ID B0CVY5_LACBS Unreviewed; 1340 AA.
AC B0CVY5;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=LACBIDRAFT_245542 {ECO:0000313|EMBL:EDR13418.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR13418.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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 ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; DS547093; EDR13418.1; -; Genomic_DNA.
DR RefSeq; XP_001875916.1; XM_001875881.1.
DR STRING; 486041.B0CVY5; -.
DR GeneID; 6071238; -.
DR KEGG; lbc:LACBIDRAFT_245542; -.
DR HOGENOM; CLU_000690_3_2_1; -.
DR InParanoid; B0CVY5; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000001194; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
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; IPR001849; PH_domain.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000001194}.
FT DOMAIN 581..608
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 879..906
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1067
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1340 AA; 152453 MW; 4081378D0A8E5A0C CRC64;
MDFPSPDAEE KKVTGQSDKE NDEKRSQYSP SRRVSVRNDS GPPLNTSKSR SALRRAFSTS
TAQTTSPDGN KDGKARWARL RALLPHIVHP DESILPGPSV VTSQAVNITD ELITGGLSTL
MLRLWFERDE KGQRRVPALF HRLRIRVSDS LHPMHHHKSV FRIECEYANG AARWVIYREL
RDFLSLHGHY AVSNVYNRNV DRMPEFPRTS LPYFKFLKKE GREKGDIVGK ADFARLQREA
LENYLIELIR GVMFHPSANR LAGFLEISAL SIALAQSGGA QYKAGYLKLE ATGNGGSGFG
RKSTSWHAQK ESRWCAVRES YLVVLEEPGE VRIYDVFFLD SGFNIERPTR YYRQNLGNLL
NHSSDPKPEG KDKDHISRPQ NFQTYLDPPE DEHRSVISSI KTGEWKDGHK TVSRTDVSKH
TFYIVNSQMR LKLIAKNERQ MLQFITALEK AASKCHFTGT HRFDSFSPIR MNVAAQWLVD
GRDYFWNLSR AILLAKETIY IHDWWLSPEL QMRRPNKDKY RLDRLLARKA KEGVMVYIIL
YQEVSNRTTP TDSNYSKQRL TSLHPNVMVQ RSPSHFQTGT YYWAHHEKMC VIDQVIAFMG
GIDLCFGRRI RWDTAQHVLT DDVADTERSE IWPGKDYSNP RVSDFHTLYK PEEDMYDRTK
TPRMPWHDVG MQIVGQPARD LARHFVQRWN YLLRIKNHTR VMPFLIPPPE FRPGELTQMG
LTGTCELQIC RSAGPWSLGT PGKIESSIQN AYLKAIQMSE HFVYMENQFF ITSTVVNEVE
IENNIGNALV QRIIRAHRDH TPWKCCILIP LLPGFTFPVD HSDASAIRII LECQSRTIAR
GPNSIFCRLR KEGIDPDDYI SVFSLRNWAK MRGDVLTTEQ VYIHGKVCIV DDRLAIIGSA
NVNERSQRGD RDSELAAVIR DTDMLDWRVT PEYEAAITMA GKPFKAGRFA HTLRVRLMRE
HLGVDVDALI EEDLNMKGSS MAESHKEPWS PNAYKTHGRR STAPSASGSS SASGSSVGEG
NLSNELKGSK MRNLAHDYYA QDAGDNLDAP RKDHNSTGTS SKAPNVPTLE EKTVAEHHPQ
ANQVDTLIDG GHDVQHQTIK EELETPSGTL TPLPTDDGVS RDALANAKTE VDGLPPRHSD
VDEEKAVSVV RSTLRKSYGS KHTPWTVPMP RPRVNAKDFE DPISDAFWKD IWVASAVHNT
EIYRKVFHAI PDDLVTTWKQ YKDFVAHHER LNKPVSQTTN EELGDEGQPA TDALSDVSKE
HVDESPPESV PNQSSAESKP RRHAKGTEPF EKWERIEMEN LLGELNGHLV LYPNRFLEGE
DSANNFLFNA DRLLPLPIYD
//
