ID G9MI10_HYPVG Unreviewed; 498 AA.
AC G9MI10;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00039846, ECO:0000256|RuleBase:RU361130};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723, ECO:0000256|RuleBase:RU361130};
GN Name=pdi1 {ECO:0000313|EMBL:EHK26345.1};
GN ORFNames=TRIVIDRAFT_111061 {ECO:0000313|EMBL:EHK26345.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK26345.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK26345.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000256|ARBA:ARBA00001182,
CC ECO:0000256|RuleBase:RU361130};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK26345.1}.
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DR EMBL; ABDF02000002; EHK26345.1; -; Genomic_DNA.
DR RefSeq; XP_013960555.1; XM_014105080.1.
DR AlphaFoldDB; G9MI10; -.
DR STRING; 413071.G9MI10; -.
DR EnsemblFungi; EHK26345; EHK26345; TRIVIDRAFT_111061.
DR GeneID; 25786771; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_111061; -.
DR eggNOG; KOG0190; Eukaryota.
DR HOGENOM; CLU_025879_5_0_1; -.
DR InParanoid; G9MI10; -.
DR OMA; FFGMKKD; -.
DR OrthoDB; 5399045at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd02961; PDI_a_family; 1.
DR CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR CDD; cd02982; PDI_b'_family; 1.
DR CDD; cd02981; PDI_b_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR005792; Prot_disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR NCBIfam; TIGR01126; pdi_dom; 2.
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 PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 4.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605792-51};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361130};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR605792-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361130}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT CHAIN 21..498
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5005133235"
FT DOMAIN 6..129
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 336..466
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 472..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 51..54
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 386..389
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 498 AA; 54623 MW; D0FE0374C87533BF CRC64;
MQQKRLTAAL LAALVAVVSA DSDVTSLTKD TFNDFINGND LVLAEFFAPW CGHCKALAPE
YEEAATTLKE KSIKLAKVDC VEEADLCKDH GVEGYPTLKV FRGLDKVTPY TGPRKADGIT
SYMVKQSLPA VSVLTKDTLE DFKTADNVVL VAYIASDDKA SNETFTAIAN ELRDTYLFGG
INDAAVAKAE GVEFPSIVLY KNFDEGKNVF SEKFDADAIR SFAKVAATPL VGEVGPETYA
GYMSAGIPLA YIFAETPEER VELSKSLKPI AEKYKGKINF ATIDAKNFGS HAANINLKTD
KFPAFAIHDI EKNLKFPFDQ EKEITEKDIA QFVDNFSAGK IEPSIKSEPI PETQEGPVTV
VVAHTYKDIV LDDTKDVLIE FYAPWCGHCK ALAPKYDELA SLYANSEFKD KVVVAKVDAT
NNDVPDEIQG FPTIKLYPAG DKQNPVTYSG ARTVEDFIEF IKENGKYKAS VEVPVETTEE
ATPEATKEAK ADEDHDEL
//
