ID M6W8Q0_9LEPT Unreviewed; 760 AA.
AC M6W8Q0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Phospholipase, patatin family {ECO:0000313|EMBL:EMO58123.1};
GN ORFNames=LEP1GSC161_3575 {ECO:0000313|EMBL:EMO58123.1};
OS Leptospira santarosai str. CBC1416.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193059 {ECO:0000313|EMBL:EMO58123.1, ECO:0000313|Proteomes:UP000012149};
RN [1] {ECO:0000313|EMBL:EMO58123.1, ECO:0000313|Proteomes:UP000012149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBC1416 {ECO:0000313|EMBL:EMO58123.1,
RC ECO:0000313|Proteomes:UP000012149};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Matthias M.A., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636}.
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:EMO58123.1}.
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DR EMBL; AKWE02000091; EMO58123.1; -; Genomic_DNA.
DR AlphaFoldDB; M6W8Q0; -.
DR Proteomes; UP000012149; Unassembled WGS sequence.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProt.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd07205; Pat_PNPLA6_PNPLA7_NTE1_like; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR PANTHER; PTHR14226:SF82; PATATIN-LIKE PROTEIN, PLPD; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51635; PNPLA; 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:ARBA00023098}.
FT DOMAIN 159..259
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 471..631
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 760 AA; 86373 MW; FB4176458FBC050B CRC64;
MDLSRSEKTL LKRLRYFRSK TSSAFPGWKD FKEEEVVAKR LNLTQWNSNI PSQETVPGSL
CLILSGKLEE TLPDSEEKDL ILRELFPGDY FLFQPDKILH SGISEILYIL PRDLSRIVSK
LPGWKKWIED LNKENHLFHV SKLRPSKKEL MSFLSSVELL FHLNKATLSD LESRMEWLVI
PGGKVLLEQG DVGDSMYILV SGRLSWTVRS KNEEILAQGE LGKGDIIGEM SLLSGDKRSA
TVVALRTSQV VRISREDFRM SFANSPEALF QITGTIVHRL GTERNQVYRK ANSVRTVSVF
SLNYTGSQDE FFGSLRNGLR NFGKTILVDY DIFSKRFGGF YKNSRKENAY RIGDLVNWFY
DLEKNYDKLI FKTDIHNPGW REACFRQSDR ILILIDPSGS IVPDYEEINS MLPEGIQKEL
VFWIDSGFTD WKRIESVLQK FPSISHSIVR RGVNEDFGRL SRRLTGKSIG VALSGGGAKG
FAHLGLLKCF EENDIPVDMI SGTSAGAIMG GLFAMGLGSS DILPLIRNFW LDRNILGDFT
FPFVSLVRGK RYSNAIHEFF KDRNIETLPI PFYAIACNLT KAERKVFDRG LLWKAVRSST
SIPGIFPPFS ENGELYVDGG LLDNLPGSIL KERGAGILIS VDLGGGGQID KDWMYHNLLG
PQYLGEAPSF FNLLFHHLKR KSLKTKYTGF AEIMMRSLML SSKNSQNRTR NSSDLYIELP
VGGYSTFDWD QFQKLYEIGY EAGNRNVHIW KNEIKKKLNS
//
