ID A0A0F8DB25_CERFI Unreviewed; 1775 AA.
AC A0A0F8DB25;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN Name=pld1_3 {ECO:0000313|EMBL:KKF93259.1};
GN ORFNames=CFO_g4394 {ECO:0000313|EMBL:KKF93259.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF93259.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF93259.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF93259.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-2015) 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 -!- 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:KKF93259.1}.
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DR EMBL; LBBL01000263; KKF93259.1; -; Genomic_DNA.
DR Proteomes; UP000034841; 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, ECO:0000313|EMBL:KKF93259.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000034841}.
FT DOMAIN 913..940
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1242..1269
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1582..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1775 AA; 197586 MW; 1A2CF92F10EDEF08 CRC64;
MRDYGSLGLS ETAPSLGDSA SRTSHPYRNI SPLALPPLNI KDALEDRLQE SPSTVSALSQ
QPATATTAAV SAVSDRRNVQ FAGPSAPSHS RQASWEENDA SRHLASSFMS KLKSLGLQSP
RSTSSVAGNS TPQSRSSSPN NSRTLPVSIE NDQSSDPALA ASVVGETDSN VNTGLDNDAD
ADADAEETAD ETMREDGDSK KTLKKKRKIR RPRLPEWASS PNTSEIAPVP LSAGLMMRHR
GSLPGLSEEA ERWSAVVSEG EGRERLEKKK RPHKRNHISR ASGTEAGLSS SRRGHMRRLT
SFGGGIDTMA SGAVSDIDGA TTPRRNFFSH ERAATLGAQG WHMVKSTLKM LRSKRDDRFN
MSKSAELISE LQAGAPAAML LATYMQRDEH GNKRIPVLLE QLQLNITDSK HRPEDDSERH
SIFTISMIYG SGPSSMQWTI TRTLSDIYQL HLRYRVKTTT ARQEGVLARY RQPKFPSAIF
PWFRSFRSHG DESDEEEEAG ESGQANLNVR EGGRSKDNST ENPDMASLPP LEEPPRIHDQ
HSRRPSSSHS RLHSRSHSRS HSLSNLTDDG GSGVDDIGIG ASYSGQLAAS ATRRRHVDRQ
RKALEKYLRE MIKWLMIRPD SNRMCRFLEL SALGVRLAAE GSHHGKECYL HIQSSKGLDF
RRVLTPGKVI ARHSRKWFLV RQSYIVCVES PENMNVYDVY LVDAAFDIGH KRKKKLFGRG
GSTPVTPVTP VALDDEDSEK GEGPINSGKH HRMTLYTSER KVKLFSRNHS VIQQFEASVR
EMLATTPWHQ PNRFDSFGPV RHNVYAQWLV DGRDYMWNVS RAIQMARDVI YIHDWWLSPE
LYMRRPAAIS QKWRLDRLLQ RKAQEGVKVF VIVYRNVEAA IPIDSTHTKF SLLNLHPNIF
IQRSPHQFKK NQFIYAHHEK LVIVDHDIAF LGGIDLCFGR WDSPQHPLTD DRPTGFEPPK
EDPNCPSGSG AGPSSGFGAG SGAGLSLHNP SRYQMFPGKD YSNPRVQDFY RLNEPYEEMY
DRSRVPRMPW HDVAMQVVGQ PARDLTRHFV QRWNYIRRGR KATRPLPFLL PPPDAKLEQL
EQLGLTGTCE VQLLRSAGNW SLGTNHTEHS IQNAYIKMIE DSDHFVYMEN QFFVTSTEFD
GVRIMNRIGD ALVARAIRAH RENQDWRCVI IIPLMPGFQN TVDNAEGTSI RLILESQYRS
ISRGPHSIFG RLGDAGINAE DYIQFFSLRQ WGKMENGVLV TEQLYIHAKI IIVDDRVALI
GSANINERSM LGDRDSEVAA VVRDTDLIDS HMAGKPYQVG RFAHTLRMRL MREHLGLDVD
EILEEDLAAE MEQEEQDDEF SCSGSDIADT DSMFSEGEHH HGNDEEVVEL EMPTSGSRAH
PNPNSHETDN HDVITEDHGI PGKTAEVHKS RGRSNTNLSR GRRPSRMSAS SAPSRPSAGA
SSTRPEQTPG PAPPPTSSHP LAADITLAPL HKDCMRDPVA PEFIDKIWNH VAANNTTLYR
RVFRCMPDNE VSTWNDYRDY MDYAERFMES MESNVADNRP SGSSHGHINH PTIDLKAAAH
AANEARNHLV IDDNALSGAV TATDGSTTTI PSTSGAGPPL GRLRVPLNID TSGSSIPAST
GAMPNPADGP SPVLPAGDTP FPPLDPSITI PPATPDGERS REKRTTFSTP SRPPITAVNG
MAHEGTSGTG AAAPQAPLST SGTLRKRKRT NTKGSRHRNN PQNPLEVLPQ HDAEELLGLM
QGPLVQFPYD WLLTEENKRN WGYQVDHVAP LQIYI
//
