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Database: UniProt
Entry: L1KKN2_9ACTN
LinkDB: L1KKN2_9ACTN
Original site: L1KKN2_9ACTN 
ID   L1KKN2_9ACTN            Unreviewed;       432 AA.
AC   L1KKN2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-SEP-2017, entry version 27.
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=STRIP9103_04893 {ECO:0000313|EMBL:EKX61346.1};
OS   Streptomyces ipomoeae 91-03.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX61346.1, ECO:0000313|Proteomes:UP000010411};
RN   [1] {ECO:0000313|EMBL:EKX61346.1, ECO:0000313|Proteomes:UP000010411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91-03 {ECO:0000313|EMBL:EKX61346.1,
RC   ECO:0000313|Proteomes:UP000010411};
RA   Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL   Submitted (NOV-2012) 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:EKX61346.1}.
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DR   EMBL; AEJC01000601; EKX61346.1; -; Genomic_DNA.
DR   RefSeq; WP_009336522.1; NZ_AEJC01000601.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EKX61346; EKX61346; STRIP9103_04893.
DR   PATRIC; fig|698759.3.peg.7909; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000010411; 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:EKX61346.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010411};
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, ECO:0000313|EMBL:EKX61346.1};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EKX61346.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010411};
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;  46229 MW;  ED073D9023BEDAE5 CRC64;
     MRTPPRFDRG HTDDLMSFLT ASPSPYHAVA NAAERLEKAG FRQVSETDAW DGSLGGKYVL
     RGGAIIAWYV PEGADPHTPF RIVGAHTDSP NLRVKPRPDT GGHGFRQVAV EIYGGPLLNS
     WLDRDLGIAG RLSLRDGTSR LVNIDRPLLR VPQLAIHLDR AVTSEGLKLD KQRHLQPIWG
     LGDDIRDGDL ISFLEQESGL PAGEVTGWDL MTHSVEPPAY LGRDKELLAG PRMDNLLSVH
     AGTAALAAVA TSGDDLPYIP VLAAFDHEEN GSQSDTGADG PLLGGVLERS VFARGGSYED
     RARAFAGTVC LSSDTGHAVH PNYAERHDPT HHPRADAGPI LKVNVNNRYA TDGSGRAIFA
     AACERAGVPF QTFVSNNSMP CGTTIGPITA ARHGIRTVDI GVAILSMHSA RELCGAKDPY
     LLTNALAAFL EG
//
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