ID   YQA4_CAEEL              Reviewed;         856 AA.
AC   Q10040;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Putative zinc protease C28F5.4;
DE            EC=3.4.24.-;
GN   ORFNames=C28F5.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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; FO080699; CCD65926.1; -; Genomic_DNA.
DR   PIR; T15688; T15688.
DR   RefSeq; NP_495575.2; NM_063174.4.
DR   AlphaFoldDB; Q10040; -.
DR   SMR; Q10040; -.
DR   BioGRID; 47824; 4.
DR   STRING; 6239.C28F5.4; -.
DR   MEROPS; M16.A10; -.
DR   EPD; Q10040; -.
DR   PaxDb; Q10040; -.
DR   PeptideAtlas; Q10040; -.
DR   PRIDE; Q10040; -.
DR   UCSC; C28F5.4; c. elegans.
DR   WormBase; C28F5.4; CE40024; WBGene00016185; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_004639_1_1_1; -.
DR   InParanoid; Q10040; -.
DR   OMA; INQVMEH; -.
DR   OrthoDB; 148438at2759; -.
DR   PhylomeDB; Q10040; -.
DR   PRO; PR:Q10040; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00016185; Expressed in material anatomical entity and 2 other tissues.
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:UniProtKB-KW.
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   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   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; SSF63411; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..856
FT                   /note="Putative zinc protease C28F5.4"
FT                   /id="PRO_0000074430"
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
SQ   SEQUENCE   856 AA;  98262 MW;  ACD5E8BB9D43E195 CRC64;
     MTKKAKRNIV HKRFDSIVKG SQDTKKYRGL ELTNGLRVLL VSDSKTRVSA VALDVKVGHL
     MDPWELPGLA HFCEHMLFLG TAKYPSEREY FKYLAANNGD SNAYTDTDHT NYSFEVRSEK
     LYGALDRFAQ FFLDPQFTES ATEREVCAVN CEYLDKVNED FWRCLQVERS LSKPGHDYSK
     FAIGNKKTLL EDPRTKGIEP RDVLLDFYKN WYSSDIMTCC IVGKESLDVL ESYLGSFKFD
     AIKNTRKERK IWKDSPFGPD QLAKRIEIVP IQNTGQVSIK FPFPDLNGEF LSQPGDYIAH
     LIGHEGPGSL LSELKRLGWV ISLEADNHTI ASGFGVFSVT MDLSTEGLEH VDDVIQLVFN
     FIGFLKSSGP QKWIHDELAE LNAVDFRFDD VKHTMEKASI LAECLHPKIR KNFETALKTS
     HHAFNLPEKN EYIPSKFDQK PREPVKSGYP RLISEDEWIQ VWFKQDNEYN SPKQGIMFAL
     TTPLVAKKSK NVVAFKSLDT IIEETYNARL AGLECQFESS SSGVQIRVFG YDEKQSLFAK
     HLVNRMANFQ VNRLCFDISF ESLKRTLTNH AFSQPHDLSA HFIDLLVVDN IWSKEQLLAV
     CDSVTLEDVH GFAIKMLQAF HMELFVHGNS TEKDTLQLSK ELSDILKSVA PNSRPLKRDE
     HNPHRELQLI NGHEHVYRHF QKTHDVGCVE VAFQIGVQST YNNSVNKLLN ELIKNPAYTI
     LRTNEALGYN VSTESRLNDG NVYLHVIVQG PESADHVLER IEVFLESARE EIVAMPQEDF
     DYQVWAMFKE NPPTLSQCFS MFWSEIHSRQ YNFGRNKEVR GISKRITKEE VINFFDRKIR
     KGGAERRKLA LGLWKK