Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Valine--tRNA ligase |
Protein Synonyms/Alias | ValRS |
Gene Name | valS |
Gene Synonyms/Alias | SSO0899 |
Created Date | 3-June-2014 |
Organism | Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) |
NCBI Taxa ID | 273057 |
Phosphorylation | Position | Peptide | Code | Type | References | 477 | PIDPIKTSPPLEKCP | S | HTP | [1] | 425 | KFKPARMSYYLEDWI | S | HTP | [1] | 427 | KPARMSYYLEDWIKS | Y | HTP | [1] | 476 | LPIDPIKTSPPLEKC | T | HTP | [1] | 426 | FKPARMSYYLEDWIK | Y | HTP | [1] | |
Reference | [1]Change of carbon source causes dramatic effects in the phospho-proteome of the archaeon Sulfolobus solfataricus. Esser D,Pham TK,Reimann J,Albers SV,Siebers B,Wright PC J. Proteome Res. 2012, Oct, 5;11(10):4823-33. [ PMID:22639831] |
Functional Description From UniProt | FUNCTION: 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) |
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| Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome |
Protein Sequence | MLFSLRNFIS YSNLYLYKNV CIGGQLLLNQ DEILKKMEEW PKHYNPKEIE EKWQKIWLSE 60 EYWRDVFRFR DEDDKAPRFV IDTPPPFTSG ELHMGHAYWV TIADTIGRFK RLEGYNVLLP 120 QGWDTQGLPT ELKVQYKLGI PKDNRQLFLQ KCIEWTEEMI KKMKEAMIRL GYRPEWERFE 180 YKTYEPKYRK IIQKSLIDMY KMNLIEMREG PVIWCPKCET ALAQSEVGYL EKEGILAYIK 240 FPLKEGGEIV IATTRPELLA ATQAIAVNPM DERYKNLVGK IALVPIFNIE VKIISDADVE 300 KEFGTGAVMI STYGDPQDIK WQLKYNLPIK VIVDEKGRII NTNGILDGLK IEQARNKMIE 360 LLKTKGYLVK VEKIKHNVLS HVERSDCLSP VEFLVKKQIY IKVLDKKQKL LEEYKKMKFK 420 PARMSYYLED WIKSIEWDWN ITRQRIYGTP LPFWYCENGH LVPAKEEDLP IDPIKTSPPL 480 EKCPLCGSEL KPVTDVADVW IDSSVTVLYL TKFYEDKNVF NRTFPASLRL QGTDIIRTWL 540 FYTFFRTLML ANNVPFTTVL VNGQVLGPDG TRMSKSKGNV VSPLDRVNDF GADAIRMALL 600 DASIGDDFPF KWDIVKGKKM LLQKLWNASR LVYPFIAKQR LDKPKSLHIV DKWILQEHKK 660 FVTKAINAYE NYDFYLVLQE LYNYFWEIVA DEYLEMIKHR LFDDDNSAKY TIQRIIRDII 720 ILLHPIAPHI TEEIYSRLFG HKKSVLLEEL PKVDDIEENK RIDELGEVIK KTNSLIRSEK 780 IKNRLSMNTP VSVKLYASKQ VIELINEVKD DVMKTLKVTN LELIESNEEK VEIKTANQSM 840 GV 842 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0002161 F:aminoacyl-tRNA editing activity IEA:InterPro GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0004832 F:valine-tRNA ligase activity IEA:UniProtKB-HAMAP GO:0006438 P:valyl-tRNA aminoacylation IEA:UniProtKB-HAMAP |
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