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Database: UniProt
Entry: A0A0M2LYL0_9MICO
LinkDB: A0A0M2LYL0_9MICO
Original site: A0A0M2LYL0_9MICO 
ID   A0A0M2LYL0_9MICO        Unreviewed;       426 AA.
AC   A0A0M2LYL0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 9.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=XM48_01005 {ECO:0000313|EMBL:KKI22590.1};
OS   Leucobacter sp. Ag1.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI22590.1, ECO:0000313|Proteomes:UP000033836};
RN   [1] {ECO:0000313|EMBL:KKI22590.1, ECO:0000313|Proteomes:UP000033836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag1 {ECO:0000313|EMBL:KKI22590.1,
RC   ECO:0000313|Proteomes:UP000033836};
RA   Pei D., Kukutla P., Yu W., Xu J.;
RT   "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT   gambiae.";
RL   Submitted (APR-2015) 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}.
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:KKI22590.1}.
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DR   EMBL; LAYO01000050; KKI22590.1; -; Genomic_DNA.
DR   RefSeq; WP_046453912.1; NZ_LAYO01000050.1.
DR   EnsemblBacteria; KKI22590; KKI22590; XM48_01005.
DR   PATRIC; fig|1642040.3.peg.3302; -.
DR   Proteomes; UP000033836; 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   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|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KKI22590.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033836};
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:UP000033836};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   426 AA;  44441 MW;  0CBA4BCD59A01978 CRC64;
     MGTVLQDRDR YIDQFTEFVE ASPTSYHAVA SLAEALVAAG FVEHREADAW LGIEPAGRGF
     VRRDGALIAW RAGSAVHAAS PVRVFGCHTD SPGFVLKPQP DTQAEGWAQL GVEVYGGPLL
     NSWLDRDLAI AGRLVLRDGS EALARTGAVA RIPQLAIHLD RGVNNGLTLD KQRHTQPIVG
     LGEVSAVELL ARSAGVDAAD VVAMDARVAD AQAPARIGAE GELLASPRLD NLSSVVAGLA
     AIVETEPAAD SIAMLAAFDH EELGSESRSG ASGPFLEEVL DRLRAGLGAD VEDAARGLAG
     SWCLSADAGH SVHPNYPERH DPQVRPRAGQ GPMLKVNANQ RYASDAHGAA LWTRCCAAAG
     IGTQEFVSNN GVPCGTTIGP LTATRIGIRT VDVGVPLLSM HSARELAHVD DLHGLAKAAG
     GFFAGA
//
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