SYV_NOCFA
ID SYV_NOCFA Reviewed; 893 AA.
AC Q5Z048;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=NFA_13480;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(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; AP006618; BAD56193.1; -; Genomic_DNA.
DR RefSeq; WP_011207878.1; NC_006361.1.
DR AlphaFoldDB; Q5Z048; -.
DR SMR; Q5Z048; -.
DR STRING; 247156.NFA_13480; -.
DR PRIDE; Q5Z048; -.
DR EnsemblBacteria; BAD56193; BAD56193; NFA_13480.
DR GeneID; 61132170; -.
DR KEGG; nfa:NFA_13480; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_11; -.
DR OMA; FATKLWN; -.
DR BioCyc; NFAR247156:NFA_RS06840-MON; -.
DR Proteomes; UP000006820; 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; 2.
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..893
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224520"
FT COILED 821..855
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 545..549
FT /note="'KMSKS' region"
FT BINDING 548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 893 AA; 98837 MW; 7CA50B88953097D7 CRC64;
MTSTAPDNSR NRADALPKSW DPSAVEAEMY ERWVSAGYFT ADPASGKPAY SIVLPPPNVT
GTLHMGHALD HTLMDTLARR KRMQGYEVLW LPGMDHAGIA TQTVVEKQLA VDGKTKEDFG
RELFVEKVWD WKRESGGAIQ WQMRALGDGV DWSRDRFTMD EGLSRAVQTM FKRLYDAGLI
YRAERLVNWS PELRTAISDI EVKHEDVEGE LVSLRYGSLN DDEPHVVVAT TRVETMLGDT
AVAVHPDDPR YRDLIGTTLE HPITGRQIPI VADDYVDPEF GSGAVKITPA HDPNDFEIGL
RHNLPMPTIM DERGRIANTG TEFDGMDRFE ARVKVRERLA REGRVVAEKR PYIHSVGHSE
RTGEPIEPRL SMQWWVKVEA LAKAAGDAVR NGQVVIHPAS QEPRWFEWVD NMHDWTISRQ
LWWGHRIPIW YGPDGEVVCL GPGETPPEGW VQDPDVLDTW FSSGLWPFST MGWPDATPEL
TKFYPTSVLV TGYDILFFWV ARMMMFGMYV AEDPALTAGK DPGQVQVPFK DIFLHGLIRD
QHGKKMSKSR GNGIDPLDWI RSYGADALRF TLARGAQPGG DLSVGEPHAL ASRSFVTKLF
NATKFALLNG AAPGELPDRG SLTDADRWIL DRLDEVLAEV DAAFDAYEFG KACEALYHFA
WDELCDWYLE LAKVQFAADG ARAESTRTVL GTVLDAVLRL LHPVIPFVTE SLWKALTGGE
SVVVAAWPTA SGVTPDADAA RRIADAQRLI TEIRRFRSDQ GLADKQKVSA KLIGVDSAEL
DALAPAIAAL ARLTEAGPDF AATASVEVRL SGATVTVELD TSGSVDLEAE RKRLEKDLAA
AQKELATTEG KLGNEAFLAK APEQVVDKIR TRRDVAAAEV ARIGARLAEL GAR
