ID A0A232FE58_9HYME Unreviewed; 605 AA.
AC A0A232FE58;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
GN ORFNames=TSAR_012956 {ECO:0000313|EMBL:OXU28719.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU28719.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU28719.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU28719.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU28719.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- FUNCTION: Putative phospholipase. {ECO:0000256|RuleBase:RU364138}.
CC -!- SIMILARITY: Belongs to the phospholipase B-like family.
CC {ECO:0000256|ARBA:ARBA00007835, ECO:0000256|RuleBase:RU364138}.
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:OXU28719.1}.
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DR EMBL; NNAY01000390; OXU28719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232FE58; -.
DR STRING; 543379.A0A232FE58; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004620; F:phospholipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.60.30; -; 1.
DR InterPro; IPR007000; PLipase_B-like.
DR PANTHER; PTHR12370:SF3; PHOSPHOLIPASE B-LIKE 2-RELATED; 1.
DR PANTHER; PTHR12370; PHOSPHOLIPASE B-RELATED; 1.
DR Pfam; PF04916; Phospholip_B; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364138};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU364138};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU364138}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 457..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 67260 MW; D0BB54D5F2339EFF CRC64;
MLKVVGASWL QTRISTYILV AVALLGIGAV ILGEFGRVEN DGTYSATVWW KRISGYRIDF
WGQGNDLKSL PLGAARAYYK TGILQTGWST LEIETSPDYP DDVQAYAAGL LEGSLTWQLI
HHHWYNTVRA ACAPRASLCR KMRRYLRENA ANARENAALL RYEDPYWHMV HLYYVQLDGL
AEGWRFAVQR SRQDVNIDPE DFLWLAMASD LPDLERANNG SDHHIASDGM IVLKAIEREH
FEPLMALAHN TAAPYSRMLR LMKRYKFSYR VSPEIDSEPV PGHSIVMTSY PGALSSQDES
YMVVGENREL IVAGTPLIID NHSLWSRLQT KDRVMSAGRI MAANRLATSG LSWSRLLDRQ
NSGTSNRQWI SIEPRTGVVS LIEQIPGFTQ HVDHTNEFRS KGYLGCTGAP YSSTIRELLG
GERDESVARA EQLALLQANI TSVEGLKALM RGEIRALSDN NKDEDSDEPL ESENTEQSPS
NPTITKSNDD NTSSSPLLSA LTSTMSSSTL LSSSSSSSSS SLSSTEQLLA YRGDLASVPR
PLGVIDSKLF LFDLDGLETF EARAGPARRI EAPAFDWTHS FPNSSHLGQP EIFSFDSLAP
AWVWL
//
