ID A0A162JIA9_9HYPO Unreviewed; 384 AA.
AC A0A162JIA9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Lipase/thioesterase {ECO:0000313|EMBL:OAA42453.1};
GN ORFNames=BBO_05116 {ECO:0000313|EMBL:OAA42453.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA42453.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA42453.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA42453.1,
RC ECO:0000313|Proteomes:UP000076863};
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 -!- 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:OAA42453.1}.
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; AZHA01000014; OAA42453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162JIA9; -.
DR OrthoDB; 1366960at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF29; LIPASE_THIOESTERASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_8G02590); 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..355
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 41998 MW; 49D8E0355427CF3A CRC64;
MATSTRTTTR SQSVKAEAAA ATTAPPPPVK IETKKLSLFG YLDMIPGLAA IVATAVASLI
TGLFRSEQDS KTYYLHVANT TLRKATHRLN PLQLQLVSPN TDIIYNQYAR ARNFQPDTVA
LAHGAQGHWV GNKNATNVFI WYHGGGFCLP ANIGYFKFFE RLLKEINAAG GDLCVFAVTY
TLAPHGRYPV QLTQSVEALR HVVEHTGRSP GNVLLGGDSA GGNLVFGVLS HLAHPHPSIA
PLHISKPLAG AAAIAPWVSL QPDLSEQVIY DGGDIVTTFV GESWSREFMG DGKADYYTDA
FDAPSSWFET FPVDKMLMLG GENEILMPMI ELFYETVKAG YPNVELFKGK RESHVAPIYN
IYVGDNTETE QGKKLKTWVI ELLK
//