ID A0A2G5UNJ6_9PELO Unreviewed; 573 AA.
AC A0A2G5UNJ6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Phospholipase B-like {ECO:0000256|RuleBase:RU364138};
DE EC=3.1.1.- {ECO:0000256|RuleBase:RU364138};
GN Name=Cni-Y37D8A.2 {ECO:0000313|EMBL:PIC41145.1};
GN Synonyms=Cnig_chr_III.g8666 {ECO:0000313|EMBL:PIC41145.1};
GN ORFNames=B9Z55_008666 {ECO:0000313|EMBL:PIC41145.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC41145.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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}.
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:PIC41145.1}.
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DR EMBL; PDUG01000003; PIC41145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5UNJ6; -.
DR STRING; 1611254.A0A2G5UNJ6; -.
DR Proteomes; UP000230233; Chromosome iii.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364138}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU364138"
FT CHAIN 19..573
FT /note="Phospholipase B-like"
FT /evidence="ECO:0000256|RuleBase:RU364138"
FT /id="PRO_5013427646"
SQ SEQUENCE 573 AA; 65284 MW; AE7768F45017A63B CRC64;
MLKFWLLLAA FLAIGAETKS IERSYTVCQQ TDGKLYSYKE GRVSDGDLCG KRLATAYFKD
EVNQTGWAFL EVDVISPKIP HYLQGYAAGF AEGRVTRDLI DLHIINTVNG YCDGAKHFCD
ELGEFMVDNL KWMEMEIKQN PEDEYWQQVN LTLNQLFGLI HGYENQLGAP INFKEIAVHP
IFMIQIAGDL EDLALKFKKP ENPKKVFSGP GHCSALVKLL PNNEDILFSH VTWSSYGTML
RINKKYSFKT GDPGQVYSFS SYPASITSTD DFILTSAKLA ILETTIGNYN EKSLDLITPN
TVLTWIRAEI AHRTASSGLQ WAEAFGRHNS GTYNNEWVVV DYKQFHRGKP VQPETGIIHV
VEQMPGHIVH SDKTAHLFRT TYWPGYNQPY YKQIIRFSDT DKMVEKYGDW YSYDKTPRAL
IFARDHKNVN DMESMIALMR SNNYTKDPLS KCDCNPPYSA ENAIACRSDL NPVNGTYPFK
SLGFRDHGAI DVKVTNSRLI QSLQFTAVSG PPGGVTKDVP IFDWRTSSLK DKVPHFGQPD
KWNFAPVTYK WRRSFLGDLR DKIYKDLKTS EDF
//
