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ECOLI:RBN

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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

PMID:16452444[1]

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
CACAO 11639

GO:0004519

endonuclease activity

PMID:16452444[1]

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
CACAO 11908

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
CACAO 11911

enables

GO:0042781

3'-tRNA processing endoribonuclease activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG14260
PANTHER:PTN000284960

F

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

PMID:10625642[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004532

exoribonuclease activity

PMID:10625642[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

PMID:19366704[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

PMID:16452444[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

PMID:15301536[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042781

3'-tRNA processing endoribonuclease activity

PMID:20489203[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016896

exoribonuclease activity, producing 5'-phosphomonoesters

PMID:19366704[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016896

exoribonuclease activity, producing 5'-phosphomonoesters

PMID:10625642[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016891

endoribonuclease activity, producing 5'-phosphomonoesters

PMID:19366704[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0034414

tRNA 3'-trailer cleavage, endonucleolytic

GO_REF:0000108

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

GO_REF:0000108

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

GO_REF:0000108

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

GO_REF:0000108

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

GO_REF:0000108

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

GO_REF:0000108

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

GO_REF:0000108

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

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013469
InterPro:IPR013471

F

Seeded From UniProt

complete

involved_in

GO:0042779

tRNA 3'-trailer cleavage

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR013469
InterPro:IPR013471

P

Seeded From UniProt

complete

enables

GO:0004527

exonuclease activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001276

F

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001276

F

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001276

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001276

F

Seeded From UniProt

complete

enables

GO:0004527

exonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0269

F

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0255

F

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0540

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

involved_in

GO:0008033

tRNA processing

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0819

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 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
  2. 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. 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. 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
  5. 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
  6. 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