ID V2YKG6_MONRO Unreviewed; 1433 AA.
AC V2YKG6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Lysophospholipase NTE1 {ECO:0000256|ARBA:ARBA00018317, ECO:0000256|RuleBase:RU362043};
DE EC=3.1.1.5 {ECO:0000256|ARBA:ARBA00013274, ECO:0000256|RuleBase:RU362043};
DE AltName: Full=Intracellular phospholipase B {ECO:0000256|RuleBase:RU362043};
GN ORFNames=Moror_4820 {ECO:0000313|EMBL:ESK92169.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK92169.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK92169.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK92169.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- FUNCTION: Intracellular phospholipase B that catalyzes the double
CC deacylation of phosphatidylcholine (PC) to glycerophosphocholine
CC (GroPCho). Plays an important role in membrane lipid homeostasis.
CC {ECO:0000256|RuleBase:RU362043}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000256|RuleBase:RU362043};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU362043}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636,
CC ECO:0000256|RuleBase:RU362043}.
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:ESK92169.1}.
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DR EMBL; AWSO01000300; ESK92169.1; -; Genomic_DNA.
DR RefSeq; XP_007848558.1; XM_007850367.1.
DR STRING; 1381753.V2YKG6; -.
DR KEGG; mrr:Moror_4820; -.
DR HOGENOM; CLU_000960_1_1_1; -.
DR OrthoDB; 5303733at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR001423; LysoPLipase_patatin_CS.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 2.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU362043};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362043};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU362043};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU362043};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362043};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362043};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362043}.
FT TRANSMEM 24..51
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362043"
FT DOMAIN 634..747
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 760..880
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1130..1294
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 258..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1433 AA; 158151 MW; 8161D3D0090D4371 CRC64;
MDAGQGLGDN ATIDRHPLVS FLSAFFWVLL WILSWAKALV AFATITVPRL IYSILSYSMT
LTLNFWSFAI IFMLSAVALN YWIRFRYLND YTQLKEPPLM KPDAKELHPD VNTDPPPPFH
NYLDDFLQAV RVFGFLEKPV FHELARHLQT RRLIAGDSIS LGQDKSFYCV IDGTVQVYAQ
TGHPADDRHG VWDNEDMNGF QLLNEVGSGG TLSSLFTILS LFTEDVKISW QDEHSEESDF
ESALDSVSQI SDRGRLNSDI PKLDLEQSAS NGRRRRSSTS STASTVHATG LKSPNARPIS
RSGYASPLYE EDHTQAFVVT ESPYPQSTYR DQSHHGLVAR ASEDTTLAVI PAEAFRRLTK
KYPKATGHIV QVILTRFSRV TFNAAHKYLG LTSEVLRTEK AINEIANHPL PPSFYEGGGL
QYLRQRFDST DKSDENDDTD YFSSRVRPSA SVSSTSRCSN SKDVLGPLPS SSRQPHSSSS
TSSFSTPFKH HTSRLSAQAG DLLTSTHTAE EGINRGPISR SFSILNTPRI RTAPMDGRRK
ANLPVHDEFD LREEVMSCIA KSIGLLQPPL SGSDSVEASP AFRAADDRRS SSGGPLLFNS
SFSSLSLLDT GDDNSSATGG SSTIASADGY MSGLDNEVEM LYFPAGSMLA RAGEHNTGLF
YVIEGFLDIL LPEAESGRIS KSSAASERAQ NVKKPQRDGR KHLFTVKPGG IAGYLASLCH
TPSYVDIIAK TDTYVGFLPS HALERILEKS PIVLLTLAKR LISLLSPLVL HIDASLDWMQ
VNAGQVLWRP NDTSDSFYIV INGRLRVIAD KDDGGVKIVG EYGQGDTVGE LDVITSSPRR
NTAHAIRDTE LIRMPQTLFN AISARNPQTT AQLLRRIASR VRDEIDASSH AQSRNSPTTE
QGYNNNLKTV AILPVTRLVP VEAFAKKLQA ALEGIGASTA YLTQASMSSH LGRHAFTRMG
KLKAAGWLAD QEQRYRTVLY VVDSAVNGNW TQTCIRQADC VMVVGMGDDP SLGEYERLLL
SMKTTARKEL ILLHPDRSVV PGSTREWLKN RPWIHQHIHV ELPGLAVPIS KFTMPKDPDP
MEKLKSLKDK VQNEIQKYRG GSHDPRPQRM PHVNDFSRLA RRICGKSIGL VLGGGGARGI
AHLGLIRALE EYGIPIDHIG GTSIGSFIGG LYAREGDILS SAGRTKQFSG RMGNIWRILS
DVTYPIVAYT TGHEFNRAIY KAFYDLHIED MWLPFYCNTT NINTSRMEIH DTGYAWRFVR
ASMTLIGLLP PLCHNGNMLV DGGYVDNLPV SAMFSMGASA VFACDVGSID DNSPRNFGDS
VSGWWLFINR WNPFSNARNI PAITEIQSRL AYVSSVKTLE EAKVAPGCLY IQMPVQEYGT
LQFGKFEELQ KVGYNAAIKI LDKWSDEGVL PSAVIDGSPS VSTKGRAARR NSI
//
