ID A0A1Q8RMT1_9PEZI Unreviewed; 1808 AA.
AC A0A1Q8RMT1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=CCHL11_05819 {ECO:0000313|EMBL:OLN85627.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN85627.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN85627.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN85627.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-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 -!- 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:OLN85627.1}.
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DR EMBL; MPGH01000162; OLN85627.1; -; Genomic_DNA.
DR STRING; 708187.A0A1Q8RMT1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000186583; 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:UP000186583}.
FT DOMAIN 903..930
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1208..1235
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1808 AA; 202461 MW; 1269F4684F300E25 CRC64;
MTEPRRDESI SPMTRSPRAA SPTAAGTPDL LAPPAPPPKD GPPAPPPKDT LTPKASTEIQ
TDPTIEARDY INGGAPHENL SPVQDGKRPA LPTLNSSDSG RLNPGGLPMM PEDETYSPEP
ASPTDRRSVQ FARTDQVLEA PASHSRQPSW EDGGKSIGSA FMTKLKQLTG SGSMQTLKTS
SSGNLNDSTP SMGSSPTTGQ FRSRIPHTLD EGGGSDADAD VEETADEGAA SDAAKPKKKR
RMRRSKKHQM SVPSTPNLRH LSGPDSPVGY GRMGLRRRLS MPDPPEHQHG MSEGEGRDQL
AGPSWMRARA GDGTESPGGG RRMGHMRRIT VLGGGGVSDG DAMTPKRPFF GNERASTWKY
VKNTLKLLRQ KKEDRFDFAK SAELMAELRA GAPAVLMLAS MIQRDEHGNK RIPVLLEQVR
LRITDSQPES DDDSERHWVF TMDLEYGSGP SRMKWTIIRT LKDIYNLHVR YKLAMSNDKY
LHGRADVGAR PKMPKFPWGA FPYLRSARNK DDSEEEEVAS IRGDDLVEGG PGEGTAAEGT
AGEGTASEWE GRGPGARKKS RLGMLGMRRK STGLTDPGES GGENQAELVQ SRKRYFERQR
RVLEKYLQDM IRWLMFRADS NRLCKFLELS ALGVRLAAEG SYHGKECYLH IQSSKGMDFR
RVLTPKKVIA RHSRKWFLVR SSYIVCVESP EKMNVYDVYL VDSKFRIVSK KSTLKQLGKG
KTKSEEKEID LTEEPDSEKH HTLTLHTAER KVKLFSRNQH IMKQFEDSIA EMLKQTKWHD
INRFDSFAPI RTGVFAQWLV DGRDYMWNVS RAISMARDVI YIHDWWLTPE LYMRRPAAIS
QKWRLDRLLQ RKAREGVKVF VIVYRNVEAA IPIDSEYTKY SLLNLHPNIF VQRSPNQFKK
NQFFFAHHEK LCIVDHDVAF VGGIDLCFGR WDCPQHPITD DKPTGFEHSE QPKDAEHCQL
FPGKDYSNPR VQDFFKLNEP YEEMYDRSKV PRMPWHDIAM QVVGQPARDL TRHFVQRWNY
VKRGRKTTRP LPFLLPPPDV KMAELDALGL TGTCEVQILR SSANWSLGIE HTECSIQNAY
VKMIEDSDHF VYIENQFFIT STEAFNTKIV NRIGDALVER IIRAHENEED WKACIVIPLM
PGFQNTVDEQ EGTSVRLILQ CQYRSICRGE GSIFSRLRAV GIEPEDYIQF YSLRQWGKIG
ARNVLVTEQL YIHAKCIIVD DRVALIGSAN INERSMLGSR DSELAAVVRD TDMIWSTMAG
RPYLVGRFAH TLRLRLMREH LGLDVDEILE EERQAELDRQ AEYEAEMNQI YAEETDSPPV
ASSSGQQSEE KPAKPPLPGQ APSFNHDAIA TADGAAEEVS TSSSSSKDED ADVRVTGNEA
HRLDIAGYGK DHWTDAAKQG LDQGRDSVIV NGREVLVKSV LPEGKGTLES PMQPHDRKLS
ADHFEEEDGG LGNDALPPIP ALNRRTTDQL GLPRTAGLPT LPAVDDTDIG GPPVHLDQSG
QPTNGPLHPL AADIRQAHID KDCMRDPINS SFFDDIWNRV AENNTKLYRR VFRCMPDSEV
LTWPDYREAM SYTERFRESL EGKTKSDETD ANSNRHQSPV TGGGVGVGAP GPSAVAKAAT
EKTEEKLHIR PEHSHHPRII IPGSNDPELN EKSEAPGSRA GPTLQADPDK TAVSGRPQDV
PSPVFSPGDM PFPAFEPGPD ANSLEPTREK SRERRTTFSP LEKPPSRDVS VPAQQAHGSV
KRRRRATTKG SRRGMPPEEV LSRPEAEELL SMIQGHVVNF PYDWLLTEEQ NGNWGFQVDG
VAPLQIYN
//
