SYV_NITMU
ID SYV_NITMU Reviewed; 926 AA.
AC Q2YB22;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=Nmul_A0742;
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000103; ABB74049.1; -; Genomic_DNA.
DR RefSeq; WP_011380099.1; NZ_FNVK01000003.1.
DR AlphaFoldDB; Q2YB22; -.
DR SMR; Q2YB22; -.
DR STRING; 323848.Nmul_A0742; -.
DR EnsemblBacteria; ABB74049; ABB74049; Nmul_A0742.
DR KEGG; nmu:Nmul_A0742; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002718; 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; -; 2.
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..926
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000022169"
FT COILED 859..924
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 536..540
FT /note="'KMSKS' region"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 926 AA; 105032 MW; 61DC0CD3483E0F4B CRC64;
MELEKSFDPR AIESRWYSRW EGEGYFRPGP AGTAGDQAPA YCIMLPPPNV TGTLHMGHAF
QHTLMDALTR YHRMRGDNTL WQPGTDHAGI ATQIVVERQL DQQSIDRRDL GREAFLARVW
EWKEESGSTI SRQMRRMGAS CDWSRERFTM DGGLSRAVTE VFVRLYREGL IYRGERLVNW
DPVLQTAVSD LEVVSAEEEG SLWHILYPFE NDLGGNQDGA KPEGLIVATT RPETMLGDMA
VAVHPDDERY RHLIGRHVRL PLCERSIPII ADAYVDPAFG TGCVKITPAH DFNDYQIGQR
HKLVPLGILT LDGKINDLAP AEYQGLDRFA ARRKIVADLE EQNLLVETKP HKLMVPRGDR
TQAIVEPMLT DQWYVTMNGL ARRGLEAVAS GEVKFIPENW AHVYNQWLEN IQDWCISRQL
WWGHRIPAWY DEDNNIFVAH NLEEAQRLAG GRKLVQDEDV LDTWFSSALW PFSTLGWPEK
TPELDTFLPT SVLVTGFDII FFWVARMVMM SLHFTGKVPF REVYITGLIR DAEGHKMSKS
RGNVLDPLDL IDGIALPDLI TKRTSGLMNP RQAESIEKIT RKQFPEGIPA FGADALRFTF
ASLASHGRDI KFDMQRCEGY RNFCNKLWNA ARYVLMNCEG KDTGLVESVP LEYSDADCWI
IGRLQQAETA VAQAYQDYRF DMAAREIYEF VWDEYCDWYL EFAKVQLNSG NEVVQRTTRR
TLARVLETAL RLAHPLIPFI TEELWQSVAP LAAKQGVSIM LQPYPQADPS KLDDTAIGNI
AALKEMINAC RTLRGEMNLS PASRVPLLAV GDVKTLAGFS PYLKALAKLS DIEIEQDLPP
AEAPVAIVGE FRLMLKIEID IAAERERLTK ELDRVQTEME KAQTKLANSN FVDRAPAKVV
EQEKERLAGF STTLGKLKEQ LQKLGC
