SYV_RICAH
ID SYV_RICAH Reviewed; 812 AA.
AC A8GPJ3;
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=A1C_05365;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
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 akari.";
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; CP000847; ABV75318.1; -; Genomic_DNA.
DR RefSeq; WP_012149948.1; NC_009881.1.
DR AlphaFoldDB; A8GPJ3; -.
DR SMR; A8GPJ3; -.
DR STRING; 293614.A1C_05365; -.
DR EnsemblBacteria; ABV75318; ABV75318; A1C_05365.
DR KEGG; rak:A1C_05365; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OMA; RQWYIRN; -.
DR Proteomes; UP000006830; 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..812
FT /note="Valine--tRNA ligase"
FT /id="PRO_1000022182"
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 812 AA; 93990 MW; 0662C9C7114CBE0A CRC64;
MTEFPKNYNF TENEKKWQQI WQAQQIYAYD PNISKEETYV VDTPPPTVSG QLHIGHVYSY
TQTDFIVRFQ RMIGKNIFYP MGFDDNGLPT ERLVEKQKQI KAYNMGRDEF IKICEEVVES
EEEKFRRLFN QIALSVDWSL EYQTISPLSR KISQMSFLDL VKKGKIYRND QPILWDPVDG
TALAQADIED KAKTSFMNYI IFKTEQGESL TIATTRPELL PACIAVFYHP DDKRYKHLAC
KSAITPLFNE KVPLLASPLV QQDKGTGLVM CCTFGDQTDI TWWKTHNLPL KTIITKKGTI
NFPHNIAIDG LKIKEARIKI IDILKEQKLI TKQEEITQTV KCAERSGAPL EILTVPQWFV
KTISHKEALL KRANELNWRP NNMKIRLENW INAISWDWCI SRQRYFGVPF PVWYSKRVGE
EGKILYADIS QLPVDPLKDL PIGYSKEEVE PDLDVMDTWA TSSVSPQLST HCISDNFAVN
KDRHNKLFPM DLRPQAHEII RTWAFYTILK AHLHQNTLPW GNIMVSGWCL AEDRSKMSKS
KGNVLVPEKL LEQYGSDVIR YWSANSKLGA DTAYSEDVMK NGKRLVNKLW NACKFIFIHC
NKLKDVDKKA SLFDIKEQIT NEFDQWMINK LVELVNAATN ELQNYEYANA MHLTEKFFWV
IFCDNYLEIS KTRSYDEENK NPQGQYSSIL TLYHVMQILL KLFAPFIPHI TEELYQILYS
ENSIHVKGNW VNYGDLHYGI DVTQSEGLIA ILDIVRKFKA ENNLSIKAPI KLLEVSGIEL
SAELTEDLKN VTSAEEIQFE GQGDKIKVNV IF