ID A0A427XRY3_9TREE Unreviewed; 402 AA.
AC A0A427XRY3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN ORFNames=EHS25_006197 {ECO:0000313|EMBL:RSH81575.1};
OS Saitozyma podzolica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Trimorphomycetaceae; Saitozyma.
OX NCBI_TaxID=1890683 {ECO:0000313|EMBL:RSH81575.1, ECO:0000313|Proteomes:UP000279259};
RN [1] {ECO:0000313|EMBL:RSH81575.1, ECO:0000313|Proteomes:UP000279259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27192 {ECO:0000313|EMBL:RSH81575.1,
RC ECO:0000313|Proteomes:UP000279259};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Saitozyma podzolica DSM 27192.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RSH81575.1}.
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DR EMBL; RSCD01000029; RSH81575.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427XRY3; -.
DR STRING; 1890683.A0A427XRY3; -.
DR Proteomes; UP000279259; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000279259};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..402
FT /note="protein disulfide-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019164775"
FT DOMAIN 12..130
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 132..253
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 402 AA; 43197 MW; B6E9B34C3C276A6C CRC64;
MRLSLSLSAA VLGLASLVRA SNVIDLDTKN FDKIVGGSKG GSLVEFFAPW CGHCKNLAPT
WEQLADAFPS DKVVIAKTDA DGVGRELGTR YGVTGFPTLK WFPAGSTEAV DYTGGRDLDS
LAAFVTEKSG VKSKIKPPPP PAAVQLDSSN FADIALDESK NVLVAFTAPW CGHCKNMKPA
YEKVARAFLP ETDCVVAQMN ADDEENKPIA SEYGVRSFPT IKFFPKGADK EPVMYSSGRS
EEQFIEFLNE NCGTHRSASG LLTEAAGKVL PLDKLASSFF TASLPERPAI LDEAKSYLAS
LSGVEKKVKD SAAYYVRAME RIVEKGEAWL TKEQARIAGL LASPSLAPTK LDELKIKANI
LSSFAVQKIT DLYEAAEEAV EGAGQVVYEA AKDAGHKIKA EL
//
