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Database: UniProt
Entry: B6QJU1_TALMQ
LinkDB: B6QJU1_TALMQ
Original site: B6QJU1_TALMQ 
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
//
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