ID I0A2F7_FERFK Unreviewed; 820 AA.
AC I0A2F7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN OrderedLocusNames=FFONT_1176 {ECO:0000313|EMBL:AFH43164.1};
OS Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940).
OC Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae;
OC Fervidicoccus.
OX NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH43164.1, ECO:0000313|Proteomes:UP000007391};
RN [1] {ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RA Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V.,
RA Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Fervidicoccus fontis complete genome analysis confirms its distinct
RT phylogenetic position and predicts its environmental function.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFH43164.1, ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RX PubMed=24366681; DOI=10.1007/s00792-013-0616-7;
RA Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V.,
RA Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA Ravin N.V.;
RT "Analysis of the complete genome of Fervidococcus fontis confirms the
RT distinct phylogenetic position of the order Fervidicoccales and suggests
RT its environmental function.";
RL Extremophiles 18:295-309(2014).
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};
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DR EMBL; CP003423; AFH43164.1; -; Genomic_DNA.
DR AlphaFoldDB; I0A2F7; -.
DR STRING; 1163730.FFONT_1176; -.
DR KEGG; ffo:FFONT_1176; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR InParanoid; I0A2F7; -.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000007391; Chromosome.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-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 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; PS50903; RUBREDOXIN_LIKE; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:AFH43164.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000007391}.
FT DOMAIN 421..473
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 820 AA; 96100 MW; 4FC82A69A69DE112 CRC64;
MENNGSSNII EEKRWDIKKE NEIIERWKKE NIGKFRKEDL GRKPTLVIDT PPPYPSGKWH
VAGAAHYVHH DMIARFFRMI GYNVLLPFYA DRNGLPVEVS VEKKTGINPH EVSSTPEGRE
KFLALCKKEL DSIEEEMVKL LERLGCSYDY WKNGTDSEEY RKLTQATFRE LWKKGLIYVA
ERPVNWCPRC KTTLSDAELE YKELETYLYY IKFKIRETND YVTVATTRPE LLSSCKALIY
HPSDPRYSGL EGKTAISPIY EKELKIYKNE NADPNFGTGL VMICSYGDED DIKMFRELGL
EPEIVVDRDG RLNEKAGFLK GMKTHEARTK IAEELEKRGL MVKKEKLMHK VPVCWRCGTP
IEFIHVREYF LKQIEFKDKL LEAIDKMKFY PEMHKQKLID WINSIKTDWP ISRDRYYATE
IPTWRCKKCN SILVPEDFKY YRPWKDEPPF EKCPVCGADK SYLEGEKKVF DTWFDSSISS
LYITGYMRDN ELYEKLKNDI LRPQGYEIIR TWLYYSILRV YQLTGRPAFK YVRITGMGLD
EKGEAMHKSK GNVIDPFPVI ESYGADAFRF WAASAAKVGY DYRFNPNLLK TGLLFTTKLW
NISRFISRFP DPGKEKAGKN TIDKAILEYT KMTLRKYISS FKEMDTYEPS NLVYSFTWDI
FASNYIELVK QRAYNLNNEW SKEDQESAWA TLHLVLRTIL LMTAPIMPFI SDEIWRLMKN
CGSIHQASLT QEINAEEGIN DKLTQIIDLM VKVNSDIWKY KKQNGLKFSD EIAKVVYIPQ
ELKEAEKDLK ALHKLKYISY EYPPPGEGAI KLDNIVYIEK
//
