ID   A0A177CSV0_9PLEO        Unreviewed;       224 AA.
AC   A0A177CSV0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-JUN-2023, entry version 20.
DE   RecName: Full=Glutathione S-transferase kappa {ECO:0000256|PIRNR:PIRNR006386};
DE            EC=2.5.1.18 {ECO:0000256|PIRNR:PIRNR006386};
GN   ORFNames=CC84DRAFT_1112430 {ECO:0000313|EMBL:OAG10281.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG10281.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG10281.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG10281.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-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}.
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DR   EMBL; KV441549; OAG10281.1; -; Genomic_DNA.
DR   RefSeq; XP_018040646.1; XM_018175319.1.
DR   AlphaFoldDB; A0A177CSV0; -.
DR   STRING; 1460663.A0A177CSV0; -.
DR   GeneID; 28758805; -.
DR   InParanoid; A0A177CSV0; -.
DR   OrthoDB; 4159077at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
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:SF13; GLUTATHIONE S-TRANSFERASE KAPPA-RELATED; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW   Transferase {ECO:0000256|PIRNR:PIRNR006386, ECO:0000313|EMBL:OAG10281.1}.
FT   DOMAIN          6..207
FT                   /note="DSBA-like thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF01323"
FT   ACT_SITE        14
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006386-1"
SQ   SEQUENCE   224 AA;  25312 MW;  6DACA51C50A404E5 CRC64;
     MSGGKITAYL DCVSPFSYFA LKHLERHRSV LESHNVEIDI VPVFLGGIME GSGNKPPWTL
     KAKALYSGPD AARAKRYFGV PKMQTPSFFP ILSLLPQRAL VYIKATYPEL FVQTFVDLFS
     AMWEEGQDVS KPDLLSVALS KRFEEVQIRE ILGKATAPEN KQVLNANTKE ALDQGAFGCP
     WFWVCNSKGE EEPFFGSDRF PFMWQHLDLP WKDVELLPPP QAKI
//