SYV_NOSS1
ID SYV_NOSS1 Reviewed; 1014 AA.
AC Q8YX97;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=all1318;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(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; BA000019; BAB73275.1; -; Genomic_DNA.
DR PIR; AC1971; AC1971.
DR RefSeq; WP_010995490.1; NZ_RSCN01000060.1.
DR AlphaFoldDB; Q8YX97; -.
DR SMR; Q8YX97; -.
DR STRING; 103690.17130665; -.
DR PRIDE; Q8YX97; -.
DR EnsemblBacteria; BAB73275; BAB73275; BAB73275.
DR KEGG; ana:all1318; -.
DR eggNOG; COG0525; Bacteria.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR BRENDA; 6.1.1.9; 8113.
DR Proteomes; UP000002483; 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; IPR025564; CAAD_dom.
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; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF14159; CAAD; 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..1014
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224428"
FT COILED 947..1014
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT MOTIF 542..546
FT /note="'KMSKS' region"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1014 AA; 113713 MW; A6906A8763528F8A CRC64;
MTATITNLPS LYDPFTTEAK WQKFWEENQI YKADPNKGGE PYCVVIPPPN VTGSLHMGHA
FESALIDTLV RYHRMQGRNT LWLPGTDHAS IAVHTILEKQ LKAEGKTRQE LGREKFLERS
WQWKAESGGT IVNQLRRLGV SVDWSRERFT LDEGLSKAVA EAFVSLYDEG LIYRGEYLVN
WCPATQSAVS DVEVESKEVE GNLWHFRYPL TDGSGYVEVA TTRPETMLGD TAVAVNPNDD
RYKHLIGKTL TLPITQQEIP IISDELVDPA FGTGCVKVTP AHDLNDFEMG KRHNLPFINI
LNKDGTLNAN GGEFAGQDRF VARKNVVSRL ETDGFLVKIE DYKHTVPYSD RGKVPVEPLL
STQWFVKIRP LADKSLAFLD EKNSPEFVPQ RWTKVYRDWL VNLRDWCISR QLWWGHQIPA
WYAVSETNGQ ITDNTPFVVA KSTNEAWEKA KSQFGENVQL EQDPDVLDTW FSSGLWPFST
LGWPEQTPDL AKYYPTTTLV TGFDIIFFWV ARMTMMAGHF TGQMPFQTVY IHGLVRDENN
KKMSKSANNG IDPLLLIDKY GTDALRYTLV REVAGAGQDI RLEYDRKKDE SPSVEASRNF
ANKLWNAARF VMMNLDGLST GDLGLGTGNS QSLELSDGVP PSLADRWIIS RYHQVIKQTT
HYIDNYGLGE AAKGIYEFIW GDFCDWYIEL VKSRLQKDAD PLSRKAAQQT LAYVLEGILK
LLHPFMPHIT EEIWQTLTQQ PEDSPQTLAL QAYPQADVNL INPALETQFD LLIGTIRTIR
NLRAEAEVKP GAKIIANLQT DSESERQILM AGQSYIKDLA KVETLTIAAG QQPSTVTKKK
PQKGLKTIGL VIAGLVFLRV ALAVADTVDN VPFLGTFFEI VGLGYSAWFV TRNLLSTPAR
KRFLAKFFAP PTEKNLSGTV QQAPEAAEKS IAGVVGTVQV VIPLAGVVDI ETLRAKLERS
ISKAETEAQS LKGRLSNPKF VDKAPADVVQ AARDALAEAE KQVEILRLRL QTLV
