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Database: UniProt
Entry: Q5CU47_CRYPI
LinkDB: Q5CU47_CRYPI
Original site: Q5CU47_CRYPI 
ID   Q5CU47_CRYPI            Unreviewed;      1113 AA.
AC   Q5CU47;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Insulinase like peptidase {ECO:0000313|EMBL:EAK89232.1};
DE   Flags: Fragment;
GN   ORFNames=cgd3_4240 {ECO:0000313|EMBL:EAK89232.1};
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:EAK89232.1, ECO:0000313|Proteomes:UP000006726};
RN   [1] {ECO:0000313|EMBL:EAK89232.1, 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:EAK89232.1}.
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DR   EMBL; AAEE01000004; EAK89232.1; -; Genomic_DNA.
DR   RefSeq; XP_626967.1; XM_626967.1.
DR   AlphaFoldDB; Q5CU47; -.
DR   SMR; Q5CU47; -.
DR   STRING; 353152.Q5CU47; -.
DR   EnsemblProtists; EAK89232; EAK89232; cgd3_4240.
DR   GeneID; 3374006; -.
DR   KEGG; cpv:cgd3_4240; -.
DR   InParanoid; Q5CU47; -.
DR   OMA; VCISENA; -.
DR   OrthoDB; 129328at2759; -.
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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          43..160
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          207..388
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EAK89232.1"
SQ   SEQUENCE   1113 AA;  130236 MW;  4A3726C8CA7EACDB CRC64;
     EKEMAIEENS SKYLEIVEDS EFIKPKESSF KCKFERLKTG LEVFLISSEK LTSTSVNLVV
     KVGSANEGSE IDGLAHFLEH SVFLGTEKFP GQNEFGKFVR TYGGATNAST DILMTHYSFF
     IPNQFLEPAL ERFCEFFKSP LFSEEYLQNE INIVENEFLS KTNNFYTLLE HVLKQIADET
     HIYSKFFYGN SKTLKKIPEK NGISLRERTI RFFEEYYGSK NMVLFILSNI SIQELSKISY
     KYFSNVRSCS RLSPKPESLS LFPELPYLGI SKKLVKIHLN INASQLMLMF SLPKKEYGLS
     RIFSQYLSFF LCPKSGEGLL NDIIQKNLCH KISLNETYSQ LGFSYITFYL FLTKEGVFNI
     REIILSLFSA FQIIKKTELI DEYIQRIANK DYLNFLKIED TLPSIQILEL LKVYYLTKGT
     PEKLFSAIYS APQFSQQVFE DFMSYLNVEN MVTIIIDSNF DLGTLIKQEI IQKSNHKDYI
     NKKYNFKDYI STIILSGRIR NIENKYLLSE KYFNTNYSIW DFTNKFLQSI SEIKIESGID
     FSNVPLPMQT INMLESSKIK NSQIKTNLKP PLLFDIAYEF EKLKLSKEKD FVFSRNLKIS
     SIWRGMFYMN VPKNIFPDSF FILRLLIPPL FGKKSFDQFS ESGFYIKDGY HSCVLIQLLS
     ELIKLKINLN FERLSKEGIS AQIYPTFRSP FPNYAIGIEY YLYGKFESLS KFTDELSHTL
     KNILKIKSEE FEFIKKNTIG KLLLIESQLL YKDLIGEAEH EVLNMGFINT KKFINLVNKV
     KITEFIKFSD LFRRICIFEG IFVGDTPANI LKAVLDGFIL NLKNFKFSEI DKPLFYVKDN
     PNNDNYLKPY YHKIFFTQNE NSNIYKRKKT QCNGFDMIDL FSIPPNKNKI YYLTKSIKSK
     HNLIRLSVFF KRESPITFFK LQIINQVFFD ILFENVRQKK QIAYEFNSEV CEVSEKTLSY
     SFVIQTDNHT ITSTIYTLLE CLKELSPTIL SEELFRVALL EKIECLEQMD SIFMEVNSFI
     TNSFNRSFNY KLREEVLASL RSLDFIQFQS WFSNSLKNVP ILITVCISEN ASASDKKICK
     KFVPPGFTKI KKPMELFEIY KVKSYYIQHR IFN
//
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