SYV_AGRFC
ID SYV_AGRFC Reviewed; 947 AA.
AC Q8UEN6; Q7CYP1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=Atu1719;
GN ORFNames=AGR_C_3157;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007869; AAK87491.1; -; Genomic_DNA.
DR PIR; AI2787; AI2787.
DR PIR; B97567; B97567.
DR RefSeq; NP_354706.1; NC_003062.2.
DR RefSeq; WP_006314374.1; NC_003062.2.
DR AlphaFoldDB; Q8UEN6; -.
DR SMR; Q8UEN6; -.
DR STRING; 176299.Atu1719; -.
DR PRIDE; Q8UEN6; -.
DR EnsemblBacteria; AAK87491; AAK87491; Atu1719.
DR KEGG; atu:Atu1719; -.
DR PATRIC; fig|176299.10.peg.1732; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; Q8UEN6; -.
DR BioCyc; AGRO:ATU1719-MON; -.
DR Proteomes; UP000000813; Chromosome circular.
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..947
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224427"
FT COILED 879..943
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 591..595
FT /note="'KMSKS' region"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 947 AA; 106674 MW; FD6256854A11A927 CRC64;
MLEKTYDSAS VEPKIAKAWD EANAFRAGAN AKPGAETFTI VIPPPNVTGS LHMGHALNNT
LQDILVRFER MRGKDVLWQP GMDHAGIATQ MVVERKLMEN QLPGRREMGR EAFVEKVWEW
KAESGGLIFN QLKRLGASCD WSRERFTMDE GLSEAVLEVF VTLYKQNLIY KAKRLVNWDP
KLQTAISDME VEQIEVKGNL WHFRYPLEKG VTYEYPVAFD ADGTPTEFET RDYIVVATTR
PETMLGDTGV AVNPEDERYK GIVGKHVILP IVGRKIPIVA DDYADPTAGT GAVKITPAHD
FNDFEVGKRC GLRAINVMNI DGTISIKENE DFLEGLSHPA ALHGAWDRLE GQDRFTARKI
IVEIFEEAGL LDKIEPHKHV VPHGDRGGVP IEPRLTDQWW VDNKTLAQPA IASVREGRTN
FVPKNWENTY FQWMENIQPW CISRQLWWGH QIPAWYGPDG QVFVEKTEEE ALQAAIQHYI
AHEGPWKAWV EEKLENFAPG EILTRDEDVL DTWFSSALWP FSTLGWPEQT PELARYYPTN
VLVTGFDIIP FWVVRMMQMG LHFMKDDAGN PVEPFSTVYI HALVRDKNGQ KMSKSKGNVI
DPLELIDEYG ADALRFTLAI MAAQGRDVKL DPARIAGYRN FGTKLWNATR FAEMNGVKRD
PHFLAETASL TINRWILTEL ANTARDVTAA LENFRFNDAS GILYRFVWNQ FCDWYLELLK
PVFSGEDEEA KRESQACAAY VLEEIYKLLH PFMPFMTEEL WAHTAGEGEE RDDLLCLTDW
PEPEFRDDAA AAEINWLIDL VSGIRSARAE MNVPPGATAS LVVVGANTST EARLDRHAAA
IRRLARADEI RGGDVAPKGS AQIIVGEATV CLPLGNLVDL AAEQARLEKA IGKVDAEMER
IDKKLSNEKF VANADPEVVA AERERKAELD VQLASLRTAL TRVSEAG
