ID   A0A1X7MZE3_9MICO        Unreviewed;       426 AA.
AC   A0A1X7MZE3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=SAMN06295885_0356 {ECO:0000313|EMBL:SMH29879.1};
OS   Rathayibacter oskolensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=1891671 {ECO:0000313|EMBL:SMH29879.1, ECO:0000313|Proteomes:UP000193711};
RN   [1] {ECO:0000313|Proteomes:UP000193711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2121 {ECO:0000313|Proteomes:UP000193711};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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; FXBM01000001; SMH29879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7MZE3; -.
DR   OrthoDB; 5288740at2; -.
DR   Proteomes; UP000193711; 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}.
SQ   SEQUENCE   426 AA;  44650 MW;  0FE90D6F04D84C38 CRC64;
     MTDHADHIAD FAAFLSASPS SFHAAAETAR RLGAAGFTGL DETASWPTAP GRYYVVRDGA
     VIAWHLPTGA DAVTPFRILG AHTDSPGFTL KPKPTIASKG WLQAGVEIYG GPLLNSWLDR
     ELELAGRLVT GDGTEVLVRT GPFLRIPQLA VHLDREVNDG LKLDRQKHTV PVFGVGDAAD
     TDLLELLAAK AGLGAASDIV GFDLVTADTQ PPARFGLDEA LFAAGRMDDL SSVHAGLVAL
     LSAGADDAQH ISMLAAFDHE ELGSATRSGA SGPFLEDVLN RIGAALGAGV DERARAIAQS
     WCLSADAGHS VHPNYPEKHD PVNQPVAGKG PLLKINASQR YATDARGTAL WADVCARAGV
     EHQEFVSNNT VPCGSTIGPL TATRLGIRTV DVGVPLLSMH SARELAHVDD LVALAKAIEV
     FFGPVD
//