ID A0A2H3T765_FUSOX Unreviewed; 1824 AA.
AC A0A2H3T765;
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=FRV6_01765 {ECO:0000313|EMBL:SCO77553.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO77553.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) 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; FMJY01000001; SCO77553.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOC1_g10006736; -.
DR VEuPathDB; FungiDB:FOC1_g10012952; -.
DR VEuPathDB; FungiDB:FOC1_g10012953; -.
DR VEuPathDB; FungiDB:FOC4_g10006869; -.
DR VEuPathDB; FungiDB:FOC4_g10011920; -.
DR VEuPathDB; FungiDB:FOC4_g10013976; -.
DR VEuPathDB; FungiDB:FOC4_g10013977; -.
DR VEuPathDB; FungiDB:FOIG_06995; -.
DR VEuPathDB; FungiDB:FOMG_06927; -.
DR VEuPathDB; FungiDB:FOXG_05506; -.
DR VEuPathDB; FungiDB:FOZG_09631; -.
DR VEuPathDB; FungiDB:HZS61_004078; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000219369; 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..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1637..1778
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..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1824 AA; 204892 MW; 5FF306141095D2A9 CRC64;
MTQHRPDGDV SPMDVSPRSV SPENPNLQPA APPVSKSTSD TLLPPVGLKI TALSDPPGST
KETKPASNEL ALGQGKAPSS AIPRSTPAST KSLKDHGIND 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 LRIPSINHDL DAAVEVEDDS SSSSSSSDSN AEVDSTVINQ
AEDKVKHELD VTGYGPDRWK SAEKSGLDAG RDSVIINGRE VLVSNISNEG KGTLQSPKET
QPHSPQPDNR YLDPGNHNDG LPPVPALNRR TTDQLGLPRP AQLPSLPISD DTDIGGPPLH
IDPETGKPVN GVFHPMAADI HLAHIDKDCM VDPVNPNFID EIWNRAAQNN TKLYRRVFRC
MPDSEVSTWA EYREYTTYGE RFRASMEGGR SRGEDSEFPP SSRHRGSTAG GAGVSAPGPE
VMAKAVETEA EKAIGRMTEK LPLGHHEEDR IKIVIPDESQ RDVDEKQAMK DGEAISSRPT
TGLENENGSD AHQHIEAPSP VYSPGDTPFP AFDGGSSGRY LDPQTGTKDR ERRTTFSTLE
KPSSRDTNAP PPGQFGSVKR RRRATTKNSR RGFSIDDMPS RGQAEELLNM VQGNIVQFPY
DWLLTEEQNG NWGYQVDGVA PLAI
//
