ID A0A0M3IKG8_ASCLU Unreviewed; 1019 AA.
AC A0A0M3IKG8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cyclic nucleotide-binding domain-containing protein {ECO:0000313|WBParaSite:ALUE_0001923701-mRNA-1};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0001923701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0001923701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000256|ARBA:ARBA00006636}.
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DR WBParaSite; ALUE_0001923701-mRNA-1; ALUE_0001923701-mRNA-1; ALUE_0001923701.
DR Proteomes; UP000036681; Unplaced.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:InterPro.
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; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
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; 1.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..43
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 49..145
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 452..616
FT /note="PNPLA"
FT /evidence="ECO:0000259|PROSITE:PS51635"
FT REGION 782..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 114617 MW; 3E3CC023F94A2CE8 CRC64;
MVHPRELIGG LQLLTSEPSF HTVRTHTAAT IAILNKEDFA ELLEIRPEVI LPVAESVIRR
LSPFLRSVDF AIDWVLLDSG QAVYRSGDVS DSLFVVLSGR LRSVEKKMLV EEFGRGDMIG
MVEVLQRVPR STTVLAIRFS QLARIPEGLL NYIKMKFPQV GFRLVHLLGH YYSSSNRRTM
VANTGFTDHL SGPIGDPRSH IKNLHTVAVI AASANVPLVP FTCELYNALN ASLRVLRLSS
KKVAEHLDPS VLEKPESIXL NASLRVLRLS SKKVAEHLDP SVLEKQADFR LMHWLNVQED
TFPLVIYECD NMATNWTRRC LRQADAILLV ANGQQKPMKQ SFVRLFGHLF LRMMEEFLSI
NPDWVRTNKE LILLWDEDTV APQGTIEWLK GSWFSGHHHI RCPKRMTQWN PSTVTEREVI
DYYEENVFWD KVDNNSDFAR LARILTGNAV GVVLGGGGAR GASHVGILRA IREHGIPIDF
IGGTSMGAMI AGLYAESDMD VEQRAKEWFM LMNSLWPKIW DLTYAHSAMF TGAGFNKTVQ
AAFSDIAIED LWLSYFCITT DISDSEMRVH RSGPLWAYCR ASMSLAGYLP PLCDPVDGHL
LLDGGYVNNL PADVMRSLGA RVVIAVDVGA ASENNLLNYG DSLNGFWVLF KKLNPFGEPV
KVLNMEEIQS RLAYVSCVRQ LEQVKKAPYC HYLRPPITQY ETLDFAKFDE IYEVGYKYGS
EKFDELVKKS DLLKNIIGPE VLRSLKLQQS RRELSKLANY DRSLASSFTN LAAQVSKIPK
VASKDSSNSG NSSDDENNAA EGWWPRSGQH SPDDLRASYV MDDEVEGYVS EPCSGYRYRA
HRSLYVDDDQ SSTEEEDVGI RATVPXQMIS VLPIGYRYRT HRSLYVDDDQ SSTEEEDVGI
RATVPIVVSG MSIALKRRQT CAEIPAVTEQ EALTMELRIP QRRRRTLTDF TDELHRMNDI
LHAGGDFVIE TSNAFTYNTT SVKTTRSKAS IIDVGNFLFH LVVAGIVASE ILMRMAVVT
//