ID   A8X9D3_CAEBR            Unreviewed;      1051 AA.
AC   A8X9D3;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Protein CBG09322 {ECO:0000313|EMBL:CAP29245.2};
GN   ORFNames=CBG09322 {ECO:0000313|EMBL:CAP29245.2,
GN   ECO:0000313|WormBase:CBG09322a}, CBG_09322
GN   {ECO:0000313|EMBL:CAP29245.2};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP29245.2, ECO:0000313|Proteomes:UP000008549};
RN   [1] {ECO:0000313|EMBL:CAP29245.2, ECO:0000313|Proteomes:UP000008549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000313|EMBL:CAP29245.2,
RC   ECO:0000313|Proteomes:UP000008549};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; HE600954; CAP29245.2; -; Genomic_DNA.
DR   RefSeq; XP_002636865.1; XM_002636819.1.
DR   AlphaFoldDB; A8X9D3; -.
DR   STRING; 6238.A8X9D3; -.
DR   MEROPS; M16.A09; -.
DR   EnsemblMetazoa; CBG09322a.1; CBG09322a.1; WBGene00030925.
DR   GeneID; 8578860; -.
DR   WormBase; CBG09322a; CBP30039; WBGene00030925; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_1_1; -.
DR   InParanoid; A8X9D3; -.
DR   OMA; VGHQWLE; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000008549; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          93..230
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          257..434
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          442..725
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          729..910
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1030..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1051 AA;  120594 MW;  BF4E1B8A2C01725F CRC64;
     MYFLSKLSRC VPSPAISQIG KRSFSNNNYS HVLRRPPSSA IRLRLVRNIS NSNPLPKMTE
     AGKNIVLKRH DLIVKGAQDV REYRGLELTN GLRILLVSDP STDKSAAALD VKVGHLMDPW
     ELPGLAHFCE HMLFLGTAKY PSENEYSKFL SAHAGNSNAY TATDHTNYHF DVKPDQLSGA
     LDRFVQFFLS PQFTESATER EVCAVDSEHS NNLNNDSWRF LQVDRSRSKP GHDYGKFGTG
     NKQTLLEDAR KKGIEPRDAL LQFHKKWYSS DIMSCCIIGK ESLDVLESYL GTYEFDAIEN
     KKVTRQVWKD FPYGPEQLGK KVEVVPIKDT RMLSISFPFP DLNTEYNSQP GHYISHLIGH
     EGPGSLLSEL KRRGWVSSLQ SDSHTQASGF GVYMVTMDLS TDGLDHVDEI IQLMFNYIGM
     LQTAGPKQWI HEELAELSAV KFRFKDKEQP MSMAINVASS LQYIPFEDIL SSKYLLTKYD
     PERIKQLLDT LKPENMYVRV VSQTFKGQEG NTTEPVYGTE FKMADIDKET MQKYENALKT
     SHHALHLPEK NEYIATKFDQ KPRETIKNEH PRLIVDDSWS RVWFKQDDEY NMPKQETKFG
     LTSPVVSQDP RSSLLSSLWL WCLSDTLAEE TYNADLAGLK CQLESSPFGV QMRVYGYDEK
     QSLFTKHLTK RMANFKIDKT RFDVLFESLK RALTNHAFSQ PYSLSQHYNQ LIVLDKVWSK
     EQLLAVCENV TLEDVQNFSK EMFAAFHLEL LVHGNSTEKE AIELSKELVD ILKGVSPNSR
     PLYRNEHCPR REMQLNNGDE YVYRHLQKTH DVGCVEVSYQ VGVQNTYDNA LVGLIDQLIR
     EPAFNTLRTN EALGYIVWTG SRLNCGTVSL NVIVQGPKSV DHVLERIEVF LETVRKEIDE
     MPQEEFDNQV SGMIARLEEK PKTLSGRFRR FWNEIECRQY DFAHREEEVK VLKSIKKEDV
     LALYDKKIRK DAPERRKLAV FVHGKGEDRE KVDGIVKKNA EAGKKEKEVE YVDQLRQFLP
     LYGRPIPAIN LKPIGVDPTE HKQPSTPKAK Y
//