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Database: UniProt
Entry: A0A317W7D2_9EURO
LinkDB: A0A317W7D2_9EURO
Original site: A0A317W7D2_9EURO 
ID   A0A317W7D2_9EURO        Unreviewed;       251 AA.
AC   A0A317W7D2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glutaredoxin {ECO:0000313|EMBL:PWY81795.1};
GN   ORFNames=BO70DRAFT_379772 {ECO:0000313|EMBL:PWY81795.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY81795.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY81795.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY81795.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PWY81795.1}.
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DR   EMBL; MSFL01000013; PWY81795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317W7D2; -.
DR   STRING; 1448321.A0A317W7D2; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_379772; -.
DR   OrthoDB; 1333222at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR011899; Glutaredoxin_euk/vir.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR02180; GRX_euk; 1.
DR   PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR   PANTHER; PTHR45694:SF30; GLUTAREDOXIN 2; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT   DOMAIN          152..217
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   REGION          104..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  27709 MW;  D5859D62563A4AAC CRC64;
     MFSQRRMRLL AIAVVMMVVM AFYYSSEARS VQNQRFYRST VAAMEARKQA KEAESAANIP
     IQKERPSWNG AKEEVKAVSD NDREAPAIPK ANVADDVEEI PIAGRTKITV PKNRNDPEKE
     KPVQVQAPEQ PEADNHANAV AELNGILKRA PIIIFSKSYC PHSARAKSIL LEKYSIVPAP
     FVVELDQHEL GQPLQTLLGE NTGRRTVPNV LVNGKSIGGG DDVAALDQKD ELASTLKSLG
     GKWVQEARRK E
//
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