ID X0IKB1_FUSOX Unreviewed; 1801 AA.
AC X0IKB1;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=FOPG_03119 {ECO:0000313|EMBL:EXL84571.1};
OS Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL84571.1};
RN [1] {ECO:0000313|EMBL:EXL84571.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54008 {ECO:0000313|EMBL:EXL84571.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW808.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXL84571.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=54008 {ECO:0000313|EMBL:EXL84571.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Annotation of Fusarium oxysporum PHW808.";
RL Submitted (MAY-2012) 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 -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
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DR EMBL; JH658811; EXL84571.1; -; Genomic_DNA.
DR HOGENOM; CLU_000690_1_0_1; -.
DR Proteomes; UP000030676; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd01254; PH_PLD; 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; 2.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
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 SMART; SM00312; PX; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963}.
FT DOMAIN 914..941
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1218..1245
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1584..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1636..1753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1801 AA; 202592 MW; 03EDEAFCB77BEF90 CRC64;
MTQHRPDGDV SPMDVSPRSV SPENPNLQPA APPVSKSTSD TLIPPVGLKI TALSDPPGST
KETKPASNEL ALGQGKAPSS AIPRSTPAST KSLKDHGISD RDFGLVVDGD GQDNSQAPSR
PSIQFTRPDG VDTPPTFMRG SSWEEPETPG KSRGASLMSK LKALTNNGGV STPKSSTVAG
PSSQGIQSNI NSPTRPSRGV PGTLTEEDTD ADADAEETAD EGSPGDDKSK KKKQKRRMRR
TKKANTSTPG TPRRFVSDID VLDSFDQLVK RRASMPDATV PDYGVSEGEG RDRLGMAFRR
GNSWMTSAVR HHGEETDEVE SPGAVGRRTG HVRRITVFGG GGVSDGDAMT PRRPFFTSER
ASTFGAQKWK QVKNTLKLLR QKKEDRFDYF KSAELMAELR AGAPAVLMLA SMIQRDEHGN
KRIPVLLEQL KLRITDSSPM EDDDKDRHWL FTIELEYGSG PSRMSWTVTR TLRDIYNLHL
RYKFAINNEK YMPGRMDLGG RPKQPKFPYS AFPYLRGARK KGEESDEEDQ ASIRGEEETA
GEGTATEAAG DGILSDPENP GGLPRRKSRN FLGMGPRRRS TGITDPGDMS NPEGPGMPAM
DMATRRQRYV EKQRRILEKY LSEMIRWLMF RADSNRLCRF LELSALGVRL AAEGSYHGKE
CYLHIQPSKG LDFRRALTPA KVISRHSRKW FLVRQSYIVC VESPENMNIF DVYLVDSKFS
ISSKRSKVKA IGSAEKKAEI DLTVEAPPDK HHTMTLRSSE RKVRLFSRNQ SVMKQFEDSI
NQMLKQTHWY QNKRFDSFSP VRNHVFAQWL VDGRDYMWNV SRAINMARDV IYIHDWWLSP
ELYMRRPAAI SQKWRLDRLL QKKAREGVKV FVIVYRNVEA AIPIDSEYTK FSLLNLHPNI
FVQRSPNQFK KNQFFFAHHE KICIVDHDVA FVGGIDLCFG RWDSPQHPIV DDKPTGFEMS
ETPKDAEHCQ LFPGKDYSNP RVQDFFRLNE PYEEMYDRSK VPRMPWHDVA MQVVGQPARD
LTRHFVQRWN YLRRGRKPTR PLPFLLPPPD ANVDELKELG LTGTCEVQIL RSATTWSLGI
EQTEHSIQNA YIKMIEESDH FVYMENQFFI TSTEAYNTRI VNRIGDALVE RIIRAHENDE
DWRCVIVIPL MPGFQNTVDE QEGTSVRLIL MCQYASICRG EQSIFGRLRA AGIEPEDYIA
FYSLRQWGIM SNDVLVTEQL YIHAKTIIVD DRVALIGSAN INERSMLGSR DSECAAIVRD
TDMINSTMAG RPYQVGRFAH TLRLRLMREH LGLDVDEILE QERQAELDRQ DFEKEMEDIY
NEENGGPADS SKLSPKRPDH LRIPSINHDL DAAVEVEDDS SSSSSSDSNA EVDSTVINQA
EDKVKHELDV TGYGPDRWKS AEKSGLDAGR DSVIINGREV LVSNISNEGK GTLQSPKETQ
PHSPQPDNRY LDPGNHNDGL PPVPALNRRT TDQLGLPRPA QLPSLPISDD TDIGGPPLHI
DPETGKPVNG VFHPMAADIH LAHIDKDCMV DPVNPNFIDE IWNRAAQNNT KLYRRVFRCM
PDSEVSTWAE YREYTTYGER FRASMEGGRS RGEDSEFPPS SRHRGSTAGG AGVSAPGPEV
MAKAVETEAE KAIGRMTEKL PLGHHEEDRI KIVIPDESQR DVDEKQAMKD EAPSPVYSPG
DTPFPAFDGG SSGRYLDPQT GTKDRERRTT FSTLEKPSSR DTNAPPPGQF GSVKRRRRAT
TKNSRRGFSI DDMPSRGQAE ELLNMVQGNI VQFPYDWLLT EEQNGNWGYQ VDGVAPLAIY
N
//
