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Database: UniProt
Entry: A0A1Y1UQF5_9TREE
LinkDB: A0A1Y1UQF5_9TREE
Original site: A0A1Y1UQF5_9TREE 
ID   A0A1Y1UQF5_9TREE        Unreviewed;      1562 AA.
AC   A0A1Y1UQF5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE            EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN   ORFNames=BD324DRAFT_641172 {ECO:0000313|EMBL:ORX40300.1};
OS   Kockovaella imperatae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cuniculitremaceae; Kockovaella.
OX   NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX40300.1, ECO:0000313|Proteomes:UP000193218};
RN   [1] {ECO:0000313|EMBL:ORX40300.1, ECO:0000313|Proteomes:UP000193218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX40300.1,
RC   ECO:0000313|Proteomes:UP000193218};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA   Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA   Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA   Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA   Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (MAR-2017) 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         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:ORX40300.1}.
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DR   EMBL; NBSH01000002; ORX40300.1; -; Genomic_DNA.
DR   STRING; 4999.A0A1Y1UQF5; -.
DR   InParanoid; A0A1Y1UQF5; -.
DR   OrthoDB; 335467at2759; -.
DR   Proteomes; UP000193218; 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; 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   Gene3D; 3.30.1520.10; Phox-like domain; 1.
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; PF00614; PLDc; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SMART; SM00312; PX; 1.
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:UP000193218}.
FT   DOMAIN          659..686
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   DOMAIN          957..984
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1126..1158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1189..1274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1376..1494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1126..1147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1562 AA;  174409 MW;  1280F2CB19D50217 CRC64;
     MEELKDEMGN SPERLPGVKK EEPPGPRTVI ELNTRTPHQH YHRQFRSLGQ GKTPILKITP
     DGEGEYPPGE TPQPSRQSSF HRPNRQSIEE RPSNEADGHW TSALDKAASS SPTSTPQRHH
     DKAMNARFSA FRESRFSETD GDHEHELAQK RWSMLRARVL PSRHNSNGPT PGPGKVSALS
     TTAINTLPVT TELFAGQLPV MMLKTWIDRD EDGRRAVPVL LGNMRFRVGD SVGVGAGKET
     GKEMFKVECE YGDGAVKWVI YRELRDFLSL HANYKAANFG TSVGGLRSSR RVEIPEFPKM
     SIPYFSRSHG KDQAQMAREA LQKYLVELIR AVIFRPESNR LCRFFELSAL TVALAPHGGF
     QGKAGFLMIP GSNASRRANQ PGLTPTSWIH NRSPKWLIVR DSYFVATEGP EDTEFYDVFI
     LDQDFAIERP KRAYRHGLHL VTGKSSIKRS HKHSATDEIE VDPENPLATE IAINSGEGKG
     PNPHTLGDDG QESYASQHTF FIVSSQRKLK LQARNARHMH QFIVSMERIA AQCIWTSRNR
     FDSFAPLRVN VAAQWLVDGR DYFWNLSRAM NMAKDRIYIH DWWLSPELYL RRPGDERYRL
     DNLLKRKAEE GVKVYVIIYN EVSDKTTPVD SLYAKKTLTG LHHNIMVQRS PSHFQTGTFY
     WSHHEKLCVI DETIAFMGGL DLCYGRWDTS QHVLTDEDHT EPDGPNGPVW RGKDYANERV
     AEYANLDKPF EDMFDRTKVP RMPWHDVGLQ IVGQPARDLC RHFTQRWNLL IRTKNHTRRM
     PFLLPPPDFT EGELGDLKLQ GTCEVQICRS VGPWSMGTLT KIEHSIQNAY CKSIQLSEHF
     VYIENQFFIT STVVDGIQIH NGIGDALVER IIRAHKEKTT WRACIVIPLL PGYTYPLDSA
     EASSVRMILE CQNRTIARGA GSIFSRLRKE GIDPDEYITF FSLRTWSKFK SGVLTTEQVY
     IHGKTMIVDD RLVLCGSANI NERSQRGDRD SELVAVIRDT DMIDSKMAGK PYKVGRFSHT
     LRMRLMREHV GIDVDSIEED QLMSREPIAP EDEIETWDPD HQQQDKDELT EGITTVSKRT
     AMERMRRTVG NAMASVTKGM SENAVDNVGR AADKIIHPIA VVKDHAFVDP RNDTPGEKSE
     RQDFSHGGGK TKGFASSIVP TLEEKTIFDR RPSATHANGK PLFDLIEESE NQQQSAGRPE
     EAEVPADAKQ NESVLEENDP SASAHAKAKA PKIHGNPHEK ELFGVPANAV DGDDAPPNDN
     TSRSEGTSDE KRAIGARQTL RKHLSAKTAM TPWSMPTPTP KINPNRFQDP LDETFWKDMW
     VAVAVHNTEI FRKVFRCIPD DLVTTWAAYK AFANHAEKHN KAPEDVAENK NEEPVKVVHD
     GPGTHGSGGG GSGGGAKSET RGADIPEGGG GGGGVGGGGG GKEEDGPTSR MEGGLMGKLG
     AKDTTSNVDP GQKVDNPSGF GEKKPDGGGD GAGGGGDAGE SLGKRVPSGP QEPWAQWERE
     EMEELLNEVR GHLGEFDKRV HYTNAIADTP SLSPPSVIYP QRFLEVEDQI GNLLFQLAAV
     QK
//
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