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Database: UniProt
Entry: A0A0J6WV15_9FIRM
LinkDB: A0A0J6WV15_9FIRM
Original site: A0A0J6WV15_9FIRM 
ID   A0A0J6WV15_9FIRM        Unreviewed;       426 AA.
AC   A0A0J6WV15;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=AB840_12540 {ECO:0000313|EMBL:KMO85627.1};
OS   Megasphaera cerevisiae DSM 20462.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO85627.1, ECO:0000313|Proteomes:UP000036503};
RN   [1] {ECO:0000313|EMBL:KMO85627.1, ECO:0000313|Proteomes:UP000036503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO85627.1,
RC   ECO:0000313|Proteomes:UP000036503};
RA   Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A.,
RA   Han S., Martens-Habbena W., Neal-McKinney J., Janagama H.K.,
RA   Nadala C., Samadpour M.;
RT   "Draft genome sequence of beer spoilage bacterium Megasphaera
RT   cerevisiae type strain 20462.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KMO85627.1}.
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DR   EMBL; LEKT01000053; KMO85627.1; -; Genomic_DNA.
DR   RefSeq; WP_048515187.1; NZ_LEKT01000053.1.
DR   EnsemblBacteria; KMO85627; KMO85627; AB840_12540.
DR   PATRIC; fig|1122219.3.peg.2586; -.
DR   Proteomes; UP000036503; 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   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KMO85627.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036503};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036503};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   426 AA;  46298 MW;  F658CF034BB81BA8 CRC64;
     MNTSIQDLLQ FIHQSTSPYH TVKTAIDQLK AAGFTELSSN TRWHLHPHGL YYVPIFDSTL
     LAFSIGANPR KHLRLAAAHT DFPCLRIKPS AAVTAGGYGK LNVEIYGGMI RESWLDRPLS
     LAGKIAITGA GPFHPDIRFI DTHRPVMTIP RLAIHMNHKI NEGITLNPQK DMLPLTTLCT
     TGEDDSAFFL SFVASVCNCT PKDILSYELT VYPAEDGCLL GLHDEFISSP RLDNLTSVLA
     CLTGLTSNTA ADGINMIALF DNEEVGSRTK QGAASLVIPN LLQRLYTNLG YDIEEYYTAL
     ADAFVLSIDV AHAMHPNVPE KCDITNVPIL GNGIALKTAC SQSYAGDAEA VAVITSLCQQ
     EKIPFQHYVN RSDIAGGSTL GSLLSANLPV RTMDIGIPIL AMHSARELMG TADQKSLQNL
     VTAFFK
//
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