HMM Summary Page: TIGR00011
Accession | TIGR00011 |
Name | YbaK_EbsC |
Function | Cys-tRNA(Pro) deacylase |
Gene Symbol | ybaK |
Trusted Cutoff | 153.25 |
Domain Trusted Cutoff | 153.25 |
Noise Cutoff | 70.15 |
Domain Noise Cutoff | 70.15 |
Isology Type | hypoth_equivalog |
EC Number | 3.6.1.- |
HMM Length | 152 |
Mainrole Category | Unknown function |
Subrole Category | General |
Author | Richardson DL, Haft DH |
Entry Date | Apr 20 1999 2:04PM |
Last Modified | Aug 12 2012 7:41PM |
Comment | This HMM represents the YbaK family, bacterial proteins whose full length sequence is homologous to an insertion domain in proline--tRNA ligases. The domain deacylates mischarged tRNAs. The YbaK protein of Haemophilus influenzae (HI1434) likewise deacylates Ala-tRNA(Pro), but not the correctly charged Pro-tRNA(Pro). A crystallographic study of HI1434 suggests a nucleotide binding function. Previously, a member of this family was described as EbsC and was thought to be involved in cell wall metabolism. |
References | DR PFAM; PF04073 RN [1] RM PMID:16087664 RT Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel synthetase.YbaK.tRNA ternary complex. RA An S, Musier-Forsyth K RL J Biol Chem. 2005 Oct 14;280(41):34465-72. Epub 2005 Aug 8. RN [2] RM 14530268 RT An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing. RA Wong FC, Beuning PJ, Silvers C, Musier-Forsyth K. RL J Biol Chem. 2003 Dec 26;278(52):52857-64. RN [3] RM 10813833 RT Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications. RA Zhang H, Huang K, Li Z, Banerjei L, Fisher KE, Grishin NV, Eisenstein E, Herzberg O RL Proteins 2000 Jul 1;40(1):86-97 |