SYV_NATPD
ID SYV_NATPD Reviewed; 872 AA.
AC Q3IUE5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=NP_0288A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48235.1; -; Genomic_DNA.
DR RefSeq; WP_011321874.1; NC_007426.1.
DR AlphaFoldDB; Q3IUE5; -.
DR SMR; Q3IUE5; -.
DR STRING; 348780.NP_0288A; -.
DR EnsemblBacteria; CAI48235; CAI48235; NP_0288A.
DR GeneID; 3703460; -.
DR KEGG; nph:NP_0288A; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 4914at2157; -.
DR Proteomes; UP000002698; 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..872
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224629"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 524..528
FT /note="'KMSKS' region"
FT BINDING 527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 872 AA; 99041 MW; 450FD04235C3DED2 CRC64;
MSEVPDSYDP DEAEQKWRDE WLESDVYSYD GDEERPDYII DTPPPYPTGN LHIGNALGWC
YMDYAARYHR LQGDDVLFPQ GWDCHGLPTE VKVEENRDIH RTDVSREQFR EWCVEHTDEQ
IAAMKETMRT LGFSQDWDHE FRTMDDSYWQ ETQRSFLQMA DSDYVYQDEH PVNWCPRCET
AIADAEVENE DREGTLYYIT FSGADNDDIE IATTRPELLP ACVAIAVDPD DDRFEGRVGD
RFEVPIFGQE VELIADDDVD GDFGTGAVMI CTFGDKQDVD WWAEHDLDLR PVVTEDGHLN
ERAGEFEGRS IDEAKDEIAT ALSKSGHLHK EEPTEQSVGC CWRCDTPIEI LSKEQWFVKV
DQEEILETAQ DIAWYPDHMY ERLEEWTEGM EWDWVISRQR VFATPIPAWE CADCGHIELA
DESEVPVDPT NDEPAVGSCP ECGSDDWVGE TDVMDTWMDS SISPLYVAGW PDETFEPVQL
REQGHDIIRT WAFYTILRTA AVTDEIPWEE ALINGMVFGD DGNKMSKSRG NFVQPEEVVE
EHSADAFRQA MALGGQPGSD IQFQWKEVTS ASRFQTKLWN ITKFASEHID ESTPDIEAPA
YRDADEWILA RCARVADEVA DDMDEYRFDS ALRTVREFVW HDLADDYLEL IKGRLYEGRP
GERKAAEHAL FVSLSASLRM LSPFAPFITE EAWSHLPADG SVHNAAWPDP PAGDEAAEER
GELIAEVAAT IRGWKSDEGK PLNADLERVE VYIDEDRPLD TYDLADTVNG PVYIEEGTPS
VELVPVGVDI EHSELGPVFR DKAGEVVGRL ESADPAELQA ELDTDGHVEF EVDGETVTVE
PEMFDIVEEQ RAESGEEVVV LEADDATVLV FE
