Difference between revisions of "Cca"
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=References= | =References= | ||
+ | ==Reviews== | ||
+ | <pubmed> 19883645 16364630 20155482 18523015 </pubmed> | ||
+ | ==Original publications== | ||
<pubmed>17179213,12526808,20360175 ,9829937, 16109934 </pubmed> | <pubmed>17179213,12526808,20360175 ,9829937, 16109934 </pubmed> | ||
==Operon and expression== | ==Operon and expression== | ||
<pubmed> 20308541 </pubmed> | <pubmed> 20308541 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:21, 17 October 2010
- Description: tRNA nucleotidyltransferase, maturation of the single-copy tRNACys, which lacks an encoded CCA 3' end
Gene name | cca |
Synonyms | papS, ypjI |
Essential | yes PubMed |
Product | tRNA nucleotidyltransferase |
Function | tRNA modification |
MW, pI | 45 kDa, 8.041 |
Gene length, protein length | 1191 bp, 397 aa |
Immediate neighbours | birA, bshA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context ![]() This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU22450
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + tRNA(n) = diphosphate + tRNA(n+1) (according to Swiss-Prot)
- Protein family: the protein is similar to the E. coli poly(A) polymerase
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 1MIV (Geobacillus stearothermophilus 44% identity)
- UniProt: P42977
- KEGG entry: [2]
- E.C. number: 2.7.7.25
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Heike Betat, Christiane Rammelt, Mario Mörl
tRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization.
Cell Mol Life Sci: 2010, 67(9);1447-63
[PubMed:20155482]
[WorldCat.org]
[DOI]
(I p)
Stefan Vörtler, Mario Mörl
tRNA-nucleotidyltransferases: highly unusual RNA polymerases with vital functions.
FEBS Lett: 2010, 584(2);297-302
[PubMed:19883645]
[WorldCat.org]
[DOI]
(I p)
Anne Neuenfeldt, Andrea Just, Heike Betat, Mario Mörl
Evolution of tRNA nucleotidyltransferases: a small deletion generated CC-adding enzymes.
Proc Natl Acad Sci U S A: 2008, 105(23);7953-8
[PubMed:18523015]
[WorldCat.org]
[DOI]
(I p)
Yong Xiong, Thomas A Steitz
A story with a good ending: tRNA 3'-end maturation by CCA-adding enzymes.
Curr Opin Struct Biol: 2006, 16(1);12-7
[PubMed:16364630]
[WorldCat.org]
[DOI]
(P p)
Original publications
Operon and expression