ID A0A2G5VKV6_9PELO Unreviewed; 376 AA.
AC A0A2G5VKV6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=SMP-30/Gluconolactonase/LRE-like region domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Cni-mec-6 {ECO:0000313|EMBL:PIC52413.1};
GN Synonyms=Cnig_chr_I.g2529 {ECO:0000313|EMBL:PIC52413.1};
GN ORFNames=B9Z55_002529 {ECO:0000313|EMBL:PIC52413.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC52413.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR602640-2};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC 2};
CC -!- SIMILARITY: Belongs to the paraoxonase family.
CC {ECO:0000256|ARBA:ARBA00008595}.
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:PIC52413.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDUG01000001; PIC52413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5VKV6; -.
DR STRING; 1611254.A0A2G5VKV6; -.
DR Proteomes; UP000230233; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004064; F:arylesterase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR002640; Arylesterase.
DR PANTHER; PTHR11799:SF28; MECHANOSENSORY ABNORMALITY PROTEIN 6; 1.
DR PANTHER; PTHR11799; PARAOXONASE; 1.
DR Pfam; PF01731; Arylesterase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR602640-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
SQ SEQUENCE 376 AA; 42424 MW; BBEAD41DBBF3B98C CRC64;
MGNNATFLHF MHRFVFWILF AMVTCFVLRI LIVLDLNKRI YNHTPGPCRV LTEKYKGTAG
LTFVESQKRV YVTLGYGKSH NMTTKTGIAF YNTNRTDGRS QQEMHDLIEM TINWNGYEHQ
NLFIPTGIDS FASSNGRILL YVINAHPDHE CIHFFQVDNQ KLNHRKSVCD SSFTSLQDLT
VVGPDRIFFT NMAAFGRGWA QVVEFALQTG QGVVYYYDGS KLSIAAPTVN APTGIGYDSK
RRILYVGSLI RESLLAYKVA KDMSLDSMYE MMLLTSPIGL FVESKSGDVW IAAHPVLHES
AWHYSNPERK NVHSSSQVLR IRIQEEGNSW VTTEPYANDG ATISASSAIV YTDDQMIIGS
SFGRLLHCDL TNSHIT
//
