ID   A0A1H0NSM6_9MICC        Unreviewed;       458 AA.
AC   A0A1H0NSM6;
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=SAMN04487914_101294 {ECO:0000313|EMBL:SDO95410.1};
OS   Arthrobacter sp. ok909.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1761746 {ECO:0000313|EMBL:SDO95410.1, ECO:0000313|Proteomes:UP000199538};
RN   [1] {ECO:0000313|EMBL:SDO95410.1, ECO:0000313|Proteomes:UP000199538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK909 {ECO:0000313|EMBL:SDO95410.1,
RC   ECO:0000313|Proteomes:UP000199538};
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; FNJS01000001; SDO95410.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0NSM6; -.
DR   STRING; 1761746.SAMN04487914_101294; -.
DR   Proteomes; UP000199538; 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; cd05658; M18_DAP; 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: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}.
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  48022 MW;  E3E3836A5CE1DBD2 CRC64;
     MSVCTDASAP APRAARARLE TMPTPSSAAD HIQDLGAYVS ASPSSFHAVH EVARRLDEAG
     FTGLDELHPW PAPAATAGKF YVVRDGALVA WVVPPGAGPI TGFNILGAHT DSPSFKLKPK
     PTTGKFGWLQ AGVEVYGGPL LNSWLDRELQ LAGRLVMRDG TQHLTATGPL LRFPQLAIHL
     DRAVNEGLAL DKQQHMNPVF GLGDPAAEDL LGLLAAKVTD AAVDPAQIGG YDVVIADTQA
     PAVFGAKREF FASGRLDNLS ATHAGLTALI AHSGTPLPEG APIAVLAAFD HEEIGSASRS
     GACGPVLEDI LVRISDGLGA SASQRRQAFA ASFCVSADAG HAVHPNYPER HDPANRPVLN
     GGPLLKINAN QRYATDAAGA ALWARLCTEA GIPYQEFVSN NVMPCGSTIG PLTATRLGIR
     TVDVGVPLLS MHSARELCGV EDPHRLATVT RTFFRTPA
//