SYV_STRCO
ID SYV_STRCO Reviewed; 874 AA.
AC O06851; Q9L1G3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=SCO2615;
GN ORFNames=SCC88.26c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 616-873.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=9503623; DOI=10.1111/j.1574-6968.1998.tb12873.x;
RA Burger A., Brandt B., Suesstrunk U., Thompson C.J., Wohlleben W.;
RT "Analysis of a Streptomyces coelicolor A3(2) locus containing the
RT nucleoside diphosphate kinase (ndk) and folylpolyglutamate synthetase
RT (folC) genes.";
RL FEMS Microbiol. Lett. 159:283-291(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; AL939113; CAB75396.1; -; Genomic_DNA.
DR EMBL; Y13070; CAA73510.1; -; Genomic_DNA.
DR RefSeq; NP_626852.1; NC_003888.3.
DR RefSeq; WP_011028455.1; NZ_VNID01000001.1.
DR AlphaFoldDB; O06851; -.
DR SMR; O06851; -.
DR STRING; 100226.SCO2615; -.
DR PRIDE; O06851; -.
DR GeneID; 1098049; -.
DR KEGG; sco:SCO2615; -.
DR PATRIC; fig|100226.15.peg.2661; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_11; -.
DR InParanoid; O06851; -.
DR OMA; FATKLWN; -.
DR PhylomeDB; O06851; -.
DR Proteomes; UP000001973; 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 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..874
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106236"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 805..871
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 531..535
FT /note="'KMSKS' region"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT CONFLICT 638..639
FT /note="KL -> NV (in Ref. 1; CAA73510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 874 AA; 97567 MW; AD11E4871786BAA0 CRC64;
MTENSQQPQP APSTELPTQY TPAEVEGQLY ERWVERGYFE ADAKSDKPPY TVVIPPPNVT
GSLHLGHAFE HTLIDALTRR KRMQGYETLW QPGMDHAGIA TQNVVERELG KEGKSRHDLG
REAFVERVWQ WKSESGGQIS GQMRRLGDAV AWSRERFTMD EGLSQAVQTI FKRLYDDELI
YRAERIINWC PRCLTAISDI EVEYQDDDGE LVSMKYGEGD ETIVVATTRA ETMLGDTAVA
VHPEDERYKH LVGKLIKLPL TDRSIPVVAD EHVDPEFGTG AVKVTPAHDP NDFEIGQRHG
LPAIAVMDEH AVITAHGPFQ GQDRLEARSA IVAALRAEGR IVAEKRPYVH SVGHCSRCKT
TIEPRLSMQW WVKVGPLAKA AGDAVRDGKV KIHPQEMEKR YFDWVDNLHD WCISRQLWWG
HRIPVWYGPE GEVVCVGPGE EPPSGEGWYQ DSDVLDTWFS SGLWPFSTLG WPEQTESLAK
FYPNSVLVTG YDILFFWVAR MMMFGLYAMD GTPPFHTIAL HGMVRDQNGK KMSKSFGNVV
NPLDWMDKYG SDALRFTLAR GANPGVDVPI GEDWVQGSRN FANKIWNATR FALMNGATVE
GPLPDASRMS STDRWILSRL NSVVAEVDAY YEDYQFAKLS DALFHFAWDE VFDWYVELSK
TTFQAGGEAA EVSKRVLGEV LDVTLRLLHP VVPFVTETLW TTLTGGESVV IAEWPTDSGF
RDAGAEREIE TVQSVITEVR RFRADQGLQP GQRVPARLTL AGSALAAHEA AVRQLLRLQP
EGDAFTATAT LPVAGVEVAL DLSGVIDFAA ERKRLAKDLA AAEKEKAQAN AKLGNEAFLA
KAPDQVVDKI RGRLAKADED ITRITAQLEK LPEA
