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Database: UniProt
Entry: A0A010NFC8_9MICC
LinkDB: A0A010NFC8_9MICC
Original site: A0A010NFC8_9MICC 
ID   A0A010NFC8_9MICC        Unreviewed;       442 AA.
AC   A0A010NFC8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   07-JUN-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=BG28_03840 {ECO:0000313|EMBL:EXF24842.1};
OS   Nesterenkonia sp. AN1.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Nesterenkonia.
OX   NCBI_TaxID=652017 {ECO:0000313|EMBL:EXF24842.1, ECO:0000313|Proteomes:UP000022206};
RN   [1] {ECO:0000313|EMBL:EXF24842.1, ECO:0000313|Proteomes:UP000022206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AN1 {ECO:0000313|EMBL:EXF24842.1,
RC   ECO:0000313|Proteomes:UP000022206};
RX   PubMed=24675854;
RA   Aliyu H., De Maayer P., Rees J., Tuffin M., Cowan D.A.;
RT   "Draft Genome Sequence of the Antarctic Polyextremophile Nesterenkonia
RT   sp. Strain AN1.";
RL   Genome Announc. 2:e00197-14(2014).
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:EXF24842.1}.
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DR   EMBL; JEMO01000015; EXF24842.1; -; Genomic_DNA.
DR   RefSeq; WP_036475746.1; NZ_JEMO01000015.1.
DR   EnsemblBacteria; EXF24842; EXF24842; BG28_03840.
DR   PATRIC; fig|652017.6.peg.1783; -.
DR   Proteomes; UP000022206; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EXF24842.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000022206};
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:UP000022206};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   442 AA;  45927 MW;  A0A4F8915F3190F8 CRC64;
     MASMTSEELI EDLADYVTAS PSSYHAATVA AQRLVSAGFT QLGEHQDWPA EPGRYVVVRD
     GAVLAWVVPA GASPMTPLRI LGAHTDSPGF KLKPKSTMIS QGWLQAGVEV YGGPLLNSWL
     DRELRLAGRL VTRDGATHLA STGPVARIPQ LAIHLDRQVN EGLKLGKQAH TAPILGLAGS
     AEQAAAADVL GLLAASAGVD PAQVDGYDVV LADAQAPATF GAAQEFLASS RLDNLSSVHA
     GLSALIGTAE AAEAGTVIPM LAAFDHEELG SASRSGAAGP FLEEVLGRIY EGLGRAAGQP
     DATTTQRAQA LAASWHLSSD AGHAVHPNYS ERHDPANRPL PNGGPLLKIN ANQRYTTDAP
     GAAMWAQVCR AAGVPTQEFV SNNDLPCGST IGPITATRLG IRTVDVGIAL LSMHSAREMC
     GVQDIAHLRD AVASFFTTSL NS
//
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