ID A1C7Y4_ASPCL Unreviewed; 1136 AA.
AC A1C7Y4;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=ACLA_075440 {ECO:0000313|EMBL:EAW14505.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW14505.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW14505.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027045; EAW14505.1; -; Genomic_DNA.
DR RefSeq; XP_001275931.1; XM_001275930.1.
DR AlphaFoldDB; A1C7Y4; -.
DR STRING; 344612.A1C7Y4; -.
DR EnsemblFungi; EAW14505; EAW14505; ACLA_075440.
DR GeneID; 4707674; -.
DR KEGG; act:ACLA_075440; -.
DR VEuPathDB; FungiDB:ACLA_075440; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_2_1; -.
DR OMA; ILYWAHH; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
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 Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 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:UP000006701}.
FT DOMAIN 313..340
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 900..927
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 127662 MW; D530BA81F4FBF10C CRC64;
MSGREDDLAY GKYYQRDDGQ GESTRGFVGD TFNKLRNTYK QHHSQSPPPG QNQPQSSYNP
GGYGGQNFSP NQGAPQTYPY GTQGQNQNEN QNPAYQEPGY QGKPAKQDKF SGLLGKFQDT
VATLGTDVAQ RLGTALDPQA YAQYGTPQPQ SQQRFGSFAA PRQANDAKWY VDGCSYFYAV
SKALESAKES IWILDWWLSP ELYLRRPPAK NEQYRLDRML HAAAQRGVRV NIIVYKEVTQ
ALTLSSSHTK HALEDLHQNI AVFRHPDHLP DRQNLHSSIT TTLQNLTLDT VSLAKMSGDA
LKGIYGMNED VILYWAHHEK LCLIDGRIAF MGGLDMCFGR WDTHQHAIAD VHPTNLDDIV
FPGQDYNNAR VLDFQDVVHW EKNQLNRERT SRMGWSDISV SLHGQVVEDL RRHFVERWNF
IYDTKYQVRK DVRYSKLALY GRPSSSTSQQ QSAANNQPQS QQQQQPHQPQ YQQQSQPQYQ
QQHQPQQPAD LSAYPPQTTV GGQGAPNYQP PSPGYGGQSP SQAQTGSHQY SYTGDSFPPP
PPGPPPTQSY GSTPTQSYGS AQSPNQGQGQ APYFPPPPTQ EGSHSQTRGM DDYYEGSRGQ
GDPDRSSFNP RRFKDEITGY GNVLRGQLAG QVHQYQDRLS SFGRPGPQQR GNMSCQIVRS
CTKWSNGTPT EHSIADAYAA IIRNSEHFVY IENQFFITAT GDSQKPVRNQ IGAAIVERIL
RAARAGQKYK IIVVIPTVPC FAGDLEDEAS LGTRAIMEFQ YNSINRGGHS IMELIAKEGY
NPMEYIRFYN LRNYDRINAN SRMSEIEQKS GVSYEDARKQ HDLNTVGPGG YGPGATRTAF
DTSVPFQQQY QQAAHQVSTT KSTSGRWDSV SECYMLHGED IRNVPWEGPS EAEIDAFVTE
ELYVHSKVMI ADDRVVICGS ANLNDRSQLG DHDSEIAVII EDQTPVQSSM NGQPWTASRF
AASLRRQLFR KHLGLLPPED PQRPDANSEP VGVPNQFDFD APESRIVADP LADTLQSLWN
TRSRTNTEVF RKVFHAVPDD TVRDWASYRE FYSYYFQGSD KQAYGKEEKD SRPSRFQYGH
VVRDNFAPGA EGVREVKELL SQVKGTLVEM PLMFLIEEDV AKSGLALNEL TEPLYT
//
