ID G3J4K0_CORMM Unreviewed; 1739 AA.
AC G3J4K0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, 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=CCM_00524 {ECO:0000313|EMBL:EGX95870.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX95870.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX95870.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX95870.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(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; JH126399; EGX95870.1; -; Genomic_DNA.
DR RefSeq; XP_006665747.1; XM_006665684.1.
DR STRING; 983644.G3J4K0; -.
DR GeneID; 18162559; -.
DR KEGG; cmt:CCM_00524; -.
DR VEuPathDB; FungiDB:CCM_00524; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_1_1_1; -.
DR InParanoid; G3J4K0; -.
DR OMA; DSLWTKH; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000001610; 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:UP000001610}.
FT DOMAIN 887..914
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1191..1218
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1548..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1739 AA; 196626 MW; 5372A23A15E74BD8 CRC64;
MARDDSVSPF SRSPQKSPIN DEPYTPPVVG GALAASTPNG AAPDDVKPGN EAHAPLSSRP
SSLSAALPHR NATGSNNTDF PGMNGDQATP DTPNTPTARV QFARFDPPDF QPSHSRHNSA
ENPDAAKSRS SSIISKLKYL APHSLQPTRP HSLDGDIQAT AASPVAGRFA GRVPDTLREE
AEETDADMEG EADADAEEEA DETHPSGHVK KKKRRMRRFV KGDGSAPSSP FRFPNDGDAF
SHRFLRRRAS MPDTSEHNQV LSEGETPQRS KRRPFVRRGH SWMNPGTPQA ETDIEALESS
NVVGRRHGHT RRITVFGGGG VSDGDAIVHR RPFFHSERAS NFGAQKWKQV KSTLKLLRQK
KDDRVDYYKS TELMAELRAG APAVLMFASM IQRDEHGNKR IPVLLEQLKL KVIHSAPGPD
DDSERHWYFT IELEYGSGAS RMVWTVVRDI RETYNLHLRY RWAMNKDMYL PGSNHLAARP
KQPAFPWGAF PVLRTVRKKK GQITEDEEEE IVSEREHHNA EDGGDIVAGD DIEATGSDGG
GNRHPRRKRS RVNLLGMRRR STGLTDNGEG PSDQGHEGMR QRFFVKQRRS LENYLAGMVR
WLMFRADSNR LCRFLELSAL GVRLAAEGSY HGKEGYLHIQ SAKGLDFRRV LTPAKVIARH
SRKWFLVRQS YIVCVDSPEN MNIYDVFLVD SKFSLVKKRN AVKKIASKKK EEIDLIAEPS
QSKRHTLTLR TSERKIRFFS RTHAIRQQFE ESITEMLRDT VWSKQQRFDS FAPVRQGVFA
QWLVDGRDYM WNVSRAINMA KDVIYIHDWW LSPELYLRRP AAISQKWRLD RLLQKKAREG
VKIFVIIYRN VEAAVPIDSE YTKSSLLNLH PNIFVQRSPN QFKKNQFFFA HHEKICIVDH
DVAFTGGVDL CFGRWDCPQH PIVDDRPTGF EMTDAPRDAE HCQVFPGKDY SNPRVQDFFR
LAEPYEEMYD RSKVPRMPWH DIGMQVVGQP ARDLTRHFVQ RWNYLRRGRK STRPLPFLLP
PPEANFDELE ALGLTGTCEV QILRSASAWS LGLIETEHSI QTAYIKMIED SEHLVYIENQ
FFISSTEAYS TRIVNRIGDA IVHRIVRAHE NGESWRCIIL IPLMPGFQNT VDEQEGTSVR
LIIMCQLKSI CRGENSIFGR LRSAGIDPED YIDFFSLRQW GIMSTDALVT EQLYIHAKTI
IVDDRVALIG SANINERSMV GHRDSEIAAI VRDTDMIWST MGGKPYQVGR FAHTLRMRLM
REHLGLDTDA IMEEERQNDV NYESFDSQMD HFYEDGRGSP NSAHNGESSK SAHPGIQHLR
SFNSELDIEM ARAVDPASSS SDDNSERKYK GKQKEQDAAF QAELHIRDVS GHGPDHWKAF
EKSGIDGGRD SVIVDGREFL VSSIDAMGKG TLEEPEHNDA HDRRKSLERI ADEKLLPPLP
PFDERAANVA DLRPAQLPTL PENKDDKAQA DNLGAFSYLA AEIKPATITK DCMADPLAPE
FIDDIWNRVA RNNTKLYRKV FRCMPDSEVK TWAEYRDFVA YGKRFHESME GRPASEEPDA
PSEAGYMNRT ASGGAIGISV PDLEALARIN GEDAEKVAAN LNNQHTNSDI TGETVDEKTG
AADEEREMGA EVEKQSTNPE TLERKTTTFA NLEKPPTKDS TTTAAAQAQF GSVKRRRRAA
TKGSRRWSNV DDMPNRTEAE GLLRMVQGNL VEFPYDWLIT EEHNGNWGYQ VDGVAPLAI
//
