SYV_MYCGE
ID SYV_MYCGE Reviewed; 837 AA.
AC P47576;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=MG334;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 801-837.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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; L43967; AAC71557.1; -; Genomic_DNA.
DR EMBL; U02249; AAD12537.1; -; Genomic_DNA.
DR PIR; I64236; I64236.
DR RefSeq; WP_010869437.1; NC_000908.2.
DR AlphaFoldDB; P47576; -.
DR SMR; P47576; -.
DR STRING; 243273.MG_334; -.
DR PRIDE; P47576; -.
DR EnsemblBacteria; AAC71557; AAC71557; MG_334.
DR KEGG; mge:MG_334; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_14; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 32262at2; -.
DR BioCyc; MGEN243273:G1GJ2-416-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 1.10.287.380; -; 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; 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..837
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106230"
FT COILED 767..837
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 514..518
FT /note="'KMSKS' region"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 837 AA; 97464 MW; 7F2FD1FE95D3D8C5 CRC64;
MKDKFSFQKN YDFNLVSDGL YEIWNNAGFF KPKDKNNSFT AILPPPNLTG TLHIGHAFEV
SITDQIMRFK KMQGFSINWI PGFDHAGIAT QTKYEKIALK ENQKYFDADD DKKSEMIMNW
ALNQSEIIKN QLKSLGVCLN WSETKFTLSE QANKIVNNCF KNLYENGFIY QAYTLVNWDT
KLNTAISNIE VINKPVNQHL HYVVYKLAND SKQELIVATT RPETIFADVC LLVNPKDKRY
TNFWNKLVVN PLTGKQIPVV TDSYVDIKFG TGILKCTPAH DFNDYEINTK YKFDFLSCID
SNGILNQNAS KFQGLSVLQA RNKIVKWLEK NKLLVKSIPL TSNVGFSERS GTVVEPMLSK
QWFVDLPKLK DHLYLKKYPD FIPKRFNKQV SNWLNKLKPW CISRQLIWGH KIPVWFENNT
GEIVVGEKPS KNLQNYTRSK DVLDTWFSSS LWPLICLNWE QDDSFHETEL LVTGYDILFF
WVLRMLFNSF FETKKLPFKT VLIHGLVRDE QNRKMSKSLN NGIDPVDLIR NYGADAVRLF
LCSNHTPGDD LIFSEQKIKS AWNFLNKLWN VTKFVIQLEN DQEISYDLDK LSLSETWILA
KLDKVIQKIT KLLDKFQLAL ANQILVKFVW DDFCNTFIEA IKKEPNQLKP QLFYTAKSVL
SNIAILLSIT VPFLSERIYQ QFNNKSVMQA TWPLATKIKI PKLFDLVLAA INDLRNYRKQ
YMLNSQQKLV VILSGKNAVD VKQYFNFSWI ELKIETNKKV SFKYQIVDDT TQRLKSLQKQ
QAFFESEVKR SQAIVKNKSF LEKAPKEKVK SEFLKLEEYQ KKLTETNQLI AKLTKAH
