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   27-MAR-2024, entry version 90.
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};
GN   OrderedLocusNames=NIS_1013;
OS   Nitratiruptor sp. (strain SB155-2).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC   Nitratiruptoraceae; 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}.
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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   KEGG; nis:NIS_1013; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_7; -.
DR   InParanoid; A6Q3R4; -.
DR   OrthoDB; 9810365at2; -.
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   CDD; cd00817; ValRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   NCBIfam; TIGR00422; valS; 1.
DR   PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 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; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF46589; tRNA-binding arm; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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
//