SYV_HERAR
ID SYV_HERAR Reviewed; 969 AA.
AC A4G1V2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=HEAR0261;
OS Herminiimonas arsenicoxydans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1;
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.-C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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; CU207211; CAL60489.1; -; Genomic_DNA.
DR RefSeq; WP_011869835.1; NC_009138.1.
DR AlphaFoldDB; A4G1V2; -.
DR SMR; A4G1V2; -.
DR STRING; 204773.HEAR0261; -.
DR EnsemblBacteria; CAL60489; CAL60489; HEAR0261.
DR KEGG; har:HEAR0261; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_4; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000006697; 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 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..969
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000022166"
FT COILED 812..839
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT COILED 904..969
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT MOTIF 559..563
FT /note="'KMSKS' region"
FT BINDING 562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 969 AA; 109124 MW; CBEFF6F01DA8A22B CRC64;
MELAKSFDPA DIEAFWRTEW EKRGYYTATT DADKPSFSIQ LPPPNVTGTL HLGHGFNQTI
MDGLTRYHRM RGFNTAWIPG TDHAGIATQI VVERQLDAQK ITRHDLGREK FIEKVWEWKE
KSGSTITGQM RRLGTSPDWS REYFTMDEPR SKVVTEVFVR LVEQGLIYRG KRLVNWDPVL
GTAVSDLEVV SEEEDGHMWN IRYPLADGST YKFPIAYDEA GNATEWEERN FIVVATTRPE
TMLGDVAVAV DPDDERYTHL VGKLLTLPLC DRAIPIIADD YVDKEFGTGC VKITPAHDFN
DYAVGQRHNL DKISILTLDA KINEHAPAAY QGMDRYAARK QIVADLDAQG LLELVKPHKL
MVPRGDRTNA VIEPMLTDQW FVAMSKPAPE GTHFPGKSIT EVALEKVASG EVKLLPENWA
NTYNQWLNNI QDWCISRQLW WGHQIPAWYD SEGKVYVARN EEEARTKAAA QGYHGPLTRD
EDVLDTWFSS ALVPFSTLGW PEETPDFKNF LPSSVLVTGF DIIFFWVARM VMMTTHFTGK
VPFNTVYVHG LIRDSSGQKM SKSKGNTLDP IDLIDGISVE DLVAKRTVGL MNPKQAASIE
KATRKEYPNG IAAYGTDALR FTMASYASLG RNINFDLHRC EGYRNFCNKL WNATRFVLMN
CEGQDCGFRD APCAAGDCAV DGKAGGYTDF SQADRWIVSK LQRTETDIAK GFADYRFDNI
ASSLYQFIWD EYCDWYLEVA KVQIQTGTEA QQRATRRTLL RVLETILRLA HPVIPFITEQ
LWQTVAPLAG HKMHPAGDSI MMQPYPEAQP GKLDEQAESW MAELKSMTDA CRNLRGEMQL
SPALRVPLIM EAGDTEQAAR LQSFAPYLQA LAKLSEVNVA DQLPESPAPV SIVGAAKLML
KVEIDVAAER ERLSKEIARL DGEITKANSK LGNENFVARA PAQVVAQEEE RVANFSATLE
KLREQFIKL
