SYV_RHOBA
ID SYV_RHOBA Reviewed; 1035 AA.
AC Q7UXH9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=RB1319;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAD72027.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294135; CAD72027.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_864348.1; NC_005027.1.
DR AlphaFoldDB; Q7UXH9; -.
DR SMR; Q7UXH9; -.
DR STRING; 243090.RB1319; -.
DR EnsemblBacteria; CAD72027; CAD72027; RB1319.
DR KEGG; rba:RB1319; -.
DR PATRIC; fig|243090.15.peg.605; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_0; -.
DR InParanoid; Q7UXH9; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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 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..1035
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224547"
FT COILED 253..281
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT COILED 967..1035
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1035 AA; 116013 MW; 628CDF9BC7A9131D CRC64;
MSEIPTRFEH AEEADKIAQA WTDAKCSHAD PESSKPPFSV VIPPPNVTGA LHLGHGLNNT
LQDIVVRRKR MQGFETLWMP GTDHAGIATQ AVVERRLKEQ EDKTRHDLGR EALVDRIWQW
KDQYEERIIG QLKRMGTSCD WERLRFTLDP ICAAAVRATF FDLFGKRRIY RGKRLVNWDT
FLQTAVSDDE VFNETKKGHF YHFRYPVIDP KPGEPEFVTI ATTRPETMLG DTAVAVHPDP
AAALDAVEAG LREKLSDANE KEAVDLNKQI EALQKRREER LPELIQLRDM AADGRKLMLP
LVDREIDLVA DEWAKPEMGS GCVKITPAHD PNDYEVGIRQ DLPMINILNS DGTLNGEGGQ
FAGLTIPKAR KAVVAALEEL GLMGDIEDRE IELPHSDRSK TPIEPYLADQ WFVAMDELAQ
SAMDAVSDER VQIFPARYRK GYLDWLSEKR DWPVSRQLWW GHRIPIWSVG GLSQQEANEL
SSELEKLAER HPDQIAQRID SDGVDAAGEP TKAVFVCIRS EDETVEADVE ALGLQQDPDV
LDTWFSSALW PHSTLGWPAQ TPELAKFYPT ATLITSRDIL TLWVARMVLM GLNNVGEVPF
SEVFIHPKIL DGLGETMSKS KGNGVDPIDV IDKFGPDALR FGLARLATET QDVRMPVQYE
CPSCEKLIDQ TKKNRALPSM DCPACGKPFS TQWAETEADK SLPKAAVVSE RFETARNFVN
KLWNASRFVM MNLDGFEPTS LDVASLPIED RWLLSRLSTV TQTVGDAIER YQFGEAARVL
YDFAWDEFCS FYVEIAKPRL SDDSQRQIAQ NVIAHGLDQL LRLLHPIMPF VTESVWNHLG
QIAPKRGVPE PAEVGPFVMT ASFPVADESH HDSKIERQFS EFQQIVAAIR QIRASQNIAP
KETVPAAIRC SASSQELLQP MTAYFEALAG AEVQSLGPDT TAFETDAHLA LPDVDVDVHV
DLEKFIDVEA ELARLEKLQG QLTGQITGKQ NKLSNESFVS RAPADIVQKE RESLAGLQTQ
LEAVAQDILK LQSKK
