ID A0A1G2F8R9_9BACT Unreviewed; 763 AA.
AC A0A1G2F8R9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=A2174_00465 {ECO:0000313|EMBL:OGZ34466.1};
OS Candidatus Portnoybacteria bacterium RBG_13_41_18.
OC Bacteria; Candidatus Portnoybacteria.
OX NCBI_TaxID=1801991 {ECO:0000313|EMBL:OGZ34466.1, ECO:0000313|Proteomes:UP000177725};
RN [1] {ECO:0000313|EMBL:OGZ34466.1, ECO:0000313|Proteomes:UP000177725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGZ34466.1}.
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DR EMBL; MHMV01000022; OGZ34466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2F8R9; -.
DR Proteomes; UP000177725; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 17..597
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 658..763
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 216..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 88138 MW; 2651B6374D3187BD CRC64;
MESENKPYNP AEIEKEIYQI WEKSGYFNPD NLKLKKGAKP FCIIMPPPNA NEALHLGHAL
TITIEDILIR FNRMRGKKTL WLPGSDHAGF ETQVVFEKKL EKEGKNRFDF DRDTLYKIIW
DYVQNNKHMM ESQTRALGAS CDWSREKFTL DPKIIEIVYA TFKKLYDDGL VYRGKRVINW
CPKHQTSFSE LEVKYEERED KLWYIKYPIV NIANGTNLDT NNTNPPQPSL KGGSDSPPLG
GVREDFEPKY IIVATTRPET MLGDTAVAVN PKDKRYKNLI GQKVKLPLTN REIAIIADSA
VEIDFGTGAV KVTPAHDQTD FEIAERHNLE ILEVISKNGK MTDIVPEPYR GLKTNEAREK
IVADLNAQGL IEKEEPYKHT VGSCYKCGRT IEPLVSEQWF IKIRPLADKA IAAVKKGQTK
FVSKKYEKIF MHWMKNIHDW NISRQIVWGI RIPAWYCQEC KNITVTDGKT PTKCEKCDSQ
KLKQEEDVFD TWFSSGQWPF ATLIASQPDD FENFYPTTVM ETGWDILFFW VARMMMMGIY
CTRKVPFKYV YLHGMIRDKD KQKMSKSKDN AINPIGVLEE RGADALRMSL VFGAGTDSDL
PFSEEKVIAQ QRFANKIWNA SKFVLSAIDD MDSPLLEKEG LGEILHPEDT DKKFTKEDKW
ILKELQTATK KITKDIEKFK FHEAAQGAYH FFWHSFCDKT IEDVKIRIAN GSKDAEAGKL
VLWTVLYNSL KLLHPFMPFV TEAIYQKLPS RPKEMLMIEE WPE
//
