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Database: UniProt
Entry: A0A0B4RZX9_9FIRM
LinkDB: A0A0B4RZX9_9FIRM
Original site: A0A0B4RZX9_9FIRM 
ID   A0A0B4RZX9_9FIRM        Unreviewed;       457 AA.
AC   A0A0B4RZX9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUL-2017, entry version 14.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=NW74_00640 {ECO:0000313|EMBL:AIZ35981.1};
OS   Parvimonas micra.
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Parvimonas.
OX   NCBI_TaxID=33033 {ECO:0000313|EMBL:AIZ35981.1, ECO:0000313|Proteomes:UP000031386};
RN   [1] {ECO:0000313|EMBL:AIZ35981.1, ECO:0000313|Proteomes:UP000031386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCOM 1535 / ChDC B708 {ECO:0000313|Proteomes:UP000031386};
RA   Kook J.-K., Park S.-N., Lim Y.K., Roh H.;
RT   "Complete genome sequence of Parvimonas micra KCOM 1535 (= ChDC
RT   B708).";
RL   Submitted (OCT-2014) 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}.
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DR   EMBL; CP009761; AIZ35981.1; -; Genomic_DNA.
DR   RefSeq; WP_041953309.1; NZ_CP009761.1.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; AIZ35981; AIZ35981; NW74_00640.
DR   KEGG; pmic:NW74_00640; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   Proteomes; UP000031386; 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   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:AIZ35981.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031386};
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:UP000031386};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   457 AA;  50889 MW;  D5FC792F7BBF1BC9 CRC64;
     MTNKSAWLQI EDAEKDLVFS FCEDYKKFLS VAKTERLACT EIIRQAKEKG FRDLEELYKS
     GEKFKAGDKF YINHKNKSVA LFVMGTEPLE NGLNIVGAHI DSPRLDVKQN PLYEANNLSK
     LKTHYYGGIK LYQYATIPLA IHGVVYNSAG EKIDIHIGED KGDPVFCVTD LLIHLSKNQL
     GKTAREALVG EQMNILMGSI PLKDTEKDAV KENVLKLIKE KYNFEEEDFK IAELEIVPAG
     EARDLGFDRS MVLSYGQDDR VCAFTTMRAI FEIENPKKTA CGLFMDKEEI GSMGNTGMAS
     YFWENTMTEL VNLEGEFCQL KVNRSLKNSK VLSADVTVGF DPDFPDVCEQ MNSAFIGSGI
     SICKYTGSGG KFGSSDANAE FLAEVRKVFK EHNVVWQTSE LGKVDQGGGG TIALLLAKYG
     AEVLDAGPAT LSMHSPYEVT SKIDVYMSYK AYKAFML
//
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