1"
FT   NON_TER         235
FT                   /evidence="ECO:0000313|EMBL:CRK36476.1"
SQ   SEQUENCE   235 AA;  25961 MW;  6FCC5606387D1EA7 CRC64;
     TYSGYMEAGL PLAYIFAETA EEREELSKAL KPIAEKQRGV INFATIDAKS FGAHAGNLNL
     QADKFPAFAI QETVKNQKFP FDQEKKITVE AITSFVDDFV AGKIEPSIKS EPIPETQEGS
     VTVVVAKNYE QIVLDDTKDV LIEFYAPWCG HCKALAPKYE ELATLYGESE FKDKVVIAKV
     DATLNDVPDE IQGFPTIKLY PAGGKQVWAD EIKLLESLIG MDAESDAFAA LEREL
//