HMM Summary Page: TIGR02258
Accession | TIGR02258 |
Name | 2_5_ligase |
Function | 2'-5' RNA ligase |
Trusted Cutoff | 65.70 |
Domain Trusted Cutoff | 65.70 |
Noise Cutoff | 47.30 |
Domain Noise Cutoff | 47.30 |
Isology Type | equivalog |
EC Number | 6.5.1.- |
HMM Length | 180 |
Mainrole Category | Transcription |
Subrole Category | RNA processing |
Gene Ontology Term | GO:0008033: tRNA processing biological_process |
GO:0008664: 2'-5'-RNA ligase activity molecular_function | |
Author | Haft DH |
Entry Date | Aug 18 2004 5:08PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This protein family consists of bacterial and archaeal proteins with two tandem copies of Pfam domain PF02834. Members for which activity has been measured perform a reversible, ATP-independent 2'-5'-ligation of what is presumably a non-phyiological substrate: half-tRNA splice intermediates from an intron-containing yeast tRNA. The physiological substrate(s) in prokaryotes may include small 2'-5'-link-containing oligonucleotides, perhaps with regulatory or biosynthetic roles. |
References | DR PFAM; PF02834; 2_5_RNA_ligase RN [1] RM 8940112 RT The 2'-5' RNA ligase of Escherichia coli. Purification, cloning, and genomic disruption. RA Arn EA, Abelson JN. RL J Biol Chem. 1996 Dec 6;271(49):31145-53. RN [2] RM 12798681 RT Crystal structure of the 2'-5' RNA ligase from Thermus thermophilus HB8. RA Kato M, Shirouzu M, Terada T, Yamaguchi H, Murayama K, Sakai H, Kuramitsu S, Yokoyama S. RL J Mol Biol. 2003 Jun 20;329(5):903-11. |