ID A0A166IAR3_9AGAM Unreviewed; 1401 AA.
AC A0A166IAR3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=PENSPDRAFT_574897 {ECO:0000313|EMBL:KZV73238.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV73238.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV73238.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV73238.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV424492; KZV73238.1; -; Genomic_DNA.
DR STRING; 1314672.A0A166IAR3; -.
DR InParanoid; A0A166IAR3; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000077086; 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 Gene3D; 3.30.1520.10; Phox-like domain; 1.
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; PF00614; PLDc; 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; PS50003; PH_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:UP000077086}.
FT DOMAIN 443..477
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 605..632
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 899..926
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1401 AA; 157708 MW; DD49CED7A51FB5F9 CRC64;
MKDDEDGRTD AEDEHEKKQQ RQGGGTNKDA HAKWNRLRFL LPHIAQQGPS PGASAINPVH
VNITDELMAS GLSVILLRLW MERDERGQRR VPVLLHRLRI RISDSLHPLH GAQSVFRIEC
EYANGAVRWV IYRQLRDFLS LHAHYTVSNA YNRNVEAMPE FPKTSLPYFK FLQKENKKDG
KQKDGGKDVA RADFARMQRE TLENYLVGLI RAVMFHPAAN RLCGFLEISA LSIHLAPTGG
AQYKAGFVRI KSSGTRGPSF GRRGTGRKDK LEQKWCAVRE SYLVAVDDPG ELAIFDVFML
DSEFRIERPT RYYRQGLNLL QGEMVRDDIA ERKNLMPPDD HHERSSMFSS IRRSFSKVVH
PRHSHDTGYT NGDAHARPSS ARTSSDSSSS SSSSSSSDER PPTPMLDPST NTNPIADDGD
QRAPGGMDGK KKKKSRMSSE MSKHTFYIVN SQMRLKLFAR SERQMLQWIA ALEKVAATSH
YTGTNRFDSF APIRLNVAAQ WLVDGRDYYW NLSRAILLAK ETIYIHDWWL SPELQLRRPN
KPKYQLDNLL KKKAEEGVKI HIIIYQEVSS RTTPVDSNYA KSRLTGLHPN IMVQRSPSHF
QTGTFYWSHH EKMCVIDETI GFMGGFDLCF GRWDTPQHSL VDDPDDPEAV IWPGKDYNNN
RVEDFHTLNK PFEDMHDRKT TPRMPWHDTG LQILGQPARD LARHFVQRWN HLLRIKNHSR
EMPFLLPPAE YKTGELANLG LTGTCELQIC RSCGPWSMGT PDRIEHSIQN AYLKAIQMSE
HFVYIENQFF ITSTMVGDVQ IENKIGDAIV ERIIRAHHEG TKWRCCVVIP LLPGYPFPLD
HNDASSVRLI LECQNRTIGR GPHSIFSRLR KEGIDPDNYF GIFSLRNWGK LRGDVLTTEQ
VYIHGKVCIV DDRLAIIGSA NINERSQRGD RDSELAAVIR DTDMVDSTMA GKPFKVGRFA
HTLRVRLMRE HVGIDVDALD EEDLLANKPE KEEHEVDPWD PDAEQRQGNE DVTAHAGHSG
RARLMAQFAG DTIGSAAQGT KDLADEAFVR LGQDVGLRRD VPTLNNANVG LGDERKTYTR
SGEEVPGFAD SVVPTLEEQA ITEGLPSKPA RGRPSTRDNE EEMKEEKSGP AQAEASTENG
QKFGAPADAS RDAATDNEPP HARSGTDDAQ GEERDAPRVR SILRKHLKAG TGGSPYVLPT
PRPEIAPDML NDPVSDDCYK QVWIAAAVHN TEIFRKVFHS VPDDLVTTWK QYIEFIAHHE
RMNKPTADHP EPVGRVPSET GDVGAPGEQD TQDHLGRAEE FAKKDEDPHS ASDSGDRAHG
TANPTTNASN LNGGGTQKGK KGKSDSGEPA FTKQERDEME ALLGELCGHL VIYPTRFLEG
EDVANNFLFN TDRLLPLPIY D
//
