ID A0A2V5IHG8_9EURO Unreviewed; 642 AA.
AC A0A2V5IHG8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Alpha/beta-hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BP00DRAFT_338827 {ECO:0000313|EMBL:PYI33513.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI33513.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI33513.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI33513.1,
RC ECO:0000313|Proteomes:UP000248817};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|ARBA:ARBA00007409}.
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DR EMBL; KZ825483; PYI33513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5IHG8; -.
DR Proteomes; UP000248817; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR CDD; cd03044; GST_N_EF1Bgamma; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 1.20.1440.110; acylaminoacyl peptidase; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR010520; FrsA-like.
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; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR PANTHER; PTHR43986:SF1; ELONGATION FACTOR 1-GAMMA; 1.
DR Pfam; PF06500; FrsA-like; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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;
FT DOMAIN 420..503
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 509..642
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 642 AA; 70631 MW; F17A7138DC37EDEE CRC64;
MFKFYPSDFF HFEFLRVLAS APAGGAETGE CLAVLPQVAD GDGEAWYRAW TAQAQQARGR
GDDALVAGDP VAAAGAYLRA SNYFRASEFF LHARPDDPRL RAAIENSVAV FDRGVDLLDR
CTVVRVQIPY ERGATLPGRL YLPLPRSAGG ADHLDRTQTL PLLVVTGGFD STQEELYFFG
PAAALPRGYA VLTFEGPGQG ICLRRDGLRL RPDWEQVTTR VLDVVEELAK DHPIDLARVA
VVGASLGGYF ALRAAADPRV RACVSCDACY DLFDVTRSRM PGWFINGWLS GRLRDGFFNW
VVDKLAGWSF QLRWEFGHSM WVYGVKTPAE VMRCMQQYHV RGYLHDIQCS TFVMGAAETF
YFTPEQNTQP IFAALGHLPP QKKRLWIGKG VEGGGLQAKI GAWASKHPPI NQPPHTTMAP
IGRLYTYVPN ARILKIQAAA ALNNLTLDIP QPFAFGTANK TPEFIRKFPT GKVPAFESAD
GHTTLVESDA IAQYVAASGP AAPALLGRNV AEQAAVRQWV CFAENEVFRH MMAVVLWRVG
MREYDAGVEG AGATGLAEAL AVLERHLAAG EKEYLATEGE LSLADLSVAS ALFWAFMHYV
DAEMRGRFPR VVRWYLRVVA AEKVKEVFGE PSLVAVRRAA PV
//
