ID   A0A1I6JDR5_9FIRM        Unreviewed;       430 AA.
AC   A0A1I6JDR5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=SAMN05661086_01595 {ECO:0000313|EMBL:SFR77091.1};
OS   Anaeromicropila populeti.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaeromicropila.
OX   NCBI_TaxID=37658 {ECO:0000313|EMBL:SFR77091.1, ECO:0000313|Proteomes:UP000199659};
RN   [1] {ECO:0000313|EMBL:SFR77091.1, ECO:0000313|Proteomes:UP000199659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=743A {ECO:0000313|EMBL:SFR77091.1,
RC   ECO:0000313|Proteomes:UP000199659};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; FOYZ01000005; SFR77091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6JDR5; -.
DR   STRING; 37658.SAMN05661086_01595; -.
DR   OrthoDB; 9764268at2; -.
DR   Proteomes; UP000199659; 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   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:UP000199659};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   430 AA;  48169 MW;  2E0D975548E93F9C CRC64;
     MNHITSDLID FIACATSPYH VVKKCKEMLI DEGFQELPFT SPWTLEKGKS YVTTPYDSTL
     FAFTLGDELL NCPHLRLATA HTDHPCFRIK PKAELSEHSY LQINTEAYGG LILNTWLDRP
     LSVAGKICLK SDSIYAPKVV FFDAKRPLLT IPNLAIHINR EVNKGIELNK QTDMRPVLGL
     LNETLNKDNF FLNFLAQELQ ISPEDILTFD LTIYNAEHPC LIGLQEDFLS SPRLDNLTSA
     LACVKGLLAD TNRNNINMIA LFDNEEIGSR TKQGADSSLT NILLDKIFTC LNLEKSILYN
     TLIDRSLILS VDVAHCLHPN YLSKNDPSNF TELGKGVVLK LDSNQKYAFD PEALSIVEQL
     CQTNKITYQK FVNRSDATSG STLGSIISSW LPVKTVDLGL PLLAMHSARE LMGTSDQEDL
     EKLIECFFNC
//