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Database: UniProt
Entry: A0A1Y1YDK0_9PLEO
LinkDB: A0A1Y1YDK0_9PLEO
Original site: A0A1Y1YDK0_9PLEO 
ID   A0A1Y1YDK0_9PLEO        Unreviewed;       222 AA.
AC   A0A1Y1YDK0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE            EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN   ORFNames=BCR34DRAFT_578869 {ECO:0000313|EMBL:ORX96067.1};
OS   Clohesyomyces aquaticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX   NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORX96067.1, ECO:0000313|Proteomes:UP000193144};
RN   [1] {ECO:0000313|EMBL:ORX96067.1, ECO:0000313|Proteomes:UP000193144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115471 {ECO:0000313|EMBL:ORX96067.1,
RC   ECO:0000313|Proteomes:UP000193144};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006386};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC       {ECO:0000256|PIRNR:PIRNR006386}.
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:ORX96067.1}.
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DR   EMBL; MCFA01000264; ORX96067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1YDK0; -.
DR   STRING; 1231657.A0A1Y1YDK0; -.
DR   OrthoDB; 4159077at2759; -.
DR   Proteomes; UP000193144; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR014440; HCCAis_GSTk.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR42943; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   PANTHER; PTHR42943:SF2; GLUTATHIONE S-TRANSFERASE KAPPA 1; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:ORX96067.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193144};
KW   Transferase {ECO:0000256|PIRNR:PIRNR006386}.
FT   DOMAIN          9..208
FT                   /note="DSBA-like thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF01323"
FT   ACT_SITE        17
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ   SEQUENCE   222 AA;  24700 MW;  A49187B5EB52DBC3 CRC64;
     MTAMAKPKIT LYIDIVSPFA YLGFYALQNF PVFKQCDVTY VPIFLGGLMK TCGNTPPLQI
     KNKDKWINTE RIRWAKLLKI PVSPTAPPGF PINTISIQRA LTSLSLSHPQ SLPSAISLFY
     QNFWVHYNTP TEPKNLLAIL TTIVGAEEAK KVVEKSTGES VKKQLTENTD LAFKDGAFGL
     PWFVATNTKG ETEAYWGVDH MGQLCDHLGL ERPGGKGWRA LL
//
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