ID A0A2H3GXZ1_FUSOX Unreviewed; 1790 AA.
AC A0A2H3GXZ1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=AU210_008027 {ECO:0000313|EMBL:PCD35457.1};
OS Fusarium oxysporum f. sp. radicis-cucumerinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD35457.1, ECO:0000313|Proteomes:UP000219602};
RN [1] {ECO:0000313|EMBL:PCD35457.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD35457.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA Rep M.;
RT "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL Environ. Microbiol. 18:4087-4102(2016).
RN [2] {ECO:0000313|EMBL:PCD35457.1, ECO:0000313|Proteomes:UP000219602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Forc016 {ECO:0000313|EMBL:PCD35457.1,
RC ECO:0000313|Proteomes:UP000219602};
RX PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA Brankovics B., Houterman P.M., Arie T., Rep M.;
RT "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT multiple cucurbit species.";
RL Sci. Rep. 7:9042-9042(2017).
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}.
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:PCD35457.1}.
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DR EMBL; MABQ02000005; PCD35457.1; -; Genomic_DNA.
DR STRING; 327505.A0A2H3GXZ1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000219602; Chromosome 7.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000219602}.
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..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1549..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1602..1742
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 1392..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1790 AA; 201464 MW; 55A69C0260FB8D94 CRC64;
MTQHRPDGDV SPMDVSPRSV SPENPNLQPA APPVSKSTSD TLLPPVGLKI 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
NQMLKQTPWY 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 LRIPTEDKVK HELDVTGYGP DRWKSAEKSG LDAGRDSVII
NGREVLVSNI SNEGKGTLQS PKETQPHSPQ PDNRYLDPGN HNDGLPPVPA LNRRTTDQLG
LPRPAQLPSL PISDDTDIGG PPLHIDPETG KPVNGVFHPM AADIHLAHID KDCMVDPVNP
NFIDEIWNRA AQNNTKLYRR VFRCMPDSEV STWAEYREYT TYGERFRASM EGGRSRGEDS
EFPPSSRHRG STAGGAGVSA PGPEVMAKAI ETEAEKAIGR MTEKLPLGHH EEDRIKIVIP
DESQRDADEK QAMKDGEAIS SRPTTGLENE NGSDAHQHIE APSPVYSPGD TPFPAFDGGS
SGRYLDPQTG TKDRERRTTF STLEKPSSRD TNAPPPGQFG SVKRRRRATT KNSRRGFSID
DMPSRGQAEE LLNMVQGNIV QFPYDWLLTE EQNGNWGYQV DGVAPLAIYN
//
