ID A0A074Y496_AURSE Unreviewed; 1755 AA.
AC A0A074Y496;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
DE Flags: Fragment;
GN ORFNames=AUEXF2481DRAFT_42977 {ECO:0000313|EMBL:KEQ92535.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ92535.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ92535.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ92535.1,
RC ECO:0000313|Proteomes:UP000030641};
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 -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
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DR EMBL; KL584770; KEQ92535.1; -; Genomic_DNA.
DR RefSeq; XP_013340988.1; XM_013485534.1.
DR STRING; 1043005.A0A074Y496; -.
DR GeneID; 25367282; -.
DR HOGENOM; CLU_000690_0_1_1; -.
DR InParanoid; A0A074Y496; -.
DR OMA; CAVHNTE; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000030641; 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; 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; 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 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};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000030641}.
FT DOMAIN 892..919
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1199..1226
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1562..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1713..1755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1755
FT /evidence="ECO:0000313|EMBL:KEQ92535.1"
SQ SEQUENCE 1755 AA; 197410 MW; 7CB4537D1457D6C4 CRC64;
MEMVAEEEAP RSLSPLARPR FAEAGSQPSS PLRTTFTPDT PTPAHTTLSN ELLRPPTAVS
VHFGPPTPAD FNLPSVKSFI NGSAPRSVSA TSPRPRPFVL RHDSDPTMRT MSRNRDASGG
SGTQTPPERR LGEDQLDAGD EHGRQGSFFS RLKAMATPTH SRHPSEFTNA SALMTPTEEL
EEPHFPIYSQ SHHDGSEAEG DIESSMDEAV EGQETRPRRK SRRKMEKTVS AGPTTPRTPR
FPSFLRDHAD HTPRLPRRAT MTDIPENSRA GVSEDEGRDR LAKSAWRRGL EGARGLSYVH
RSNRSNNEAA EQSDSNRPTT ARRFTGFGAL DGSASPWRGR GERQQSTSAQ KWKQVKAGLK
LLGQRKKDER VKVDHQKSTE LMAELLAGSP AAIFLASMYQ RDEHGRRKIP VLLEQLKITI
PSSQNRETKS GDRHMVFTIN LEYGSGPSRM SWTIHRSLRD FSNLHLKYKF QSQSERYSIL
KTEDRTKAKI PRFPRSAFPY LRGVRGLADE EEDEDDNAIA EVSGQEGEAS GPERPGMKKR
RRTSFALSRR KSSIGHASGP DGVTGEVARA GSIAGAPGGA KAKDVYNERQ RRKLENYLQQ
MIRWLVFRPD STRLCKFLEL SALSLRLSVE GGYHGKEGLM SIISKPNIDL RRRPVTGSVS
AFKRNAEPKW FMIRHSYIVA LDSPESLEPR EVFLVDSDFT TDKVSKKRLR DQTAEELAKT
AGNAAQPKHH ILRLYNAERK LKMLAKNERQ LVQFQESIDF MVRNTIWSLK HRFDSFAPVR
KNVFARWLVD GRDHMWQVSR AIDNARSFVY IHDWWLSPEL YLRRPAAISQ KWRLDRLLLR
KAQEGVKIFV IVYRNIESAI PIDSEYTKTS LLDLHPNICV QRSPNQFRQN QFFWAHHEKL
VVIDNAMAFV GGVDLCFGRW DDPHHSLTDD KLTGFEMDME EARTADNCQV WPGKDYSNPR
VQDFYGLDRP YEEMYDRTKV PRMPWHDIAM TIVGQPARDV ARHFVQRWNY VLRQRVPSRP
TPILLPPPEF DQSELERLGM TGTCQVQILR SCTAWSIGTP NKTECSIMNA YVYLIENSQH
FVYIENQFFI TSCVVEGTPI LNKIGDALVK RIELAHERGD KWRACLVIPL MPGFQNQVDS
QDGTSVRLIM QCQYRSICRG ESSIFGRLRA QGIDPTQYIE FYALRQWGKI GPRKCLTTEQ
LYIHAKCMVV DDRSVIIGSA NINERSMLGS RDSEVAAIVT DQEMIPSFMG GKPYDVGTFP
HSLRMRLMRE HLGIDVDEIY RRECEAEKAM QDEEMERIYR DDYDTPPETP RAHGGLTEEN
LSQNSEPDGK ANVLHNFLSE TNSGSSHQLD GTNSRRKSTD KGHDADVTGY GVDNMKGLEG
IADTNARDTY ITSHGREVLR NHNLLDGGPH PRSSSVRRDI IHHLHELPQN AIEAGRLLPP
IMPPRMNTRE LGLTLLSQLP ALPVLDDSDI GGPSLLKDVS SENAHIINPL LNSMPRPVVD
EDCMRDPLEN DFYKKIWHQV AENNTRIYRQ VFRCMPDSDV QSWQSYNQFN AYNEKFMLSQ
GMGTSSPLSK SAGDAPDTSG PPGSGGTDTL SSAAALSERA SKHASNRFSG LSKLFGNRPS
TSQSNITAAN GELSEKQALE GDAAPTPDDV TNEETVDEKV AAAQRNDTAN TEATLAPPPL
DGVPTNISSN TAPRARARTI QFPEMTEKEK NFEPGALPHA ATIGANISHS TSTKKRRNRA
NTKGSAKLNA EQEIL
//
