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Database: UniProt
Entry: A0A1M6NSL7_9CLOT
LinkDB: A0A1M6NSL7_9CLOT
Original site: A0A1M6NSL7_9CLOT 
ID   A0A1M6NSL7_9CLOT        Unreviewed;       430 AA.
AC   A0A1M6NSL7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Aminopeptidase II. Metallo peptidase. MEROPS family M29 {ECO:0000313|EMBL:SHJ98655.1};
GN   ORFNames=SAMN02745163_03001 {ECO:0000313|EMBL:SHJ98655.1};
OS   Clostridium cavendishii DSM 21758.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121302 {ECO:0000313|EMBL:SHJ98655.1, ECO:0000313|Proteomes:UP000184310};
RN   [1] {ECO:0000313|EMBL:SHJ98655.1, ECO:0000313|Proteomes:UP000184310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21758 {ECO:0000313|EMBL:SHJ98655.1,
RC   ECO:0000313|Proteomes:UP000184310};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQZB01000012; SHJ98655.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6NSL7; -.
DR   STRING; 1121302.SAMN02745163_03001; -.
DR   Proteomes; UP000184310; Unassembled WGS sequence.
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:SHJ98655.1}; 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:UP000184310}.
SQ   SEQUENCE   430 AA;  48368 MW;  F5D28BD60EC661E2 CRC64;
     MKSSIIDVIT KYFIIVGCEI MNFNKNLRKY ATLAVRTGIN IQPGQTLVIN SPVECLDFTR
     LAVEEAYKAG AKEVVVHWND EITTKYKYLY SPLEIFETLP DWSRDSLIYY ARLGAAFLSI
     SASDPELLKG IDTKKIKANQ KSRSIALSEF QTRLMSNKNV WSVVSIPTKA WSKKIFSELN
     DEDAVNRLWN EIFKIVRIDK EDPVAAWNEH KKNLKEKMNY LNNKNLKELH FKNSLGTDFH
     LELATDAIWV GGADYSEEGI EFIANMPTEE VFSMPKKTGV NGIVHSSKPL NYAGNIIDNF
     SITFKDGKVV DFTAENGYES LKSLIETDEG SHYLGEVALV PFDSPISNSN IIFFNTLYDE
     NASCHLALGK AYSGCVKNGD NLSEEELANK GANDSLTHVD FMIGTSDLSI TAIDFDGNNH
     HIFRDGNWAF
//
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