SYV_PASMU
ID SYV_PASMU Reviewed; 954 AA.
AC Q9CMK5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=PM0818;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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; AE004439; AAK02902.1; -; Genomic_DNA.
DR RefSeq; WP_010906864.1; NC_002663.1.
DR AlphaFoldDB; Q9CMK5; -.
DR SMR; Q9CMK5; -.
DR STRING; 747.DR93_1658; -.
DR PRIDE; Q9CMK5; -.
DR EnsemblBacteria; AAK02902; AAK02902; PM0818.
DR KEGG; pmu:PM0818; -.
DR PATRIC; fig|272843.6.peg.827; -.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000000809; 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; -; 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..954
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224524"
FT COILED 883..953
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; 108685 MW; 456267FE93012245 CRC64;
MTQNFEMADR FTPSAVEQAL YKHWEESGYF KPSEDTSKPS YSIAIPPPNV TGSLHMGHAF
QQTLMDILIR FNRMEGHNTL WQTGTDHAGI ATQMVVERKI AAEEGKTRHD YGREAFIDKI
WDWKAYSGGT ISQQMRRLGN SIDWERERFT MDEGLSDAVK EVFVRLHEEG LIYRGKRLVN
WDPKLHTAIS DLEVENKESK GSLWHFRYPL ANGAKTADGK DYLVVATTRP ETMLGDTAVA
VHPEDERYQS LIGKTVVLPL ANREIPIIAD DYVDREFGTG VVKITPAHDF NDYEVGKRHQ
LPMVNVMTLN ADIRAEAEII GSDGKILESY TALIPTKYQG MERFAARKQI VADFEELGLL
DEIKPHDLKV PYGDRGGVPI EPMLTDQWYV SVKPLAEVAV KAVEDGEIQF VPKQYENLYF
SWMRDIQDWC ISRQLWWGHR IPAWYDEQGN VYVARDEAEV RAKHNLPADL ALKQDEDVLD
TWFSSGLWTF STLGWPKQTP DLKMFHSTDV LITGFDIIFF WVARMIMFTM HFVKDENGKP
QVPFKTVYVT GLIRDEQGQK MSKSKGNVID PLDMIDGIDL ESLLEKRTGN MMQPQLAEKI
AKATIKAFPE GIAEHGTDAL RFTLTALATN GRDINWDMKR LEGYRNFCNK LWNASRFVLT
NDKLDLSEGS VEYSVADRWI QSEFNRTVEA FRNALAQFRF DLCATALYEF TWNQFCDWYL
ELTKPVLVNG SVAQKRGASQ TLINVLEKLL RLTHPVMPFI TEEIWHKVKA FAGVSGDTIM
LQAFPQFEQS ALDYQAEAEI NWMKEVIVAV RNIRAESNIP PSKGLDLLLR NLSEADQNAL
ENNRTLIQAM AKLDAIRVLE AGEDAPLSVA KLVNNAELLV PMAGFINKEA ELARLNKEIE
KYQGEIQRIE NKLANEAFVA KAPPAVIEKE RAKMAEYAEG LNKLKQQYLA IEAL
