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Database: UniProt
Entry: G0VQC9_MEGEL
LinkDB: G0VQC9_MEGEL
Original site: G0VQC9_MEGEL 
ID   G0VQC9_MEGEL            Unreviewed;       428 AA.
AC   G0VQC9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=MELS_1436 {ECO:0000313|EMBL:CCC73657.1};
OS   Megasphaera elsdenii DSM 20460.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC73657.1, ECO:0000313|Proteomes:UP000010111};
RN   [1] {ECO:0000313|EMBL:CCC73657.1, ECO:0000313|Proteomes:UP000010111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC73657.1,
RC   ECO:0000313|Proteomes:UP000010111};
RX   PubMed=21914887; DOI=10.1128/JB.05861-11;
RA   Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., Sauer M.;
RT   "Genome Sequence of the Ruminal Bacterium Megasphaera elsdenii.";
RL   J. Bacteriol. 193:5578-5579(2011).
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; HE576794; CCC73657.1; -; Genomic_DNA.
DR   RefSeq; WP_014016387.1; NZ_CP027570.1.
DR   AlphaFoldDB; G0VQC9; -.
DR   STRING; 1064535.MELS_1436; -.
DR   GeneID; 69663539; -.
DR   KEGG; med:MELS_1436; -.
DR   eggNOG; COG1362; Bacteria.
DR   HOGENOM; CLU_019532_2_0_9; -.
DR   Proteomes; UP000010111; Chromosome.
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   Reference proteome {ECO:0000313|Proteomes:UP000010111};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   428 AA;  47476 MW;  92FE1C034B8497E7 CRC64;
     MTYDYTQDLL KFIQRSPSPY HTVQASRTYL DQAGFQALAL SKTWHLAPNS AYYVPLYDSG
     LVAFRTGSDV RRHLRLSAAH TDFPCLRLKY RPELRQHGYL KLNAEVYGGL LRESWLDRPL
     SLAGTVALQS KDAFRPEVRL IDIGRPVLTI PRLAIHMNRQ ANDGVALNPQ KDLLPVMGLD
     DQALTNHFFL DFLSEKCHCL PEAILSYDLT VYPCETGCSL GWHDEFISSP RLDNLTSVLA
     CLMGLVKEDR ADGLNVTALF DNEEVGSQTK QGADSQILPG ILRRIYHAFG FTDDDFSADL
     GRAFMLSVDV AHAIHPNVPE KCDVTNQPVM GHGVALKIAS SQRYAGDATA VAVVKALCRE
     NEIPYQVFMN RSDIPGGSTL GSLLSANLPL RTMDIGIPIT AMHSCRELMG AADEESLVRL
     IRAFFGHK
//
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