ID E3LZN8_CAERE Unreviewed; 555 AA.
AC E3LZN8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=CRE_05715 {ECO:0000313|EMBL:EFO87552.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; DS268420; EFO87552.1; -; Genomic_DNA.
DR RefSeq; XP_003110259.1; XM_003110211.1.
DR AlphaFoldDB; E3LZN8; -.
DR STRING; 31234.E3LZN8; -.
DR EnsemblMetazoa; CRE05715.1; CRE05715.1; WBGene00053046.
DR GeneID; 9824135; -.
DR KEGG; crq:GCK72_018801; -.
DR CTD; 9824135; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; E3LZN8; -.
DR OMA; FKANRFR; -.
DR OrthoDB; 2874784at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF45; ASPARTIC PROTEASE 6; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 110..423
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 316
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 141..145
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 555 AA; 61851 MW; 2245428BE6A6A119 CRC64;
MCSPKRLMMQ NSKRRIKDGV RKWEINHFSF SIMRSVWLQS FVVGLCCLVV LSSGAFHQSR
IAWRPSKRME MMRTGEWATY KKYLDRQRKL SPWQLQSLPQ NVNDFADFEY LGNITIGTPP
QPFLVVLDTG SANLWIPGLS CKTNCDSKRK FDSSKSSTFV KNGQSWTIQY GSGAAAGIIG
QDTVKIGATG EDQLTIPKTT FGIANQISAD FKSDATDGIF GLAFTTLAVD GVVPPLINAI
KQGLLDQPLF SVFLEHRGTL TNVGGGVFTY GAVDTTNCGP VIGYQPLSSA TYFQFKANRF
RLGKYLNAKI VDVISDTGTS FLGGPSVVID EMAKQAGATY DILGEAYIID CDATPGPLGV
TIGGHDYQIE HYNYISNVGD GTCVLTLFPM DFGGFGPTWI LGDPFIRQYC NIYDLGNLRM
GFAPSLQPAP TKAFIFYFCF KMKNALLILL FLFLEPFNSQ NHDGGRLMMM DKHMRRLNLT
DIHFTDPNGV VRVDTVMNKY NSSREELIRI LKDNVNETAY NMVKNKPQRV DEWNKKAVDL
PHPIHSSQYN KTAKG
//
