ID   AMP12_ENCCU             Reviewed;         864 AA.
AC   Q8SRG3;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable M1 family aminopeptidase 2;
DE            EC=3.4.11.-;
GN   OrderedLocusNames=ECU08_0070;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; AL590448; CAD26312.1; -; Genomic_DNA.
DR   RefSeq; NP_597136.1; NM_001041745.1.
DR   AlphaFoldDB; Q8SRG3; -.
DR   SMR; Q8SRG3; -.
DR   STRING; 284813.Q8SRG3; -.
DR   GeneID; 859558; -.
DR   KEGG; ecu:ECU08_0070; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_0070; -.
DR   HOGENOM; CLU_003705_2_3_1; -.
DR   InParanoid; Q8SRG3; -.
DR   OMA; FGNETHY; -.
DR   OrthoDB; 110058at2759; -.
DR   Proteomes; UP000000819; Chromosome VIII.
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; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.10.390.10; -; 1.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; SSF63737; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..864
FT                   /note="Probable M1 family aminopeptidase 2"
FT                   /id="PRO_0000095102"
FT   ACT_SITE        326
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         289..293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            413
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   864 AA;  97521 MW;  EF65005145C57CF5 CRC64;
     MRWIKVMAGL LPMIGSKGAD EKDSSQQRRL SRVVVPEHYD LHVKILDAGF CGSVGIRVMI
     SQDVSEIVLN AKELEIRDAG IVVEGARIPG RVVVGEAEKE LEVVRIVFPS SLRAGPGYLT
     MEFCGDYNNG LVGLYKSGGP KEVYSTHFEP TDARWVFPCF DQPDMKATFK ISIDAGSKFT
     VLANTQAIPS LREEYGDRKI EYFEETCKMS TYLVAFVVGE LSYIEDWSKD GVRLRVYGDS
     SEVEWGRYGL EVGKRCLEYF SEYFGVGYEF PRAGSAKIDM VGIPNFSSGA MENWGLITFR
     RESLLYVPGK SNVEDMKNVA ETVCHELGHM WFGNLVTMSW WDDLWLNEGF ATWVSFKGME
     NIGSVVSWDV WGEFVLWNVV RGMVDDGLGK SHQIRMNVTD PGEIGEIFDS ISYCKGASVI
     RMIERYVGES VFMLGIRRYI KEHMYGNGNA MSLWKAIGEE YGEDISEMVE GWISQAGYPV
     VSVQDCGSSL VLSQSRYSML GKSDDSLWTI PVVVSWEGKG QERIELRGRE TTVRKRSSVY
     KVNAEYGGFY RVLYDSAGLS GLESRIDSLS VVDRVNVIED VFGLGFGLYG GLEHGLRRIS
     EYYSDSYHVA RSGIEKLLRL RSVFYDDAEI VSLIDKKVRK MILPCVGRID VFDIGTSVES
     VSMNKYVLSV GVEVGIREAV EKVQELWRRH VEAGEELGEL RWIVYKAVVD ENLGYMMDKY
     KNGDTPGMRR EVMNGFSGIK REENFLDVVG NLSQFSVEDI GVVIGSISRG GAFRDAMVEY
     VVSHGEELYL MVHKNAMLYN MIIMSLRHVS GDLIVEKVER FLSGIKHSGS NLSIEKVRNE
     IQWRRRMRGI REEVLRGLLP EAEK