ID B6GWY3_PENRW Unreviewed; 290 AA.
AC B6GWY3;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Pc12g00040 protein {ECO:0000313|EMBL:CAP79631.1};
GN ORFNames=Pc12g00040 {ECO:0000313|EMBL:CAP79631.1}, PCH_Pc12g00040
GN {ECO:0000313|EMBL:CAP79631.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP79631.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP79631.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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DR EMBL; AM920427; CAP79631.1; -; Genomic_DNA.
DR RefSeq; XP_002556910.1; XM_002556864.1.
DR AlphaFoldDB; B6GWY3; -.
DR STRING; 500485.B6GWY3; -.
DR GeneID; 8316385; -.
DR KEGG; pcs:Pc12g00040; -.
DR VEuPathDB; FungiDB:PCH_Pc12g00040; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR OMA; CEPCTAV; -.
DR OrthoDB; 1038at2759; -.
DR BioCyc; PCHR:PC12G00040-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c12.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR CDD; cd02984; TRX_PICOT; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10293:SF73; GLUTAREDOXIN-3; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724}.
FT DOMAIN 1..114
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 116..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 290 AA; 30647 MW; D114083C0B08347E CRC64;
MSTLTEITSE ADFSSHLSSL SPSALVVLYF HTPWAAPCAQ MGAVLSALAS QYPATAPPTI
SFVSINAEEL PDISEEYDVS AVPFVVCLRS GQILESISGS DAVKVRDAVE RHAGRGNVAG
AVGPMDSAKA NIPPPLSAVP REDGPLTATQ APVTASEPPA ADAANATPVA SAPALTPEQS
REALFARLEQ LVKAASVMLF MKGTPSSPQC GFSRQLVGIL RERSVKYGFF NILADEDVRQ
GLKEYAEWPT FPQLWVNGEL VGGLDIVREE INSDPDFLKD HSVSKPTAAA
//
