SYV_PELUB
ID SYV_PELUB Reviewed; 875 AA.
AC Q4FM20;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SAR11_0960;
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC Pelagibacteraceae; Candidatus Pelagibacter.
OX NCBI_TaxID=335992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062;
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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; CP000084; AAZ21768.1; -; Genomic_DNA.
DR RefSeq; WP_011282067.1; NC_007205.1.
DR AlphaFoldDB; Q4FM20; -.
DR SMR; Q4FM20; -.
DR STRING; 335992.SAR11_0960; -.
DR EnsemblBacteria; AAZ21768; AAZ21768; SAR11_0960.
DR GeneID; 66295450; -.
DR KEGG; pub:SAR11_0960; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002528; 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; -; 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..875
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224525"
FT COILED 810..875
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 525..529
FT /note="'KMSKS' region"
FT BINDING 528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 875 AA; 101993 MW; F2F6FD92B09C00DC CRC64;
MSNDKYIHTD VEDKIYSYWE KNNLFKPTKN KKQFSVVIPP PNVTGSLHMG HALNNSIQDL
LVRYHRMNNY ETLWQPGTDH AGIATQALVE KKLTADGIDK NEIGREKFIE KVWEWKEEHG
DIILNQLKKL GCSCDWSRNA FTMDENLSKS VLKVFVELHK KGLIYKDKKL VNWDTVLKTA
ISDLEVDQRE VNSKIYYIQY PIEASSDFIT IATTRPETML GDTAIAVNPK DDRFKHLVGK
FVTVPIVGKK IKIIEDEYAD PEMGTGALKI TPAHDFNDYE VGQRNNLEII NIFTEGGKVN
ENAPKEYIGL DRFEARKRII KELKEKEFFV KEENIKNKVP YGDRSNSIIE PFLTEQWFVD
AKKLSIKAKD IVNSKKTNFF PANWSKTYFQ WMNNIEPWCI SRQLWWGHQI PAWYGPDKKI
FVAINEEEAK LDAKKFYNKD VDLIRDPDVL DTWFSSGLWP FATLGWPDNK EYVDKFYPTS
VLVTGFDIIF FWVARMIMFG MEFLDKEPFK DVYVHALVKD EKGQKMSKSK GNVINPLDLI
EKYSADALRF TLLSMASPGT DVKLSEDRVK GYRNFLNKLW NANNFLITNN CDFSKIDEKP
ILSININKWI YAELIETKNK IEKNLKDYRF DEAAKNAYQF TWHSYCDWYL ELSKTILFSE
DEKAKDEVRQ VSAYVFKQIL ILLHPFIPFV TEEIWLNNKF DNTGKDFLML ANWPSGEFER
DTSINQVEKI ISIVSELRSF KNELSVSPGS FIDISIETVS KKEQSFFTEN EIILKKLGRI
KNLYNKDLDK PTATLMVSGD LFKVYFDEDV DLELIKKNLT TRQNKYQEEM NKISQRLANK
GFVDRAPKDI VDQEKTNYNN LKNDVERISI TIKGL
