ID   A0A026W9E0_OOCBI        Unreviewed;       896 AA.
AC   A0A026W9E0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=X777_07103 {ECO:0000313|EMBL:EZA52722.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA52722.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA52722.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC         ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000798,
CC         ECO:0000256|PIRNR:PIRNR009376};
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC       {ECO:0000256|PIRNR:PIRNR009376}.
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DR   EMBL; KK107321; EZA52722.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026W9E0; -.
DR   STRING; 2015173.A0A026W9E0; -.
DR   EnsemblMetazoa; XM_026975378.1; XP_026831179.1; LOC105281694.
DR   OMA; HSNIMVI; -.
DR   Proteomes; UP000053097; Unassembled WGS sequence.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR   CDD; cd01254; PH_PLD; 1.
DR   CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR   CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR   Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|PIRNR:PIRNR009376};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT   DOMAIN          255..282
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          712..739
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   896 AA;  101886 MW;  93B3A76B4E469805 CRC64;
     MRGKEGTILK RTGSGGRTRC NVCGLFECGF CLKCSYLCNS ICGKWHKRHL VVKDTFVAYL
     NPQDGTVRSV ILMDNGFGIS FGMYSTGSRN GIQIANLSRH IVIECWTRRK AKEWMEFIQE
     VGNKEGKDFI QTNPHNSFAP YRSSVPATWF VDGADYMAAV ADALENAREE IFIADWWLSP
     EIHMKRPILN GDYWRLDKIL QRKAFEGVKV FILIYKEIEV ALGINSYYSK QRLVEQCPDN
     IKVLRHPDHA RAGVFLWAHH EKIVVIDQSL AFLGGIDLCY GRWDNSEHRL TDLESIHQSS
     IYIPSKDKLV NTSSKKVLDR DTQRHVFLPL AIATNTIAMA TTRSIPLLPM VDDEAQKALV
     LSTLPRDNSL FMLQEKEDRV KCNTPELERK NLFGVARTTV DKVKDTVRVK RQELINMMYS
     SHEANDDGNV TDNGQVSTLP ESEDTVDFAC SLKPTTKLWL GKDYTNFIVK DFNDLAKPYQ
     DLVDRTTTPR MPWHDIGILV QNAAARDVAR HFIQRWNAAK LEKAKQNLCY PYLLPKSYQD
     CKSYDPFIKE ANKHNVKCQV LRSVSSWSAG FLDPETVERS IQEAYIDAIS KAERYIYIEN
     QFFITLASMD KTGVKNRIGE TLLKRILRAH KEGAVFRVFV VMPLLPGFEG EVGGPSGTAL
     RAITHWNYAS ISRGKDAILN RLTEAGIEDP SEYITFHGLR THSMLNGTLV TELIYVHSKL
     MIVDDNTVIC GSANINDRSM VATRDSEIAV IIHDQEFEDG RMNSIPFPCG KFASSLRKQL
     FREHLGLMNI RDDINIDDAI IKSFYKDVWC ARSKRNTEIY EEVFQCVPTD KIVNFAMLKQ
     YQDEEPISLS NPLLAQEMVE GIKGYLVDLP LNFLCNEDLK PAAGTVEGIM PTALWT
//