SYV_HALSA
ID SYV_HALSA Reviewed; 881 AA.
AC Q9HMG9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=VNG_2547G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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 -!- 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; AE004437; AAG20602.1; -; Genomic_DNA.
DR PIR; F84404; F84404.
DR RefSeq; WP_010903904.1; NC_002607.1.
DR AlphaFoldDB; Q9HMG9; -.
DR SMR; Q9HMG9; -.
DR STRING; 64091.VNG_2547G; -.
DR PaxDb; Q9HMG9; -.
DR PRIDE; Q9HMG9; -.
DR EnsemblBacteria; AAG20602; AAG20602; VNG_2547G.
DR GeneID; 5954081; -.
DR GeneID; 62885664; -.
DR KEGG; hal:VNG_2547G; -.
DR PATRIC; fig|64091.14.peg.1973; -.
DR HOGENOM; CLU_001493_0_2_2; -.
DR InParanoid; Q9HMG9; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 4914at2157; -.
DR PhylomeDB; Q9HMG9; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..881
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224622"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 528..532
FT /note="'KMSKS' region"
FT BINDING 531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 881 AA; 99196 MW; 9C83F900A70BE192 CRC64;
MTELPDSYDP NSIEPKWQDE WQERDVYRFD PSESDTQYVI DTPPPYPSGN LHLGHALGWS
YIDFVARYRR LKGDAVLFPQ GWDCHGLPTE VKVEEVNDIH RTDVPSDEFR EMCIDWTEDR
IDEMKATMQE LGFSQDWDSE YRTMDPEYWG KTQESFSEMA DAGMVYRDEH PVNWCPRCET
AIADAEVENI DREGTLHYVT FDGVDNGDIE IATTRPELLA ACVGIVVSPD DDRYADRIGD
TFEVPLFGQD VELLADDDVD ADFGSGAVMV CTFGDKQDVE WWMDHDLDLR TVFTEDGHLN
EAAGEFAGLA IDDAKTQVAE ELDDQGYLND TEPTEQSVGS CWRCDTAIEI LSKEQWFVEV
DQDRILDAAA DAEWVPEHMH DRLVEWTEGM DWDWVISRQR VFATPIPAWE CNECGHWEIA
GREQAPVDPT EDDPAVEACP ECGGDDWAGE TDVMDTWMDS SITPLHLSGW PEGTTLDEFE
SVDLRPQGHD IIRTWAFYTL LRTGALTDEQ PWDDVLVNGM VFGEDGNKMS KSRGNFVQPD
EAIAEYSADA VRQALALGGR PGSDVQFQWK EVKSASRFLT KLWNITKFST GHFDEDTPAI
QDPAYRDADR WLLSELSTVC EDVDEAMSEY RFDRALRSLR EFAWEDLADD YVELVKGRLY
NGRPGERAAA EHTLYTAVTA VTRLLAPFSP HTTEEIWQSL PGTEGSVHAA TFPSVEYRDA
DAELAGKRIA EVAREIRAWK SDQGMPLNAD LDRVELYFDD SDDDAARLDT YDLSETVNAP
IRLIDGRPDV ELVPVDVDGD DSEIGPEFRS DAGTVMEAIA AADPAAIQAQ IHSGDTVTVE
ADGESFDLDA DWLTVTEEYR ASSGEEVTVI EASFGTVIIY E
