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Database: UniProt
Entry: A0A133ZNE6_9FIRM
LinkDB: A0A133ZNE6_9FIRM
Original site: A0A133ZNE6_9FIRM 
ID   A0A133ZNE6_9FIRM        Unreviewed;       432 AA.
AC   A0A133ZNE6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF1866_01627 {ECO:0000313|EMBL:KXB56952.1};
OS   Lachnoanaerobaculum saburreum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnoanaerobaculum.
OX   NCBI_TaxID=467210 {ECO:0000313|EMBL:KXB56952.1, ECO:0000313|Proteomes:UP000070394};
RN   [1] {ECO:0000313|EMBL:KXB56952.1, ECO:0000313|Proteomes:UP000070394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00896 {ECO:0000313|EMBL:KXB56952.1,
RC   ECO:0000313|Proteomes:UP000070394};
RA   Oliw E.H.;
RL   Submitted (JAN-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXB56952.1}.
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DR   EMBL; LSDA01000096; KXB56952.1; -; Genomic_DNA.
DR   RefSeq; WP_060931348.1; NZ_KQ959831.1.
DR   AlphaFoldDB; A0A133ZNE6; -.
DR   STRING; 467210.HMPREF1866_01627; -.
DR   PATRIC; fig|467210.3.peg.1613; -.
DR   OrthoDB; 9764268at2; -.
DR   Proteomes; UP000070394; 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   432 AA;  48158 MW;  C614D7675A188100 CRC64;
     MEILRDLMNF LDSSVTMFHA INECEKVLQN CGYIYLPENE KWNIRAGKYY TKRNSSSLIA
     FDIANGDYHF QISAAHSDSP TFKLKDRPII ESNGYLKLNV EAYGGMIDAT WLDKPLTLAG
     RVMVDTGCGI ETRLLYIDKD LLIIPNVPIH FNREINKGFA FNNQVDMLPV FSAGNLSEAD
     FDKMLAKELG VKPEAILAKD LYLVNRQKAT VIGYDNELIS SGRLDDLECV YTSLLGFIEA
     MNNDHINVFA VFDNEEVGSV TKQGAMSTFL VSTLNRINKA LGKSDEDYYR AIAKSMLISC
     DNAHAIHPNH PELFDVKNRP VLNKGIAIKE SANQKYTTDA FSRAVLKKIL DKNNIPYQTF
     ANRSDIIGGS TLGNLSNTAV SMNAVDIGLP QLAMHSAYET AGAKDVEYAI EALRAFFETN
     IDIKDDKVSL EV
//
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