SYV_SYNP6
ID SYV_SYNP6 Reviewed; 909 AA.
AC Q5N3J4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=syc0936_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008231; BAD79126.1; -; Genomic_DNA.
DR RefSeq; WP_011243248.1; NC_006576.1.
DR AlphaFoldDB; Q5N3J4; -.
DR SMR; Q5N3J4; -.
DR STRING; 269084.syc0936_c; -.
DR PRIDE; Q5N3J4; -.
DR EnsemblBacteria; BAD79126; BAD79126; syc0936_c.
DR KEGG; syc:syc0936_c; -.
DR eggNOG; COG0525; Bacteria.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001175; 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; 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.
FT CHAIN 1..909
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224586"
FT COILED 841..909
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 909 AA; 102990 MW; B50EA68C63C0FBD0 CRC64;
MTTSASQLQT QYSPAATEVR WQKLWEETSA FQANSQSSAE PYCIVIPPPN VTGSLHMGHA
FEASLIDVLI RFQRMRGKNA LWLPGTDHAS IAVQTILDRQ LREEGLSRYD LGREKFLERA
WQWKAESGGT IVGQLRRLGV SVDWSRERFT MDEGLSKAVL EAFIQLYEEG LIYRGQYLVN
WCPASQSAVS DLEVEMKEVD GSLWYFRYPL TDGSGHLEVA TTRPETMLGD TAVAVNPQDK
RYQHLIGKTI TLPLVQREIP IIADPWVEAE FGTGCVKVTP AHDPNDFAMG QRHQLPLITV
MNKDGTMNEN AGQFEGLDRF EARKAVVAAL EEAGFLVKVE DYRHSIPISD RGKVPVEPLL
STQWFVKIEP LAQRALEALN GEEGPRFVPE RWTKVYRDWL ENLRDWCISR QLWWGHQIPA
WYAVSETNGV VTDSTPFVVA KSAEEAQQQA IAQFGPDVVL QQDEDVLDTW FSSGLWPFST
LGWPNQTEDL ETFYPTSTLV TGFDIIFFWV ARMTMMAGHF TGKMPFKDVY IHGLVRDENN
KKMSKSAGNG IDPLILIDRY GTDALRYALI REVVGAGQDI RLDYNRKTDE SATVETSRNF
ANKVWNASRF VMLNLDDKTP EQLGMAATAD LELADRWILS RYHATTEALI NQIEAYDLGA
AAKQLYEFIW GDFCDWYIEL VKPRLYGEDA QSRLVAQQTL AQILEGILRL LHPFMPHVTE
EIWHTLNQVG EDQFLALQSF PQPQSEWIQP ELDREFQLMI DVIRTLRNLR AEAGLKPGQK
ITAILQSDSE SERCNLEQSQ AYIRDLTKTE MLTIVESLTE EPQALVGVTA TVQVLLPLAG
LVDLAALQTK LSRNLEKVEK EIKSLSGRLN SSNFVDKAPA EVVAETRENL LEAEKQAELL
RDRLTRLQA
