ID A0A1Y1YB74_9FUNG Unreviewed; 1008 AA.
AC A0A1Y1YB74;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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=K493DRAFT_260887 {ECO:0000313|EMBL:ORX95016.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX95016.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORX95016.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX95016.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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|ARBA:ARBA00000798,
CC ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, 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:ORX95016.1}.
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DR EMBL; MCFE01000189; ORX95016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YB74; -.
DR STRING; 1314790.A0A1Y1YB74; -.
DR InParanoid; A0A1Y1YB74; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000193498; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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; 2.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
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; IPR001849; PH_domain.
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 InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
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 Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP000193498}.
FT DOMAIN 61..191
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 434..461
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 791..818
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 1008 AA; 116998 MW; 256407A008BCDE0C CRC64;
MNRMSSSVIF NTTNWKKGKP KSVSEMTRLS PLMETALAVP MFWVQRDEWG LKPPPIVFKF
LKLRITESDI NPNKHIHHDH FYFRIELEYG DVKWVVYRRM YDFVRLHTLL TFRHFQGKLP
KIPAFPSQLS YAVDKVLDKV HGGTGRDERL RQIAYERRKA VEKYLLKLMS VLNLKVTFEF
CAFLEASSIS LIRDLGWKGI EGYLDNRVKK TTGRCCSGTR PSRWRSDWIA IRDSCVIFCN
SISDSSPKDI LLCNKHFVVE HSLESKNPLR RRTITIGNRF RRIDLRASSE AHVHEWIKNL
EQIQKNSIWV QRHRFDSFAP VRDNVKARWY VDGLDYFHDL SEAILNAKHT IYIEDWWLSP
EMYMRRPPKD NQEFRLDRLL LKKAEEGLAI YIVVYKEVTY ALPISSQYTK ETLKNLHPNI
VVQRHPDHVP GGTMFWAHHE KMCIVDSKVA FLGGLDLCFG RWDTHTHRLA DYHKNPEDEI
WPGQDYSNPR IKDFRNVQQF DIDLINRKKF SRLPWHDVGL CVYGNTARDV EKHFIERWNF
IKSWKATQKQ NIPYLIPKGE YAIGREDNEQ KGSCRVQVLR SSSEWSSGIE REHSIYDAYI
ECIRKAKHFI YIENQFFVTS AADTSGYTVK NKIGMALVER IKKAHQEKAK FKVIVIMPLL
PGFENSIDAS NATTIRLVMH WQFMSICKGK NSVFECLTAA GIVPEDYITF FGLRNYDIIK
NPNYTGPNPQ SSVDDEFTID EPDENDPDAE IDQIFVEATK SENVPISLTP AGSNVVTRHE
KIPSEGRFIT ELTYIHSKLI IIDDRIVLCG SANINDRSML GNRDSEVALI IEDEEGVPSR
MNGKEYLASK FAYTLRCHLF KEHLGLLPDM DMAELTKPSF DSANESVPEG KKTEINADEI
VMDPLSDNFS KFWLKTAQEN TELFRDVFRC VPDDTVTTWD EYKAFVPDPH ITKYGHQALT
NLPKDAVRGL LSHVKGHLVQ FPTQFLKEEN LNAAVFSREF LVPVDVFI
//
