ID F4B4C1_ACIHW Unreviewed; 816 AA.
AC F4B4C1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=Ahos_1346 {ECO:0000313|EMBL:AEE94229.1};
OS Acidianus hospitalis (strain W1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=933801 {ECO:0000313|EMBL:AEE94229.1, ECO:0000313|Proteomes:UP000008458};
RN [1] {ECO:0000313|EMBL:AEE94229.1, ECO:0000313|Proteomes:UP000008458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1 {ECO:0000313|EMBL:AEE94229.1,
RC ECO:0000313|Proteomes:UP000008458};
RX PubMed=21607549; DOI=10.1007/s00792-011-0379-y;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA She Q., Liu S.J., Garrett R.A.;
RT "Genomic analysis of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 15:487-497(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W1;
RA You X.Y., Liu C., Wang S.Y., Jiang C.Y., Shah S.A., Prangishvili D.,
RA Liu S.J., Garrett R.A.;
RT "Genomic analyses of Acidianus hospitalis W1 a host for studying
RT crenarchaeal virus and plasmid life cycles.";
RL Extremophiles 0:0-0(2011).
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};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|RuleBase:RU363035}.
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DR EMBL; CP002535; AEE94229.1; -; Genomic_DNA.
DR AlphaFoldDB; F4B4C1; -.
DR STRING; 933801.Ahos_1346; -.
DR KEGG; aho:Ahos_1346; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR Proteomes; UP000008458; 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: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 CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035}.
FT DOMAIN 27..580
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 623..765
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 816 AA; 95213 MW; 453A55F799A212CD CRC64;
MLSQEYVTKK MEEWPKHYNP AEIEPKWENL WLSKEYWEKV FRFDEKSNKP VFYIDTPPPF
TSGELHMGHA YWVTIADAIA RFKKLQGYNV LIPQGWDTQG LPTELKVQYK LGIPKENREL
FLQKCIEWTN EMINRMKTAM IRLGYRPDWE DFEYKTYSPE YRKVIQKSLI DMYKMGIVKI
KEGPVYWCPK CETAVAQSEV GYLEKEGVLV YIGFPLKAGG EIVIATTRPE LLAATQAIVV
NPTDERYKDL IGKTAIVPIF NKEVKIIADE AVEKDFGTGA VMVSTYGDPQ DIKWKLKYNL
PSTEIIDNKG RIKGTGILDG LTVPQAKQKM IEILKEKGYV RRIEKIKHNV LSHTERSDCL
SPIEFLTKKQ IYIDVLKFKD KLLEEYKKMQ FKPSRMSYYL EEWIKSLEWD WNISRQRVYG
TPLPFWYCDN NHLIPAKEED LPVDPTKTKP PYEKCPYCGL PLKPVTDVAD VWIDSSVTVI
YLSGFYTNKE RFAKAFPASL RLQGTDIIRT WLFYTFFRTL MLTGNVPFKQ VLINGQVLGP
DGSRMSKSKG NVVSPLERVN EFGADAIRMT LLDASIGEDF PFKWDNVRGK KLLLQKLWNA
SRLSYPFIHG KNISKPNDLH VLDKWILIKH KKFVKKAIEA YNSYDFYIII DELYNYFWET
VADEYLELIK YRLFNEDQSA LYTLRRILKD IIILLHPIVP HITEEIYSRL FGDKISVLLE
ELPNVDDIEE DNEAEKIGDY VKKFNSMVRT SKIKNKMSIV TPVNVKLYAS NEMIESIKKV
ENDVKITLKI NSLEYIPSQD REEVIIEKYE NQPMGV
//
