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Database: UniProt
Entry: A0A397H400_9EURO
LinkDB: A0A397H400_9EURO
Original site: A0A397H400_9EURO 
ID   A0A397H400_9EURO        Unreviewed;       245 AA.
AC   A0A397H400;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Glutathione S-transferase 3 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CDV56_105861 {ECO:0000313|EMBL:RHZ57479.1};
OS   Aspergillus thermomutatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ57479.1, ECO:0000313|Proteomes:UP000215305};
RN   [1] {ECO:0000313|EMBL:RHZ57479.1, ECO:0000313|Proteomes:UP000215305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ57479.1,
RC   ECO:0000313|Proteomes:UP000215305};
RA   Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA   Perkins V., De Repentigny L., Dufresne S.F.;
RT   "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT   (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT   aspirate.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|ARBA:ARBA00007409}.
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:RHZ57479.1}.
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DR   EMBL; NKHU02000078; RHZ57479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397H400; -.
DR   STRING; 41047.A0A397H400; -.
DR   VEuPathDB; FungiDB:CDV56_105861; -.
DR   OrthoDB; 1762998at2759; -.
DR   Proteomes; UP000215305; Unassembled WGS sequence.
DR   CDD; cd03046; GST_N_GTT1_like; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF9; GLUTATHIONE S-TRANSFERASE 1; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDG01150; Main.1:_Beta-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000215305}.
FT   DOMAIN          20..102
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          108..241
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   245 AA;  27820 MW;  A1CD99DF351F3C26 CRC64;
     MIILSSTIHL FFKVFLNIIY NMLIVHHLQR SQSERIVWLC EELGIPYELR TYQRDAKTLL
     SPPALQQLHP TQAAPVIQDG DTTHAESGAI VEYILSKYGD RKLTIAPTAD NYSDYLYFLH
     FANGYFQPAV MGFSRLLRSG ISPEDPSAKY AKRNFDQALK ILDDRLKKNA WLAGEEFTAA
     DVMSVFTLTT ARLFCPYSLE GYEGILAYLQ RVNQRESYQT AMAKGDPGLV PLIGAEKPRP
     LRPRL
//
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