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Database: UniProt
Entry: A0A174DLL0_9CLOT
LinkDB: A0A174DLL0_9CLOT
Original site: A0A174DLL0_9CLOT 
ID   A0A174DLL0_9CLOT        Unreviewed;       462 AA.
AC   A0A174DLL0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   Name=apeA {ECO:0000313|EMBL:CUO26383.1};
GN   ORFNames=ERS852471_01231 {ECO:0000313|EMBL:CUO26383.1};
OS   Clostridium disporicum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=84024 {ECO:0000313|EMBL:CUO26383.1, ECO:0000313|Proteomes:UP000095594};
RN   [1] {ECO:0000313|EMBL:CUO26383.1, ECO:0000313|Proteomes:UP000095594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5834856 {ECO:0000313|EMBL:CUO26383.1,
RC   ECO:0000313|Proteomes:UP000095594};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) 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; CYZX01000007; CUO26383.1; -; Genomic_DNA.
DR   RefSeq; WP_055264749.1; NZ_CYZX01000007.1.
DR   AlphaFoldDB; A0A174DLL0; -.
DR   OrthoDB; 89722at2; -.
DR   Proteomes; UP000095594; 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   CDD; cd05659; M18_API; 1.
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:UP000095594};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   462 AA;  51628 MW;  C0D0F078ED15B7C3 CRC64;
     MSEEKTKNAW LKFDEKGRLD IFNFCEGYKN YMSVCKTERE SVLEAIRLAE EKGYKDLNLV
     IKNGETLKSG DKVYLNNKDK ALVLFLIGNE PIENGMRIIG SHVDSPRLDL KQHTLYEDGQ
     MALMDTHYYG GIKKYQWIAL PLAIHGVVVK KDGTKIDVVI GEDDNDPVVG ISDLLVHLSG
     EQLQKKANEV IHGEDLNVLV GNIPLEGKEN DAVKANILKL LKDKYDFEEE DFISAEIEVV
     PAGKARDLGL DRSMVMAYGQ DDRICAYTSL MALLDLDKVE KTSVILLVDK EEVGSQGATG
     MHSRFFENAV AEIMDRLGQY SELKLRRALS NSAMLSADVT AAFDPNYASA YERKNTAYFG
     RGLVFSKYTG ARGKSGCNDA NPEFIAWLRN IMDKNNIAYQ TAELGKVDQG GGGTIAYILA
     EYNMEVIDCG VALQNMHAPW EVSSKVDIYE TMRGYKTFLI EK
//
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