ID A0A2N1J818_9BASI Unreviewed; 788 AA.
AC A0A2N1J818;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN ORFNames=MVES_003383 {ECO:0000313|EMBL:PKI82683.1};
OS Malassezia vespertilionis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=2020962 {ECO:0000313|EMBL:PKI82683.1, ECO:0000313|Proteomes:UP000232875};
RN [1] {ECO:0000313|EMBL:PKI82683.1, ECO:0000313|Proteomes:UP000232875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWHC:44797-103 {ECO:0000313|EMBL:PKI82683.1,
RC ECO:0000313|Proteomes:UP000232875};
RA Lorch J.M., Palmer J.M., Vanderwolf K.J., Schmidt K.Z., Verant M.L.,
RA Weller T.J., Blehert D.S.;
RT "A novel species of cold-tolerant Malassezia isolated from bats.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol +
CC H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043665};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+);
CC Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043831};
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DR EMBL; KZ454994; PKI82683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1J818; -.
DR STRING; 2020962.A0A2N1J818; -.
DR OrthoDB; 1943592at2759; -.
DR Proteomes; UP000232875; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF5; ABHYDROLASE_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000232875}.
FT DOMAIN 202..328
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 149..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 788 AA; 88927 MW; 162515DF7896E366 CRC64;
MTVSTLGILA HVTPALIKNA FRNYVRFWIT LGDGSKRLSA NEFYYNQVFL MIKELADYLT
HETAEDVQKL TDTQLPAPPW ASSRKVMIPM STCSDAAQYL IEYFGPQSLQ EVVGGARWWQ
MRTLEGVPGE WISQYTDYHT VVRASEGKNT SLSTSMAKHM TRNTQNRNPR HEQPNQPYEQ
PNSEAGRYAD TDEERTRLTR VMLYFHGGGY YFGSNETHRF MILRIARKFG GFAFAVNYRK
APQYPFPCAI QDCLAAYLYL TRPPPGAKHA PVPPESIVFG GDSAGGGLAL AVLQVLRDLE
LPLPAGAVLL SPWCDLTHSF PSILQNTKTD YIPPYSFIHK PSAMWPLPTD TGVFAHSWCM
FGKRRSRSVP PPAACKQEEV VNVTDPTGKS IPVTSQVQMY ATNAQLFHPL CSPALSGSLG
GLPPLFVLAG DAEVLRDEAI YIAHKAAHPD RFPLRDELMD RYPSMRKMQA KYYHQPTKVH
LQVYDAQCHV FPMFLLTTPA KYAFRALTSF IKYVTGAPCM EVPQASGAQK EWQYSGTDGD
AFFQPNEESV YSGKVPLHRH AFDGNMIRER VDYTGKVRPM EAPETMQALR MPFGRVGMVN
YDTYHRFQEG HTIWDNRYQH STKRAQKKRA KYERRFARFL EKAQDEGLLD DMGDLDISAS
GTHWTDLAAF GPTDLHNEAP PPSSVVRRRD TPESLSMLKL ALYQRAQRRK SLGLAGNAPP
HKDEALHLRR SASFCSTWSG ATIGENEPRM RGTGEHRPTD DTGKPLSKRF GLWKSLLFRF
GDTRGKEL
//