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Database: UniProt
Entry: A0A0N0S562_9ACTN
LinkDB: A0A0N0S562_9ACTN
Original site: A0A0N0S562_9ACTN 
ID   A0A0N0S562_9ACTN        Unreviewed;       432 AA.
AC   A0A0N0S562;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-SEP-2017, entry version 8.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467};
GN   ORFNames=ADK41_28850 {ECO:0000313|EMBL:KOT32531.1};
OS   Streptomyces caelestis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT32531.1, ECO:0000313|Proteomes:UP000037773};
RN   [1] {ECO:0000313|EMBL:KOT32531.1, ECO:0000313|Proteomes:UP000037773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT32531.1,
RC   ECO:0000313|Proteomes:UP000037773};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, 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:KOT32531.1}.
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DR   EMBL; LGCN01000228; KOT32531.1; -; Genomic_DNA.
DR   RefSeq; WP_030819942.1; NZ_LGCN01000228.1.
DR   EnsemblBacteria; KOT32531; KOT32531; ADK41_28850.
DR   PATRIC; fig|36816.3.peg.6252; -.
DR   Proteomes; UP000037773; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KOT32531.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037773};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037773};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        86     86       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       157    157       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       408    408       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   432 AA;  45879 MW;  35115DD4264A9BE2 CRC64;
     MSAPSRFDRG HTDDLMSFLA ASPTPYHAVA NAAERLEKAG FRQVAETDAW DGSAGGRYVL
     RGGAIIAWYV PEGADAHTPF RIVGAHTDSP NLRVKPRPDS GAHGWRQLAV EIYGGPLLNS
     WLDRDLGLAG RLSLRDGSTR LVDVDRPLLR VPQLAVHLDR SVNSDGLKLD KQRHMQPVWG
     LGDDVRDGDL IAFLEETAGI PSGEVTGWDL MVHSVEPPAY LGRDRELVAG PRMDNLLSVH
     AGTAALAAVA GKGSGLSHIP VLAAFDHEEN GSQSDSGADG PLLGGVLERS VFARGGSYED
     RARAFAGTVC LSSDTGHAVH PNYAERHDPT HHPRVDGGPL LKVNVNNRYA TDGFGRAVFA
     AACEKAGVPF QSFVSNNAMP CGTTIGPITA ARHGIRTVDI GVAILSMHSA RELCGAKDPF
     LLANALVAFL DG
//
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