SYV_HELHP
ID SYV_HELHP Reviewed; 899 AA.
AC Q7VHN2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=HH_0933;
OS Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=235279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51449 / 3B1;
RX PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA Shen Z., Weber J., Frosch M., Fox J.G.;
RT "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT hepaticus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP77530.1; -; Genomic_DNA.
DR RefSeq; WP_011115773.1; NC_004917.1.
DR AlphaFoldDB; Q7VHN2; -.
DR SMR; Q7VHN2; -.
DR STRING; 235279.HH_0933; -.
DR EnsemblBacteria; AAP77530; AAP77530; HH_0933.
DR KEGG; hhe:HH_0933; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_7; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002495; 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; 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..899
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224487"
FT COILED 836..898
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT MOTIF 544..548
FT /note="'KMSKS' region"
FT BINDING 547
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 899 AA; 102812 MW; 0DE4FF6E80E89D3D CRC64;
MESKAQEKQE QKKGYNPQDI ESRFYAICEK RGYFEIEGNK SLWQGCAPKC FSIMMPPPNV
TGVLHIGHAL TFTLQDIITR FKRMEGFKTL YQPGLDHAGI ATQNVVLKQL LAQGITKESL
GREAFIAKVW EWKEQSGGEI LNQMRHLGIT PAWSRLRFTM DKGLQKAVKK AFVQWYNQGL
IVQDNYMVNW CVNDGALSDI EVEYEQNHGK LYYLRYPIKD SAQSLIVATT RPETFFGDTG
VMVNPNDERY KHLIGKSVIL PLLGREIPII ADSHVDMSFG SGCVKVTPAH DMNDYEVGKR
HNLPFITIFD EKGIFNKNAG IFQGQERLES RPLIVQKLQE NGFVEKIEDY TNQVGKCYRC
GNIVEPYISK QWFVKKETAH NAIQRVNNGE LHFYPAQWLN NYNAWMRELK DWCISRQLWW
GHRIPVWYCE CGNKVASESD NPICPQCQST ITKQDEDVLD TWFSSGLWAF STLGWGNEDT
NTQPPLYHAN DLAEFYPNSL LITGFDILFF WVARMILSGE SLLDSLPFKD VYLHALVRDE
NGQKMSKSKG NIIDPMEIIS SYGADTLRFT LAILCAQGRD VKLSTQSLEI SKNFTNKLYN
ATNFLNMYLE QLGGKEALKK GFGDINHIHI NTPLGQYMLV RFYTATNEVR AALENYRFND
GASILYRFLW GEFCDWGIEL AKASKDSIYE LGAIFKAALI LLHPYMPFIT DALWHTLNAS
DIQTSDSIMI HSYPKAMEKN EQHSQLERTF EVIQDVITSI RRLKAMLELG STNIECIFVK
LNAPFEHSLL EQFVCKLAKV KTLCITQQKP KDCVGDVSKY CECYIQLGEI DLQAIGTRLH
NQRQKLEKEI TKLQAMLGNE NFIKNAPKAV MEQNQSALHN AQEKLDKINA ELIALGLQS
