ID B6AIS8_CRYMR Unreviewed; 459 AA.
AC B6AIS8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=CMU_010670 {ECO:0000313|EMBL:EEA08119.1};
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:EEA08119.1, ECO:0000313|Proteomes:UP000001460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN66 {ECO:0000313|EMBL:EEA08119.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001335};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; DS989737; EEA08119.1; -; Genomic_DNA.
DR RefSeq; XP_002142468.1; XM_002142432.1.
DR AlphaFoldDB; B6AIS8; -.
DR STRING; 441375.B6AIS8; -.
DR EnsemblProtists; EEA08119; EEA08119; CMU_010670.
DR GeneID; 6997640; -.
DR VEuPathDB; CryptoDB:CMU_010670; -.
DR eggNOG; KOG2596; Eukaryota.
DR OMA; GPILKVN; -.
DR OrthoDB; 1156at2759; -.
DR Proteomes; UP000001460; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Reference proteome {ECO:0000313|Proteomes:UP000001460};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 459 AA; 51747 MW; CE1FEB16B11DB40A CRC64;
MKPAHKDFTE KFLNYLNSTG SPYHTVNEMV EVLEKSGFVR YNGDLKKDGK YYLTFNYSTL
LAFHIGPDFD LNNQRSTAVI AGAHTDSPCL RIRPNSITHN EGFTQLSVST YGGGLWHTWF
DRGLGVAGKV VTTNCREKLI RIQEPICIIP NLAIHLQLGD EHKSFTFDKE SHLQPIISCT
AHDSSLEDQS NFKQVCTLPK ELLNKICDQT ELQPNEVLSY DLCLMDSVPS RFAGINEEFI
DSPRLDNLGG TYSCFYGLIL ASENNKHDII MVASFDHEEV GSKSYTGSQS DILRQILTEL
LSKLAEVETF SFQHFMYRSM FLSVDMAHGV HPNYPERHQR DHKPVFKGGI VLKHNFNQSY
STDCTTASYI KAIAQKANIP LQEFLVKNNS PCGGTIGPIV ACKLGVRTAD IGVPMLAMHS
IREFMAADDI YILMDFIKSY FELWGEFKGQ SLLLDDLHI
//
