ID A0A1F5GE21_9BACT Unreviewed; 731 AA.
AC A0A1F5GE21;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=A3D07_03020 {ECO:0000313|EMBL:OGD90123.1};
OS Candidatus Curtissbacteria bacterium RIFCSPHIGHO2_02_FULL_42_15.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1797716 {ECO:0000313|EMBL:OGD90123.1, ECO:0000313|Proteomes:UP000177124};
RN [1] {ECO:0000313|EMBL:OGD90123.1, ECO:0000313|Proteomes:UP000177124}
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:OGD90123.1}.
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DR EMBL; MFBF01000054; OGD90123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5GE21; -.
DR STRING; 1797716.A3D07_03020; -.
DR Proteomes; UP000177124; 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 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 6..565
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 630..727
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 731 AA; 85111 MW; 62E56C0EAB2128DC CRC64;
MTDEKQIYNF WENTGLFKAN IKSSKKTFSL LIPPPNLTGE LHIGHAMQHS VLDAIARFRR
LQGFDVLLLP GVDHAGIAFE NTFDKELKKQ NLSKEKLGRE KWLEAAWQFK ENIYNSVSQS
WRFMGLSADW SQEVFSLDEK RKTAVFHQFK KYYDDGLIYK GPYIVQWCPK CNTAIEDLEM
EYEEKKEKLY YVRYQVKGQG SKVKGQNFIE IATTRPETIF ADTAVAFYRN HPKFKKFVGQ
KVINPLTKNA IPVIEDKRVE KDFGTGALKI TPAHDILDYQ IGKDHKLEIL HAVNKEGRLT
DITGEFCGQK IDEAKEKVVE KLRTLGALSK EEDYIHSVAV CERCKTTIEP LISEEWFVRV
EKLAKGAIDV IKKDKIKFLP SNYAKILTDW LNNIHDWCIS RSLWWGHRIP VWYPSTREVH
PERGRRARSG SSDMKVSLDP PGPDWKQDEQ VLDTWFSSGL WPLSTLGWPD KTKEFDRYFP
WDFEISAPEI KYLWIARMVM ISNYFTGKKP FKTMFFHGTL RDLEGRKFSK SLGNGIEPQY
LIDKWGTDAT RMALYTYSIP GRDGRVSKET LDERGKNFRN FATKLRNIAR FVLELKPPGA
SHSRPDRESD SHFRGNDKEA VEKVIMPKDD QWIMGKLAKT TKTVTKHLEN LELHLASEEI
YEFIWHKFAD DYIEASKSRR PEAQSTLENI LKQTLILLHP FMPFLTEELY QKFEDKQKSI
LLEKWPSATN A
//
