ID A0A1D6H3L5_MAIZE Unreviewed; 343 AA.
AC A0A1D6H3L5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=protein disulfide-isomerase {ECO:0000256|ARBA:ARBA00012723};
DE EC=5.3.4.1 {ECO:0000256|ARBA:ARBA00012723};
GN ORFNames=ZEAMMB73_Zm00001d015747 {ECO:0000313|EMBL:AQK69417.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK69417.1};
RN [1] {ECO:0000313|EMBL:AQK69417.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK69417.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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}.
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DR EMBL; CM000781; AQK69417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6H3L5; -.
DR SMR; A0A1D6H3L5; -.
DR STRING; 4577.A0A1D6H3L5; -.
DR ExpressionAtlas; A0A1D6H3L5; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd00238; ERp29c; 1.
DR CDD; cd02998; PDI_a_ERp38; 1.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.20.1150.12; Endoplasmic reticulum resident protein 29, C-terminal domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR011679; ERp29_C.
DR InterPro; IPR036356; ERp29_C_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01126; pdi_dom; 1.
DR PANTHER; PTHR45672:SF9; PROTEIN DISULFIDE ISOMERASE-LIKE 2-1; 1.
DR PANTHER; PTHR45672; PROTEIN DISULFIDE-ISOMERASE C17H9.14C-RELATED; 1.
DR Pfam; PF07749; ERp29; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF47933; ERP29 C domain-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AQK69417.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 105..136
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 105..134
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 135..253
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 343 AA; 37624 MW; A6DFD0D146A09368 CRC64;
MASQCAPPLP PRPRATAPFL LGHAPPHARP PRCAALTPSV LAATRPCFLA STRVLLRPQS
EEAPASCSWS PSDPLLCASP ASALLVAWRR RHSPAMGCKA CDKPKPNYRK GLWSLEEDQK
LRDYILLHGH GCWSALPMKA GTNVKIAAIP SSVVVLTSET FDSIVLDEFY APWCGHCKHL
APIYEKLASV FKQDDSVVIA NLDADKHTDL AKKYGVSSFP TLKFFPKGNK AGEDYDGGRD
LDDFVKFINE KCGTSRDPKG HLTSEARLVP SLNPLVKEFL NAVDDKRKEV LSKIEEDVAK
LSGSAAKHGN IYVTAAKKIM DKGSDYTKKE TERLHRMLEK VGI
//
