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Database: UniProt
Entry: A0A1V1I4C6_9FIRM
LinkDB: A0A1V1I4C6_9FIRM
Original site: A0A1V1I4C6_9FIRM 
ID   A0A1V1I4C6_9FIRM        Unreviewed;       409 AA.
AC   A0A1V1I4C6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Aminopeptidase 2 {ECO:0000313|EMBL:CED94977.1};
GN   ORFNames=CRIB_2381 {ECO:0000313|EMBL:CED94977.1};
OS   Romboutsia ilealis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Romboutsia.
OX   NCBI_TaxID=1115758 {ECO:0000313|EMBL:CED94977.1, ECO:0000313|Proteomes:UP000245622};
RN   [1] {ECO:0000313|EMBL:CED94977.1, ECO:0000313|Proteomes:UP000245622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIB {ECO:0000313|EMBL:CED94977.1,
RC   ECO:0000313|Proteomes:UP000245622};
RA   Hornung B.V.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M29 family.
CC       {ECO:0000256|ARBA:ARBA00008236}.
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DR   EMBL; LN555523; CED94977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1I4C6; -.
DR   Proteomes; UP000245622; Chromosome chr1.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR   InterPro; IPR035097; M29_N-terminal.
DR   InterPro; IPR000787; Peptidase_M29.
DR   PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   PRINTS; PR00919; THERMOPTASE.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:CED94977.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245622}.
SQ   SEQUENCE   409 AA;  45976 MW;  6269DA292835A9C8 CRC64;
     MSFEKNLDKY AKLAVKVGVN IQEGQILLVR SPIECAPFVR KVIKHAYEAG AKNVHIEWSD
     EECTLLKYLH APDETFNEFP KWISDQYVDI AKEGGAFLTV YAQNPDLLKD VDPQRVANFQ
     KASGIALKEW RSYTLSDKCK WSIVSIPTEA WATKVFPNVS TDEAIDKLWD AIFKCTRVDN
     EDPVDAWKKH NADLKSRMDF LNNKNFQTLK FKSSKTDLTM ELPEGHIWLS GASKDPNGID
     FNANIPTEEV FSMPHKFKVN GIVHSTKPLV YGGNIIDDFS LTFKDGKIVD FTAEKGAETL
     GKLIDTDEGS HYLGEVALVP FRSPISDTNI VFFNTLFDEN ASCHFAIGSA YNTCIKNGDD
     IKDDDLDKYG VNSSLTHVDF MIGSNDMNIV GITHEGEEVQ VFKDGNWAF
//
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