ID G8JH45_ARAHA Unreviewed; 148 AA.
AC G8JH45;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=At3g48690-like protein {ECO:0000313|EMBL:AET78946.1};
DE Flags: Fragment;
OS Arabidopsis halleri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81970 {ECO:0000313|EMBL:AET78946.1};
RN [1] {ECO:0000313|EMBL:AET78946.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CZ8-19 {ECO:0000313|EMBL:AET78946.1}, F1-16
RC {ECO:0000313|EMBL:AET78955.1}, and F1-2 {ECO:0000313|EMBL:AET78956.1};
RX PubMed=22069475; DOI=10.1371/journal.pone.0026872;
RA Roux C., Castric V., Pauwels M., Wright S.I., Saumitou-Laprade P.,
RA Vekemans X.;
RT "Does Speciation between Arabidopsis halleri and Arabidopsis lyrata
RT Coincide with Major Changes in a Molecular Target of Adaptation?";
RL PLoS ONE 6:E26872-E26872(2011).
RN [2] {ECO:0000313|EMBL:AET78946.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CZ8-19 {ECO:0000313|EMBL:AET78946.1}, F1-16
RC {ECO:0000313|EMBL:AET78955.1}, and F1-2 {ECO:0000313|EMBL:AET78956.1};
RA Roux C.B., Castric V., Pauwels M., Wright S.I., Saumitou-Laprade P.,
RA Vekemans X.;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000256|ARBA:ARBA00010515}.
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DR EMBL; JN973880; AET78946.1; -; Genomic_DNA.
DR EMBL; JN973889; AET78955.1; -; Genomic_DNA.
DR EMBL; JN973890; AET78956.1; -; Genomic_DNA.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblPlants.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR PANTHER; PTHR23024; ARYLACETAMIDE DEACETYLASE; 1.
DR PANTHER; PTHR23024:SF467; CARBOXYLESTERASE 12-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 3: Inferred from homology;
FT DOMAIN 1..148
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 38
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AET78946.1"
FT NON_TER 148
FT /evidence="ECO:0000313|EMBL:AET78946.1"
SQ SEQUENCE 148 AA; 16460 MW; F5450F899E213FCC CRC64;
DDSWTALKWV FTHIXGSGQE DWLNKHADFS KVFLSGDSAG ANIVHHMAMR AAKEKLSPDL
NDTGISGIIL VHPYFWSKTP IDEKDTKDET LRMKIEAFWM MASPNSKDGS DDPLLNVVQS
ESVDLSELGC GKVLVMVAEK DALVRQGW
//
