ID A0A1V6SRZ3_9EURO Unreviewed; 1798 AA.
AC A0A1V6SRZ3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=PENFLA_c026G07929 {ECO:0000313|EMBL:OQE16817.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE16817.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(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|ARBA:ARBA00000798};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE16817.1}.
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DR EMBL; MLQL01000026; OQE16817.1; -; Genomic_DNA.
DR STRING; 254877.A0A1V6SRZ3; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000191342; 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 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};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Reference proteome {ECO:0000313|Proteomes:UP000191342}.
FT DOMAIN 439..645
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 909..936
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1215..1242
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1311..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1428..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..1664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1798 AA; 203586 MW; 1CC5791191FA3303 CRC64;
MSASSIHQDV ETGSLKVDTK KQEPLLASNK SKLASPLPSS TESNKAASAK HTQPTDDRET
GGILGDKENA RPSSLKQSSP RGRSSLSTRP PNRSAEDPQP WSRHQRQSSN PGMSPPSRAQ
SVQFRDTDTE APDASHSRSQ SRPASEHGDD DDQGPKGKQS LFGKLKLLAT APNFTSHSRS
PSGASTDFRP APGDIATPGS ERGEFRFPEP LQEEGSEIDA DAEESGGEQR DTREKRKTQR
RRKQWEEEAG SNTAPTTPKT TRRPSFHFSS SFAPFENYRT NLFPRRASTT DFTPQQREGV
SEDEGRERLS RRMRSRPWAN TRVSSYTDGP DANPDEQRPS NLRRLTGFTG PSGNDESLTA
GWRRHRTERG TSASAQRWKQ IKAGLKLIGQ RRRPDNAVDN KKSAELLAEL ASAVPAALIL
ASAFQRDEHG SKRIPILLEQ LKVRVTDSRI DSHSGDRHLV FRIEMEYGSG MTRMKWIIFR
TLRDFANLHL KYKLHLGTQK YIQLRTSENS PSLPRFPRSA FPYMRGVRGL ESEFEDEDEE
GGYETGAEGM SGTERPPTKK KQNQQSHQRR VSGPLARRKS SITNQEGDSA AGPSSTHEGG
ARKETYPGKQ RKKLELYLQK MIRFLIFRAD SNRLCKFLEL SALGVRLAAE GSYHGKEGFL
IIQSSKGLDF RKALTPSLVK NRHSPKWFLV RHSYVVCVDS PEEMNIYDVF LVDSHFKIQT
PKLSLRKQNP KDLAKSAKQS ARHPQHHTLR LENSERKLKL LARNERQLQQ FEDSIRFMVA
NTPWLRPNRF DSFAPVRQNC FAQWLVDARD HMWVVSRAIN QAKDVIYIHD WWLSPELYMR
RPAAISQKWR LDRLLQQKAR EGVKVFVIMY RNINSAIPID SEYSKFSLLD LHPNIFVQRS
PNQFRQNTFF WAHHEKLCLI DHTIAFVGGI DLCFGRWDTP QHQLTDDKPT GFETTDGPKD
ADHCQLWPGK DYSNPRIQDF YDLDKPYEEM YDRNVVPRMP WHDISMHVVG QPARDLTRHF
VQRWNYILRQ RKPTRPTPFL LPPPDFNPAD LEALGLDGTC EVQILRSSSM WSTGTPDVVE
HSIMNAYVKL IEESEHFVYI ENQFFISTCE IEGRKIENLI GDALVERIVR AAKNEEAWRA
VIVIPLMPGF QNTVDSEGGT SVRLIMQCQY RSICRGETSI FGRLRALGIE PEDYIQFYSL
RTWGKIGPHK ALVTEQLYIH AKCMIVDDRA AIIGSANINE RSMLGSRDSE VASVVRDTDM
MMSSMNGKPY LVGRFPHTLR MRLMREHLGI DVDELMEHDF ATEEELRKIQ VAEGSDHPVD
NRERRNSASS AIERQDEREM VERRHRVQDE FLSRSEDMYS FNHDVDWEQG GNPNLKSNRK
LTADPRVTEN PDHRKDVEGD GPDHLTAAAQ AGLTVGRDSE METNGREALL SPIAPEGKGT
IERPRSSQQK PPGTPSTRKD RRPGSSSETN ASSEINGNVP SQGHGITGSS TRESETGGTS
LNTPREDNET LKHHHPSVPE VKRIFIDNDC MRDPIIDGFY LDTWQAVAEK NTKIYRSVFR
CMPDSEVKNW KEYKEYATYG ERFAEVQSQQ GNKSAQPQPK QNGPPPAGAT VGSPMSIASQ
MSFITPRAEG PQADPKSPQT IDEKVGAGNE TGRPQSEQLA KQETLSSIDE KAALKTVSDP
NLLVNVSNGT SDENGVATGE DMEKSRTTPG HVDYSEAVNL NLNSSSQSRR RRRRATTIGS
KRDPHGADEY LDKGRAEDLL NNTQGHLILW PYDWLEKEEQ GGNWLYALDQ ISPLEIYN
//
