ID E3NSK6_CAERE Unreviewed; 430 AA.
AC E3NSK6;
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_16551 {ECO:0000313|EMBL:EFO90315.1};
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}.
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DR EMBL; DS269985; EFO90315.1; -; Genomic_DNA.
DR RefSeq; XP_003088614.1; XM_003088566.1.
DR AlphaFoldDB; E3NSK6; -.
DR STRING; 31234.E3NSK6; -.
DR MEROPS; A01.A84; -.
DR EnsemblMetazoa; CRE16551.1; CRE16551.1; WBGene00074700.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; E3NSK6; -.
DR OMA; SIWQYMT; -.
DR OrthoDB; 2874784at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF86; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..430
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003179023"
FT DOMAIN 69..426
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 100..117
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 334..386
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 430 AA; 47752 MW; 743B4CC2F6101CD5 CRC64;
MMYFQFLILL VSIIAAYSLF QIPLEKVESL RFKLMREGKW KDYKEFKNII RSLSDAYSGS
LFDYETAGYV GKITVGTPQQ EFRVVMDTGS SNFWIPDSTC GMEWLSCGRP VSGDATCYGS
YCVPGGPNTT ASCTTQNKFD SSKSTSYVKF GNSFRFDYGV DNANGLLGYD TVRFGGMSDN
QLVVPGVTVA QAVCFPTFFE QTNIDGIMGL GFQWNAQQDI VPPFVNAYEN NIVSPVFHVY
LQKGPNGAGQ ITYGGRDTTN CKVVNEYHPM TTYAAYQFYL TLVSAGKYYS SKGWTALADT
ANSFITGPAG VIAGIADAVG AKWDTYTDTY WIPCEPKVTT QMVNFTIGGT IYPVTAENLI
VPYRKFCILY YTSDIQFSAN KTGYICMFAI LPLSNNGFGP SWVLGDPFHR EFCSLYDMGR
QRMGFSAHMN
//
