ID A0A0D2C6L0_9EURO Unreviewed; 836 AA.
AC A0A0D2C6L0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 05-FEB-2025, entry version 37.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=PV07_09259 {ECO:0000313|EMBL:KIW26135.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW26135.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW26135.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW26135.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847044; KIW26135.1; -; Genomic_DNA.
DR RefSeq; XP_016246351.1; XM_016396495.1.
DR AlphaFoldDB; A0A0D2C6L0; -.
DR STRING; 569365.A0A0D2C6L0; -.
DR GeneID; 27348453; -.
DR VEuPathDB; FungiDB:PV07_09259; -.
DR HOGENOM; CLU_000690_2_2_1; -.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
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; 2.
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:SF128; 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; 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:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT DOMAIN 192..219
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 623..650
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 536..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 96070 MW; 0B9A2876FCDE2F45 CRC64;
MQALREKLKD SKLHDAKIEA IHFKHKIGKL KNLVNKNHRH DEAHEQETDR KRTAICESHR
FESFFPEREN NRIKWYVDGR DYFWAVSVGL ENAKETIYIA DWWLSPELFL RRPPFFNQEW
RLDQTIKRAA ERGVQVYVIV YKEVQQALTC NSAHTKHALR ALCPEGSPGH GNIHVLRHPD
HNVFENLGDM TFYWAHHEKF IVIDYHLAFI GGLDLCYGRW DLRQHLLADV HPSGVVNEIF
PGQDFNNNRI MDFHTVEDWS NNELNKTDYG RMPWHDVAMA LIGESVLDIA EHFVLRWNFV
KRDKYKRDEG VDYLCMSTRA KADGSNPDED LIAIQRPKHP VGKYIEHPLS PLEGKGLQNA
GTVHAQLVRS SDDWSSGILL DHSIQTAYVE VIESAQHYVY IENQFFITAT GEHQSPVHNR
IGRAIVNACL RAAKENRKFR VIILIPAIPG FAGDLRSDAA IGTRAIMDYQ YKSINRGEHS
IFGQLKAAGV DPTQYIFVFN LRAYDRIDKT PSLIQQEKES GVSYQQLQRA EAEEIMGSGI
HGYEGEKTEK ESRGTGSHVS EDEQHAIIDR KRRFEAARKK LDVKDPVTSA ESIAEDAMAR
GGLVSEEPWE GEPEAEKDNF VQEELYIHAK LLIADDKTVI CGSSNINDRS LMGSHDSELA
IVMTDTKVLE STMDGKPYQA GYHAASLRRH IWREHLGLIE AQSVDASNDP NAQPPTVCMN
DEYSGEEWEF VADPLSDVLW EKWTTQATTN TDVYRYLFRA DPDNHIKTWK DYDDFAPRKT
IKQGHLHDPH MPVELVRKEL DKIRGHLVWM PLDFLCEEEM AERGIQVNAY TESVYT
//
