ID B6QJU1_TALMQ Unreviewed; 830 AA.
AC B6QJU1;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=PMAA_091640 {ECO:0000313|EMBL:EEA22537.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA22537.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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DR EMBL; DS995902; EEA22537.1; -; Genomic_DNA.
DR RefSeq; XP_002148704.1; XM_002148668.1.
DR AlphaFoldDB; B6QJU1; -.
DR STRING; 441960.B6QJU1; -.
DR VEuPathDB; FungiDB:PMAA_091640; -.
DR OrthoDB; 335467at2759; -.
DR PhylomeDB; B6QJU1; -.
DR Proteomes; UP000001294; 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: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; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896:SF128; 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; 2.
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:UP000001294}.
FT DOMAIN 192..219
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 617..644
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 697..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 95704 MW; C65E6F66636225AC CRC64;
MDALREKLQH TKLHDIKAQA SHLKHKIGKL ENLFNPNHRH DEAHEQEVDI KRTAIAESHR
FQSFAPERDG NKVKWYVDGS DYMWAVSVAL DRAKETIYIA DWWLSPELFL RRPPNLNQEW
RLDHVLKRRA EAGVQIYVIV YKEVDRALTC NSAHTKHALR NLCPEGSKGA GNIHVLRHPD
HNIFENLGDM TFYWAHHEKF VVIDYEIAFI GGIDLCFGRW DNHQHALADV HPAGIENEIF
PGQDFNNNRI MDFQSVEDWQ TNELNKTDFG RMPWHDVAMG LIGDCVYDIA EHFVLRWNCV
KRDKYKRDTK VDYLLIEGRT GEDEGLIAVQ RPKFPCGEYI QHPLRPLSTK PRGEQGTVHA
QVVRSSGDWS SGILTEHSIQ NAYSEIISKA EHYVYIENQF FVTATGDQQH PVQNTIGRAI
VEAVVRAGKE GRKFRVIIII PCIPGFAGDL RENAAAGTRA IMDYQYKSIT RGENSIFEQV
RAQGVDPTEH IFFFNLRSYD RINKTKELVE QEEKSGVHYQ DIQRANAEQI MGESVHPDVG
EEGVLHEHSY HIRREREKKI DSVRKFEEQR KKTCDGDREI KSNDSIAQNA LLKQRKVSEE
YWEDDDPEKE KENFVQEELY VHDKLCIVDD RIIICGSANI NDRSQLGDRD SELAIVLEDT
DMIDSTMNGK PYRAARLAAT LRRHLWREHL GLLLPQEFDS SNNPNAQPPG DCPNSNGEGP
EYEFVADPLG EELWEAWTSQ ATTNTEVYRF LFRADPDDNI KTFEEYDQFA PKKSIKQGHL
HDPFLPVSVV RENLDKIKGH LVWMPLDFLK DAEMSEPGLS VNQVTVSIYT
//