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Database: UniProt
Entry: C9SB65_VERA1
LinkDB: C9SB65_VERA1
Original site: C9SB65_VERA1 
ID   C9SB65_VERA1            Unreviewed;      1713 AA.
AC   C9SB65;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN   ORFNames=VDBG_01724 {ECO:0000313|EMBL:EEY15615.1};
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN   [1] {ECO:0000313|Proteomes:UP000008698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC   {ECO:0000313|Proteomes:UP000008698};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS985215; EEY15615.1; -; Genomic_DNA.
DR   RefSeq; XP_003007536.1; XM_003007490.1.
DR   STRING; 526221.C9SB65; -.
DR   GeneID; 9534999; -.
DR   KEGG; val:VDBG_01724; -.
DR   eggNOG; KOG1329; Eukaryota.
DR   HOGENOM; CLU_000690_0_1_1; -.
DR   OMA; DSLWTKH; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000008698; Unassembled WGS sequence.
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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT   DOMAIN          837..864
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          1141..1168
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1245..1271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1478..1667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1518..1537
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1551..1570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1608..1636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1713 AA;  192398 MW;  13744149DBA4BC82 CRC64;
     MGDNRRDDSV SPMTRSPKPT RVAIAGSPDR PASPLPSILK SSPLAGSPNN VESTTEARDY
     MNGGLPHRHQ SPVDPLGRPI PPALYVPSTL NNSSDMNDRT PDPPFLQENG GNSEPTSPGG
     GRRSVQFARA DVVLDAPPAH THSRNTSWDD PAKSLSSSLM NKLKQFAGSS TQIPRSPSSG
     ALGEAGSQAL NASPTVTRGG SRIPGTLAEE GSDIDADAEE TADEGAVSDT IQSRLGLRRR
     LSMPDPPDHQ HGLSEGEGRD QLTTPSWMRG NSWIVGSTRS LRNESRDTGG PSTRGPGHVR
     RITVLGGGGA SDGDAMTPRR PFFSGERAST FGVQKWKQVK NTLKLLRQKK EDRFDFAKSA
     ELMAELRAGA PAALMLASMI QRDEHGNKRI PVLLEQWTII RTIKDVYNLH VRYKFAMSND
     KFIHGRADIG SRPKQPKFPW AAFPYLRGAR TKDESEEDDM ASVRGDDPAE QTPGERTVDE
     TADETDGRPQ GGRRKKSRLG MLGMRRRSTG LTDPGETSAL EGHAEMMQSR RRYVERQRRV
     LEKYMQDMVR WLMFRADSNR LCKFLELSAL GVRLAAEGSY HGKECYLHIQ SSKGLDFRRV
     LTPEKVIARH SRKWFLVRSS YIVCVESPEN MLVYDVYLVD AKFRIASKKS SLKHIGSSGT
     REIDLTKEPP PDKHHTLTLH TSERKVKLFS RNQAVLKQFE DSIAEMLKQT KWHSVNRFDS
     FAPVRQGVFA QWLVDGRDYM WNVSRAISMA RDVIYIHDWW LSPELYMRRP PAISQKWRLD
     RLLQRKAREG VKVFVIVYRN VEAAIPIDSE YTKHSLLNLH PNIFVQRSPN QFKKNQFFFA
     HHEKLCVIDH DIAFVGGIDL CFGRWDCPQH PCVDDKPTGF EQSEQPKDAL HCQLFPGKDY
     SNARVQDFYK LNEPYEEMYD RGKIPRMPWH DIGMQVVGQP ARDLTRHFVQ RWNYIRRGRT
     TTRPLPFLLP PPDVKPGEME GLGLTGTCEV QILRSACNWS LGIDDPEHSI QNAYIKMIED
     SDHFVYMENQ FFITSTEVMN TKIVNRIGDA LVERIIRAYN NEEDWKACIV IPLLPGFQSR
     VDEQEGTSVR LILQCQFYSI CRGENSIFGR LRAAGIEPED YIQFYSLRQW GKMGSGELVT
     EQLYIHAKCI IVDDRVALIG SANINERSLR GDRDSELAAI VRDTDMIWST MGGKPYRVGR
     FAHTLRLRLM REHLGLDVDE ILEEERQAEL DKEEEMAAQM DEIYNDEPTT PGFDADEAGP
     SNSAPSASNE DHLWLSDARR FNRDADATPL SRSEAASMVE EKDLRVFNTE HALEVEGYGP
     DHWKAAEKRG LDTGRDSVII NGREVLVHNN DKLPPMPALN RRTTDQLGLL RANQLPTLPA
     VDDTDIGGPP VYLDVNGQPS MGPAHPLAAD IKQARLDKDC MRDPVNFSFM DEIWNRVAEN
     NTKLFRRVFR CMPDSEVLTW NDYRDFTSYN ERFVNSMQGK KAGEEPEVAP EAAEQSNAAG
     SGGAGIGIPG PAAIAKAATD KMEEKTGLDK VKEHVHPPKI MVPSNTTGNE EFNEKADRAA
     RRDKVDHQGV APRNGADPEK SIPFDAPSPI LPAGDTPFPA FDGAEEPSTL PTREKSRDRR
     ATFQPTEKEP ARDRDRSASG QQNQGSVRRR RRATTKGSRR GGTPEDVLPA AEAEELLNLI
     QGHLVQFPYD WLATEEQNGN WGFQVDGVAP LQI
//
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