ID A0A101VHA2_9SPHN Unreviewed; 598 AA.
AC A0A101VHA2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=APF78_00285 {ECO:0000313|EMBL:KUO54388.1};
OS Sphingomonadales bacterium BRH_c3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX NCBI_TaxID=1734408 {ECO:0000313|EMBL:KUO54388.1, ECO:0000313|Proteomes:UP000061825};
RN [1] {ECO:0000313|EMBL:KUO54388.1, ECO:0000313|Proteomes:UP000061825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c3 {ECO:0000313|EMBL:KUO54388.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUO54388.1}.
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DR EMBL; LOET01000093; KUO54388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VHA2; -.
DR Proteomes; UP000061825; 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 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; 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; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
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 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 15..590
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT NON_TER 598
FT /evidence="ECO:0000313|EMBL:KUO54388.1"
SQ SEQUENCE 598 AA; 67670 MW; 01207ED98E6DB589 CRC64;
MQLPKTFDPA AIEAKWYSHW EDNGLFRPAR PDAQPFTIVN PPPNVTGSLH IGHALDNTLQ
DVVIRYERLR GKDALWVVGT DHAGIATQMV VERQLEERQD KRTNYTREEF IAKVWEWKEE
SGGTITRQLR RLGCSMDWSR EQFTMDPHFT RAVTKVFVDL YNRDLIYRDK RLVNWDPKLK
TAISDLEVET HDVQGHFWHF KYPLAGGVTT ADGADHLVVA TTRPETMLAD MAVAVHPDDA
RYKSVVGKHV VLPITGRRIP IVADEHADPE LGSGCVKITP GHDFNDFEVG KRAGIAPADM
LNMLDAEARV CQTSDGLIPG ELLSLDRFDA RKAVVERLKA EGCQISYVDK DGVEHDAEPR
TIATPFGDRG GVVIEPWLTD QWYVNAEKLA KKPIEAVKSG EIEIVPKSWE KTFFNWMENI
QPWCVSRQLW WGHRIPAWYG PDGAVFVAES EEEAEAQAGA GVTLTRDDDV LDTWFSSALW
PFATLGWPNP PQNGEDLLSR HYPNSLLISG FDILFFWDAR MMMMGQAMTG QNPWPRLYLH
GLVRAPDGQK MSKSKGNVVD PLGLIDNYGA DALRFFMAAM ESQGRDIKMD EKRVEGYR
//
