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Database: UniProt
Entry: B6AII5_CRYMR
LinkDB: B6AII5_CRYMR
Original site: B6AII5_CRYMR 
ID   B6AII5_CRYMR            Unreviewed;      1073 AA.
AC   B6AII5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Peptidase M16 inactive domain-containing protein {ECO:0000313|EMBL:EEA08026.1};
DE            EC=3.4.24.56 {ECO:0000313|EMBL:EEA08026.1};
GN   ORFNames=CMU_031670 {ECO:0000313|EMBL:EEA08026.1};
OS   Cryptosporidium muris (strain RN66).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=441375 {ECO:0000313|Proteomes:UP000001460};
RN   [1] {ECO:0000313|EMBL:EEA08026.1, ECO:0000313|Proteomes:UP000001460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN66 {ECO:0000313|EMBL:EEA08026.1,
RC   ECO:0000313|Proteomes:UP000001460};
RA   Lorenzi H., Inman J., Miller J., Schobel S., Amedeo P., Caler E.V.,
RA   da Silva J.;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; DS989736; EEA08026.1; -; Genomic_DNA.
DR   RefSeq; XP_002142375.1; XM_002142339.1.
DR   AlphaFoldDB; B6AII5; -.
DR   STRING; 441375.B6AII5; -.
DR   EnsemblProtists; EEA08026; EEA08026; CMU_031670.
DR   GeneID; 6997464; -.
DR   VEuPathDB; CryptoDB:CMU_031670; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   OMA; RIMTHVI; -.
DR   OrthoDB; 198750at2759; -.
DR   Proteomes; UP000001460; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
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, ECO:0000313|EMBL:EEA08026.1};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001460};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          33..138
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          193..339
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   1073 AA;  125565 MW;  01B72A270B3C243E CRC64;
     MGSQNNIIKD EEFIKPITEY RKFRYYELNN KIKVFLIHDS NAVYSNLALS ISVGKFMGFY
     NNINLPSFLL YGLFMGSRKF PSIHEFDNFL SSHGGEIEKE ITDRNSYYYL GIPSNYLNLA
     LKRFSEFFKT PLFDRNGLIN QLRRFSQIFR DYYPGNLLNT SELIHEISYL NSLNKINCSS
     REFDINNEYE YIRNEIIKFF REYYSADLMT LIIIDSKPFN ILEKYVSEFF LNIQNNNKIL
     STFHISDKNV EPLLIYIGKI IHVKYNNPIN KIKLIFPITY KVSNDKLLSF QYIIDTLGHR
     MKGSLVEFLK QRCWIEDLSL FVSSSEFGYS FIEISIDLTY IGINYLAYIL KSIYASINIL
     KNKAINPDII DDRIKIEEIN FYYRESLNNK ELIYTIIENY SSHRYLPNEV LIGNVTIDKA
     DTKDIQEAIK ILNPKNMILI IFSQNFVLTG MNMLLNNVEF MNELKLNMDN KFYNSLINDI
     ENSDIRFDDL KYKEIKYHIE KLHPLFLNYL DKVDNVIQNT TFYYDLPDKN ECIPSLIEDY
     TSNIMYQQYP IPLKDAINRY LNENYSEGCR VKLSMISPSF ENIFYFPILG STNVKTSLSF
     RIMTHVISKS SLILPKALES TSRLLSTLNI LYRAIEIEIS SIIYSVTQAG NNVKLLVTKE
     SEFGGSPFGL EILLLGYYPS LIIFIENFFT TLSNLNKIAE LSFQQAKFNY QNYLKFQIYE
     TTSIEQSLNA LSDITLMQNM SYKLLMKQCS KIKLEDVIEL ANYIAQYGEI EGLIVGNLDP
     IRAHKLINNI LKWLKHNEEK YHVSSKIDIT KSIKIARSTT LEGTRDSIEY YETLDLLSLV
     NSNRNTYYYQ LNKNINDKRS HVLLFLGMGA ADYVSLVLLN MLKRIMSRIS QSGDNSELKL
     DINVTIRFHV IGSSFAGLLF YAESTNRNIK FLTENILKFY RTFFESDNSI SLSDFEEARK
     QYLHQLHFKP TKLVDISNEF YSQLVNRQIK FNTKISKILY LQNLNYEKLN SFSSAMRNSP
     KVIIATQSQI GTNLDELCKY SPIRFQKITS KDELFYIEGI RTYKFPLKMS DKY
//
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