ID A0A1H3J1A6_9PROT Unreviewed; 919 AA.
AC A0A1H3J1A6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
GN ORFNames=SAMN05421754_10079 {ECO:0000313|EMBL:SDY33780.1};
OS Nitrosomonas sp. Nm58.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=200126 {ECO:0000313|EMBL:SDY33780.1, ECO:0000313|Proteomes:UP000199646};
RN [1] {ECO:0000313|Proteomes:UP000199646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm58 {ECO:0000313|Proteomes:UP000199646};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNPQ01000007; SDY33780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3J1A6; -.
DR STRING; 200126.SAMN05421754_10079; -.
DR Proteomes; UP000199646; 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; 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: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:UP000199646}.
FT DOMAIN 16..606
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 650..799
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 854..918
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 852..879
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 529..533
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 919 AA; 105140 MW; 13C303060FA4406F CRC64;
MELAKSFDPK LIEARWYSEW ESSGYFRPTN EKGAAAYCIV LPPPNVTGTL HMGHAFQHTL
MDALIRYHRM LGHNTLWQPG TDHAGIATQI VVERQLDQEN IDRRELGREA FLKRVWKWKE
ESGSTITRQM RRMGTSCDWS RERFTMDEML SQAVTEVFVR LYREGLIYRG KRLVNWDPVL
QTAVSDLEVI SVEETGSLWH ICYPFEQDTS ATLQEGGLVV ATTRPETMLG DMAVAVHPED
ERYRHLIGRH LRLPLSERTI PIIADDYVDP TFGTGCVKIT PAHDFNDYQV GLRHKLVPLN
IFTLDGKISE FAPAEYQGMD RFEARKRIIS DLEAQGLLVE TRSHKLMVPR GDRTQTVIEP
MLTDQWYVAM EGMAKRGLEA VASGEVRFTP ENWTHVYNQW LENIQDWCIS RQLWWGHRIP
AWYDEDGNVT VAHNLEEARQ LSGKESLRQD EDVLDTWFSS ALWPFSTLGW PQQTAELKTF
LPTSVLVTGF DIIFFWVARM VMMSLHFTGK VPFREVYVTG LIRDSEGQKM SKSKGNVLDP
LDLIDGILLP ELVKKRTIGL MNPKQAESIE KNTRKQFPQG IPAFGTDALR FTFASLASHG
RDIKFDLQRC EGYRNFCNKL WNATRFVLMN CEGQDTGLDD TLPLAFSHAD KWIIGRLQQA
EHSVAQAFNG YRFDLAAREI YEFIWDEYCD WYVEFAKVQL NFGSDAEQRT TRRVLVRVLE
TALRLAHPVI PFVTEELWQK VAPLAGKQGK NIICQPYPLA DLTRIDEEVS SRIALLKEII
NACRGLRGEM KLSPAARIPL LIEGDQSALA GFSAYLMALA KLSNVEIMPN GFPDADAPIA
VVGEFRLLLK IEIDVSAERE RLQKEILRLE VEISKARAKL DNPDFVQRAP EKVVTQERGR
LAGFNAMLSK LIEQLQRLN
//
