SYV_RICCK
ID SYV_RICCK Reviewed; 813 AA.
AC A8EZQ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=A1E_04565;
OS Rickettsia canadensis (strain McKiel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=293613;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=McKiel;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia canadensis.";
RL Submitted (SEP-2007) 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_02005}.
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_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR EMBL; CP000409; ABV73838.1; -; Genomic_DNA.
DR RefSeq; WP_012149033.1; NC_009879.1.
DR AlphaFoldDB; A8EZQ5; -.
DR SMR; A8EZQ5; -.
DR STRING; 293613.A1E_04565; -.
DR EnsemblBacteria; ABV73838; ABV73838; A1E_04565.
DR KEGG; rcm:A1E_04565; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000007056; 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; 3.40.50.620; -; 2.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
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 PRINTS; PR00986; TRNASYNTHVAL.
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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..813
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000022184"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 536..540
FT /note="'KMSKS' region"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 813 AA; 94182 MW; 6BBD31F4D556CBD3 CRC64;
MKAFPKNYNF TENEKKWQRI WQEKQIYAYD PNISKEETYI VDTPPPTVSG QLHIGHVYSY
TQTDFIVRFQ RMIGKNIFYP MGFDDNGLPT ERLVEKQKQI KAYNIGRNKF IQICEEVVAS
EEEKFRGLLN KIALSVDWSL EYQTISPLSQ KISQMSFLDL VKRGEIYRND QPILWDPVDG
TALAQADIKD TENSSLMNYI TFKTEQGEPL TIATTRPELL PACVAVFYHP DDRHYKHLAG
KFVITPLFKD KVPLLADPLV QQDKGTGLVM CCTFGDQTDI TWWKTHNLPL KTIITKKGTI
DFPNDIGIDR LKIKEARAKI IDILKEQNLL IKQEEITHIV KCAERSGSPL EILTMPQWFV
KTISHKEALL KRANELNWHP KNMKIRLENW INAISWDWCI SRQRCFGVPF PVWYSKRVGE
EGKILYADIA QLPVDPLRDL PIGYSRDEVE PDLDVMDTWA TSSVSPQLST HGISDDFAIN
KNRHDKLFPM DLRPQAHEII RTWAFYTILK AHLHQNTLPW KNIMVSGWCL AEDRSKMSKS
KGNVLVPEKL LEQYGSDVIR YWSANSKLGA DTAYSEDVMK NGKRLVNKLW NAAKFVSIHL
HKLKDQDKKA KLLEVKEIIT NEFDKWMINK LVELVNAVTN ELQNYEYANA MHLTEKFFLA
VFCDNYLEIS KTRAYDEDNK NLSGQYSSIL TLYHVMQTLL KLFAPFMPHI TEELYQILYN
DKESIHIKGT FANHDNLHYN IDTKQAEGML KILDIVRKFK AEKNLSIKAP IKLLKISGIV
LSEELAEDLK NVTSAEEIKF EIQDNKIKID III