ID A0A074WT80_9PEZI Unreviewed; 1688 AA.
AC A0A074WT80;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=M436DRAFT_38817 {ECO:0000313|EMBL:KEQ76410.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ76410.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ76410.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ76410.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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}.
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DR EMBL; KL584703; KEQ76410.1; -; Genomic_DNA.
DR RefSeq; XP_013430880.1; XM_013575426.1.
DR STRING; 1043004.A0A074WT80; -.
DR GeneID; 25409084; -.
DR HOGENOM; CLU_000690_0_1_1; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000027730; 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 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; 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:UP000027730}.
FT DOMAIN 768..795
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1075..1102
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1604..1636
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 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1550..1580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1688 AA; 190511 MW; A21B01601FD547C6 CRC64;
MTPPERRPGL GDDHIEGADE HGRQGSFFSR LKAMATPTHS RHPSEFTNAS VLMTPTEELD
EPHFPIYSQS QHDGSEAEGD IEESSMDEAH ENHEPRQKRK ARRKMDKTAS AGPSTPRTPR
FPSFLRDHAD RTPRLPRRAT MTDIPENSRA GVSEDEGRDR LAKSAWRRGL EGARGLSYAP
RSSRPTNDAA EQSDSNRPPT ARRFTGFGAL DGSASPWRGR GERQQSTSAQ KWKQVKAGLK
LLGQRKKDER VKVDHQKSTE LMAELLAGSP AAIFLASMYQ RDEHGRRKIP VLLEQLKITI
PSSQNRESKS GDRHMVFTIN LEYGSGPSRM SWTIHRSLRD FSNLHLKYKF QSQSERYSIL
KTEDRSKAKI PRFPRSAFPY LRGVRGLADD EEEEDDNAIA EASGPDGEAS GPERPGMKKR
RRTSFALSRR KSSTGHASGA ENGDATRAGS IVGGGAKAKD LYNERQRRKL ENYLQQMIRW
LVFRPDSTRL CKFLELSALS LRLSVEGGYH GKEGLMSIIS KPNIDLRRRP VTGSVSAFKR
NAEPKWFMIR HSYIVALDSP ESLEPREVFL VDGDFTTDKA SKKRLRDQTA EELAKTAGNA
TQPKHHILRL YNSERKLKML AKNERQLVQF NESIDYMVRN TVWSLKHRFD SFAPVRKNVF
ARWLVDGRDH MWQVSRAIDN ARSFVYIHDW WLSPELYLRR PAAISQKWRL DRLLLRKAQE
GVKIFVIVYR NIESAIPIDS EYTKASLLDL HPNICVQRSP NQFRQNQFFW AHHEKLVVID
NAMAFVGGVD LCFGRWDDPH HSLTDDKLTG FELDMEGPRT ADNCQVWPGK DYSNPRVQDF
YALDRPYEEM YDRTKVPRMP WHDIAMTIVG QPARDVARHF VQRWNYILRQ RVPSRPTPIL
LPPPEFDQSE LERLGMTGTC QIQILRSCTS WSIGTPNKTE CSIMNAYVYL ITNSEHFVYI
ENQFFITSCV VEGTQINNKI GDALVERIEL AHQRGDKWRA CLIIPLMPGF QNQVDSQDGT
SVRLIMQCQY RSICRGESSI FGRLRAQGID PTQYIEFYAL RQWGKIGPRK CLTTEQLYIH
AKCMVVDDRS VIIGSANINE RSMLGSRDSE VAAIVTDQEM IPSLMGGKPY DVGTFPHTLR
MRLMREHLGI DVDDIYRREC EAEKAFQDEE MERIYRDDSI TPPETPTAAH GLTEENLQYN
SEPDGKAGVL QNFLNETNTT HTGQVDGAGS KKQSFDIKHD LDVAGYGPDN MKNLENVADM
SARDTYITPH GKEVLKSANL LDAAARPRSS SVRRDIINHH IYDHPHNATE AGRILPPPMP
PRMNTRELGL THLSQLPPLP VSDDSDIGGP SLVKEVNSEN AHVINPLLNS MTRPLVDEDC
MRDPLDNDFY KKIWHQVAEN NTRIYRQVFR CMPDSDVQSW AEYRQFNAYS EKFMQSQGMG
MGSPFSKPSG DAPDTSGPPG SGGTDALSSV ANPSERIAKH ASNRFSGLSK LFGGRPGTSQ
STATAATADI SEKQGLDGGP RASDSALTNH ADDATAAEEP FDEKAAAARN DTATTDTTLA
APLDGVPTNT TSSTPFRPLK SRTIQFPEMT EKEKNFEAGP FQHAATVSGS GNMQHSTSTK
RRRNRANTKG SMRNGGVFEP EVLTKDEAEG LLKLVQGHLV VWPYDWLERE EKGGNWLYNI
DQIAPLEI
//
