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Database: UniProt
Entry: A0A0L0BAW7_9MICC
LinkDB: A0A0L0BAW7_9MICC
Original site: A0A0L0BAW7_9MICC 
ID   A0A0L0BAW7_9MICC        Unreviewed;       427 AA.
AC   A0A0L0BAW7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-OCT-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=AC792_15045 {ECO:0000313|EMBL:KNC17245.1};
OS   Arthrobacter sp. RIT-PI-e.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1681197 {ECO:0000313|EMBL:KNC17245.1, ECO:0000313|Proteomes:UP000053253};
RN   [1] {ECO:0000313|Proteomes:UP000053253}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-e {ECO:0000313|Proteomes:UP000053253};
RA   Tran P.N., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-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:KNC17245.1}.
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DR   EMBL; LGIU01000098; KNC17245.1; -; Genomic_DNA.
DR   RefSeq; WP_049831302.1; NZ_LGIU01000098.1.
DR   EnsemblBacteria; KNC17245; KNC17245; AC792_15045.
DR   PATRIC; fig|1681197.3.peg.513; -.
DR   Proteomes; UP000053253; 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   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:KNC17245.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053253};
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:UP000053253};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   427 AA;  44708 MW;  EB05105AB2377438 CRC64;
     MSPSPAHITD LGACVTASPS SFHAVAEAAR RLSAAGFRPL AEQDAWDGGP GRYHVVRDGA
     LIAWHVPDSA DATTGFHILG AHTDSPSFKL KPKPTTGKYG WLQAGGEVYG GPLLNSWLDR
     ELALAGRLTL RDGSEHLVAT GPLLRFPQLA IHLDRAVNDG LALDKQRHMN PVWGLGDHAD
     EDLLGVLAAD AGVDPGEIGG FDVVVADTQE PRVLGARGEF LASGRLDNLS SVHAGLTALL
     DAAEHGPADG PIAVLAAFDH EEVGSGSRSG ASGPFLEDML LRISLGLGAG TEERLRALAS
     SFCVSADAGH AVHPNYAERH DPANLPVLNR GPLLKINANQ RYTTDAPGAA YWAALCRDSG
     VPYQEFVSNN VMPCGSTIGP LTATRLGIRT VDVGTPLLSM HSARELCGVD DPGHLATVTA
     AFFRGGR
//
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