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ECOLI:RBN
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | rbn (synonyms: elaC, rnz) | |
Protein Name(s) | Ribonuclease BN (ECO:0000255 with HAMAP-Rule:MF_01818)
RNase BN (ECO:0000255 with HAMAP-Rule:MF_01818) Ribonuclease Z homolog (ECO:0000255 with HAMAP-Rule:MF_01818) RNase Z homolog (ECO:0000255 with HAMAP-Rule:MF_01818) | |
External Links | ||
UniProt | P0A8V0 | |
EMBL | U58768 U00096 AP009048 | |
PIR | B64998 | |
RefSeq | NP_416771.4 WP_001300687.1 | |
PDB | 2CBN | |
PDBsum | 2CBN | |
ProteinModelPortal | P0A8V0 | |
SMR | P0A8V0 | |
BioGrid | 4263118 | |
DIP | DIP-9498N | |
IntAct | P0A8V0 | |
MINT | MINT-1275952 | |
STRING | 511145.b2268 | |
PaxDb | P0A8V0 | |
PRIDE | P0A8V0 | |
EnsemblBacteria | AAC75328 BAA16095 | |
GeneID | 946760 | |
KEGG | ecj:JW2263 eco:b2268 | |
PATRIC | 32119903 | |
EchoBASE | EB4008 | |
EcoGene | EG14260 | |
eggNOG | ENOG4105IES COG1234 | |
HOGENOM | HOG000272419 | |
InParanoid | P0A8V0 | |
KO | K00784 | |
OMA | SYAFCSD | |
OrthoDB | EOG61P6TK | |
PhylomeDB | P0A8V0 | |
BioCyc | EcoCyc:G7175-MONOMER ECOL316407:JW2263-MONOMER MetaCyc:G7175-MONOMER | |
BRENDA | 3.1.26.11 | |
SABIO-RK | P0A8V0 | |
EvolutionaryTrace | P0A8V0 | |
PRO | PR:P0A8V0 | |
Proteomes | UP000000318 UP000000625 | |
GO | GO:0042781 GO:0004532 GO:0004518 GO:0008270 GO:0090503 GO:0034414 GO:0008033 | |
Gene3D | 3.60.15.10 | |
HAMAP | MF_01818 | |
InterPro | IPR001279 IPR013469 IPR013471 | |
Pfam | PF12706 | |
SMART | SM00849 | |
SUPFAM | SSF56281 | |
TIGRFAMs | TIGR02651 TIGR02649 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0004519 |
zinc ion binding |
ECO:0000314 |
F |
In Fig. 1b, the ZiPD dimerization interface is in the region of helices α1, α2, and α3, and the dimer is arranged with the monomers in a head-to-head fashion with the exosite tails extending away from each other. A narrow cleft is formed jointly by the two monomers in which the active site and metal coordination residues are present. |
complete | |||||
GO:0004519 |
endonuclease activity |
ECO:0000314 |
F |
E. Coli's ZiPD gene has been identified as an endonuclease which cleaves the 3′ extension from various tRNA precursors, which makes it a tRNase Z enzyme. This was proven by comparing the structure of E Coli's tRNase Z to the structure of various known tRNase Z structures. This comparison can be seen in figure 4. |
complete | |||||
GO:0000100 |
S-methylmethionine transmembrane transporter activity |
other:GO REF: 10097147 |
ECO:0000250 |
UniProtKB: P0A8V0
|
F |
Blastp results showed 100.0% sequence similarity with Bacillus phage Vinny and HHpred showed a 100% probability and a e-value of 3.2E-28 |
complete | |||
enables |
GO:0042781 |
3'-tRNA processing endoribonuclease activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG14260 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0008033 |
tRNA processing |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004532 |
exoribonuclease activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004518 |
nuclease activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0042781 |
3'-tRNA processing endoribonuclease activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016896 |
exoribonuclease activity, producing 5'-phosphomonoesters |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016896 |
exoribonuclease activity, producing 5'-phosphomonoesters |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0016891 |
endoribonuclease activity, producing 5'-phosphomonoesters |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0034414 |
tRNA 3'-trailer cleavage, endonucleolytic |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0042781 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0034414 |
tRNA 3'-trailer cleavage, endonucleolytic |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0042781 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0090502 |
RNA phosphodiester bond hydrolysis, endonucleolytic |
ECO:0000366 |
evidence based on logical inference from automatic annotation used in automatic assertion |
GO:0016891 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0090502 |
RNA phosphodiester bond hydrolysis, endonucleolytic |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0016891 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0090503 |
RNA phosphodiester bond hydrolysis, exonucleolytic |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0004532 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0090503 |
RNA phosphodiester bond hydrolysis, exonucleolytic |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0016896 |
P |
Seeded From UniProt |
complete | ||
involved_in |
GO:0090503 |
RNA phosphodiester bond hydrolysis, exonucleolytic |
ECO:0000364 |
evidence based on logical inference from manual annotation used in automatic assertion |
GO:0016896 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0016891 |
endoribonuclease activity, producing 5'-phosphomonoesters |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0042779 |
tRNA 3'-trailer cleavage |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004527 |
exonuclease activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001276 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0004519 |
endonuclease activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001276 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0008033 |
tRNA processing |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001276 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0008270 |
zinc ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
UniRule:UR000001276 |
F |
Seeded From UniProt |
complete | ||
enables |
GO:0004527 |
exonuclease activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004519 |
endonuclease activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004518 |
nuclease activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0008033 |
tRNA processing |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 Kostelecky, B et al. (2006) The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins. J. Bacteriol. 188 1607-14 PubMed GONUTS page
- ↑ Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 Callahan, C et al. (2000) Purification and characterization of the tRNA-processing enzyme RNase BN. J. Biol. Chem. 275 1030-4 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 Dutta, T & Deutscher, MP (2009) Catalytic properties of RNase BN/RNase Z from Escherichia coli: RNase BN is both an exo- and endoribonuclease. J. Biol. Chem. 284 15425-31 PubMed GONUTS page
- ↑ Vogel, A et al. (2004) Identification of metal binding residues for the binuclear zinc phosphodiesterase reveals identical coordination as glyoxalase II. Biochemistry 43 10379-86 PubMed GONUTS page
- ↑ Dutta, T & Deutscher, MP (2010) Mode of action of RNase BN/RNase Z on tRNA precursors: RNase BN does not remove the CCA sequence from tRNA. J. Biol. Chem. 285 22874-81 PubMed GONUTS page
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