Unfortunately due to lack of commercial feasibility, the SkyBLAST service has been suspended from December 1st, 2025.
All subscriptions for paid accounts have been paused. For further information or enquiries, please email [email protected]
LOCUS WP_017009038 160 aa linear BCT 02-JUN-2019 ACCESSION WP_017009038 VERSION WP_017009038.1 KEYWORDS RefSeq. SOURCE Enterovibrio norvegicus ORGANISM Enterovibrio norvegicus Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; Enterovibrio. REFERENCE 1 (residues 1 to 160) AUTHORS Kumar,S., Das,M., Hadad,C.M. and Musier-Forsyth,K. TITLE Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK JOURNAL J Phys Chem B 117 (16), 4521-4527 (2013) PUBMED 23185990 REFERENCE 2 (residues 1 to 160) AUTHORS An,S. and Musier-Forsyth,K. TITLE Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel synthetase.YbaK.tRNA ternary complex JOURNAL J. Biol. Chem. 280 (41), 34465-34472 (2005) PUBMED 16087664 REFERENCE 3 (residues 1 to 160) AUTHORS Wong,F.C., Beuning,P.J., Silvers,C. and Musier-Forsyth,K. TITLE An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing JOURNAL J. Biol. Chem. 278 (52), 52857-52864 (2003) PUBMED 14530268 REFERENCE 4 (residues 1 to 160) AUTHORS Zhang,H., Huang,K., Li,Z., Banerjei,L., Fisher,K.E., Grishin,N.V., Eisenstein,E. and Herzberg,O. TITLE Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications JOURNAL Proteins 40 (1), 86-97 (2000) PUBMED 10813833 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR00011.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..160 /organism="Enterovibrio norvegicus" /db_xref="taxon:188144" gene 1..160 /gene="ybaK" Protein 1..160 /product="Cys-tRNA(Pro) deacylase" /GO_function="GO:0002161 - aminoacyl-tRNA editing activity [Evidence IEA]" /GO_process="GO:0043039 - tRNA aminoacylation [Evidence IEA]" /calculated_mol_wt=16855 Region 1..157 /region_name="YbaK_like" /note="YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, ProX, and PrdX. The primary function of INS is to hydrolyze...; cl00022" /db_xref="CDD:444658" Site order(46,101..102,129) /site_type="active" /note="putative deacylase active site [active]" /db_xref="CDD:237976" ORIGIN 1 mtpaiilaek sgisfhvhsy ehdpnnthfg leaasvlgqd asrvfktllf tmngdpkklt 61 vaivpvagql dlkaaakaag akkaemanpv iaekttgyvv ggisplgqkk rlptlldksa 121 eqfetiyvsa grrgleielt psdlltltqg kmaeigkegk