ID A0A1B9HXG8_9TREE Unreviewed; 860 AA.
AC A0A1B9HXG8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=I206_05813 {ECO:0000313|EMBL:OCF47948.1};
OS Kwoniella pini CBS 10737.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296096 {ECO:0000313|EMBL:OCF47948.1, ECO:0000313|Proteomes:UP000094020};
RN [1] {ECO:0000313|EMBL:OCF47948.1, ECO:0000313|Proteomes:UP000094020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10737 {ECO:0000313|EMBL:OCF47948.1,
RC ECO:0000313|Proteomes:UP000094020};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus pinus CBS10737.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000094020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10737 {ECO:0000313|Proteomes:UP000094020};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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; KI894014; OCF47948.1; -; Genomic_DNA.
DR RefSeq; XP_019009167.1; XM_019157527.1.
DR AlphaFoldDB; A0A1B9HXG8; -.
DR STRING; 1296096.A0A1B9HXG8; -.
DR GeneID; 30174182; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000094020; 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; cd00138; PLDc_SF; 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 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; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 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:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000094020}.
FT DOMAIN 194..221
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 641..668
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 98473 MW; 5DBB6DA70DAAE3FB CRC64;
MSTPIADHHS SSKRPHPTSN PFSKLRSKVD HLQSDLSKLG IAISTTLNPN HRHDEAWEQE
VDAKIEAIRD GHRFRSFAGE RDGNVVKWHV DGHDYFWAMS EMIDQAKESI MILDWWLSPE
LQLRRPAALF PEWRLDRLIQ RKAEEGVRVY VMVYKEVDLS MSLSSKHTKH ALEDLHDNIC
VMRHPDHSGG ELVYYFSHHE KLCLVDNKIA AMGGLDACFG RWDTRNHPLA DVHPTEFYKS
LFPGQDYNNS RIMDFQTVDK YTSNALALQE APRMPWHDVS LTMMGPSVVD LIQHFCERWN
FVKNIKYKHD HRMEWLALPF QKLIKDNEFR LHHPHLSEWK DHGRQFFHPY HFPPSEAPRA
SEPVPYGTCR VQVLRSAADW SHGILLENSI QQAYISLIRE ANHCIYIENQ FCELFHTFIS
SCKEGQPVKN LIALALAQRV ISAAKEGRKF KIIVLIPAVP AFPGDIQSQS GLKAIMEAQY
RTINRGGASI FEMIKEAGFE PYFWNLRSYD RINNPKARIK RMEEKSGVTF HEAQVALAKV
YVGSDDVGGG QDETVNIEQA HDQTAGVDQI NKKDTVEKAI KLPKTIDDAK RIIERFQNGR
SNDDKHVSDN VGQHAMLDKT SLAEEQWDGT DEEELACYVS EILYIHSKLM IVDDRRVICG
SANLNDRSQV GDHDSEIAVV IEDADMIESK MDGKKYMASN YATTLRRTLM REHLGLLPPQ
PPFDSAEHPN DGMHPAPHSL RYDFGSAEDL AVEDVLSDEF ENLWVGTGRG NREIFEKIFR
PVPNDSIRNW EDYKKYLAPN AGISSGHIAN REMSLAQVKE ELGKVKGHLV DMPCDFCIDL
KWMTEGDWLS VNSYTLALYV
//
