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Database: UniProt
Entry: G4ZM53_PHYSP
LinkDB: G4ZM53_PHYSP
Original site: G4ZM53_PHYSP 
ID   G4ZM53_PHYSP            Unreviewed;      1817 AA.
AC   G4ZM53;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   ORFNames=PHYSODRAFT_286421 {ECO:0000313|EMBL:EGZ16020.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ16020.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ16020.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ16020.1,
RC   ECO:0000313|Proteomes:UP000002640};
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).
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};
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DR   EMBL; JH159155; EGZ16020.1; -; Genomic_DNA.
DR   RefSeq; XP_009529769.1; XM_009531474.1.
DR   STRING; 1094619.G4ZM53; -.
DR   EnsemblProtists; EGZ16020; EGZ16020; PHYSODRAFT_286421.
DR   GeneID; 20640357; -.
DR   KEGG; psoj:PHYSODRAFT_286421; -.
DR   InParanoid; G4ZM53; -.
DR   OMA; YTKRSLM; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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; 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   SMART; SM00155; PLDc; 2.
DR   SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        260..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        589..614
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          858..885
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          1256..1283
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          713..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1539..1655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1665..1684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1817 AA;  203737 MW;  3BC86D3F54B896C0 CRC64;
     MPGPDDDAVE QTAAVRTNSS GYGLKAAPSF STSGLGSVAS VNSYRSSSVD GQEVDVDDCN
     EECADSDILE SPNDGEMTIM NDDDADLSEE EEEVMEHSID FSVNRATVTR AGVIPCCVFV
     ARVRWGTTDW EIYFGQKQIL RLHFQLHLYC LLHRHKFMRG VHLPWTIWRE KRAEKRVADV
     YVVQDYIRTL LKDRDLRNSE PLLSFLEVSP SRAMLRLGPS LKEGYVHMRI NGPFQLPLYT
     CFNRTIEALY RHLYRAWMRI AFVSAIVGFI FPVCLVIVTS LPTFFSPQKE LVNSDSGTKE
     VSTKLNTAGV FLGLAVLAGI IFFAGFVYKF FQHRLGVIRR WVVLKPSCFA AYRNRNDREP
     SEVFLFDKTF TARKGSYRQG VSWMPSGLVV GSKAGDIEID TGHYYTRLTA FIALMGVCYG
     IMRLSNSIYD FETLSLDKSL GVPITNASGY ENWTETNDIE YCGYYFTVPH GVTVYVESDE
     DNAVVSQLQM PSANSMTANL GYFWQSDSMG NSLNVITNAV GAGTMMSVVK PIDAKNDRFF
     ESGTNYSLPS VGNLTLEGVD TDIDVQSYSN VDSLCAISVR ISPVTWRSYI FYIMFLFAGG
     IIAPVVGFLA NYFVTYLGVW HPHVRRDHWF RCVRRLQKLK RHETSTRFNS FAPQHVSTLA
     DDDSAAIVAK AKAARLPPVA VGNTSGSAIN QVVDSVVKLE AEAVARLGSG NLTSASRVDS
     STQSEESFEA PPPPPSAVSW HVDAEDTYEA MYKAISNAKY EILIAGWWVC PDLFLLRPGR
     KLPPREPDED PNGQQVNKTM LRQLLMKKAE AGVKIYVLIY REVKLALTLN SAYTKRSLMV
     HPNIRVLRDP IFQIQSLGFW SHHEKIVCID QSLAFVGGLD LCFGRYDHHG HPISDPSDDP
     VWRGKDYSNP IIKDFVRVNK PFEDLIDRGS QPRMPWHDVH CSISGPPVQD VAYHFIQRWN
     FVCSKNDYQL RTGWCICFRS RRFKFLPKCL VPMDFNGWTL QYPSSDPEAM LERDGSTRTT
     IPLVREDSLS MVEPFQVVQS LNPMYPCAAT GPQWPPTSSL NPLNPIRPPI TSASGTAGQL
     DDGEVLRAQR GESILQVFHP SASICNIQVC RSVSMWSAGV PTEASIQAAY MDVIANSKHY
     LYIENQFFIS GMDGNGIVRN RILQALVDRI ERAVQRDEKF RVYVVMPLLP AFEGNVRSHE
     LTNLHAVMHW QFATICRGRY SLFEALKGVT NHPEQYVAFF GLRKYGIMPN GCVSTEQIYI
     HSKLMIADDR CAIIGSANIN DRSMNGDRDS EIALVIEDMQ YEDGVMNEKP YRRGVAASKL
     RMQLFREHLG LTDDDLSIVD ATSDRTWQAI KATASSNTKI FETVFDCAPS NRMRAFVNFQ
     SIEVTQIFEN QRMNVLKVPG RAHVWDAQNL KDGDYAPWTD VNGVPIAADR VDLRDFEVDN
     FRDRKKKLFS MDHDGWCYAR NFSIFQEVRT MKTDYKKREK LQHLVADRLM AQVRRRRWVK
     KGLLPPRPDP RDSSFSIASD DEEHGRFYSL WRRLQQGDFS RSNSVSTPTN FSHLDTGGSI
     ANSVSVGGTH QGRRLHNSSS LPLDGPIMMS NTTPSRPAVL GDNPSYPNSP SVASFQTPQS
     PSMNALQGGP RSVRGGRTQS LLGTGGGVRT RANTRSARGS FIGMFSVTSG NRNDTDDDSS
     DAGSDYGGGH GIRASLKRWY SAVDVLDFGR RSKFNAEYFD GDDHLNGDDP LLEEGQGSYH
     AATREGLLME EGAEGSDAED ADCQISHVQT AATVRKEDET RARGQLSEIR GHLVEFPLDF
     LVEEILKPSV LPADIHI
//
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