ID H6PUX8_RICP3 Unreviewed; 812 AA.
AC H6PUX8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02005,
GN ECO:0000313|EMBL:AFB26675.1};
GN OrderedLocusNames=RSA_05865 {ECO:0000313|EMBL:AFB26675.1};
OS Rickettsia philipii (strain 364D).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=481009 {ECO:0000313|EMBL:AFB26675.1, ECO:0000313|Proteomes:UP000007997};
RN [1] {ECO:0000313|Proteomes:UP000007997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=364D {ECO:0000313|Proteomes:UP000007997};
RA Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT "Complete genome sequence of Rickettsia philipii strain 364D.";
RL Submitted (FEB-2012) 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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC Rule:MF_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02005}.
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DR EMBL; CP003308; AFB26675.1; -; Genomic_DNA.
DR RefSeq; WP_014364947.1; NC_016930.1.
DR AlphaFoldDB; H6PUX8; -.
DR KEGG; rph:RSA_05865; -.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000007997; 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; HUPs; 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 NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02005};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02005};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02005};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02005}.
FT DOMAIN 16..573
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 624..772
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 536..540
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 812 AA; 94218 MW; C13B3233046BBAC1 CRC64;
MKEFPKNYNF TENEKKWQQI WQEKQIYAYN PNVAKEETYV IDTPPPTVSG QLHIGHVYSY
TQTDFIVRFQ RMMGKNIFYP MGFDDNGLPT ERLVEKQKQI KAYNMERSEF IKICEEVVES
EEEKFRSLFN QIALSVDWSL EYQTISPLSR KISQMSFLDL VQKEEIYRTN QPILWDPVDG
TALAQADIED KEQTSLMNYI TFKTEQGDPL TIATTRPELL PACVAVFYHP DDGRYKHLAG
KSAITPLFNE QVPLLADPLV RQDKGTGLVM CCTFGDQTDI TWWKTHNLPL KTIITKKGTI
DCQHETSIDG LKIKEARTKI IDILKEQELL IKQEDITHTV KCAERSGAPL EILTVPQWFV
KTISHKEALL KRANELNWHP KNMKIRLENW INAISWDWCI SRQRYFGVPF PVWYSKRVGE
EGKILYADVT QLPIDPLKDL PMGYSKEEVE PDYDVMDTWA TSSVSPQLST HGISDDFAVN
KDRHDKLFPM DLRPQAHEII RTWAFYTILK AHLHQNTLPW KNIMISGWCL AEDRSKMSKS
KGNVLVPEKL LEQYGSDVIR YWSANSKLGA DTAYSEDVMK NGKRLVNKLW SAAKFVFIHF
DKLKGEDKKA SLLDIKEKIT NEFDKWMVNK LVELVKLATN ELQNYEYANA MHLTEKFFWV
VFCDNYLEIS KTRSYDEEHQ NPQGQYSSIL TLYHVMQTLL KLFAPFMPHI TEELYQILYS
ENSIHVKGSW VNYSDLNYEI NAKGAEGLLE ILDIVRKFKA EKNLSIKAPI KLLEVSGIVL
SAELAEDLKN VTSAEEIQFE MKDDKIKVNI IL
//
