ID A8WMU3_CAEBR Unreviewed; 294 AA.
AC A8WMU3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Protein CBG00329 {ECO:0000313|EMBL:CAP21798.2};
GN ORFNames=CBG00329 {ECO:0000313|EMBL:CAP21798.2,
GN ECO:0000313|WormBase:CBG00329}, CBG_00329
GN {ECO:0000313|EMBL:CAP21798.2};
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:CAP21798.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP21798.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP21798.2,
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 DDI1 family.
CC {ECO:0000256|ARBA:ARBA00009136}.
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DR EMBL; HE600968; CAP21798.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WMU3; -.
DR STRING; 6238.A8WMU3; -.
DR WormBase; CBG00329; CBP05742; WBGene00023735; -.
DR eggNOG; KOG0012; Eukaryota.
DR HOGENOM; CLU_1020221_0_0_1; -.
DR InParanoid; A8WMU3; -.
DR OMA; TEIWSAK; -.
DR OrthoDB; 1332686at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05479; RP_DDI; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR12917; ASPARTYL PROTEASE DDI-RELATED; 1.
DR PANTHER; PTHR12917:SF1; AT13091P; 1.
DR Pfam; PF09668; Asp_protease; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..294
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002731741"
FT DOMAIN 186..226
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
SQ SEQUENCE 294 AA; 33432 MW; 427F88B2DE34690A CRC64;
MRILTFLFGA LVFANLYAWT FAAQEMDHSD WKRDPPSRVL SLLTAQCIKH EESCQSFVQM
NIIKIEDLIK LLATFKSAPE AELIDRISPE DRMETIIFNN FNRYSIDFLV LCGDTEIWSA
KESNGAHFDL SPYCDQNLMI YHRECEKYKV LKELRKAYKN ATDKLSQFFV KSPMPHINLK
IEGFQITALV DTGAQLSIIT RSVAEKCGIF QKLDSRFQVD AQGIGGVSQA LGKILDVELE
FSGYFLPVVL AVFEECSLGC VLIIGVDILT AYCANVDFKN KCVRFNEELE VEMV
//
