SYV_MYCMS
ID SYV_MYCMS Reviewed; 872 AA.
AC Q6MTU2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=MSC_0303;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(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; BX293980; CAE76944.1; -; Genomic_DNA.
DR RefSeq; NP_975302.1; NC_005364.2.
DR AlphaFoldDB; Q6MTU2; -.
DR SMR; Q6MTU2; -.
DR STRING; 272632.MSC_0303; -.
DR EnsemblBacteria; CAE76944; CAE76944; MSC_0303.
DR KEGG; mmy:MSC_0303; -.
DR PATRIC; fig|272632.4.peg.323; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001016; 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; 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 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..872
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224512"
FT COILED 796..872
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 523..527
FT /note="'KMSKS' region"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 872 AA; 103264 MW; 0C1A5C13836D3371 CRC64;
MKKQLNPKYD HLQVEKDKYQ YWLDKNLFKA DINSNKPKFS IILPPPNVTG KLHIGHAWDT
SLQDAIIRFK KLTGYDTLFL PGMDHSGIST QVKVEAKLKQ QGIDKNKLGR EKFLLEAWKW
KEEYANIIRK QWAKLGLSLD YSTEKFTLDE DINQIVKEIF VKFYNDQIIY KDKQIVNWDP
EQKTAISNVE VIYKETQSKM YYFKYILEDS NEYLTVATTR PETMFADQCL VVNPNDSRYQ
KYINKKVINP VNKQVIPIIS DEYVDIEFGT GVMKCTPAHD LNDYHLGIKH NLKMPICLNI
DGSVNQLGGK YQGLDRFVAR KKIIKNAIKE DLFVKEEDII NQVGFSERSN AIVEPYLSDQ
WFVKMDKFKN MVIDLQNSDN KINFYPNRFS DVLNRWMTDA HDWCISRQLW WGHQIPCWYH
KKTNEMYVGI NPPSDIENWT QDQDVLDTWF SSGLWAFSTL LNNKGLESEY FKNYFPTSVL
VTGYDIIFFW VARMIFQTLE YTKQIPFKDV LIHGLVRDES NRKMSKSLGN GIDPMDVINN
NGCDSLRLFL LTNSTPGQDI RYSNEKILAS WNFINKLWNA SRYVFLNLDE DFKFDPNFYK
TDLEITNQWI LTQLSKTQTY VYEKMNKYEF SLAGNHLWDF VWNKYCSWYI EFSKVNLNND
KFTHQTKQTL FYVLKEILIM LHPLIPFVSE EIYLNMMLKE SILLEQWTNL NSNYDTSFID
DVIKMITSIR EFRNTKNIKN DVCLSVNISN TNQNHTKLFK KHFDQIYNFL FNFCNTKLVD
EAIKNKTSLS IDEYFIEIAN DSFINKNELI KELEQKQNYL NNEITRSQKI LNNQEFIKKA
KPEKIQSEKI KYQNYLDQLQ AIKDKLKELT ND
