ID N6YL57_9RHOO Unreviewed; 994 AA.
AC N6YL57;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02004,
GN ECO:0000313|EMBL:ENO83072.1};
GN ORFNames=B447_01676 {ECO:0000313|EMBL:ENO83072.1};
OS Thauera sp. 27.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=305700 {ECO:0000313|EMBL:ENO83072.1, ECO:0000313|Proteomes:UP000013140};
RN [1] {ECO:0000313|EMBL:ENO83072.1, ECO:0000313|Proteomes:UP000013140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=27 {ECO:0000313|EMBL:ENO83072.1,
RC ECO:0000313|Proteomes:UP000013140};
RA Liu B., Shapleigh J.P., Frostegard A.H.;
RT "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENO83072.1}.
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DR EMBL; AMXB01000002; ENO83072.1; -; Genomic_DNA.
DR RefSeq; WP_002935895.1; NZ_AMXB01000002.1.
DR AlphaFoldDB; N6YL57; -.
DR eggNOG; COG0525; Bacteria.
DR Proteomes; UP000013140; Unassembled WGS sequence.
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 CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 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; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02004};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000013140}.
FT DOMAIN 16..674
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 723..874
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 928..993
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 597..601
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 994 AA; 111628 MW; C58F29750CB999BC CRC64;
MELAKSFEPA DIERRWYPEW ESRGYFDAGL DKSNPNAFCI LLPPPNVTGT LHMGHGFNQT
IMDALTRYHR MRGDNTLWQP GTDHAGIATQ IVVERQLDAQ GISRHDLGRE KFLEKVWEWK
EYSGGTITRQ MRRLGTSPDW KRERFTMDEG LSKTVTETFV RLYNEGLIYR GKRLVNWDPK
LGTAVSDLEV VSEEEDGKLY HILYPFTDGP IGELRGLTVA TTRPETLLGD VAVMVHPEDE
RYAHLIGKTV ALPLTGRHIP IIADDYVDRE FGTGCVKVTP AHDFNDYAVG QRHKLDMIVV
LKLDGSVPAV AERYTSDGIT LDGVAMPATV AGLDRVPARD AVVTELEQLG LLIEVKAHKM
QVPRGDRTSV VIEPMLTDQW FVAMSKPGAD GKSITQKALE VVASGEIKFY PENWVNTYNQ
WLNNIQDWCI SRQLWWGHRI PAWYDEEGKI YVASCEEEAI HAWKADLQAE IDALTAEVQA
RQSQGQTAAD YPAIAERLAV LHARHDAGHL RQEDDVLDTW YSSALWPFST LDWTPEWPGK
SNDALDLYLP STVLVTGFDI IFFWVARMVM MTKHITGKIP FRHVYVHGLI RDAEGQKMSK
SKGNVLDPID LIDGIALDEL VGKRTYGLMN PKQAQSIEKK TRKEFPEGIP AFGTDALRFT
FASLASPGRD IKFDLARCEG YRNFCNKLWN ATRFVLMNCE GQDCGIGDNV ACSTEVLDFS
FADRWVVSRL QRTEAEVATQ FEAYRFDLVA RAVYEFVWDE YCDWYLELAK VQIQTGTPAQ
QRATRRTLLR VLETVLRLAH PLIPFITEEL WQTVAPLAGR RDGDSIMRVR YPQADMSRID
EACEAKVAEL KAMVYACRNL RGEMNISPAQ RLPLVAAGDK AALAVYAPYL AGLAKLSDVQ
IVDEIGADEL APVAVAGATR LMLKVEIDIA AERERLGKEI ARLEGEIAKA EGKLGNASFV
DRAPAAVVQQ ERDRLAGFKV TVDKLKPQLA KLGG
//
