ID A0A1J4VVV6_9BACT Unreviewed; 808 AA.
AC A0A1J4VVV6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
DE Flags: Fragment;
GN ORFNames=AUJ71_01140 {ECO:0000313|EMBL:OIO39257.1};
OS Candidatus Omnitrophica bacterium CG1_02_49_16.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1805290 {ECO:0000313|EMBL:OIO39257.1, ECO:0000313|Proteomes:UP000182296};
RN [1] {ECO:0000313|EMBL:OIO39257.1, ECO:0000313|Proteomes:UP000182296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_49_16 {ECO:0000313|EMBL:OIO39257.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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 -!- 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:OIO39257.1}.
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DR EMBL; MNVU01000020; OIO39257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4VVV6; -.
DR STRING; 1805290.AUJ71_01140; -.
DR Proteomes; UP000182296; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
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; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-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 Pfam; PF10458; Val_tRNA-synt_C; 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; SSF46589; tRNA-binding arm; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:OIO39257.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 2..493
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 541..682
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 741..805
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 746..808
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OIO39257.1"
SQ SEQUENCE 808 AA; 93466 MW; 44EE013924196D29 CRC64;
VVEKSLREEG ISRHTLGREK FLERVWKWRE KYGHTIINQL KRLGASCDWD RTRFTMDEGL
SVAVREVFVR LYEKGLIYRG KYIINWCPRC QTALSDEEVQ HKDITGYLYY LKYAIEGSDQ
YLVIATTRPE TMLGDTAVGY NPSDERYQYL EGKTALLPLL NRRLKIIKDS SIDPKFGTGA
LKITPAHDPV DFNLAQKHNL EFINILNPDG TLNAQAGSFQ GLDRFEARRK IIAELEDRRI
LLETKEHVHA VGHCYRCQTI VEPYLSLQWF VHMKPLAKPA IVAVKEGKIV FVPKRWTKVY
LEWMTHIKDW CISRQIWWGH RIPVWYCSQC RAQHTPGGEA FKKFEFTGKV YKEPGMIISR
HTPEKCPDCG STNLAQDADV LDTWFSSWLW PFSTLGWPGK NKDLDFFYPT VCLVTGYEII
FFWVARMIMS GFEFMGKEPF KQIYIHGIVR DETGAKMSKS LGNAVDPINI IDDFGADALR
FAVISITSEG QDVFASKEKL EVGRNFSNKI WNAARFAIMN MSLKSEDLKK APKISALNPV
DRWIMSRLNQ TIVEVGKSLD TLRFNEAAAT LYDFFWHQFC DWYLEFAKPN ITSKETQWVL
YTVLNDSLKL LHPFMPFITE EIWQKIPHEG DSIMVNAWPK SNKKWLDKKT EAEVSLIISE
IQAIRNVRSA WQINPKDPVS AVVKASRDKE LGILKKYSSY IAQMARISAL QIGKNLVRPK
ESAVANIGRV ETYVVLSGLI DIRMERQRIE LALSDVEKMM KNLEGRLRNT DFINKAPKDI
VDKERRKAKE LENRKKRLEE NLRTLADA
//
