SYV_TREDE
ID SYV_TREDE Reviewed; 909 AA.
AC Q73MZ2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=TDE_1364;
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS11881.1; -; Genomic_DNA.
DR RefSeq; NP_971970.1; NC_002967.9.
DR RefSeq; WP_002678931.1; NC_002967.9.
DR AlphaFoldDB; Q73MZ2; -.
DR SMR; Q73MZ2; -.
DR STRING; 243275.TDE_1364; -.
DR EnsemblBacteria; AAS11881; AAS11881; TDE_1364.
DR GeneID; 2739465; -.
DR KEGG; tde:TDE_1364; -.
DR PATRIC; fig|243275.7.peg.1310; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_12; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008212; 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; -; 2.
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..909
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224591"
FT COILED 843..902
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 52..62
FT /note="'HIGH' region"
FT MOTIF 542..546
FT /note="'KMSKS' region"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 909 AA; 103905 MW; 5C6C961DB1887F98 CRC64;
MSEKLQAIEL EKSYNPKEFE ERIYSFWEAN KCFSPIKKKN TKNTFTVVIP PPNVTGVLHV
GHALDETLQD VIVRYHRMKG DETLWIPGTD HAGIATQSVV EKKLKAEGKN RRDLGREAFI
EKVWEVKNEH HSIITKQLRK MGVSVDWDRE RFTLDEGLSQ AVREVFVSLY EQGLIYQGNY
LVNWCPSCGT AISDDEVEHE DRKGGMYHIY YKLADGAVLQ NEAGEKIQEI EIATTRPETL
LGDTAIAVHP EDPRYASIIG KEVILPLANR KIPVIADSYV DKEFGTGVVK ITPAHDPNDW
EVGKRHNLPV LNILNPDGTL NDAVPEKYRG LSTEKARKAV IEDLEELGLF KNEEKIKHAV
GCCYRCHTSI EPYVSKQWFV KMQPLAQKAL DAWKKGDVVF YPQKWENTYA HWMNNIRDWC
ISRQLWWGHR IPVWYCADCG KTIVSRTDIT ECPHCKSKNI KQDEDVLDTW FSSWLWPFST
LGWPEKTEDL ARFFPTSALV TGHDIIFFWV ARMIMASLQF TGKAPFKDIF IHGLVRDKQG
RKMSKSLGNG IDPLVAIEEF GADAMKFTLT FMCGSQSQDF LIDMESFKLG SKFANKVWNA
SRYILGNLAG RTIVPVGRDG SLNSLKELDR WIYHELNEAA QTVRSSLDSY RYNEAAQKVY
EFFWNNFCDW YVEGTKLSFK YGDEKEKDRA ASVLLAVLEE SLRLLHPFLA FVTEEIYSKL
PGNCAEGALP RAKILMTSDY PEEKKERIDE AASIRFRTLQ EIVRNIRALR AECGIDPQLK
LKVSLYIEKN SPAEAARENS EIIEMLSGLS GLDFIDSLKE KPASSIGVVG AGFEAFLITG
DSIDIDQLKK RFEKELEKNE QNASKIDSKL KNENFVKNAP PEVIEGEKEK HAEFLRRIEK
LKGYLEGMR
