SYV_GEOSL
ID SYV_GEOSL Reviewed; 887 AA.
AC Q74BJ6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=GSU2045;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(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}.
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DR EMBL; AE017180; AAR35421.1; -; Genomic_DNA.
DR RefSeq; NP_953094.1; NC_002939.5.
DR RefSeq; WP_010942688.1; NC_002939.5.
DR AlphaFoldDB; Q74BJ6; -.
DR SMR; Q74BJ6; -.
DR STRING; 243231.GSU2045; -.
DR PRIDE; Q74BJ6; -.
DR EnsemblBacteria; AAR35421; AAR35421; GSU2045.
DR KEGG; gsu:GSU2045; -.
DR PATRIC; fig|243231.5.peg.2081; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_7; -.
DR InParanoid; Q74BJ6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000577; 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 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..887
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224482"
FT COILED 817..885
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT MOTIF 527..531
FT /note="'KMSKS' region"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 887 AA; 100798 MW; 7CE8249E121D21FF CRC64;
MAEKELAKVY EPTAVERKWY ETWEQEGYFR ANPDSGKPSY SIVIPPPNVT GALHMGHALN
NTLQDILCRW KRMNGYEVLW MPGTDHAGIA TQNVVERQLA GEGTSRHELG REAFIERVWK
WKAESGGQII GQLKRLGASC DWGRERFTMD EGLSRAVREV FVRLYEEGLI YRDNRLINWC
PRCHTALSDI EVEHEDKAGN LWHIRYPVVG EPGRFVVVAT TRPETMLGDT AVAVHPEDER
YADLVGKKVL LPLVNREIPV VADGYVDREF GTGVVKITPA HDFNDFEVGR RHNLDLLNVF
DESAVVNSAG HQYEGMERFA ARKRVVEDLE ALGLLEKIDD HAHAVGGCYR CKTVVEPYLS
LQWYVKVGPL AERALAAVKD GRTRIVPQQW ENTYYDWMEN IKDWCISRQI WWGHRIPAWY
CDHCGETTVA KIDPTVCAAC GSDEIRQETD VLDTWFSSAL WPFSTMGWPD RTPELAAFYP
TSCLVTGFDI LFFWVARMMM MGLHFMNEVP FSDVYIHALV RDAQGQKMSK SKGNVIDPLV
VIDQYGTDAF RFTLAAFAAQ GRDIKLAEER IAGYRNFVNK IWNASRFALM NLEGFEPDTV
DPATLDLSNA DRWILHRLNS AAAETAEALE AYRFNDAAGT LYRFTWSEFC DWYIELAKDD
LYRGDDARKE TARYVLWLVL ENLLRLLHPF MPFITEEIWQ TLPGARPAPS IMVAGYPRSV
PERDFPDGAA EMELVMEVIR GIRNIRGEMD VAPSREIAAI LSCGSAESLH LLKRNEVYVM
SLARLSDLAI GQQLERPADA AIQVAGDVEI AVPLKGLVNV EEEEKRLLKE IGKLDKEIEM
FGRKLENPSF VERAPADVVA KEREKLAEVT QKKDVLLASL EKIRKLA
