ID A0A168B4I4_9HYPO Unreviewed; 575 AA.
AC A0A168B4I4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glutathione S-transferase domain-containing protein {ECO:0000313|EMBL:KZZ94784.1};
GN ORFNames=AAL_04895 {ECO:0000313|EMBL:KZZ94784.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ94784.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ94784.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ94784.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ94784.1}.
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; AZGY01000010; KZZ94784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168B4I4; -.
DR STRING; 1081109.A0A168B4I4; -.
DR OrthoDB; 767442at2759; -.
DR Proteomes; UP000078544; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00299; GST_C_family; 1.
DR CDD; cd00570; GST_N_family; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43968; -; 1.
DR PANTHER; PTHR43968:SF6; GLUTATHIONE-DEPENDENT DEHYDROASCORBATE REDUCTASE; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000078544};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZZ94784.1}.
FT DOMAIN 312..395
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT REGION 31..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63790 MW; DF43B5DF7F6FAEEB CRC64;
MADPASVPGS SSAAGLPGVG QFRLHLHPHL PHHHHYHHHH DRPPLQPPQV DGGQFGILAP
ETLPLDAQQQ QQPSQWNAPV ARHGANADNP ENITSAGKLP AKLVVNPPDL EAWREKLFNV
DGVMVLTDEQ FETYFPHVDN VYSHRSTQRY KRKPFISHYW DCRMKGRPPG TPKSKDPAKQ
TRKRSARERD LCHVKIRITE YLPGATVDID RDALDAAAAA MLSSLGQQQQ QQQQQRFWTI
QRVNGNGVAG NNGVPGPHRH SLAKSDEIKK NSVQRYLAQR DREAKRAQRP PPLPRKYTGA
AAATIKKHSA HQALKLYAAC YCPFSQRVWM ALELKGFPYQ YVEVEPLKLT AGPDITGFAA
ASPRGTVPAI RHGGWTCTES AVILEYVRAG LTWYSLDVNS LRADDFPPNV AQLEDLDGSV
PRLLPGDDAQ HRATCRLWVN HINTLIVPAF YALLRANDAN AQSHSTSDLQ THITSLVLAA
DSEGPLFAGP GGDLCLVDVH FAPFAVRLSR VLKPARGWTD PVPGTRWNRW LDALETNAHL
KATMSADGLY TDTMDVLLQE QEQEQRQGQG QGQAR
//