ID E6PYR1_9ZZZZ Unreviewed; 938 AA.
AC E6PYR1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 Name=valS {ECO:0000313|EMBL:CBI00070.1};
GN ORFNames=CARN3_1052 {ECO:0000313|EMBL:CBI00070.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI00070.1};
RN [1] {ECO:0000313|EMBL:CBI00070.1}
RP NUCLEOTIDE SEQUENCE.
RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA Le Paslier D.;
RT "Diversity of trophic interactions inside an arsenic-rich microbial
RT ecosystem.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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:CBI00070.1}.
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DR EMBL; CABN01000086; CBI00070.1; -; Genomic_DNA.
DR AlphaFoldDB; E6PYR1; -.
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; 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; 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:CBI00070.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CBI00070.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 55..607
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 663..815
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 871..935
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
SQ SEQUENCE 938 AA; 106107 MW; 4F44BF0774A4F076 CRC64;
MRAPESMPHD LPKAYDPTAI EDHWAEYWVR EQIFTQPALQ DAQAVQMQAF LDRLQDEYKS
PFTILLPPPN VTGRLHMGHM LNQTEMDILT RWQRMRGERS ALWVPGTDHA GIATQMMVER
QLAEQGLSRQ ELGRDAFLDR VWAWKKLYGG AILDQMKRLG ASVDWSREYF TMDDNLSVAV
REAFVRLHEQ GLIYRGAYIV NWCPRCQTAI SDLEVVHEEQ NGKLWEIRYP VAGHASQFLT
IATTRPETLL GDVAVAIHPE DERFLHLHGK KLLLPLVGRE IPIVLDDWVS RDFGTGAVKV
TPAHDPNDFA LGQRHHLPSI NVMDDQGRIN AEGGAYTGLD RYVARKRILA DLETQGLLAT
VRDHKLSAGV CDRCKTVVEP RLSEQWFLRI QPLAEKAIQA VELGTIRFTP EQYKKTYLNW
MTNIHDWCLS RQLWWGHRIP AWHCADCNKM TVARQDPTAC AHCGSSRIKQ ETDVLDTWFS
SGLLPVSVFG WPFADGKPSA DFATFYPTSL LVTGFDILFF WVARMIMLGC WFTQDIPLPD
GLPRRFEDTV PFREVYIHAL VRDAHGDKMS KTKGNVVDPI ETVRQYGTDA VRFTLASMAS
PGTDIAFNIA RTEGYRAFAN KIWNAARFIF MNVDRAAEVG IVVDLNQAGG MPVVSVEAPI
EARWIVAELH RTTSAVNLSL ENYRFDEAAN FIYQFFWGQF CDWYLEIVKL RLNFTESQNL
PAASAALNTL VIVFEAALRL LSPFMPFLTE EIWHAIYNGN PPWKSIALAK YPLAQTGAIE
NAAIEAMESL QSLITEVRAL RKEIGVEEKA QTPVLIRTDV HLQKVFSENQ PMIERLARVS
EIRFESLLSE DLTTRSTANF DVAVVYQRTV DVAAESERLN KEIARLEKGL LSAEKQLGNS
SFLSKAPVAV VDGLKKQQTE TTLLLAKAQQ ALAALGKS
//
