SYV_MYCPU
ID SYV_MYCPU Reviewed; 827 AA.
AC Q98QV4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=MYPU_2570;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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; AL445563; CAC13430.1; -; Genomic_DNA.
DR PIR; A90544; A90544.
DR RefSeq; WP_010925061.1; NC_002771.1.
DR AlphaFoldDB; Q98QV4; -.
DR SMR; Q98QV4; -.
DR STRING; 272635.MYPU_2570; -.
DR EnsemblBacteria; CAC13430; CAC13430; CAC13430.
DR KEGG; mpu:MYPU_2570; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; MPUL272635:G1GT6-258-MON; -.
DR Proteomes; UP000000528; 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; 3.40.50.620; -; 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; 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; 2.
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..827
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224514"
FT COILED 765..827
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 511..515
FT /note="'KMSKS' region"
FT BINDING 514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 827 AA; 98163 MW; CD7D402ECDC349FB CRC64;
MDSKYNHYEI EKDKNQKWID KKYFINHDLD KKPFSIILPP PNVTGQLHLG HALNGYLQDS
VIRYKKLEGY DVLFLPAMDH AGIATQIKVE ESLAKENLLK QDIGREKFLK FSYQWKDKYA
NIIKSQWNKL GLALDYSSER FTLDQDSKDT VNKVFIDLYN AGIIYQGVKG INWDPLQKTA
LSNVEVINKE TPQKMYYIKY FLENSDEFVE IATVRTETLY SDRAIGINPN DLRAKNYVNK
FVIHPLTKKR LPIITDDYID QSFASGFMKI SAHSLADIDI LNKNNLEIVE SIDESGFLTN
ICDEFEGMER FEAREKIAQK LQKENLISRV ENYSSNIGYS DRTKVPIEIL VKKQWFVKMD
LFSKMVLDSL ESKNKVNFYP SRFKKNLEGW MNKTYDWTIS RQLWWGHQIP AWYKDEQTKV
QLNSPGPDWT QDPDVLDTWF SSAIAPFSFF GWPNTYKKLK RYYPTSLLVT GHDIIFFWVS
RMYFSGLYFM KDKPFNDVLL HGLIRDEQRR KMTKSLGNGI DPMVLIDQYG SDSLRWFLIT
NTTPGLDITY NEEKIKSSWN FMNKLWNIAR FINLQENTKK VSMSKYDYWI SDKFNKVESY
VKKFMKKYEF TLIGKEIYKF IINDFSSWYL EFSKITKNID FQKVIFKRLL LLLHPFIPFL
TDHLFKIIYD QELLEHTFEN KKLKTQKNNV DQLILVIRAI REFREKYQIS KKEKIKYWIQ
DCQFLQEDID AINFLTFSEL SQNSENMTIV ENIKIFMILP KNIEENLSKE KAQKIEFLKF
EIKRAQSLLL NEKFISKAPT LKVEEEKAKL EKYQLQLKEL LDEKIIE
