SYV_CORJK
ID SYV_CORJK Reviewed; 932 AA.
AC Q4JWU8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=jk0550;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=306537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411;
RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI36709.1; -; Genomic_DNA.
DR RefSeq; WP_011273214.1; NC_007164.1.
DR AlphaFoldDB; Q4JWU8; -.
DR SMR; Q4JWU8; -.
DR STRING; 306537.jk0550; -.
DR PRIDE; Q4JWU8; -.
DR EnsemblBacteria; CAI36709; CAI36709; jk0550.
DR KEGG; cjk:jk0550; -.
DR PATRIC; fig|306537.10.peg.562; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_11; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000545; 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; -; 3.
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; 2.
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..932
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224468"
FT COILED 863..929
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 75..85
FT /note="'HIGH' region"
FT MOTIF 568..572
FT /note="'KMSKS' region"
FT BINDING 571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 932 AA; 104813 MW; E67C2E72F2147002 CRC64;
MPCLARLLDL ADVSDSSSKA NGSNPIGADR SAQLPAAWDP AAVEENLYQG WVDSGYFKAD
PSSDKPPFSI VLPPPNVTGQ LHMGHALDHT LMDAMARRKR MQGFEVLWLP GSDHAGIATQ
TKVEANLKET EGKDRFDYGR DAFVGKVWEW KDRYGGVIQR QMRAIGDSVD WSRERFTLDD
GLSRAVQTMF KELFDAGLIY RANRMVNWSP VLQTAISDIE VVYSDDEGEL VSIRYGSLED
SEPHVVVATT RVETMLGDVA VAVHPEDERY TDLVGKSLPH PFLPDRQMIV VADDYVDPEF
GTGAVKITPA HDPNDFAMGQ RHDLPMPVIM DETGHIANTG TEFDGMERYE AREKIRLALE
EQGRIVARKF PYVHSVGHSE RSKEAVEPRL SEQWFVKVEE LAKMSGDAIR SGDSVIHPSS
QEPRWFDWVD DMHDWCISRQ LWWGHRIPIW YGPNGEIVCC GPDDEAPTGE GWYQDEDVLD
TWFSSALWPF STMGWPEKTP ELEKFYPTSV LVTGYDILFF WVARMMMFAT FASKHTPEIL
GTGKDGRPQI PFNDIFLHGL VRDEHGRKMS KSLGNGIDPM DWVRDYGADA LRFTLARGAN
PGSDLPVGED AAQSSRNFAT KLYNATKFAL MNGARVGELP ARETLTDADR WILDRLEEVR
QLVDDALDRY EFSLANENLY RFAWGEFCDW YLEIAKVQIP RDWDSATEEQ VQRGIRTQIV
LGRVLDSVLR LLHPAMPFVT ETLWKALTDG EEGYSESLVT ADWPTADLTN GGAQTDADAV
RRMADVDKLV TELRRFRSDQ GVKPSQKVPA KLDFAAADLA NFEEAVRSLV RLETPEEDFA
ETASIEVRLS QATIAVQLDT SGTVDVAAER KRLEKDLAAA QKELDNAAKK LGNENFLAKA
PEKVVEGIRE RQRVAQEEFE RITARLEGLP KA
