ID   A0A168JTN0_CORDF        Unreviewed;       855 AA.
AC   A0A168JTN0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=LEL_00408 {ECO:0000313|EMBL:OAA80863.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA80863.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA80863.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA80863.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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|PIRNR:PIRNR009376};
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC       {ECO:0000256|PIRNR:PIRNR009376}.
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:OAA80863.1}.
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DR   EMBL; AZHF01000001; OAA80863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168JTN0; -.
DR   STRING; 1081108.A0A168JTN0; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000076881; 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; 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   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   InterPro; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896:SF128; PHOSPHOLIPASE; 1.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR   SMART; SM00155; PLDc; 2.
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:UP000076881}.
FT   DOMAIN          210..237
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          640..667
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   855 AA;  98463 MW;  A39FA11832351170 CRC64;
     MTGSGEKGES GGNAFTNFVG DMKEKLHDSK LHDVKVALHH KKNQFGKIGN IFNHNHRHDE
     AHEQACDEKR TAACDSHRFE SYFPERDGNL VKWYVDGRDY FWAVSVALEQ ATESIYIADW
     WLSPELFLRR PPHYKQEYRL DQILKRKAEA GVKIFVMVYK EVEAALTCNS IHTKHALQAL
     CPEGTPGHGN IRILRHPDHN PFENVADTTM YWAHHEKFIV IDYAIAFIGG LDLCFGRWDA
     HHHPLADVHP EGVTEEIWPG QDFNNNRVMD FQKVEDWQQN ELSKASYGRM PWHDVAMSVI
     GPCVYDIAEH FVLRWNFTKR DKYKRDERYD WIVLEGREGE DEDLVGVQRP KHPCGDYVKH
     PLTSLATKNL DNRGTVHAQI VRSSADWSSG ILTEHSIQNA YCEVIRKAEH YVYLENQFFI
     TATGENQSPI HNTIGRAMVE AVLRAAKEER KFRIIVLIPA IPGFAGDLRD NAASGTRAIM
     DYQYKSICRG EHSIFGQIKA QGVDPKQYIF FFNLRSYDRL NKTKALVEAE EKSGVKYQDV
     QRAEAEEIMK EGIHGTNDAG HNERDEHMGT LAQQKSKEKA AVVESAMEAK RRFEAEMPEE
     KDTKLPSLAH HAMAGQGPIT EEPWDDEDDK ELEIRNWIQE ELYIHSKLLI ADDRVVICGS
     SNINDRSQLG YHDSELSIVM EDTRRIPSSM DGKTFEAGYH AATLRRYLWR EHLGLLPPQN
     FDAADDINAQ PPSVNPENDI YDQDESYKFV EDPLGDELWD LWTSRADRNT EIFRHLFHCD
     PDDHIKTFED YDRYLPPRGV KAGHIFDQFM PAADARAKLD EIKGHLVWMP MDFLQDAEMA
     ERGLQVNSWT ESVYT
//