ID A0A2N6NH60_BEABA Unreviewed; 508 AA.
AC A0A2N6NH60;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=PDI {ECO:0000313|EMBL:PMB66620.1};
GN ORFNames=BM221_007613 {ECO:0000313|EMBL:PMB66620.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB66620.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB66620.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB66620.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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:PMB66620.1}.
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DR EMBL; MRVG01000008; PMB66620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NH60; -.
DR OMA; FFGMKKD; -.
DR Proteomes; UP000235728; 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:UP000235728};
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..508
FT /note="Protein disulfide-isomerase"
FT /evidence="ECO:0000256|RuleBase:RU361130"
FT /id="PRO_5014493233"
FT DOMAIN 15..131
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 299..469
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 469..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 53..56
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
FT DISULFID 389..392
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR605792-51"
SQ SEQUENCE 508 AA; 55521 MW; 4913A334E98400D6 CRC64;
MQHKRICLGL FAAFASLVTA ADESDVTQLT GKTFDDFVKA NDLVLAEFFA PWCGHCKALA
PEYEEAATSL KEKNIKLAKI DCTEEAELCQ THGVEGYPTL KVFRGADNVA PYSGQRKAAA
ITSYMVKQSL PAVSTLEKDT LEDFKTADKV VVVAYIAEDD KTSADVFQTV AEKYRNDYLF
GSVADANLAE AEDVTAPAVV LYKSFDEGKT IFKGKKFDAD AIEEFTKTAA TPLIGEIGPE
TYAGYMSAGL PLCYIFAETE EERADLAKAL KPVAEKHKGK VNFGTIDAKA FGAHAGNLNL
ASDKFPAFAI QDIEGNKKYP FDQEKKITEK TIGKFVDDYV AGKIEPSIKS EPIPESQDGP
VTVVVAKNYD DIVLDNNKDV LIEFYAPWCG HCKALAPKYD QLGAAFQESD FKDKVTIAKV
DATLNDVPDD IQGFPTIKLY PAGDKKNPVT YEGARTPEDL VEFIEKNGKH KASVSLKEDA
TEEAAPAASK EKKAVEEAEE VEEDHDEL
//
