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Database: UniProt
Entry: W5TDV3_9NOCA
LinkDB: W5TDV3_9NOCA
Original site: W5TDV3_9NOCA 
ID   W5TDV3_9NOCA            Unreviewed;       429 AA.
AC   W5TDV3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   22-NOV-2017, entry version 19.
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=NONO_c05940 {ECO:0000313|EMBL:AHH15406.1};
OS   Nocardia nova SH22a.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH15406.1, ECO:0000313|Proteomes:UP000019150};
RN   [1] {ECO:0000313|EMBL:AHH15406.1, ECO:0000313|Proteomes:UP000019150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH22a {ECO:0000313|EMBL:AHH15406.1};
RX   PubMed=24747905;
RA   Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT   "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT   Analysis of the Complete Genome of Nocardia nova SH22a.";
RL   Appl. Environ. Microbiol. 80:3895-3907(2014).
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}.
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DR   EMBL; CP006850; AHH15406.1; -; Genomic_DNA.
DR   RefSeq; WP_025346936.1; NZ_CP006850.1.
DR   EnsemblBacteria; AHH15406; AHH15406; NONO_c05940.
DR   KEGG; nno:NONO_c05940; -.
DR   PATRIC; fig|1415166.3.peg.607; -.
DR   KO; K01267; -.
DR   Proteomes; UP000019150; Chromosome.
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:AHH15406.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019150};
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:UP000019150};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        84     84       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       158    158       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       403    403       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   429 AA;  45496 MW;  8D800ED25307CA2C CRC64;
     MSVPTTATAS GLCAFVDSSP SPFHVCRTAA AELAAHGFTE LPETRPWTRT EAIGRYFVIR
     GGSLVAWVSG KRNPAGAFRV VGAHTDSPNL RVKQHPDLAV AGWQLIGLEP YGGAWLNSWL
     DRDLGISGRL TVRAGDGLGE RLVRIDDPLV RVPQLAIHLS EDRRGVTLDP QRHVNGIWGL
     GERPRSFITY VAEWAGVPVD DVLGWELMTH DLEPSRLVGR DQDLVSAPRL DNQATCYAGL
     RAFLAAADTA GDTTPVLAMF DHEEVGSQSD RGAQSDLLPA ILERIVLARG GGRADYLAAL
     AGSICASGDM AHATHPNYPE RHEPAHRIEV GGGPVLKVNQ NLRYATDAVG AGAFALACAQ
     AGVPLQRYVH RADLPCGSTI GPMTAARTGM PTVDVGAPQL AMHSARELMG ADDVGAYAAA
     LAAFLAPGR
//
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