ID A0A2J6T205_9HELO Unreviewed; 1819 AA.
AC A0A2J6T205;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=K444DRAFT_45172 {ECO:0000313|EMBL:PMD57055.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD57055.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD57055.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD57055.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) 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};
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DR EMBL; KZ613847; PMD57055.1; -; Genomic_DNA.
DR STRING; 1095630.A0A2J6T205; -.
DR InParanoid; A0A2J6T205; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000235371; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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 Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
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 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:UP000235371}.
FT DOMAIN 913..940
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1218..1245
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1651..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1711..1770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1819 AA; 203615 MW; 30B76145B13B4ABC CRC64;
MAQRNDESLS PMTRSPRSGS PVHSNANGTA NARQSGLRTE LSVDGLPGAA HDFAPPVLAA
NGGTSKAGVD AVDYFHGGFP HESQRPPFMT GAGVSSSNSP TRQSALKHTP GSFSQDGVAA
TAGTSTPPGR RSVQFARADP GTSSHVRSES WEDGEIPSKD RRGQSLMSKL KALATTGALQ
THSRSQSNTA NSFEDDTGSA PLSPTTERAT RLPYTLQEEG SDVDADAEET ADEGNIADAA
RAKKKRRFRR PLETANGSQT APNTPRVRGM GATDSPGGSS RQIPFLTRRA TDGSLDQRGH
LSEGEGRDRL NGQSAWRRGS SWIAGARGAS YGGQQQADLD GTPTSRRPGQ FRRMTGLGGG
QSDGDGQTPR RPFLGAERAT TFGAQRWRML KHGLKLLGQK KEEHKVDYLK SAELMAELRA
GAPAALMLAS MIQRDEHGNK RIPVLLEQLK LHITDSRPSV EEPTESERHL VFRIELEYGS
GLNRMKWVIH RSLRDFANLH LRYKLQGSSD KYIQLRSDVD SRPKQPRFPK SAFPYFRGVR
GLGESEEDEA DNIRVDETVG EATHSENERK RKKRRPSLAG TRRKSSAAPQ DPNTGAVIGM
GQQSQQTRIY NEKQRRRLEQ YLQEMIRWLI FRADSNRLCR FLELSALGVR LAAEGSYHGK
EGYLIIQSAN GLDVRRLLKP SNIFARHSPK WFLVRHSYIV CVDSPENMHI YDVYLVDPKF
EIRQKRRRLK EMDKKEMMET AGTSAKHPQH HSLKLQNSER KIKLLAKNER QLRQFEDSLN
YMLSTTPWSK ENRFGSFAPV RTGVYAQWLV DGRDYMWNVS RAINMAKDVI YIHDWWLSPQ
LYMRRPAAIS QKWRLDRLLQ KKARDGVKIF IIIYRNVEAA IPIDSEFTKF SMLDLHPNIF
VQRSPNQFKK NQFFFAHHEK ICVVDHTVAF VGGIDLCFGR WDTPQHSVVD DKPTGFEQSD
LPKDADHCQL WPGKDYSNPR VQDFFQLNEP YAEMYDRSKT PRMPWHDIAM QVVGQPARDL
TRHFVQRWNY VLRGRKPTRP TPFLLPPPDY NSADLEALGL TGTCEVQILR SASDWSLGLT
EVEHSIMTAY CKMIEESEHF VYIENQFFIT SCETMNTKIV NRIGDAIVER ATRAYQSGES
WRCVIIIPLM PGFQNTVEEA EGTSVRLIMQ CQFRSICRGE GSIFGRLRTQ GIEPEDFVQF
YSLRTWGKIG PNKMLVTEQL YIHAKVIIVD DRIALIGSAN INERSMLGVR DSECAAVVRD
TDMLWSIMDG EPYLVGRFAH TLRMRLMREH LGLDVDEVME EERRVELDRE EEEYETRMNG
IYDGNDSETD RAKAREAQSV LLPDQALRIA NHERMRSFNH DVDWEEEGNP NVAPESYKSV
TTDKRVIGNK AHAAEVDGEG PDQLKAAEKT GIVRGRDSVL ADGGREVLVA DIASEGKGTV
SHPNRPHDRP PPVHHRGSDG SGSAGNDKVP PMPSFPRRTT DQLGLSQLSQ LPALPITDDT
DIGGPPVHLD ATGRPAPKEF NPLTADIKIA HVDKDCMRDP LNDSFFEDTW RQIADNNTKI
FRRVFRCNPD SEVTNWHEYG EFMAYAERLA QSQGGKSTEW EEQEAAGKSG PPGASSTAAG
MAAVPVLSNL TEKINRHGQD DRPLGTVAEI AENAREDNAK RTDTGREGGM NGHLDGIDEK
AELRAEEPAS PILPAGDETF PSLDSTLLDT STAAAETAPQ PVTSTPAPRK TTFSSTTPTT
NPATNGSANK GSGKRRRRGT TKNKFSGSDD LLSRQDAEEL LGLVQGHLVF FPYDWLIKEE
LNSNWLYQVD QVAPLQIYN
//
