ID A0A072PFV8_9EURO Unreviewed; 253 AA.
AC A0A072PFV8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN ORFNames=A1O9_06573 {ECO:0000313|EMBL:KEF58647.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF58647.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF58647.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF58647.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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|ARBA:ARBA00000710};
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409, ECO:0000256|RuleBase:RU003494}.
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:KEF58647.1}.
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DR EMBL; AMGV01000004; KEF58647.1; -; Genomic_DNA.
DR RefSeq; XP_013261237.1; XM_013405783.1.
DR AlphaFoldDB; A0A072PFV8; -.
DR STRING; 1182545.A0A072PFV8; -.
DR GeneID; 25281490; -.
DR VEuPathDB; FungiDB:A1O9_06573; -.
DR HOGENOM; CLU_011226_14_0_1; -.
DR OrthoDB; 1404190at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd03048; GST_N_Ure2p_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; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01151; Main.2:_Nu-like; 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:UP000027920};
KW Transferase {ECO:0000313|EMBL:KEF58647.1}.
FT DOMAIN 4..90
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 97..231
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 253 AA; 29143 MW; FE8CFB6F47E10ECB CRC64;
MGEDKTITFY TAFSPNGHKI AITLEELGLP YEMVHVNLPA IQHKEPWFMK INPNGRIPAL
TDTLEDGTQI NLFESGSIQQ YLVDRYDTEN KISYPRGTKE FYQTNNWLFF QNAGIGPMQG
QANHFVRYCL SSEPEQYSKD RYVNETRRLY RTLNKHLQDS QSKYLVGDKC TIADIAISSW
ANITAFAGVD ISEFPYVGGW QARMAQRPAV HKGSQTPKKV DLEKLEMDPE AFKTYLKTNE
AWIKHGMDED RKK
//
