ID A0A2T6ZUR4_TUBBO Unreviewed; 853 AA.
AC A0A2T6ZUR4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=B9Z19DRAFT_1100937 {ECO:0000313|EMBL:PUU79232.1};
OS Tuber borchii (White truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42251 {ECO:0000313|EMBL:PUU79232.1, ECO:0000313|Proteomes:UP000244722};
RN [1] {ECO:0000313|EMBL:PUU79232.1, ECO:0000313|Proteomes:UP000244722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tbo3840 {ECO:0000313|EMBL:PUU79232.1,
RC ECO:0000313|Proteomes:UP000244722};
RG DOE Joint Genome Institute;
RA Murat C., Kuo A., Barry K.W., Clum A., Dockter R.B., Fauchery L., Iotti M.,
RA Kohler A., Labutti K., Lindquist E.A., Lipzen A., Ohm R.A., Wang M.,
RA Grigoriev I.V., Zambonelli A., Martin F.M.;
RT "Draft genome sequence of Tuber borchii Vittad., a whitish edible
RT truffle.";
RL Submitted (APR-2017) 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|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
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:PUU79232.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NESQ01000097; PUU79232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6ZUR4; -.
DR STRING; 42251.A0A2T6ZUR4; -.
DR Proteomes; UP000244722; Unassembled WGS sequence.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Reference proteome {ECO:0000313|Proteomes:UP000244722}.
FT DOMAIN 212..239
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 637..664
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 853 AA; 97262 MW; 0DF0049783D4848E CRC64;
MSAQTYLRDY PENVTESGPK THKLQQRVRS TRIFGLIVQI VHFKNRLGKY KNLINRNHRH
DELHEKLVDE KREQIKSKNR FNSFAEPRVG NGVKWYIDGR DYFWAVSMAL DNARETIYIA
DWWLSPELFL RRPPYYNMEW RLDKVLKRRA EAGVKIYVIV YKEVTQALTC NSAHTKSVLE
NLCPRGSPGH GNIVTMRHPD HSPFAHAADM TFYWAHHEKF IVVDSRVAFA GGLDLCFGRW
DLKQHPLADI HPAGVKNEIW PGQDFNNNRV MDFHDVQDWK QNQLNKKDYG RMPWHDVSLG
FVGPAVLDLA EHFVSRWNFI KRDKYKRHSS YPWIQLTYSP GDILGVSHPR FPVGGYVKHP
LHPYSESADH SPKGSCQVQL VRSAADWSHG ILKEDSIANA YKKLISEAQH YVYIENQFFI
TATGEDQAPI RNTIGRAIVD AVVRAAKEKR KFRVIVVIPS IPGFPGDLRD NAAIGTRAII
DYQYKSICRG EHSIMQMIEQ QGIDPKQYIF FFNLRIYDRL PKSKALEEAE KKAGVSYAHL
QRAHAAEVMG EGGVTQGRGW DDTSAEGPID SGGGAGCRRE LGKKKDGFEK LKGEAQRKGL
LNQPDSIAKD AMLGGDTVTS ELSSEEEGSE KENFINEELY VHAKVLIIDD RVALVGSANI
NDRSQLGDHD SEVAVIVEDQ DTIATRMNGE EYSAARFATT LRRALWREHL GLLPPQSLDA
KEDPNAHPPG HGGNEWDENS KEDEFVIDPL NEKLWQMWTG NASHNTEVYR ELFHCDPDET
IRTWKDYDQF LPRSKGVKTG HLAVGHDVTV EQVREKLGSI RGHLVWMPLC FLEEEELAEK
GLQVNALTES IYT
//
