SYV_HISS2
ID SYV_HISS2 Reviewed; 954 AA.
AC B0USP0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=HSM_0803;
OS Histophilus somni (strain 2336) (Haemophilus somnus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=228400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2336;
RG US DOE Joint Genome Institute;
RA Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA Dyer D.W., Inzana T.J.;
RT "Complete sequence of Haemophilus somnus 2336.";
RL Submitted (FEB-2008) 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; CP000947; ACA32476.1; -; Genomic_DNA.
DR AlphaFoldDB; B0USP0; -.
DR SMR; B0USP0; -.
DR STRING; 228400.HSM_0803; -.
DR EnsemblBacteria; ACA32476; ACA32476; HSM_0803.
DR KEGG; hsm:HSM_0803; -.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
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.
FT CHAIN 1..954
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000088563"
FT COILED 883..954
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 560..564
FT /note="'KMSKS' region"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 954 AA; 109533 MW; 24AECDD79247BB89 CRC64;
MTKQFTMEDR FNPSAVEQAL YQHWESRGYF KPSEDINAPS YCIAIPPPNV TGSLHMGHAF
QQTLMDTLIR FNRMEGNNTL WQTGTDHAGI ATQMVVERKI AAEEGKTRHD YGREAFINKI
WDWKAYSGGT ISQQMRRLGN SIDWDRERFT MDEGLSNAVK EVFVRLHEEG LIYRGKRLVN
WDPKLHTAIS DLEVENKESK GSLWHFRYPL ANGAKTAEGL DYLVVATTRP ETMLGDTAVA
VHPEDERYQS LIGKTVVLPL ANREIPIIAD EYVDREFGTG VVKITPAHDF NDYEVGKRHG
LPMVNVMTLN ADIRAEAEII GTDGKPLAGY DAPIPADYQG LERFVARKKI VADFEALGLL
DQIKPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLAEVAT KAVENGEIQF VPKQYENLYF
SWMRDIQDWC ISRQLWWGHR IPAWYDEQGN VYVARDEAEV RSKYGLTSDV ALKQDEDVLD
TWFSSGLWTF STLGWPEQTK ELKMFHPTDV LITGFDIIFF WVARMIMFTM HFIKDENGKP
QVPFKTVYVT GLIRDEQGQK MSKSKGNVLD PIDMIDGISL EDLLEKRTGN MMQPQLAEKI
AKATRKEFEH GISAHGTDAL RFTLAALASN GRDINWDMKR LEGYRNFCNK LWNASRYVLT
HEKLDLSEGE AEYSLADRWI ESQFNRTIDA FRTALKQYRF DLVANTIYDF TWNQFCDWYL
ELTKPVFAHG TDAQKRGTSR MLLNILEKLL RLAHPIIPFI TEEIWQKLKG VMKLSGDTIM
LQPFPHAEES KFDPVAESQM DWLKEVIVAV RNIRAECNIS PSHALELLLR NISEETKICL
ENNRTLLQSM AKLSTITLLD ANEEPPLSVT KLVENNEIFI PMAGFINKEQ ELTRLTKEIE
KLKGEIVRIE NKLSNEAFIT KAPEQVIAKE REKMQGYLDN IEKLQQQYQA IETL
