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
//