SYV_TREPA
ID SYV_TREPA Reviewed; 956 AA.
AC O83998;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=TP_1035;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC26589.1; -; Genomic_DNA.
DR PIR; B71250; B71250.
DR RefSeq; WP_010882479.1; NC_021490.2.
DR AlphaFoldDB; O83998; -.
DR SMR; O83998; -.
DR STRING; 243276.TPANIC_1035; -.
DR EnsemblBacteria; AAC26589; AAC26589; TP_1035.
DR KEGG; tpa:TP_1035; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_12; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000811; 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..956
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106241"
FT COILED 885..911
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 69..79
FT /note="'HIGH' region"
FT MOTIF 566..570
FT /note="'KMSKS' region"
FT BINDING 569
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 956 AA; 107363 MW; 7D50583C7C6BA35A CRC64;
MTQKLQKIVL PPVYGPADFE ARVYACWEQR QAFSPRARGS GTSDSEGCDG HSRQIEGGAR
TFVIAIPPPN ITGVLHMGHC LNTVLQDIVI RYQRMAGACT LWIPGTDHAG IATQHVVERA
LRKEGIHKRE VTREQFVART QQIKDSHQDT IRMQLRKMGA SCDWTCERFT LDAGMSASVR
EAFVTLYERG LLYRSMYLVN WCPRCGTALS DDEVFHQEKD GALYYVRYPL LPRTEEEGNG
VPPPLGTAQV GETIIIATTR PETILADVAV AVHPDDARYQ SLIGRKVCVP MVNRIVPIIA
DSYVAQDFGT GMVKITPAHD PNDWDIGTRH SLEAINMLNP DGSLNDQVPA AYRGLSCAQA
RIQIVADLQA HGLLSREERI VHSVGVCYRC EAVIEPYLSL QWFVKMKPLA SQALAAWKRA
DVQFHPKKWE NTYVRWLEHI RDWCISRQLW WGHRIPVWYC AQCAQQTVSR VDVQRCAHCG
SADITQDPDV LDTWFSSWLW PFSTLGWPQE TQKLRAFYPT SAVITAYDII FFWVARMIMA
GLEFTQTVPF RDVYLHGLVR DKQGRKMSKS LNNGVDPLHI IRTYGADALR FTLAFMCAQG
QDVLIEMDSF KMGSRFANKV WNASRYILGN LEGRRVYAIA HVSLTELDRW IFHTFNETVQ
QVRTALEAYR FNDAAQAVYE FFWNSFCDWY VEASKCSFQK PDEQEKDRAA SVLCTLLEET
LRLLHPFLPF VTEEIYRSLS PSVHDTTQAI PSGAHALLMC APYPVYVPSR VDARACAHIG
AVQEIVRAVR TLRAACGIDP QKAVSVRLRP SSPAQDANAA AQVSCVHDPG AVARTYEELI
CVLAGISSLV YLESDAPKPQ VAVATAGTGF ELFLVTTEGI DRTMLCARLQ KAWQKARQKV
QQVERKLADA QFCTHAPEEV VTAERKKLAE ARATCHTLAG YLADMNGKPG PLSDSD
