SYV_CLOTE
ID SYV_CLOTE Reviewed; 880 AA.
AC Q891R5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=CTC_02302;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015927; AAO36780.1; -; Genomic_DNA.
DR RefSeq; WP_011100441.1; NC_004557.1.
DR AlphaFoldDB; Q891R5; -.
DR SMR; Q891R5; -.
DR STRING; 212717.CTC_02302; -.
DR EnsemblBacteria; AAO36780; AAO36780; CTC_02302.
DR GeneID; 64179620; -.
DR KEGG; ctc:CTC_02302; -.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001412; 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..880
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224463"
FT COILED 717..741
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT COILED 810..880
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 527..531
FT /note="'KMSKS' region"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 880 AA; 102443 MW; 111925BCE67CC7A0 CRC64;
MNDNINIAKT YDPKEFEERI YKMWEEGEYF TPKVDKDKKP YTIVMPPPNI TGKLHLGHAL
DNSMQDFLIR VKRMQGYSTL WLPGQDHASI ATEVKVENEL LKTGLKKKEM GREAFLERVW
EWSEEYRGRI RDQLKKLGSS ADFTRESFTM DDNLDKAVRA VFVKLYEEGL IYKGNRIVNW
CPKCMTALSD AEIEYEENYG NFWHVKYPLV DSEEYLEIAT TRPETMLGDT AVAVNPNDER
YKHLIGKKLM LPLVNREIPI VADDYVDVEF GTGAVKITPA HDPNDYEVGK RHDLEEIIIM
NENGTINELG GKYSGMDRYE ARKAIVEDLK KEGFLVKVKE HIHNVSCHDR CNTIIEPMIS
KQWYVKMKEL AKPAIEVVKS GEIKFVPERF DKTYFNWMEN IQDWCISRQL WWGHRIPVWY
CKDCGETIVS LEEAKKCSKC SSENLIQDED VLDTWFSSAL WPFSTLGWPD KTEDLEYFYP
TDVLATGYDI IFFWVARMIF SGLHNMKEIP FKTVLIHGIV RDSEGKKMSK SLGNGVDPLE
VIDKYGADAL RFMLITGNAP GNDIRFYEER VESARNFANK IWNASRYVMM NLDKNLMEKY
KDCKDYNIAD TWILSRLNEV IKEVTDNIEK FELGMASQKV YDFMWNEFCD WYIELSKPVL
YGEDEKAKGV TFNVLFNVLT SGLKLLHPIM PFITEEIFIN IQEEEKTITT SKWPEFKEEL
KNEEVEKKMS HVIEAIKAIR NVRIEMDVPP SRKAKIMIYA LDGIDAFKDG KIYFEKLASA
SEVEFLNSKE EAPENAVSAV TKGAEIYIPL FDLVDLEKEM ERLNKEREKL EKEIERVDKK
LSNENFVKKA PEAVVNEEKA KGEKYKEMLE AVLERIKSLK
