ID A0A0A2TGE6_9FIRM Unreviewed; 400 AA.
AC A0A0A2TGE6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=JT05_13450 {ECO:0000313|EMBL:KGP74927.1};
OS Desulfosporosinus sp. Tol-M.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP74927.1, ECO:0000313|Proteomes:UP000030439};
RN [1] {ECO:0000313|EMBL:KGP74927.1, ECO:0000313|Proteomes:UP000030439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Abu Laban N., Tan B., Dao A., Foght J.;
RT "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT probing of toluene- degrading methanogenic culture enriched from oil sands
RT tailing of Alberta, Canada.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:KGP74927.1}.
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DR EMBL; JQID01000193; KGP74927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2TGE6; -.
DR STRING; 1536651.JT05_13450; -.
DR Proteomes; UP000030439; Unassembled WGS sequence.
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 Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:KGP74927.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000030439}.
FT DOMAIN 1..353
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 364..397
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGP74927.1"
FT NON_TER 400
FT /evidence="ECO:0000313|EMBL:KGP74927.1"
SQ SEQUENCE 400 AA; 46056 MW; C579689CA10788CD CRC64;
YNTLWLPGTD HAGIATQARV EEQLAIEGTN RLELGRERFL ERVWDWKRQY GGQITRQLRR
LGASCDWERE RFTMDEGCSK AVREAFVTLY NKGLIYRGNY IINWCPKCHT TISDIEVEHV
DREGNLYHLC YPVKDSDETF VVATTRPETM FGDTAVAVHP DDERYRHLIG KTVLLPLTER
EIPIIADDYV DREFGTGALK ITPAHDPNDF EIGLRHQLPQ IVVLDKEAKM NENAGPYRGM
DRFEARLAVV KELLAQGILL KTEPYAHAVG ECYRCSTVIE PMVSKQWFVK MEPLAKPAIE
VVKGGSLEFI PERFAKIYLG WMENIRDWCI SRQLWWGHRI PVWYCEDCGL EICAGDDPLT
CPTCGADRLL QDPDVLDTWF SSGLWPFSTL GWPRKTPEQE
//
