SYV_PROMT
ID SYV_PROMT Reviewed; 933 AA.
AC Q46IA7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=PMN2A_1281;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(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}.
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DR EMBL; CP000095; AAZ58771.1; -; Genomic_DNA.
DR RefSeq; WP_011295625.1; NC_007335.2.
DR AlphaFoldDB; Q46IA7; -.
DR SMR; Q46IA7; -.
DR STRING; 59920.PMN2A_1281; -.
DR EnsemblBacteria; AAZ58771; AAZ58771; PMN2A_1281.
DR KEGG; pmn:PMN2A_1281; -.
DR HOGENOM; CLU_001493_0_2_3; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR PhylomeDB; Q46IA7; -.
DR Proteomes; UP000002535; 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; Reference proteome.
FT CHAIN 1..933
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224532"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 866..932
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 57..67
FT /note="'HIGH' region"
FT MOTIF 557..561
FT /note="'KMSKS' region"
FT BINDING 560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 933 AA; 105937 MW; A518759154005130 CRC64;
MIERVKTTKL SEASGLPKTY DPVGTENRWQ KAWEEKGAFK PDPSAPGDPF SVVIPPPNVT
GSLHMGHAFN TALIDTVVRY KRLKGNNVLC LPGTDHASIA VQTILERQLK EEGKNRRDLG
RASFLEKAWE WKEKSGGRIV DQLKRLGYSV DWSRERFTLD EGLSKAVSEA FVRLHEKGLI
YRGEYLVNWC PASGSAVSDL EVEMKEVDGH LWHFRYPLVT SSVSSAKQIS YLEVATTRPE
TMLGDVAVAV NPSDERYKDL IGEKLTLPLV GRTIPIIGDP HVDKDFGTGC VKVTPAHDPN
DFEIGQRHDL PQITVMTKKG TMNHNAGQFE GLDRFEAREA VIDSLKEIGL LTKIEAYKHS
VPFSDRGKVP VEPLLSTQWF VKMDPLSSSC SEFFEKGQPK FIPNRWSKVY RDWLTDIRDW
CISRQLWWGH RIPAWFVISQ TDNKVVNETP YIVARTEDEA KKLAREKYGD SVKIEQDEDV
LDTWFSSGLW PFSTLGWPDE THPDFQRWYP TNTLVTGFDI IFFWVARMTM MAGVFTERMP
FADVYIHGLV RDEQNRKMSK SAGNGIDPLL LIERYGTDAL RFALVREVAG AGQDIRLDFD
RKNQTSATVE ASRNFANKLW NATRFALINL EDQDYENLES YDSSKLQLSD RWILSRLARV
NHETANRYEN YALGEAAKGL YEFAWNDFCD WYLELIKRRL NNSENLSSDE LLDRKIAKSV
LYKVLSDLLI MLHPLMPHLT EELWHGLTGL DEDQFLALQP WPKSNEQDLN LDLESSFSDL
FASIRLIRNL RAVAGLKPSQ KVPVMLVSGK EVLQKTLTTS INDIAVLTKA KEVQILSPEQ
AKSLPSMKAL AGVSGELEVV LPIEGLIDIA SLRSRLEKDL NKAQKEIESL SGRLANKNFV
DKAPKDVVEE CRANLTESEA QVRLVKERLM GLD
