ID A0A319BUD8_9EURO Unreviewed; 1830 AA.
AC A0A319BUD8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN ORFNames=BO82DRAFT_218351 {ECO:0000313|EMBL:PYH76061.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH76061.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH76061.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH76061.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ821769; PYH76061.1; -; Genomic_DNA.
DR STRING; 1448315.A0A319BUD8; -.
DR VEuPathDB; FungiDB:BO82DRAFT_218351; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000248340; 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 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:UP000248340}.
FT DOMAIN 468..673
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 937..964
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 1243..1270
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1620..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1830 AA; 207739 MW; A69F0B6170307F7D CRC64;
MTDPLTEPSE ARSSENTQAR HYWRRPEPIS LSDGTKLSSS NPSSPSIIPK TDTQHLAEEE
EHDQLNDLPP LQDTAETLTK NKSKARAGQA SGYPEDWTTS GNAISGDNPG LLMPRRMNET
PEGSQTSGSR KPQPPLPAAS RRPSVQFTRD PPEVDPLTEL PSSRPPSVKG DDTDLGLRGK
QSLLTKLKSF AASPSFVSHS RSASGATLSD FRATNNDLAT PSSERGEFRF PNTLEEEGSD
IDADAEESAG ENRVHQPKKK KKQRRRQKDE STSQTQPNTP KATTRPSFHL PSSFAPFENY
RSNFFPRRGS TGNFIPQQRE GVSEDEGRDR LNRDTAWRRR SVWLANARGL TYGGRQLDTP
TNPDERRPSN LRRLTGLAGP SDNTEGTAPP WRRHRADRGS SLSAQKWRQI KAGLKLIGQR
RKVDNTVDHA KSAELLAELT SGVPAALILA SMFQRDEHGS KRIPILLEQL KVRVTDSKID
SHSGDRHLVF RIELEYGSGM TRMKWIIHRT LRDFANIHLK YKLHFGTQKY IQLRNTESGQ
NLPRFPRSAF PYLRGVRGLE SDMEDEEDDG GYETAAEVTS GNERGGKKQH QQLPRRPSGG
MSRRQSSATI PDGENPAGSS GPVEAGFANK KETYPERQRK KLESYLQKLI RFLIFKPDSN
RLCKFLELSA LGVRLAAEGS YHGKEGYLVI QSSKGLDFRR ALTPGMVKKR HSPKWFLVRH
SYVVCVDSPE EMNLYDVFLV DPFFKLQTQK VSLRNQKAKD FAKSATESAR HPQHHTLRLE
NSERKLRLLA RNERQLHQFE DSIRFMVNNT PWARPNRFES FAPVRQKCFA QWLVDARDHM
WVVSRAINQA KDVIYIHDWW LSPELYMRRP AAISQKWRLD RLLQRKAREG VKIFVIMYRN
INSAIPIDSE YSKFSLLDLH PNVFVQRSPN QFRQNTFFWA HHEKLCIIDH TLAFVGGIDL
CFGRWDTPQH LLTDDKPTGF ETREGPKDAD HCQLWPGKDY SNPRIQDFYD LDKPYEEMYD
RNIIPRMPWH DISMHVVGQP ARDLTRHFVQ RWNYILRQRK PTRPTPFLLP PPDFDAADLE
ALGLDGTCEV QILRSSSMWS TGTPDITEHS IMNAYVKLIE ESDHFVYIEN QFFISTCEID
GRKIENQIGD ALVERITRAA KNKEVWRAVI VIPLMPGFQN TVDSEGGTSV RLIMMCQYRS
ICRGETSIFG RLRALGIEPE DYIQFFSLRS WGKIGPQKQL VTEQLYIHAK CMVVDDRAAI
IGSANINERS MLGSRDSEVA AVVRDTDMIW SSMNGRPYLV GRFPHTLRMR LMREHLGVDV
DELMEHSLAT EEELLRIQIA EEGSKPSETN EAPDSESLML EKRDERDMIE RRHRIQDEFL
SRSEDMHSFN HDVDWEQGNN PNLKSNRKLT ADPRVTSNPE HKKDVDGLGP DRLQVAQEAG
LEKGRDSEIL EDKAEVLISP IASEGKGTLQ QPKRPSQRTV RHTNPHSTND ARQAPSGLVA
QGNEGAHVVE GVANIRHPAL APEHETETSN SGNLTASRDI GDNAKSYLYA PEVKHIFIDK
DCMRDPILDL FYLDTWSAVA EKNTKVFRSV FRCMPDSEVK SWKEYKEYTA YGDRFAEMQN
QHGAKVQQPS SQRQTGPPGT AAGFPGAAAG IKHSVASHSH GTEAHKVERK EQTTVEKPGN
CESGSVQGPN EQPHEMANHE GLSPIDEKSA LNAADGSASR RVQNGRTEDS GSSGEDVEKH
RSDRPAIDYS DALNRNATGQ SRRRRRRATT LGSKRDFHAD EVMDKQRAED LLNQVQGHLI
LWPYDWLEKE EQGGNWLYTL DQISPLEIYN
//
