| Tag | Content |
|---|
| CPLM ID | CPLM-010078 |
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 | MPN_480; MP361 |
Created Date | July 27, 2013 |
Organism | Mycoplasma pneumoniae (strain ATCC 29342 / M129) |
NCBI Taxa ID | 272634 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 93 | AGIATQTKYEKLARE | acetylation | [1] | | 96 | ATQTKYEKLARETNP | acetylation | [1] |
|
Reference | [1] Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium. van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ, Kühner S, Kumar R, Maier T, O'Flaherty M, Rybin V, Schmeisky A, Yus E, Stülke J, Serrano L, Russell RB, Heck AJ, Bork P, Gavin AC. Mol Syst Biol. 2012 Feb 28;8:571. [ PMID: 22373819] |
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 46 56 "HIGH" region.
MOTIF 514 518 "KMSKS" region.
BINDING 517 517 ATP (By similarity). |
Keyword | Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 838 AA |
Protein Sequence | MDKQFSFQGQ YDFKTVSTGL YDSWSSASFF KPQKNKVPFT AILPPPNLTG TLHIGHAFEV 60
SITDQIMRFK RLRGYGVNWI PGFDHAGIAT QTKYEKLARE TNPEYFQAPR KQKVKMIMDW 120
ALTQGDTIQS QIKSLGASLN WNQVNFTLSK KASQIVNDSF IQLFEQGFIY QAETLVNWDT 180
KLNTAISNIE VINKPVDQQL YYIAYKLANN PKKRLVVATT RPETIFVDVC LFVHPKDKHY 240
HSFVKQKVVN PLTGALMPVF TDSYVDKKFG TGVLKCTPAH DFNDFALNEK YRLPFVSCID 300
HNGLLNEHAK QFTGLTVSAA RQQVVEFLQT QKLLVKTMPL TSNVGFSERS DTVVEPLLSK 360
QWFVDLPKLK KALAIKKYPE LIPKRFNKQV TRWLSQLKPW CISRQLIWGH PIPVWTHKQS 420
GALHVGSTAP TDKQNYTQST DVLDTWFSSS LWPLICLDWH KNKHFVPTDL LVTGYDILFF 480
WVLRMTFNSY FQTKQLPFKQ VLIHGLVRDA QNRKMSKSLN NGINPMDLIR DYGADATRLF 540
LTSNHTPGDD LIFNEQKLKS AANFLNKLWN VTKYVLQLGE QAKTVPSTHL PSTLSERWIW 600
AKLKQLIVQT TKLLDKYQLA LANQALVNFI WNDFCNTFIE TIKQEDTALL PQLYTTAKTV 660
LSTAVVMLST VTPFLAERIY QQFHSGSVMQ ASWPTAKAVK PPKLFADVVE AVSSLRHYKA 720
NNQLVANQNL AVVLSGKAAP VVQNYFHFNW VDLRIEVNKT PGFQIKIVDN AANNLAHLEK 780
QRSFYLAEVQ RSQAITTNPA FLKKAPPHKV KAELLKLEEY QKKLAEVNHL IAKLTKAE 838 |
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 | |