SYV_THEVB
ID SYV_THEVB Reviewed; 913 AA.
AC Q8DIS8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=tlr1503;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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_02004}.
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_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
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_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR EMBL; BA000039; BAC09055.1; -; Genomic_DNA.
DR RefSeq; NP_682293.1; NC_004113.1.
DR RefSeq; WP_011057343.1; NC_004113.1.
DR AlphaFoldDB; Q8DIS8; -.
DR SMR; Q8DIS8; -.
DR STRING; 197221.22295228; -.
DR EnsemblBacteria; BAC09055; BAC09055; BAC09055.
DR KEGG; tel:tlr1503; -.
DR PATRIC; fig|197221.4.peg.1577; -.
DR eggNOG; COG0525; Bacteria.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000440; 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; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 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; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
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 Pfam; PF10458; Val_tRNA-synt_C; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF46589; SSF46589; 1.
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; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..913
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224585"
FT COILED 839..907
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 541..545
FT /note="'KMSKS' region"
FT BINDING 544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 913 AA; 103194 MW; 9A40A7DC250BBCF5 CRC64;
MTDAITLPSQ YDPKQTEAKW QQLWESSGVF HADPNHPGKP YCIVIPPPNV TGSLHMGHAF
EHALIDVLIR YHRMIGRNVL WLPGTDHASI AVSTILDQQL QAEGTNRFAL GREAYLKRAW
AWKESSGKTI VGQIRRLGLS VDWSRERFTM DEGLSRAVLT AFNRLYEAGL IYRGQYLVNW
CPASQSAVSD LEVENREVQG HLWYLRYPLT DGSGYLEVAT TRPETMLGDT AVAVHPEDDR
YRHLIGKTLR LPLMNREIPI IGDPLVDPTF GTGCVKVTPA HDPNDFVMGQ RHRLPMMNLM
NKDGTLNENA GEFAGLDRFV ARKQVVARLE AEGFLVRVED YKHTVPYSDR GKVPIEPLLS
TQWFVKIRPL ADAALKALDR QHSPRFIPDR WAKVYRDWLV NLRDWCISRQ LWWGHQIPAW
YVVSETNGEV RDDTPFVVAM DETAARAKAI AQFGEDIELQ QDQDVLDTWF SSGLWPFSTL
GWPDDTPDYR RYYPNTTLVT GFDIIFFWVA RMTMMGQYFT GKIPFRDVYI HGLVRDENNK
KMSKSANNGI DPLILIEKYG TDALRYSLVK EVVGAGQDIR LAYNRKTDES ATVEAARNFA
NKLWNASRFV LLNLEGQTPG QLGTPRRQDL TASDRWILSR YHTAIQTTRE RIESYGLGEA
AKGLYEFIWG DFCDWYIELV KPRLQGENAK AKRTAQQVLA TVLDGTLKLL HPFMPHITEE
IWHTLHQVAD NEVLAVQPYP KANRRAIDPD LEAQFSLLIE TIRTIRNLRA EAGIKPGLYI
AALIEASAEE APIFEAGAAD IQHLARLESL TIGSGLQIPQ RVFSGVVGKS EVLIPLAGVV
DLEALVSKLQ KEGDRLRKEI QSLTARLNNP NFVNKAQPEV VAAAQAQLAA AQQQLAIIEH
RLQSLGVDDK TQP
