ID   Q5CU46_CRYPI            Unreviewed;      1198 AA.
AC   Q5CU46;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Secreted insulinase like peptidase, signal peptide {ECO:0000313|EMBL:EAK88947.1};
GN   ORFNames=cgd3_4250 {ECO:0000313|EMBL:EAK88947.1};
OS   Cryptosporidium parvum (strain Iowa II).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK88947.1, ECO:0000313|Proteomes:UP000006726};
RN   [1] {ECO:0000313|EMBL:EAK88947.1, ECO:0000313|Proteomes:UP000006726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX   PubMed=15044751; DOI=10.1126/science.1094786;
RA   Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA   Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA   Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA   Anantharaman V., Aravind L., Kapur V.;
RT   "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL   Science 304:441-445(2004).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAK88947.1}.
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DR   EMBL; AAEE01000004; EAK88947.1; -; Genomic_DNA.
DR   RefSeq; XP_626968.1; XM_626968.1.
DR   AlphaFoldDB; Q5CU46; -.
DR   STRING; 353152.Q5CU46; -.
DR   EnsemblProtists; EAK88947; EAK88947; cgd3_4250.
DR   GeneID; 3373885; -.
DR   KEGG; cpv:cgd3_4250; -.
DR   InParanoid; Q5CU46; -.
DR   OrthoDB; 200200at2759; -.
DR   Proteomes; UP000006726; Chromosome 3.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 3.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
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; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
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:UP000006726};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1198
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004254240"
FT   DOMAIN          93..203
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          253..426
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1198 AA;  138880 MW;  BA7ECBC67177FECF CRC64;
     MVYSLRLIIV LLPLFFISYF QQTLNDELYS ICFTNLSFED NKVSDSNNVV SEKEEEKNDN
     PNFNYESLVY TSSMKPISDQ SFKLLKLNND IEVILNSAPN VDECTASILN RVGSMHDPSN
     LHGLGFYLMN IMLSASNSDV GSGLYDFCID NSLSLSYQIY STYSLFHVTT PMVLLENVLK
     LVSEMLKSPV FTDEVMEKAL NILENKTTLD NHSYNIFSTN LVLSDPKSIF TRDRFGSRDT
     LKTIPQSKKI DVKQSLIKFF NEQYSSNRLM LSLKCNLPIQ VMQDLVAKYF NGIINKNLPI
     NTQYKSINNL IINPLSYSVG KIMYRIDESN QTLMLLFPLK NYLQPYMKSG PIFFINNYIC
     ANKEGTLMRF LKQKNYIKNM NCHVSNDMSG FSNIQFSFNL TNNGLFNVQN IIRAFFLSIN
     KIKDLKLDIN IYNKTNQNIL KEIKSSNKYF ANLNSLSILN NYFKFNSSSF KSIILGVNEF
     SNFDLNLHRQ ILMEINPQNM IIIFNLKGDK ETIEDTGELT LFDQSILNKD CTKYEEFLSQ
     NKKFRYVVLT NVLSKEFKEV IKTNNKFRFI LEEQNFCLKK YISHFPESLT QELKIYDKDK
     DPKTRDNLEK YNIVERLAVP KKLRDLLSSD SSQRATNFPQ FQDFYYFIPH IVPTHKIYLA
     INFFFPFENK KMASIRSTRI ATILLFIKEI LLSFSENISS HLANHSIDFI PKIYLPYDSI
     VNAFGLSLSL GSVPNAFSQF LSNLSINLNS YIDLDEKIFH DFVSYLRKVQ VEKSKSPNFI
     EKVNQINLNH LISTETVLNE LQTLKVEEVR EVFQTIIRQS QISGVIYGNL TPLDAEKYLS
     RLFSNLIGET PKKKTLIFKS GRKSGVSMRL RYSRMITKIG SRRAKTRKIA LSKRKKSLTK
     NNDQRTKISN TTKIINRIKT TNKTKTTNKT KIIKSEMLSK SKLYKLYSSA VSKSNSEECK
     NLQILDMSSI RPISKFFLYE NTNDKVNVSI LWIYIDKASP ESFIFTQYLK LIIENRLNYL
     QKNNNNINTY IKNYHISSSS YLISIEGSSS KEDSNAINEL LLSYLDTFIS SGSSIFNLDL
     FNSIKESLLK KYKKEGHYLD SLVVNIFEEI INKRFDFTRF RSVVNLLDRL TFENFTSNLE
     KVRKSAFYIL YSMSYKSQPI VPNGFTHLRD PTDIFKLHGI KTFKPAYSRV DKQLNNLP
//