SYV_GLOVI
ID SYV_GLOVI Reviewed; 897 AA.
AC Q7NCQ9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=glr2919;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(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; BA000045; BAC90860.1; -; Genomic_DNA.
DR RefSeq; NP_925865.1; NC_005125.1.
DR RefSeq; WP_011142913.1; NC_005125.1.
DR AlphaFoldDB; Q7NCQ9; -.
DR SMR; Q7NCQ9; -.
DR STRING; 251221.35213489; -.
DR EnsemblBacteria; BAC90860; BAC90860; BAC90860.
DR KEGG; gvi:glr2919; -.
DR PATRIC; fig|251221.4.peg.2948; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_3; -.
DR InParanoid; Q7NCQ9; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR PhylomeDB; Q7NCQ9; -.
DR Proteomes; UP000000557; 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; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
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..897
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224483"
FT COILED 839..897
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 532..536
FT /note="'KMSKS' region"
FT BINDING 535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 897 AA; 101225 MW; B4ED97F44F6FDD10 CRC64;
MARTLPSQYD PFDAEPRWQR FWEEHRFFSP AADGPGKPFS LVLPPPNVTG SLHMGHALCF
TLPDVVVRYR RMKGFKTLWL PGTDHASIAV HTVLEKQLRQ EGKTRFDLGR EAFLERAWAW
KERSQDTIRG QLRRLGLSLD WTRESFTLDE KRNRAVVKVF VDLHRKGLIY RGKYLVNWCP
ASQTAVSDLE VDDKEEKGHL WQLRYPVADS DEFLVVATTR PETMLGDTGV AVHPEDPRYK
HLIGREAELP ILGRRIVIVG DEAVDREFGT GAVKVTPAHD PNDFEIGKRH GLPMINLLNP
NGTYNENAGP YAGLDRFVVR KQVVARAAAE GWLVGIEDHV HNVPYSERGG VPIEPYLSDQ
WFLDVSGMAT RVLEAFDSQN QPAFVPERWG KVYRDWLVRI RPWNISRQLW WGHRIPAWFV
AGSEGEYVVA HDEAEAFAVA RERYGPDVQL QRDQDVLDTW FSSSLWPFTT LGWPDQTEDL
GVFYPNALMS TGFDIIFFWV ARMAMMAGEF TGQIPFETVY INGLVRDEKG QKMSKTKGNG
IDPIEMMDKY GTDALRYTLV REVTGAGQDV RFDYNRKTGE SGAVDASKRF ANKIWNASRF
VLMNLDELTP AALGAADPGS LTLEDRWILG RLGQTARQID ELLGRYALGE AARSLYEFIW
DDFCDWYVEL AKPRLEALET RRGAQQVLAA VLDRTLRLLH PWMPHLSEEI WQLLHQPLEV
ASICVQPFPT GTDLPAEPPA EFALMQQIVR TIRNLRAFAQ VPPLRTLPAV RLASRNAEER
AAIDATRQAI AHLGRVEQLP LEEVADEHLK QVAVGVAGTV QVMLPLGGLV DVAALAGKLR
RSLEKLDKES GVLAARLDNA SYLANAPAEL VTESRAKLAE QRAQAAILAE QLARLEN
