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 27-MAR-2024, entry version 100.
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; HDMAGFY; -.
DR OrthoDB; 3085317at2759; -.
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; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 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 PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
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; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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
//
