ID A0A094DEL9_9PEZI Unreviewed; 878 AA.
AC A0A094DEL9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=V497_05157 {ECO:0000313|EMBL:KFY57900.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY57900.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY57900.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFY57900.1}.
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DR EMBL; JPJZ01000993; KFY57900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DEL9; -.
DR STRING; 1420910.A0A094DEL9; -.
DR HOGENOM; CLU_000690_2_2_1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000029268; 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; 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:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268}.
FT DOMAIN 236..263
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 664..691
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 100098 MW; EB028EE090F5BE57 CRC64;
MGNQVLHSCP AGPSGREIPR CEGCPQAPLL APERQVRENK PGGCQSFSDS QEASRPPPLT
PHSTNNSRHE LGKFANLINS NHRHDEEHEK ETDNKRTGIA DGHRFKSFAP ERHDNDVKWY
VDGRDYYWAV SEALEAAKET IYIEDWWLSP ELFLRRPPYY NQEWRLDQVL KRKAEQGVKI
YIIVYREVEA ALTCNSEHTK NALRDLCPEG SPGYGNIILM RHPDHNVFEN AADMTFYWAH
HEKFIVIDYA LAFIGGLDLC FGRWDSHQHA LADVHPAGVA EEIWPGQDFN NNRVMDFHNV
DDWSQNQISK AEYGRMPWHD TAMGVIGDCV LDIAEHFVLR WNFVKRDKYK RDKNYPWLIM
EGREGENEDI IGVQRPKHPV GGYVKHPLTP LSTKKLGKQG SVHAQIVRSS DDWSSGILTE
HSIQNAYCQL IRNAEHYVYI ENQFFITATG EHQAPVKNLI GAAIVDAVLK AAKEARKFRI
ILVIPAIPGF AGDLRDDAAA GTRAIMDYQY KSICRGEHSI FGRIKAAGVD PEQYIFFFNL
RSYDRLNVTP KIKKQEEASG VSYQEVQQAE AEKIMGDGVA GKEGDDKRVS GPQEPGHKEP
SNTAEQEKET DAIRKFEAHR DESDGREAES KDSVAKNAML GQPSLASEAW DGDDQEEAKL
WIQEELYVHG KLLIVDDRIA ICGSSNINDR SQLGYHDSEI AIVMEDTEVL QSTMNGQPYE
ARRHAATLRR YLWREHLGLL PPQELDASND PNAQPPPTKN DAQEDEHYEF VADPLGDELW
NMWTRRATQN TKVFRQLFHA DPDNCVKTFE EYENYLPPKG HRAGHIFDKQ RAATEIREQL
DTVKGHLVWM PLEFLKDVDM AEKNAGMAVN QWTESIYT
//
