ID A0A191HXC4_9FIRM Unreviewed; 874 AA.
AC A0A191HXC4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ORFNames=AZF37_05885 {ECO:0000313|EMBL:AMP21418.1};
OS endosymbiont 'TC1' of Trimyema compressum.
OC Bacteria; Bacillota.
OX NCBI_TaxID=243899 {ECO:0000313|EMBL:AMP21418.1, ECO:0000313|Proteomes:UP000196836};
RN [1] {ECO:0000313|EMBL:AMP21418.1, ECO:0000313|Proteomes:UP000196836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1 {ECO:0000313|EMBL:AMP21418.1};
RA Shinzato N., Aoyama H., Saitoh S., Nikoh N., Nakano K., Shimoji M.,
RA Shinzato M., Satou K., Teruya K., Hirano T., Yamada T., Nobu M.K.,
RA Tamaki H., Sanghwa P., Kamagata Y.;
RT "Complete genome sequence of the intracellular bacterial symbiont 'TC1' in
RT the anaerobic ciliate Trimyema compressum.";
RL Submitted (MAR-2016) 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 ---------------------------------------------------------------------------
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; CP014606; AMP21418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A191HXC4; -.
DR KEGG; ett:AZF37_05885; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000196836; 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 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:UP000196836}.
FT DOMAIN 13..561
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 604..751
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 810..874
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 808..870
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 522..526
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 874 AA; 101207 MW; 4CB47F6471411FE8 CRC64;
MSSKYNAKEV ESKWYPWWEK NGYFHQEVDE SKEPFCIVMP PPNVTGQLHL GHAMDNTLQD
ILIRFKRMEG YNTLWVPGTD HAGIATQARV EEELKKTEGL TRQDLGREAF LEKVWNWKAL
YHKRITSQLR LLGSSCDWQR ERFTLDDGCL DAVKEVFIRL YEKGLIYRGK YIVNWCPSCL
TTISDIEVEH EDDESSLWHI RYPIDGTRDY ITIATTRPET MLGDTAIAVA PDDERYQDYI
GKFAILPLIN RKIPIIADDY VDKSFGTGAV KITPSHDPND FEIAGRHNLP QIVVIDQKGN
MTGDVGKYLG MDRDSCRVAI VEDLEKAGFL ISIEPHTHAV GKCYRCGTII EPLVSSQWFV
KMDSLAKRAL EEVKKGEAKF ITERFTKVYT SWLENIKDWC ISRQLWWGRR IPVWYCEDCG
EMMGSKESLE KCTKCNSTNI YQDPDVLDTW FSSALWPFST LGWPEKTKEL EQFYPTSVLV
TGRDIIFFWV ARMLFMGLEF MDKVPFKEIF IHGLILDSKG RKMSKSLGNG IDPIEIIENY
GADTLRFMLV TGNTPGNDIS FQKDRLEGVR NFCNKIWNAS RFLMMNLEGC NGEMPNKSLF
TLADKWILNE YNETIKKVTH NFDEYELGEG ADTIYDFIWN SFCDWYIEIA KNRLYNGTAE
EKIVVKWILN KVLIGSMKLL HPFMPFITEE IWQHLPHKGE TIMLDSWPTV NEEECFITEK
NQMESIMETI RLVRNIRAEI NVPLGKKASI YLFVKNENEE LAKLAIPYLE TMANSEAVTI
GFEGDDKPAK AATGITKKFE VYLPLEHLID MSAERKRLEK ELAHLEKEVQ RIEKKLNNEG
FVKKAPAKVI EGEKEKLAGY REQYNAVKER WEDL
//
