| Tag | Content |
|---|
| CPLM ID | CPLM-015041 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Valine--tRNA ligase |
Protein Synonyms/Alias | Valyl-tRNA synthetase; ValRS |
Gene Name | valS |
Gene Synonyms/Alias | RPA2583 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 281 | EKGSGAVKITPAHDF | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner (By similarity). |
Sequence Annotation | MOTIF 45 55 "HIGH" region.
MOTIF 571 575 "KMSKS" region.
BINDING 574 574 ATP (By similarity). |
Keyword | Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 957 AA |
Protein Sequence | MIEKTYQPAD IEARISRAWE DAEAFKAGRP ERRDAVPYSI VIPPPNVTGS LHMGHALNNT 60
LQDILCRFER MRGRDVLWQP GTDHAGIATQ MVVERQLMER QEPSRRDMGR AKFLERVWQW 120
KAESGGVIVN QLKRLGASCD WSRERFTMDE GLSRAVAKVF VELHRQGLIY KDKRLVNWDP 180
KLLTAISDLE VQQIEVKGNL WHLRYPIEGK TFDPADPSSF IVVATTRPET MLGDSAVAVN 240
PEDERYTHLV GKHVILPLVG RRIPIVADEY SDPEKGSGAV KITPAHDFND FEVGKRHHLP 300
QINVLDIEGK ISVADNSAYL EGLPEGAREF AGEIDGTDRF VARKIIVARL DDFGFLEKIE 360
PNVHMVPHGD RSGVVIEPFL TDQWYVDAKT LAQPAIAAVR SGETTFVPKN WEKTYFEWME 420
NIQPWCISRQ LWWGHQIPAW YGPDGKVFVA ETEEEAVGNA LGYYVEQEVI TPAQAHDMAE 480
DPAKREGFIT RDEDVLDTWF SSALWPFSTL GWPDETPELD RYYPTNVLVT GFDIIFFWVA 540
RMMMMGLHFM DDVPFPTVYI HALVRDEKGA KMSKSKGNVI DPLNLIDEYG ADALRFTLAA 600
MAAQGRDIKL ATSRVEGYRN FATKLWNACR FAEMNGCVAP AGFDYTAAKE TLNRWIAHET 660
VRAVREVTEA IESYRFNDAA EAAYRFVWNV YCDWYLELAK PVLMGEEGAA KTETRAMVAW 720
ARDEILKILH PFMPFITEEL WAVTAPRDGL LALAPWSRKG GISDEEVSVL AASAATDPMA 780
GPAMLAIPEP QEPDFTDDAA EAEIGWVVDL VTAIRSVRAE MNIVPSTLTP LVLAGASADT 840
NARASRWSDV IKRLARVGEI SFADAAPQGA VQLLVRGEVA ALPLKGVVDF AAEQARLEKE 900
LGKAEADIKR AEAKLANEKF VANAAEEVVE EEREKREAAV ARKVKILEAL LRLKNAS 957 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0004832; F:valine-tRNA ligase activity; IEA:HAMAP. GO:0006450; P:regulation of translational fidelity; IEA:GOC. GO:0006438; P:valyl-tRNA aminoacylation; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |