ID   A0A0S4IX51_BODSA        Unreviewed;       676 AA.
AC   A0A0S4IX51;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
GN   ORFNames=BSAL_73185 {ECO:0000313|EMBL:CUG06600.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG06600.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CYKH01000609; CUG06600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4IX51; -.
DR   VEuPathDB; TriTrypDB:BSAL_73185; -.
DR   OMA; LQIYYHY; -.
DR   OrthoDB; 180150at2759; -.
DR   Proteomes; UP000051952; 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; -; 2.
DR   InterPro; IPR007000; PLipase_B-like.
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:UP000051952};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364138};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU364138"
FT   CHAIN           18..676
FT                   /note="Phospholipase B-like"
FT                   /evidence="ECO:0000256|RuleBase:RU364138"
FT                   /id="PRO_5006621748"
FT   TRANSMEM        634..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   676 AA;  75552 MW;  461364B89DDE284A CRC64;
     MAFPLLIAIF LVAAVAALPS SDLPNITDPS AFVNQTYLLV TNTPNVIGNY SITMLNGPVH
     PGNETTASHV VAEIIYNKSY DQIGWDFVQV TANQDLLNSE EDKGFTAYYA AGYLEGYVTA
     VKIGQVFVGN NLTYPQPPAV ADWVDRHIAF MKSQATDNMR AGYPSAFWTQ LGNLVAQMEG
     IAAGYMQYVV DHHRVGAENQ PNLTFTEIFL LNFNNELGDI FNVVNVSSFE SEVFAPKQRT
     AVSAKHDNKL MPFKNKNLHC SALVKVTSND IFFSHVTWGG YNTMVRQYKV YKFQTTVSMS
     AVAGTIASGD DWYQTSNMLG VQETTNDYYN NSLFQFVIPE SSSEFLRVMV ATFLANNGRE
     WVELFQFNNS GTYCNQWMVL DYKLYTPGAV GDALPDNLLW VAEQIPGNVT SADVTFVLRA
     TTYWASFNIP YFPNIYNLSG FAALEEEFGP VNSYTKYARP EIFKRNNTDV VDLESMRRMM
     RYNNWEFDPL SVIPMRRMMR YNNWEFDPLS VIPLCPECNP KGSPWLTISS RGDLVDSSFI
     LPANKDYGSQ FEQAPMGGID NKIGSYEMIS KGAMGTVICG PTYDQQPVFN FSKVFPDLRP
     PGSANYFDFP YVFFNVVGQP PQGTGSDNND TRNVIIGVCV GVPVALIAVS FVVYRYRKNA
     DEDGTYAPVN QGNNLV
//