ID N1UHH5_9LEPT Unreviewed; 806 AA.
AC N1UHH5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Phospholipase, patatin family {ECO:0000313|EMBL:EMY15455.1};
GN ORFNames=LEP1GSC043_3759 {ECO:0000313|EMBL:EMY15455.1};
OS Leptospira weilii str. Ecochallenge.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049986 {ECO:0000313|EMBL:EMY15455.1, ECO:0000313|Proteomes:UP000012249};
RN [1] {ECO:0000313|EMBL:EMY15455.1, ECO:0000313|Proteomes:UP000012249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ecochallenge {ECO:0000313|EMBL:EMY15455.1,
RC ECO:0000313|Proteomes:UP000012249};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Haake D.A., Matsunaga J., Vinetz J.M.,
RA Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (FEB-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:EMY15455.1}.
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DR EMBL; AHMI02000091; EMY15455.1; -; Genomic_DNA.
DR AlphaFoldDB; N1UHH5; -.
DR Proteomes; UP000012249; 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; 1.
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 203..303
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 517..677
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
SQ SEQUENCE 806 AA; 91646 MW; CD2D729421F910F2 CRC64;
MIGPVRSFIV GKADSIVFVY RIRIFVPWKG SFTAQNFTEK RLLEYGFSPF QKKILKQLRY
FRSKTSSAFP GWKDSKEEEI VTKRLNLTQW DANIPSPQTV SGSLCLVLSG KIEETLLDAE
EKDLILRELF TGDYFLFQPD KILHSGISEI LYILPDDLSR IVSKLPGWKK WIEDLNKENH
LFHVSKLRPS KKELMSFLSS VELLFHLSKV TLSNLESRME WLVIPGGEVL LKQGDVGDSM
YILVSGRLSW TVRSKNEEIL AQGELGKGDI IGEMSLLSGD KRSATVVALR TSQVVRISRE
DFRMSFANSP EALFQITGTI VHRLNTERNQ NYRKANSVRT VSVFPLNLTG SPEDFFHSLQ
NGLKNFGKSI LVNYNVFTKM IGLRESDKNS EKTNVYRIGD LVNWFYDLEK NYDKLIFKTD
THNSGWRETC FRQSDRILVL IDPNKPIVLD YGKVNSMFPE EIQKELVFLI DSAFTDWKKI
ESILQKFPSI SHSIVRRDVN ADFGRLSRRL TGKSIGVALS GGGAKGFAHL GLLKCFEEND
IPVDMISGTS AGAIMGGLFA MGLGSSDILP LIRNFWLDRN ILGDFTFPFV SLVRGKRYSN
AIHEFFKDRN IETLPIPFYA IACNLTRAER KVFDRGLLWK AVRSSTSIPG IFPPFSENGE
LYVDGGLLDN LPGSILKERG AGILISVDLG GGGQIDKDWM YHNLLGPQYL GEAPSFFNLL
FHHLKRKSLK TKYTGFAEIM MRSLMLSSKN NQNRTRDSSD LYIELPVGGY STFDWDQFQK
LYEIGYEAGR KNVHIWKNEI KKKLNS
//