ID   A0A317WP37_9EURO        Unreviewed;       281 AA.
AC   A0A317WP37;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:PWY88206.1};
GN   ORFNames=BO70DRAFT_427031 {ECO:0000313|EMBL:PWY88206.1};
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:PWY88206.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY88206.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY88206.1,
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   -!- SIMILARITY: Belongs to the FAX family. {ECO:0000256|ARBA:ARBA00006475}.
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:PWY88206.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MSFL01000005; PWY88206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WP37; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_427031; -.
DR   OrthoDB; 2438320at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR026928; FAX/IsoI-like.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   PANTHER; PTHR12289; METAXIN RELATED; 1.
DR   PANTHER; PTHR12289:SF41; METAXIN-1 HOMOLOG; 1.
DR   Pfam; PF17172; GST_N_4; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01200; SUF1.1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW   Transferase {ECO:0000313|EMBL:PWY88206.1}.
FT   DOMAIN          26..131
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF17172"
FT   REGION          46..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  30445 MW;  0F52D1EB487173E5 CRC64;
     MSLPTSIPTI ILHRGLPGTA KYTWSPFVTK LEARFRFGNL PYQTATGSPR SAPKGKVPYI
     TIDSDSNSDS DPSPAKTLSD STLITNSLIE DGLLPDLNGP LDALSKVTDS GIRALLEDKL
     YFLQGHEKWI QNYAAMRSHI LASLPYPVQV VVGYMIYRKQ VATLYGQGAM RFSDEERTAM
     KREVWGEIGA LLAESKIKAT SAGAGGGKDG GGGEKGPFWV LGGEGPTEAD ASLFGFVVGG
     LVCSACPETQ VIVRELPVVV EYARRIHDRF FPEYELWDGG V
//