ID   A0A0S4JCU5_BODSA        Unreviewed;       789 AA.
AC   A0A0S4JCU5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
GN   ORFNames=BSAL_12330 {ECO:0000313|EMBL:CUG87850.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG87850.1, 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; CYKH01001593; CUG87850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4JCU5; -.
DR   VEuPathDB; TriTrypDB:BSAL_12330; -.
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; -; 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; 1.
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..19
FT                   /evidence="ECO:0000256|RuleBase:RU364138"
FT   CHAIN           20..789
FT                   /note="Phospholipase B-like"
FT                   /evidence="ECO:0000256|RuleBase:RU364138"
FT                   /id="PRO_5006622339"
FT   TRANSMEM        741..762
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   789 AA;  86685 MW;  6C35D9302268F8D0 CRC64;
     MHPMMAIIAV ALLTSAALAA EFAVPPQNLF TAFYRNELTD AVEAGFTLTP DSSRPCASIA
     VHNLGVNATG WDAVYVTVPA EFADSDNATV VAQGYYCAGY AEGYSTGARI LQQHWNMEIT
     DEWNDAIPET RMWINNHTAY MDAQVAANPT DSYWQQVGNF LTQLKGMHAG YTAWADGQLP
     SANTTPLEFL DIFLINFVFE FYDVATAMEV LYPPTMRSLV PSAAGSGVSL TPRTERGRRV
     YGSHCSALIK KTDDGDLIMS HNTWSTFESM LRQYKTYVFG SAYSVSFSSY PGTIHSGDDF
     YVLGSDFTVQ ETTNENNNPV TTAPYVDALA VSEFIRVMVS NRFATNGSHW ADLFCSYNTG
     TYNNQWMVVD MAKFTLSMGT VTNDTLWIIE QMPNMCKKGD QSAILESAGY WASYNRPFYA
     DVFAWGGFLA HEQEYGTLFS YADNYRANIF RRNESRVTSV ETMKDLMRYN DYLHDPFSIV
     PNCTNCSPVY SPYLSIACRA DLVPRNASYG VMDQFIGQYD TAAIDAKIIS ASLMRQPTVS
     PWIISSPTYG GSSNIPPFRF STSLYNQSRH QGIPDTMNFD WLQSDAAFNG APSVNPNAAT
     ADIGSLSVHY STTNYSNTNF AESLYYLFVS VCAMRGAPLP SRELILAMTQ VQVSSRYGFN
     LYVVPFHFIA VDQPAAAPAP APVNATHLLA VGAAASVGFS VQDAYNALLF ASDAELSTVG
     ISSVTYTTTT TTDPDETPHK WTWILGTCVG GVALVALIVV VIRRKVGGGG YEHVREDGDL
     SAMNKFDQA
//