SYV_NITSB
ID SYV_NITSB Reviewed; 871 AA.
AC A6Q3R4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=NIS_1013;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009178; BAF70123.1; -; Genomic_DNA.
DR RefSeq; WP_012082386.1; NC_009662.1.
DR AlphaFoldDB; A6Q3R4; -.
DR SMR; A6Q3R4; -.
DR STRING; 387092.NIS_1013; -.
DR EnsemblBacteria; BAF70123; BAF70123; NIS_1013.
DR KEGG; nis:NIS_1013; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_7; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001118; 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..871
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000022170"
FT COILED 805..871
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 534..538
FT /note="'KMSKS' region"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 871 AA; 100866 MW; 74A573E74706C8E7 CRC64;
MSKATKYDPK KVERQFYQIW ETRGYFETDG NKKIQNGKTF CIMMPPPNVT GRLHIGHALT
FTLQDIMVRY KRMDGYETLW QPGTDHAGIA TQNVVEKQLL SKGIKKEEIG REKFLEYVWK
WKEESGNAIV TQLRLLGVSP AWSRERFTMD KGLKNAVREA FVNLYYEGLI VKGNYMINWC
THDGALSDIE VEYEEKEGAL YHIKYPIVGS DEYLVVATTR PETYFGDTAV MVNPNDERYK
HLIGKKVRLP LINREIPIIA DEHVDMEFGT GAVKVTPAHD PNDYEVGKRH NLPFITIFDE
NGILNEEAGE FAGIERLEAR KKVVEKLEQE GFIEKIEPHK HQVGHCYRCG NVVEPYISPQ
WFVKAEIAKE AVKKANEGET KFYPPQWLNN FNAWMRELRD WCISRQLWWG HRIPVWYCRA
CGHEWASKKE HEESCPKCGS TDIYQDPDVL DTWFSSALWP FSTLGWGNGD WGKGVKWFED
DLKKFYPNDL LITGFDILFF WVARMMMMGE HFLHKLPFKD VYLHALVRDE HGQKMSKSRG
NVIDPIDTIE EYSADALRFT LAALAVQGRD IRLSKERLEL YRNFTNKLYN AARFLQIHQE
KFDDLQNIQI KTDLGKYILS RFGLAIQEVR NNLNSYRFND AATTLYRFLW GEFCDWGIEL
SKVNKDAIAE LGAIFKESMK LLHPFMPFIT EFLYQELSGT SIEENESIMI QPYPKAAPID
EEIMKRFETI IDAIVSIRRA KALIDMANKT IPKVLIKGDL EESAKAYISK LAKVETIEFV
SEPAENAVTD IGNYVEVFIP LEGIDLTPIL NRLNKQKEKL QKEIDKLSRM LSNENFVKNA
PQAVVEQNRA ALAEAQNRLA TIEEELARLT R
