SYV_RHOPA
ID SYV_RHOPA Reviewed; 957 AA.
AC Q6N6N1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=RPA2583;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; BX572601; CAE28024.1; -; Genomic_DNA.
DR RefSeq; WP_011158133.1; NC_005296.1.
DR AlphaFoldDB; Q6N6N1; -.
DR SMR; Q6N6N1; -.
DR STRING; 258594.RPA2583; -.
DR PRIDE; Q6N6N1; -.
DR EnsemblBacteria; CAE28024; CAE28024; RPA2583.
DR GeneID; 66893652; -.
DR KEGG; rpa:RPA2583; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; Q6N6N1; -.
DR BioCyc; RPAL258594:TX73_RS13170-MON; -.
DR Proteomes; UP000001426; 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..957
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224548"
FT COILED 887..946
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 571..575
FT /note="'KMSKS' region"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 957 AA; 107229 MW; EC181102C5A4F7AD CRC64;
MIEKTYQPAD IEARISRAWE DAEAFKAGRP ERRDAVPYSI VIPPPNVTGS LHMGHALNNT
LQDILCRFER MRGRDVLWQP GTDHAGIATQ MVVERQLMER QEPSRRDMGR AKFLERVWQW
KAESGGVIVN QLKRLGASCD WSRERFTMDE GLSRAVAKVF VELHRQGLIY KDKRLVNWDP
KLLTAISDLE VQQIEVKGNL WHLRYPIEGK TFDPADPSSF IVVATTRPET MLGDSAVAVN
PEDERYTHLV GKHVILPLVG RRIPIVADEY SDPEKGSGAV KITPAHDFND FEVGKRHHLP
QINVLDIEGK ISVADNSAYL EGLPEGAREF AGEIDGTDRF VARKIIVARL DDFGFLEKIE
PNVHMVPHGD RSGVVIEPFL TDQWYVDAKT LAQPAIAAVR SGETTFVPKN WEKTYFEWME
NIQPWCISRQ LWWGHQIPAW YGPDGKVFVA ETEEEAVGNA LGYYVEQEVI TPAQAHDMAE
DPAKREGFIT RDEDVLDTWF SSALWPFSTL GWPDETPELD RYYPTNVLVT GFDIIFFWVA
RMMMMGLHFM DDVPFPTVYI HALVRDEKGA KMSKSKGNVI DPLNLIDEYG ADALRFTLAA
MAAQGRDIKL ATSRVEGYRN FATKLWNACR FAEMNGCVAP AGFDYTAAKE TLNRWIAHET
VRAVREVTEA IESYRFNDAA EAAYRFVWNV YCDWYLELAK PVLMGEEGAA KTETRAMVAW
ARDEILKILH PFMPFITEEL WAVTAPRDGL LALAPWSRKG GISDEEVSVL AASAATDPMA
GPAMLAIPEP QEPDFTDDAA EAEIGWVVDL VTAIRSVRAE MNIVPSTLTP LVLAGASADT
NARASRWSDV IKRLARVGEI SFADAAPQGA VQLLVRGEVA ALPLKGVVDF AAEQARLEKE
LGKAEADIKR AEAKLANEKF VANAAEEVVE EEREKREAAV ARKVKILEAL LRLKNAS
