ID B8MNP6_TALSN Unreviewed; 1832 AA.
AC B8MNP6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=TSTA_103560 {ECO:0000313|EMBL:EED14135.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED14135.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
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).
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; EQ962658; EED14135.1; -; Genomic_DNA.
DR RefSeq; XP_002486373.1; XM_002486328.1.
DR STRING; 441959.B8MNP6; -.
DR GeneID; 8103059; -.
DR VEuPathDB; FungiDB:TSTA_103560; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_0_1_1; -.
DR InParanoid; B8MNP6; -.
DR OMA; DSLWTKH; -.
DR OrthoDB; 335467at2759; -.
DR PhylomeDB; B8MNP6; -.
DR Proteomes; UP000001745; 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; cd01254; PH_PLD; 1.
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.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EED14135.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745}.
FT DOMAIN 492..692
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 956..983
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1262..1289
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1482..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1640..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
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 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1489..1508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1640..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1723..1767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1832 AA; 207700 MW; EE35C01815C4207B CRC64;
MADLNDSSQL GSVSHANNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNSNSNSPGR TPKKFLRQHR PASPGKDSSS SPFIPPTNDF GEHSDVFTHN KPAKYPSSSR
AGTIVDQPIQ EEIELDGKDG EVHDGTGIPP EGQNNPASTD HELAERRQSL DFAAGQEDGN
NDISAKDRKH SLFNKLRALA ATPSFPSHSR SASVATAPIG TGIDNGPINH DLLTPGSERG
EYPFPEAASD AGSEGDADAE ESAGEQRLRL RRRRKTQRPR PTKELKEPHD SAPATPRPNA
TTPGIFSFNS FHPSEMTRPS LFLRRANTDM SGHLRDPVSE DEGRNRLNMD SQWRKRSNAW
LSSARGLTYS GRTDTQNTNN TNNSANTDER RPMNFRRLTA FAGPSGDQEG IREVWRRHKA
ERGSSLSAQK WRQIKAGLKM IGQRRKADNT IDHAKSAELL AELTSGIPAA LILASMFQRD
EHGSKRIPIL LEQLKVQITD SRFDSHSGDR HLVFRIELEY GSGMTRMKWI IHRTLRDFAN
LHLKYKLQIG TQKYIQLKTQ ESGHFLPRFP RSAFPYLRGV RGLDSEREEE DDDGGGYETG
AEATSGNEAR RKMKKRRSSF AITRRRSSTG VTLENDATAG EGAATATSER RSYSERQRKK
LENYLQKMIR FLIFRPDSNR LCKFLELSAL GVRLAAEGSY HGKEGFLIIQ SAKGLDFRKA
LRPALLKNRH SPKWFLVRHS YVVCVDSPEE MNIYDVFLVD PYFKLQSQKL RLRDQKAKEI
ARTAKDSAAH PQHHTLRLEN SERKLRLLAR NERQLHQFED SIRFMVENTP WSKPNRFDSF
APVRKNCFAQ WLVDGRDHMW LVSRAINQAK DVIYIHDWWL SPELYMRRPA AISQKWRLDR
LLQRKAQEGV KVFVIMYRNI NSAIPIDSEY SKFSLLDLHP NIFVQRSPNQ FRQNTFFWAH
HEKLCIVDHT LAFVGGIDLC FGRWDTPQHL LTDDKPTGFE SPDGPKDTDH CQLWPGKDYS
NPRVQDFYDL DKPYEEMYDR NVIPRMPWHD ISMHVVGQPA RDLTRHFVQR WNYILRQRKP
TRPTPFLLPP PDFNPADLEA LGLDGTCEVQ ILRSASSWSL GTPDVTEHSI MNAYVKLIEQ
SEHFVYIENQ FFISTCEIDG RKIENLIGDA LVERIIRAAH NKENWRAVVV IPLMPGFQNT
VDSEGGTSVR LIMQCQYRSI CRGETSIFGR LRAEGIEPED YIQFFSLRTW GKIGPNKQLV
TEQLYIHAKC MIVDDRAAII GSANINERSM LGSRDSECAA IVRDTDMIWS TMDSKPYLVG
RFPHTLRMRL MREHLGIDVD EILDHDLSAE ATGRTRRDSE VDAASLDSQA NGGVHNGERE
KQDEREMIER RHRIQDEFLV RSEDMHSFNH DVDWEQGNNP NLKSSRKLTA DPRVTENAEH
RNEVAGNGAD HMKISLEAGV GFGRDSAILQ DTTEVLVNDV AAEGKGTLSN PRKTHKPSEQ
EQLRKDSAKE AVLPPTPSQI EPALDVPETP FSRLQPLPQT NDADIGGPML PHKEPNGVGG
HPLASSIRQP FVDEHCMRDP VNETFYFDTW HKIAENNTKI YRTVFRCMPD SEVKSWKEYK
EYTMYGEKFV EAQNQQIEAR KSQSTGAVNN NQSAVSMETT VQPEAEKTEK TEGVTSNGES
QTSVVDEKAA LKETDISNDT IQQQQTRTTD IAEAENVPTP TEEINKEART PSGSTPGPAP
GSQPASVGYS GALNMNMTQP GSTTRRRRTA TRGSRREFHA SDGVIDLRHA EELLGMTQGH
LIAWPYDWLE KEEQGGNWLY TLDQISPIEI YN
//
