ID A0A1L9MQU9_ASPTC Unreviewed; 1234 AA.
AC A0A1L9MQU9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=ASPTUDRAFT_59504 {ECO:0000313|EMBL:OJI79419.1};
OS Aspergillus tubingensis (strain CBS 134.48).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767770 {ECO:0000313|EMBL:OJI79419.1, ECO:0000313|Proteomes:UP000184304};
RN [1] {ECO:0000313|Proteomes:UP000184304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 134.48 {ECO:0000313|Proteomes:UP000184304};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(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|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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DR EMBL; KV878208; OJI79419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9MQU9; -.
DR STRING; 767770.A0A1L9MQU9; -.
DR VEuPathDB; FungiDB:ASPTUDRAFT_59504; -.
DR OMA; ILYWAHH; -.
DR Proteomes; UP000184304; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
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 Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 5.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
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:UP000184304}.
FT DOMAIN 303..330
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1000..1027
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 137841 MW; D4F87B2A373AF583 CRC64;
MTRPEDDLAY GQYYQDSARG ASSGDSSRGL SDTFKKLKQT YKSHQSQQGS SQQTQQSQQS
QSASYYNTSN QTYQTQGPSQ SQPHPPPQQQ QQPHPSKPQK QDKFSGLFGK LEEFGNEVAQ
KLGTALDPQA YAEYGAPKPQ TENRFGSFAS PRQGNEVKWH VDGCAYFYAV SKALESAKEY
IWVLDWWLSP ELYLRRPPAK HEQYRLDRML LAAAQRGVRV NIIVYKEVTQ ALTLSSHHTK
HHLEDLHENI AVFRHPDHLP DRQELEASIH TSLQNLSLDA GNLAKMSEDA IKGIYGMHED
VILYWAHHEK LCLIDGRIAF MGGLDMCFGR WDTNQHELAD VHGQDLNKIV FPGQDYNNAR
VSDFHDVAHW EQNQLDRKDT SRMGWSDISV SLHGPVVEDL RKHFVQRWNF IYDSKYQSRN
NSRYARLSLY GRPTSGPQQQ GPQQGGQAQK PPASPQPGAT GPPAPSWQQQ AASPQPGANP
GPPAPSWQQQ AAPSQSAHAP STSSSSTPSW QQQQTGVAAT QPSSAANPAT PTWQQQAPAP
QGGYPVSHSP NPSSQEKPSW QQQTAQPGSY NQPPAQNTGS QEKPSWQQQP AQPTGYNQPQ
TQSTGSQEKP SWQQQSSEPP AYSAHPQQHY TYSGDSFPPP PPGPPPAQGS AQTSYQAYNP
QQQQQQSHTP TQAQSQGQTQ YYPPPPSQEI HHSQTRGIHD ASGGYGDSER GFNPRRLREN
FMDYGNVLRG ELAGQIHQYQ DRFSTHGRQA SQPRGNMTCQ IVRSCSKWSN GTPTEHSIQD
AYAAVIRNSQ HFIYIENQFF ITATGDAQKP VENKIGVAIV ERILRAARAG EKFKIIVVIP
SVPCFAGDLS DESTLGTRAI MEFQYNCINR GGSSIMEMIA KEGFNPMDYI RFYNLRNYDR
INVSGPLMQA EQQSGVNYED ARRQQDVATG GPGSYGPGAP RAAFDTTAPY QQYQQAAQQV
GGKSGQWDSV SSCYMLNGPD IRNVPWNGPP EAEIDAFVTE ELYVHSKVMV ADDRVAIVGS
ANLNDRSQLG THDSEIAIII EDYTPVQSRM NGQPWTASRF AASLRRQLFR KHLGLLPPQD
PERPDGNFEP VGVPNTTDFE SPESQVVADP LADTLHSMWN TRARTNTEVF RKVFHSVPDD
TVRNWATYKE FYGYYFHNAD KQAYGEDESR PARYKYGHVV RDDFPPGPEG VRQVKELLSQ
VKGTLVEMPL MFLIEEDVAK EGLTLNEITE PIYT
//
