SYV_PARMW
ID SYV_PARMW Reviewed; 914 AA.
AC Q7U3N4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, 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=SYNW2396;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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; BX569695; CAE08911.1; -; Genomic_DNA.
DR RefSeq; WP_011129249.1; NC_005070.1.
DR AlphaFoldDB; Q7U3N4; -.
DR SMR; Q7U3N4; -.
DR STRING; 84588.SYNW2396; -.
DR EnsemblBacteria; CAE08911; CAE08911; SYNW2396.
DR KEGG; syw:SYNW2396; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_3; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001422; 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..914
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224587"
FT COILED 847..914
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 538..542
FT /note="'KMSKS' region"
FT BINDING 541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 914 AA; 101672 MW; E865813770584A93 CRC64;
MPELAKTYDP VGTEARWQQA WEDQGAFHPD PKAPGEPFSV VIPPPNVTGS LHMGHAFNTA
LIDTIVRYQR LAGKNVLCLP GTDHASIAVQ TILEKQLKQE GKTRHHLGRD GFLERAWQWK
AESGGRIVGQ LRRLGYSVDW QRQRFTLDEG LSEAVKEAFV RLHEQGLIYR GEYLVNWCPA
SGSAVSDLEV EMKEVDGHLW HFRYPLSSGD GHLEVATTRP ETMLGDTAVA VNPTDERYAH
LVGQTLTLPF VGREIPIVAD DHVEKDFGTG CVKVTPAHDP NDFAIGQRHG LPQITVMRKN
GTMNKEAGQF EGLDRFEARK AVVAGLDELG LLVKVEDYRH SVPYSDRGKV PVEPLLSTQW
FVRTEPLAAR CREALEKQDP RFIPERWEKV YRDWLTDIRD WCISRQLWWG HRIPAWFVIS
ETGGKYTDTT PYVVARNEVE ALEKAKAKYG AAAVIEQDED VLDTWFSSGL WPFSTLGWPD
AESADLQRWY PTSTLVTGFD IIFFWVARMT MMAGAFTGEM PFQDVYIHGL VRDEQNRKMS
KSAGNGIDPL LLIDRYGTDA LRFALVREVA GAGQDIRLDY DRKTDTSATV EASRNFANKL
WNATRFALMN LGDETPAQLG DPDPAALQLA DRWILSRLAR VNRETAERYS NYGLGEAAKG
LYEFAWNDVC DWYLELSKRR LNPGENPSAE ALADQRVAKQ VLAKVISQMH QMLHPLMPHL
TEELWHSVTG KSETTFLALQ PWPALQESAL DDALEASFAD LIGAIRVVRN LRAVAGLKPS
QSVPVRFVTG RGELAAVLNQ GTADITALTR AESVAVMAPA EADAAPVAKA LAGVSGELQV
LLPIEGLVDL DALKGRLEKD IAKAEKEIKG LAGRLGNPNF ADKAPPEVVA ECQANLDEKQ
AQADLARKRL ADLS
