ID S5ZD29_9CREN Unreviewed; 808 AA.
AC S5ZD29;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02005};
GN ORFNames=N186_02635 {ECO:0000313|EMBL:AGT34908.1};
OS Thermofilum adornatum.
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=1365176 {ECO:0000313|EMBL:AGT34908.1, ECO:0000313|Proteomes:UP000015543};
RN [1] {ECO:0000313|EMBL:AGT34908.1, ECO:0000313|Proteomes:UP000015543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1910b {ECO:0000313|Proteomes:UP000015543};
RX PubMed=24029764;
RA Dominova I.N., Kublanov I.V., Podosokorskaya O.A., Derbikova K.S.,
RA Patrushev M.V., Toshchakov S.V.;
RT "Complete Genomic Sequence of 'Thermofilum adornatus' Strain 1910bT, a
RT Hyperthermophilic Anaerobic Organotrophic Crenarchaeon.";
RL Genome Announc. 1:e00726-13(2013).
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_02005}.
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_02005};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02005}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02005}.
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DR EMBL; CP006646; AGT34908.1; -; Genomic_DNA.
DR RefSeq; WP_020962212.1; NC_022093.1.
DR AlphaFoldDB; S5ZD29; -.
DR GeneID; 16573173; -.
DR KEGG; thb:N186_02635; -.
DR PATRIC; fig|1365176.7.peg.519; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000015543; 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; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
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 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; 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_02005};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02005}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02005};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02005}; Reference proteome {ECO:0000313|Proteomes:UP000015543}.
FT DOMAIN 18..573
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 613..756
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 808 AA; 93562 MW; 12387ABC4B2A060B CRC64;
MAEFKLPKVY DFKLVEEKWQ KTWEEKGLYR FRREDRTRPT FSIDTPPPYP SGDLHVGNAL
NFSYIDFVAR YKRMRDYNVF FPQGWDCHGL PTEVRVERAI GKRRSEVDPL EFLRLCKEYT
LKWIGDMRAA LKRLGLSIDW TTEYMTMNPD YWRRTQLSFV EMYKKGLIYR GEHPVIWCPR
CETAIAEAEV EYVEKSRPLY YIKFKVAETG EDVVIATTRP ELLASCVAVA VNPTDERYRS
LQGKHAVVPI YERKVPIIFD EDVDKTFGTG AVMICTYGDK TDVKWQKKHN LPLIISITDN
GRMNGNTGPL QGLPIEEARK KIAEILREKG LLVKTENIQS TVGTCWRCHT PVEILPKKQW
FVKSTALNEK VLEEAKRINW VPPYMYKRLE NWVLNLDWDW VISRQRLFAT PIPVYYCKDC
GAELVVPPEK LPHDPRFDSP PFEKCPKCGS KNIVPERDVM DTWMDSSITA AVHAGWPDNF
DERLFPADLQ PNGYDIIRTW DYYLLLRGIA LFGKPQFKTA LINGMVRGTD GRMMHKSYGN
YVAVTEVLEK YGADSFRLWV AMAASTGQDV RFSWEGVDYA HRFLVKIWNA ARLASSFIEE
VPPPSMEELS HVDHWILREL SETIRQVTSS LENYQFQEAS QRLVDFAWHK LCDHYLEIIK
YRLSQGDRVA KYVLRLVLLR TIQMLSVFAP HVSEEIYQEV LKGSENWESI TTSPWPEQVE
YDAEKAKTGE IVVAIIAEGR RAKHDAKIPL SKEISKLTIY TTMHLEELRK ATGDIAGTLR
AQKVEVTSSG RGDRAVPEYP EITISLQP
//
