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Database: UniProt
Entry: A0A068YSR8_9BURK
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ID   A0A068YSR8_9BURK        Unreviewed;       992 AA.
AC   A0A068YSR8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000256|HAMAP-Rule:MF_02004};
OS   Polaromonas sp. CG9_12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS50529.1, ECO:0000313|Proteomes:UP000043372};
RN   [1] {ECO:0000313|EMBL:CDS50529.1, ECO:0000313|Proteomes:UP000043372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Smith H.J., Foreman C.M., Ramaraj T.;
RT   "Draft Genome Sequence of a Metabolically Diverse Antarctic Supraglacial
RT   Stream Organism, Polaromonas sp. Strain CG9_12, Determined Using Pacific
RT   Biosciences Single-Molecule Real-Time Sequencing Technology.";
RL   Genome Announc. 2:1-2(2014).
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner. {ECO:0000256|HAMAP-Rule:MF_02004}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR   EMBL; CCJP01000005; CDS50529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068YSR8; -.
DR   STRING; 1504672.gene:199030774; -.
DR   eggNOG; COG0525; Bacteria.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000043372; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; 2.
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:0000256|HAMAP-Rule:MF_02004};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_02004};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000043372}.
FT   DOMAIN          45..663
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          719..868
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          927..990
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   COILED          932..992
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           70..80
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           586..590
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   992 AA;  111619 MW;  915FADE265C36A4D CRC64;
     MTHAATPTPT APATDAAKVF PLTPGLDSLA KSFEPADIER HWGPLWEQSG QYEPTLDAAK
     PSFAIQLPPP NVTGTLHMGH AFNQTIMDSL TRYHRMKGDN TLWVPGTDHA GIATQIVVER
     KLQSETGKTR HDMGASPAEA RKNFVAKVWE WKEESGSTIT RQMRRMGDSV SWKHEYFTMD
     PKMSKVVTST FVQLYEQGLI YRGKRLVNWD PVLKSAVSDL EVESEEEDGF MWHIRYPLAD
     GAGDITVATT RPETMLGDVA VMVHPEDERY VHLIGQQVTL PLCGRTIPVI ADDYVDKDFG
     TGVVKVTPAH DANDYAVGQR HNLPIICVLT LDAAINDNAP EKYRGMDRFV ARKAVVADLE
     AQGFLVEVKK HKLMVPRCTR TSQIIEPMLT DQWFVAVNKV SEQDPTGKSI AQKAIDAVDS
     GAVRFVPEQW VNTYNQWMGN IQDWCISRQL WWGHQIPAWY DEDGQVYVAV DEAEAKERYW
     EEKHKQEPEL VPLLIKLKYS EVKLRRDEDV LDTWYSSALV PFSSLGWPEK TKELDLFLPS
     SVLVTGYDII FFWVARMIMM TTHFTGQVPF QHVYIHGLVK DSQGKKMSKS EGNVLDPVDL
     IDGIELAPLL DKRSQGLRKP ETAPQVRKNT EKEFPAGIPA YGADALRFTF ASLASLGRSI
     NFDSKRCEGY RNFCNKLWNA TRFTLMNCEG QDCGLREHTK AECAPGGEME NYLDFSQADR
     WIASTMQRVE ADVAKGFVEY RLDNVAGHIY QFIWDEFCDW YLEIAKVQIQ TGNDAQKRAT
     RRTLIRTLEG ILRLAHPLIP FITEELWQKV APVAGKAGPF IGQAPYPQSQ PEKIDPQAEA
     HVAKLKTLVD ACRNLRGEMK VSPATRLPLL VVGDDDFINA VAPVLKSLAK LSEVKLFAME
     AQWVAAAEAA PVAVIGDARI CLYMEVDVAA EKARLGKEAA RLEGELVKVQ AKLANETFVA
     KVPPAVLETE RRRLTEFTNT LEKIREQLAR HK
//
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