ID A0A286UBU8_9AGAM Unreviewed; 1746 AA.
AC A0A286UBU8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=PNOK_0710000 {ECO:0000313|EMBL:PAV17036.1};
OS Pyrrhoderma noxium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV17036.1, ECO:0000313|Proteomes:UP000217199};
RN [1] {ECO:0000313|Proteomes:UP000217199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA Kikuchi T., Tsai I.J.;
RT "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT Hymenochaetales Members.";
RL bioRxiv 0:0-0(2017).
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|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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:PAV17036.1}.
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DR EMBL; NBII01000007; PAV17036.1; -; Genomic_DNA.
DR STRING; 2282107.A0A286UBU8; -.
DR InParanoid; A0A286UBU8; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000217199; Chromosome 7.
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 CDD; cd06093; PX_domain; 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; IPR001683; PX_dom.
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 SMART; SM00312; PX; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
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:UP000217199}.
FT DOMAIN 547..803
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 931..958
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1228..1255
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 18..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1746 AA; 197023 MW; 8A49B7E53C28CCE0 CRC64;
MNGFADVVQH AINAKKITDT DGETERASNA PINEQSIPDI YSVMGNGAHA TSSPKTPPAL
RHFKTDSINR AGSQDSSGSS PPPSHTQTTR SPHDSPSSRT GPPRSFSYSI TRSPNLSRQN
TRAVEDDIEE EVSGGPDYGA GDENDGGYGF PADSEGGINA GSSVETRPGA GSRLRSSFRG
ALEYIDPEQR EKEREAMEKR EKNRMSKIAG EDSWINPLKW LNGEVATQES PQTDGEGWTS
YFDFLKPGDK GKEKENTEDE AETAAETSSE KKRHKRMKGA SISGHSPDRS ASHDDQEKAP
TRKRIERSHS MPHMKRPSPK KTYSTKGAPR WNRLRSLIPS IAQQGRTEAR QGQIAVQPHV
VNITDELIAG GLSALMLKLW FERDERGARR IPVLLHRLRV RISDSIHPLK GNKAVFRIEC
EYANGAVRWV VYRQLRDFVS LHTHYKLSNT FNRNVDALPE FPRTSLPYFK FLREKGKENE
REIGRADFAI MQREALENYL IGLIRAVMFH PTSNRLAGFL EISALSIQLA QSGGWQAKAG
LLTIEPASKK SGGFGRRNAS WSDKKKQRWC ALREGYLVAV EDPAETTIWD VFLLDSDFKI
ERPKRYYRQG FHILHSSTKD DELSRKLTNN SSSRADGDTH STLGKVKAKF RSFRVGQHHR
SRSSGHVQWS NGPGGSLDRN REHTRTHSGV TSASESESDR TDSEDEDRSP MVDPSTNIDP
LRADGKRGSR GANTRETDGE GDINDNPDLE KAEKQMQKKK GKRSKDVSKH TFFVSNSQMR
LKLYAKSERQ MQQWITALER VAQSSYWTGS NRFGSFAPIR LNVAAQWLVD GRDYMWNLSR
AIMLARERIY IHDWWLSPEL QMRRPHKERY RLDKLLERKA KEGVKIYVIL YQEVSNRTTP
TDSNYTKQRL TSLHPNILVQ RSPSHFQTGT FYWAHHEKLC VIDEAIAFMG GVDLCFGRWD
TPQHILIDDP DLEEEGSTQI WPGKDYSNAR ISDFFTLTKP FEDMYDRQKV PRMPWHDVGM
HIVGQPARDL CRHFVQRWNY LLRIKNHSRT MPFLLPPPDF KPHELDEQGL TGTCEIQICR
SCGPWSMGTS TRVESSIQNA YLKAIQMSDH FVYIENQFFI TSTTVNDTVI ENRIGDALVS
RIIRAHREGT NWKACIMIPL LPGFPFPVDH SDASSVRIIL ECQNRTICRG PHSIYGRLRK
EGINPEDYIT VFCLRNWGKL PGNVLTSEMV YIHGKVCIVD DRLAIIGSAN INERSQRGDR
DSEIAAIIRD TDMIDGTMDG KPYKVGRFAH TLRVRLMREH IGVDVDAIYE EDLMSTEPSK
DQMSQEAWDP ESEQQEGMNG VTQIGKTSAR SRVGEALDEI KDSAKQVLHG TEDDTAKDAG
HIAQKVGLVS KASDAAVDDK ALREERQTYT RDGEKEPGFT SSIVPTLEEK TIIEQRPPKE
QVDGELPPTY RSETVESGGP PEARVHDGSH ELYGAPANSV PQADNEVPHA RDAKSDPTLD
TTDEEKAALH ARRTVRKHLE AGITNPVCDV FWKNTWVACA VHNTEIFRKV FHCIPDDTVT
TWKQYKEFVL HHERMNKPVK DTSEPLGRVP SEAGDEDAPG RDKNTSLRAE DGARQDTLRA
KSSVRSNGTH HSRNSLPQAE SKSRTPTPEG LDGHKPSVGH GGYSNSNYNN ITNGSGGVGA
HDTEIRRAPS RADRPFEKWE RDEMEKLLGE LRGHLVLYPT RFLEGEDAAN NFLFNADRLL
PMPIYD
//
