ID   A0A1H9PNX2_9CORY        Unreviewed;       411 AA.
AC   A0A1H9PNX2;
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=SAMN05661109_00415 {ECO:0000313|EMBL:SER50026.1};
OS   Corynebacterium cystitidis DSM 20524.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1121357 {ECO:0000313|EMBL:SER50026.1, ECO:0000313|Proteomes:UP000198929};
RN   [1] {ECO:0000313|EMBL:SER50026.1, ECO:0000313|Proteomes:UP000198929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20524 {ECO:0000313|EMBL:SER50026.1,
RC   ECO:0000313|Proteomes:UP000198929};
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; FOGQ01000001; SER50026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9PNX2; -.
DR   STRING; 1121357.SAMN05661109_00415; -.
DR   Proteomes; UP000198929; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   411 AA;  43593 MW;  2734903A84D93C1D CRC64;
     MSQIRDLIDF IAASPSAFHA AREVADRLTA AGFTEHSCTR SGAHSALGTE PGGHVLVDGG
     AVVAYWIPEV PNPAFRIIGS HTDSPGFMLK PTPDFHAHGF HQLAVEVYGG PILASWFDRE
     LTFAGRIVLA DGTSRLVNTG AVARIPHLAI HLERSQELQP DKQAHMQPIM GAGQSESIMD
     VVAEAADVDK RYIVSHELIS ADAQEGVVFN DMVAAGRLDN LSSVYASMTA LLGAIDEAQD
     IVVLAAFNHE EVGSQSTTGA SGPLLERCLT TIARAFGDPF EMFAASSLVS ADAAHSVHPN
     YAGKHDPTHR PLLNEGPVLK INANQRYASD AVTEALWINA CRAADVPVQT FVGNNSVPCG
     STIGPLAATR LGIRTVDVGV PLLSMHSARE LAGTQDQLWF ARALTAYLAG N
//