ID V5FIC8_BYSSN Unreviewed; 865 AA.
AC V5FIC8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=PVAR5_6191 {ECO:0000313|EMBL:GAD97514.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD97514.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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:GAD97514.1}.
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DR EMBL; BAUL01000202; GAD97514.1; -; Genomic_DNA.
DR AlphaFoldDB; V5FIC8; -.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_000690_2_2_1; -.
DR InParanoid; V5FIC8; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000018001; 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; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF186; PHOSPHOLIPASE D; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 3.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 1.
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:UP000018001}.
FT DOMAIN 214..241
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 29..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 97715 MW; 2B43D3C5C916B5DA CRC64;
MPELYEPEYQ AEPQQEGLMS RIIDSVGETV IGSDDKKEED ASPEDEVAAS NTSHRYDSFA
PERGSNQVKW HVDGCNYFHA VSIALEQAKE TIWILDWWLS PELYLRRPPA KNEQYRVDRM
LQAAAERGVH VNIIVYKEVT QALTLSSEHT KQHLESLHPN IRVFRHPDHV PDEKEVADSV
LSKLKGLVLD TAKLSNMSND EVKQIYGSKE ETVLYWAHHE KLCLIDGKIA FMGGLDMCFG
RWDTNQHGIA DFHPANLDEI VYPGQDYNNA RVLDFQDVAH WEQNQLDRKA TPRMGWSDIS
VSLRGPVVED LRRHFVERWN FIWKTKYNAD HEDNRYSRLT LHREPASGGL EGNTSNEQGW
SLSGFGHALH DQFHHYIGGG HHSSSGAGSF KCQIVRSCSQ WSHGVPTEHS IANAYAAIIR
DSKHFVYIEN QFFITATGDD QKPVENTIGA AIVERILRAA RAGEKYKVIV VIPSVPAFAG
DLMDDSALGT RAIMEFQYNS INRGGNSIME LISKEGYDPV DYIRFFNLRN YDRINAGGAA
SRIERESGVD YEDARKQQDI ATAGYGGYGP GASNDDVETS GSYEQYQETA QQSSAGSRWD
SVSECYMLGG EDIRNVPWDN SGDMDEIDAF VSEELYVLIA DDRVVICGSA NLNDRSQLGT
HDSEIAIIIE DSTPYETTMD GRPWTASRFA TSLRRQLFRK HLGLLRAQDC TRLNANAEPV
GVPNDDDLDS EESQLVADPL SDEFQDLWIS RAHTNTEVYR EVFHPVPDDT VRNWDTYKEF
FEKYFHKAVE NADGEEGLLE KPAKYQWAHV VRENFPEGPE GARQVKELLS KVKGTLVEMP
LVFLVEEDVA KTGLSLNAVT EPIYT
//
