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Database: UniProt
Entry: A0A0X3UU05_9ACTN
LinkDB: A0A0X3UU05_9ACTN
Original site: A0A0X3UU05_9ACTN 
ID   A0A0X3UU05_9ACTN        Unreviewed;       431 AA.
AC   A0A0X3UU05;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-NOV-2017, entry version 10.
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=ADL22_25885 {ECO:0000313|EMBL:KUL36000.1};
OS   Streptomyces sp. NRRL F-4489.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL36000.1, ECO:0000313|Proteomes:UP000053256};
RN   [1] {ECO:0000313|EMBL:KUL36000.1, ECO:0000313|Proteomes:UP000053256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL36000.1,
RC   ECO:0000313|Proteomes:UP000053256};
RA   Millard Andrew;
RL   Submitted (OCT-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:KUL36000.1}.
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DR   EMBL; LLZI01000254; KUL36000.1; -; Genomic_DNA.
DR   RefSeq; WP_066984575.1; NZ_LLZI01000254.1.
DR   EnsemblBacteria; KUL36000; KUL36000; ADL22_25885.
DR   Proteomes; UP000053256; 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   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|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KUL36000.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053256};
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:UP000053256};
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       407    407       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   431 AA;  46061 MW;  3ECC63780336EAA6 CRC64;
     MTNSARFDRG HTDDLMSFLA ASPSPYHAVA NAAERLEKAG FRQVAETDEW DGRSGGRYVL
     RGGAIIAWYV PEGAEPSTPF RIVGAHTDSP NLRVKPIPDT GSRGWRQIAV EIYGGTLLNT
     WLDRDLGLSG RITLADGSDR LVHVDRALLR VPQLAVHLDR SVNSEGLKLD KQRHMTPIWG
     LGEVAEGDLI AFVAEEAGVP AEDVKGWDLM VHSVEPPAYL GRDRELLAGP RMDNLLSVHA
     GTAALAAAAT SDTRPAAIPV LAAFDHEENG SQSDTGADGP LLGTVLERSV FARGGTYEDR
     ARAFAGTICL SSDTGHAVHP NYSERHEPGH HPMPNGGPIL KVNVNQRYAT DGSGRAVFAA
     ACERAGVPWQ SFVSHNAMPC GTTIGPITAA RHGIRTVDIG VAILSMHSAR ELCGAEDPYL
     LANALTAFLE S
//
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