ID   A0A317VBR9_9EURO        Unreviewed;       580 AA.
AC   A0A317VBR9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Haloacid dehalogenase {ECO:0000313|EMBL:PWY70402.1};
GN   ORFNames=BO70DRAFT_373803 {ECO:0000313|EMBL:PWY70402.1};
OS   Aspergillus heteromorphus CBS 117.55.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY70402.1, ECO:0000313|Proteomes:UP000247233};
RN   [1] {ECO:0000313|EMBL:PWY70402.1, ECO:0000313|Proteomes:UP000247233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY70402.1,
RC   ECO:0000313|Proteomes:UP000247233};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. S-2-
CC       haloalkanoic acid dehalogenase family. {ECO:0000256|ARBA:ARBA00008106}.
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:PWY70402.1}.
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DR   EMBL; MSFL01000030; PWY70402.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317VBR9; -.
DR   STRING; 1448321.A0A317VBR9; -.
DR   VEuPathDB; FungiDB:BO70DRAFT_373803; -.
DR   OrthoDB; 35622at2759; -.
DR   Proteomes; UP000247233; Unassembled WGS sequence.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   GO; GO:0019120; F:hydrolase activity, acting on acid halide bonds, in C-halide compounds; IEA:InterPro.
DR   CDD; cd03190; GST_C_Omega_like; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006328; 2-HAD.
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; IPR047047; GST_Omega-like_C.
DR   InterPro; IPR016639; GST_Omega/GSH.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01493; HAD-SF-IA-v2; 1.
DR   NCBIfam; TIGR01428; HAD_type_II; 1.
DR   PANTHER; PTHR32419:SF25; GLUTATHIONE S-TRANSFERASE (EUROFUNG); 1.
DR   PANTHER; PTHR32419; GLUTATHIONYL-HYDROQUINONE REDUCTASE; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDG01206; Xi.1; 1.
DR   SFLD; SFLDG01148; Xi_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT   DOMAIN          420..544
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   580 AA;  66982 MW;  772A7142BA9EBEE6 CRC64;
     MPINPLPQVL FFDVFGTVVE WRFCVTKALV EAAELALLDP EKRLPANLHE RAEGMTFRDW
     QVIVEEWRKS YGQFTRNFDP SHGFVSVDDH HYTAIHKLLQ QRGLEDLFTD DERWNLALCW
     HRLEPWPDSV EGLRLLNRRF CTCTLSNGNM SLLEDLRNYG SLPFTDVASA EQFGAYKPSP
     QVYQGAASRF GLETSQCAMV AAHLYDLKAA KALGFSTIYV ERAQEEAFTA AQIAEAKQEG
     FVDQWISLGS DGLIEEFKVH RHADADGHFR RKDSVFRSFV SGGPNALFPA EKNRYVLYLN
     YGCPWAHRTN LVRSLKGLED LIQLVVLDPE LGPDGWFFSG RNGSAERDPL YGFTKLSQFY
     FKANPGYEGR YTVPMLWDKK KETIVNNESS EIIRMFYIGF DHLLPEELRE ISRPGGGFYP
     AHLRPEIDAM NEWVYHKINN GVYKTGFATT QEAYDENVYP LFEALDRVEQ HLGHQPYLFG
     ENITEADIRL YTTICRFDVA YYLIFRCNLR MIRHDYPRID RWYRRLYYDE TERTRGGAFK
     KTTFLELYKI NYLKALGKRS GSTQTIIPAG PSPDILPLEA
//