SYV_SULTO
ID SYV_SULTO Reviewed; 809 AA.
AC Q972A3; F9VNY2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=STK_12240;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC inadvertently accommodate and process structurally similar amino acids
CC such as threonine, to avoid such errors, it has a 'posttransfer'
CC editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC dependent manner. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02005};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated threonine is translocated from the
CC active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR EMBL; BA000023; BAK54490.1; -; Genomic_DNA.
DR RefSeq; WP_010979244.1; NC_003106.2.
DR AlphaFoldDB; Q972A3; -.
DR SMR; Q972A3; -.
DR STRING; 273063.STK_12240; -.
DR PRIDE; Q972A3; -.
DR EnsemblBacteria; BAK54490; BAK54490; STK_12240.
DR GeneID; 1459223; -.
DR KEGG; sto:STK_12240; -.
DR PATRIC; fig|273063.9.peg.1384; -.
DR eggNOG; arCOG00808; Archaea.
DR OMA; FATKLWN; -.
DR OrthoDB; 4914at2157; -.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..809
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224636"
FT MOTIF 60..70
FT /note="'HIGH' region"
FT MOTIF 546..550
FT /note="'KMSKS' region"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 809 AA; 94902 MW; 3ACEEF83F1600F41 CRC64;
MLSQEEINKK LEEWPKHYNP KEIELKWQQI WLSKEYWEKV FRFKDEDEKS PVFVIDTPPP
FTSGELHMGH AYWVTIADTI GRFKRLQGYN VLLPQGWDTQ GLPTELKVQY RLKIPKENRE
LFLKKCVEWT EDMIKKMKEA MIRLGYRPEW ERYEYRTYEN SYRKIIQKSL LEMYKLGLIE
IREGPVYWCP KCETALAQSE VGYLEKDGIL AYIRFPLKDG GEIIIATTRP ELLAATQAVA
VHPEDERYKG LIGKIAIIPL FNKEVKIIGD DAVEKEFGTG AVMISTYGDP QDIKWQLKYN
LPTTELIDEK GRIKNTNGLL DGLKIEEARK KIIELLKEKG YLVKIENFKH NVLSHTERSD
CLSPIEFLVK KQIFIKTLQF KDKLLEEYKK MKFIPSRMAY YLEDWIKSLE WDWNISRQRV
YGTPLPFWYC DNNHLIPARE EDLPLDPTKT KPPYEKCPQC GLPLKPVTDV ADVWIDSSVT
VIYLTGFYTD KRKFEKTFPA SVRLQGTDII RTWLFYTFFR TLVLTGNIPF KEVLINGQVL
GPDGTRMSKS KGNVVNPLDK VDEFGADSIR LTLLDARIGD DFPFKWETVR GKKLLLQKLW
NAGRLSYPFI GKKKFDRPSN LHPIDRWILQ EHKRFVKKSI EAYNNYDFYQ VVESLYSYFW
ETIADEYLEL IKHRLFAEDL SALYTLSRVF KDLLIILHPI APHITEEMYN RLYGDKISII
LEGLPNVDDI EEDPNIDTLG KYIKTTTSTI RTLKIQNRIP IPVSINVKLV GPKEYIETIK
RVEDDIIKTL KIEKIVYEEG EEIKAELLS
