AMP11_ENCCU
ID AMP11_ENCCU Reviewed; 864 AA.
AC Q8SQI6; O62582;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable M1 family aminopeptidase 1;
DE EC=3.4.11.-;
GN OrderedLocusNames=ECU01_0140;
GN and
GN OrderedLocusNames=ECU01_1470;
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 [GENOMIC DNA].
RX PubMed=11013707; DOI=10.1089/omi.1.1998.3.1;
RA Duffieux F., Peyret P., Roe B.A., Vivares C.P.;
RT "First report on the systematic sequencing of the small genome of
RT Encephalitozoon cuniculi (Protozoa, Microspora): gene organization of a 4.3
RT kbp region on chromosome I.";
RL Microb. Comp. Genomics 3:1-11(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [3]
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; AJ005644; CAA06646.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD24886.1; -; Genomic_DNA.
DR EMBL; AL391737; CAD25018.1; -; Genomic_DNA.
DR RefSeq; XP_965851.1; XM_960758.1.
DR RefSeq; XP_965983.1; XM_960890.1.
DR AlphaFoldDB; Q8SQI6; -.
DR SMR; Q8SQI6; -.
DR STRING; 284813.Q8SQI6; -.
DR PRIDE; Q8SQI6; -.
DR GeneID; 860187; -.
DR GeneID; 860321; -.
DR KEGG; ecu:ECU01_0140; -.
DR KEGG; ecu:ECU01_1470; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0140; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_1470; -.
DR HOGENOM; CLU_003705_2_3_1; -.
DR InParanoid; Q8SQI6; -.
DR OMA; YVEDRTS; -.
DR OrthoDB; 110058at2759; -.
DR Proteomes; UP000000819; Chromosome I.
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 1"
FT /id="PRO_0000095101"
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"
FT CONFLICT 720..722
FT /note="YKN -> HKY (in Ref. 1; CAA06646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 864 AA; 97364 MW; 44DD93320CC5B153 CRC64;
MRWIKVMAGL LPMIGSKGAD EKDSSQQRRL SRVVVPEHYD LHVKILDAGF CGSVGIRVMI
SQDVSEIVLN AKELEIRDAG IVVEGARIPG RVVVGEAEKE LEVVRIVFPS SLRAGPGYLT
MEFCGDYSNG LVGLYKSGGP KEVYSTHFEP TDARRAFPCF DQPDMKATFK ISIDAGSKFT
VLANTQAIPS LREEYGDRKI EYFEETCKMS TYLVAFVVGE LSYIEDWSKD GVRLRVYGDS
SEVEWGRYGL EVGKRCLEYF SEYFGVGYEF PRAGSAKIDM VGIPNFSSGA MENWGLITFR
RESLLYVPGK SNVEDMKNVA GTVCHELGHM 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
