ID   A0A1Y4ND15_9FIRM        Unreviewed;       469 AA.
AC   A0A1Y4ND15;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-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=B5F08_06505 {ECO:0000313|EMBL:OUP78723.1};
OS   Anaeromassilibacillus sp. An172.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaeromassilibacillus.
OX   NCBI_TaxID=1965570 {ECO:0000313|EMBL:OUP78723.1, ECO:0000313|Proteomes:UP000195869};
RN   [1] {ECO:0000313|Proteomes:UP000195869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An172 {ECO:0000313|Proteomes:UP000195869};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OUP78723.1}.
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DR   EMBL; NFKS01000010; OUP78723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4ND15; -.
DR   OrthoDB; 89722at2; -.
DR   Proteomes; UP000195869; 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:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 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:UP000195869};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   469 AA;  52353 MW;  FAAF8705D46CE8A0 CRC64;
     MSKKKEEKSE IKELKEQLFT RTDKGIASMK ESEIKKADKY CEDYKKFIDH SKTEREAVKT
     AVKLAEKAGF VPFEQDKKYK AGDRIYYVNR HKALALAVIG KKGVKDGVRL AIAHIDSPRI
     DLKPNPMYEA SGLAMFKTHY YGGLKKYQWT ALPLSLHGVV IKTDGTKIEI NLGEKDDEPC
     FCITDLLPHL AKEQVQKPMA KVFTGEELNI LAGSRPYDNN GESDLVKLNI MSILNKKYGI
     TEEDFLSAEL SFVPALKTRD VGFDESMIGG YGHDDRVCAY PALTAILETE MPENTVITML
     ADKEETGSDG NTGMQSDFLR YFIYDLAKAE GEEGYRVLSK SKCLSADVNA AFDPTYASVY
     ETQNCSYLNK GVVISKYMGH GGKYDTSDAS AEYMGEIRSM LEKNNVSWQT GELGKVDMGG
     GGTIAKYVAN MNVDVIDLGV PVLSMHAPFE IVSKTDVYMA YRAFYCFFN
//