ID A2RA59_ASPNC Unreviewed; 359 AA.
AC A2RA59;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN Name=tigA {ECO:0000313|EMBL:CAK47274.1};
GN ORFNames=An18g02020 {ECO:0000313|EMBL:CAK47274.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK47274.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK47274.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000256|ARBA:ARBA00006347, ECO:0000256|RuleBase:RU004208}.
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DR EMBL; AM270398; CAK47274.1; -; Genomic_DNA.
DR RefSeq; XP_001398661.1; XM_001398624.2.
DR AlphaFoldDB; A2RA59; -.
DR SMR; A2RA59; -.
DR EnsemblFungi; CAK47274; CAK47274; An18g02020.
DR GeneID; 4989762; -.
DR KEGG; ang:An18g02020; -.
DR VEuPathDB; FungiDB:An18g02020; -.
DR HOGENOM; CLU_038617_1_1_1; -.
DR OrthoDB; 52245at2759; -.
DR Proteomes; UP000006706; Chromosome 8L.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd00238; ERp29c; 1.
DR CDD; cd02998; PDI_a_ERp38; 2.
DR Gene3D; 1.20.1150.12; Endoplasmic reticulum resident protein 29, C-terminal domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR011679; ERp29_C.
DR InterPro; IPR036356; ERp29_C_sf.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01126; pdi_dom; 2.
DR PANTHER; PTHR45672:SF11; PROTEIN DISULFIDE-ISOMERASE C17H9.14C; 1.
DR PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR Pfam; PF07749; ERp29; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF47933; ERP29 C domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CAK47274.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..359
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002645054"
FT DOMAIN 8..129
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 131..250
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 359 AA; 38592 MW; 346B64197BA37608 CRC64;
MVRLSNLVSC LGLASAVTAA VVDLVPKNFD DVVLKSGKPA LVEFFAPWCG HCKNLAPVYE
ELGQAFAHAS DKVTVGKVDA DEHRDLGRKF GVQGFPTLKW FDGKSDEPED YKGGRDLESL
SSFISEKTGV KPRGPKKEPS KVEMLNDATF KGAVGGDNDV LVAFTAPWCG HCKNLAPTWE
ALANDFVLEP NVVIAKVDAD AENGKATARE QGVSGYPTIK FFPKGSTESV PYEGARSEQA
FIDFLNEKTG THRTVGGGLD TKAGTIASLD ELIASTSAAD LAAAVKKAAT ELKDKYAQYY
VKVADKLSQN AEYAAKELAR LEKILAKGGS APEKVDDLIS RSNILRKFVG EEKEAKDEL
//
