ID A0A2J8DU65_VERDA Unreviewed; 865 AA.
AC A0A2J8DU65;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=BJF96_g5406 {ECO:0000313|EMBL:PNH31245.1};
OS Verticillium dahliae (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=27337 {ECO:0000313|EMBL:PNH31245.1, ECO:0000313|Proteomes:UP000236305};
RN [1] {ECO:0000313|EMBL:PNH31245.1, ECO:0000313|Proteomes:UP000236305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12008 {ECO:0000313|EMBL:PNH31245.1,
RC ECO:0000313|Proteomes:UP000236305};
RA Fan R., Armitage A.D., Cascant-Lopez E., Sobczyk M., Cockerton H.M.,
RA Harrison R.J.;
RT "Comparative genomics yields insights into virulence evolution of
RT Verticillium dahliae.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:PNH31245.1}.
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DR EMBL; MPSH01000017; PNH31245.1; -; Genomic_DNA.
DR OMA; EWRLDQI; -.
DR Proteomes; UP000236305; 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; 2.
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}.
SQ SEQUENCE 865 AA; 99488 MW; 205C636E17E376F6 CRC64;
MPSTNDENKK KVESGSGASF KDKLKAPFQK LEEKLEGTHL HDAKIHITHK KHQIGKFANL
FNRNHRHDEE HEQATDDKRQ KIRDEHRYDS FFPERDGNII KWYIDGRDYF WAVSEALEAA
QETIYICDWW LSPELFLRRP PHDNQQWRLD QVLKRRAEAG VKIYVTVYRE VEAALTCNSA
HTKHALHGLC PEGSPGYGNI KVMRHPDHNV LENAADMTLY WAHHEKFIVI DYRMAFIGGL
DLCFGRWDTQ THALADVHPE GVKNEVWPGQ DFNNNRVMDF KNVDDWKQNE LSKTRYGRMP
WHDVSMGVIG PCVYDIAEHF VLRWNFIKRD KYKRDDRYDW IQLAGRTGED EDLVGVQRPK
HPVGEYLMHP LTPLETKNLE NRGTVHAQIV RSSDDWSSGI LLDHSIQNAY SKTILEAEHY
VYIENQFFIT ATGEHQSPVH NTIGLAIVQA VLRAAEEKRK FRIIVCLPAI PGFAGDLRDE
AAMGTRAIMD YQYKSICRGE HSIFEQIKAK GVNPREYIFF FNLRSYDRLV TTPALLEQEK
KTGVSYQQVQ RAEAEEIMSE GIHGAVDPTG HGERDKHMGS AQDQDPNLAT PEVEKALDAK
QRFEAAMPEG KLTAAPSLAH HAMAGNERSL LDEPWDDEDL ETEIQNWVQE ELYIHSKLLI
ADDRIVICGS SNLNDRSQLG LHDSELSIVM EDRAQFTSTM NGQPFEAGVH AGTLRRYLWR
EHLGLLPAQG LDGTGLQNAQ PPGEKSPNDP FDRDESWDIV ADPLSDDLWE MWTSQATKNT
DIYRHVFHAD PDDHIKNFDD YDRYLPPKGI KSGHVYDLFM PAEDARKKIA QIKGHLVWFP
LEFLRDAEMA ETGLQVNQFT ESIYT
//
