ID H3H2Y0_PHYRM Unreviewed; 1113 AA.
AC H3H2Y0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra84787, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra84787}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra84787};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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|PIRNR:PIRNR009376}.
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DR EMBL; DS566122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3H2Y0; -.
DR STRING; 164328.H3H2Y0; -.
DR EnsemblProtists; Phyra84787; Phyra84787; Phyra84787.
DR VEuPathDB; FungiDB:PSURA_84787; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_0_1; -.
DR InParanoid; H3H2Y0; -.
DR OMA; HSNIMVI; -.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004630; F:phospholipase D activity; IBA:GO_Central.
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; IBA:GO_Central.
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:SF76; 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; 1.
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:UP000005238}.
FT DOMAIN 494..521
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 871..898
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 126382 MW; CEF80617BA3DA52F CRC64;
MDATEQQPTS SPSVADVVTA AQQQQQEPQQ HQPPAHATSS VFDTTRTGPA STAGGRPRSD
SADYFGFLHH NPDEDIYVFE EPPEVHVLGG RFQESWPTRY VEYDVELKYK NYKWKVEIPK
SSIQSLWFYI KSRPHLRHAP SSAAAQVAEE ERAEHGAGAP GVPGPTPAAA DSRWPQLRKL
FLTSADKSVG PEMVALVQQL LEMVVKVPRL LRSPYVAALF QVSNSTFDDE MGRTSVREGW
LKTRFWLKGN RENVRINRAS ASWDNECFNC MCVVKRVNFR AKRLRWVSLK TSSIAIFDSI
EDTIARKAFL FDSKFNIERG LATTGSSTTL LVSNSTYVLQ MEAKSKQALT KWANDIRRVA
EASNWSQSHR DGSFSIPRNP VHMTSFAQWY VDGIGAYEAI YHAIQSATKE IFIAGWWVCP
TIHLLRPAEK YPESRLDLAL QKKAEEGVQV YVLMYKEISV ALTLNSMFSK QVLSKLHKNV
HVLRDPDFLM KQLGLWSHHE KIVSVDQRVS FVGGLDLCFG RWDTHTHELF DEPGKPTDFV
GKDYSNPREK DFVEVDRPEE DMIDRNVVPR MPWHDCHCRL EGQPARDVAR HFVQRWNYSV
STRKKSRKLH HLVPMKDYPV TVIDKKGPQQ LTKRLQKAVH AVRAMRGLSR ARANTDNRGF
NSDRRMARML SGQHESGTMP ILQEDSGEVM LDLPDHDEDN DEVFERHKQE VAARGYRVHT
QILRSLSLWS GGVATERSIQ NAYIRLIGSA QHFVYIENQF FVSGLEGDHG CSNRIANALV
ERIRRASDNN EKFRVIVVMP LLPAFPGKPD DKDASSLRGV MHWQYRTICR GEHSIYQRLY
QELEDDDPFK YIAFYGLRNH SNREDQQAQT EEVYIHSKVM IVDDRACIIG SANINERSMC
GDRDSEIAVM VEDHEMEEEI AIADGTYNVG KFAHSFRMKL FEEHFGVEPG TPLYNKYQDP
VSKDAWFSMQ EQAMNNHQIY DSVFGCLPSD SVTSFAQIDE HIQSAQGLDT SGRGAEEAVA
AAMNSGTTDI ASNNGDQGRS SSLSDRAMSP QTSARGRKSV FSGAMNVNMK ESAHIAQQKH
ELSNVQGHIV YFPLKFLVDE QLEPKLFPAE LFQ
//
