SYV_OCEIH
ID SYV_OCEIH Reviewed; 883 AA.
AC Q8EPN2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=OB2061;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR EMBL; BA000028; BAC14017.1; -; Genomic_DNA.
DR RefSeq; WP_011066456.1; NC_004193.1.
DR AlphaFoldDB; Q8EPN2; -.
DR SMR; Q8EPN2; -.
DR STRING; 221109.22777745; -.
DR EnsemblBacteria; BAC14017; BAC14017; BAC14017.
DR KEGG; oih:OB2061; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_9; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 32262at2; -.
DR PhylomeDB; Q8EPN2; -.
DR Proteomes; UP000000822; Chromosome.
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 Gene3D; 1.10.287.380; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR11946; PTHR11946; 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; SSF46589; SSF46589; 1.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..883
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224521"
FT COILED 813..848
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 52..62
FT /note="'HIGH' region"
FT MOTIF 529..533
FT /note="'KMSKS' region"
FT BINDING 532
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 883 AA; 103087 MW; F51DC447C0B364A5 CRC64;
MEQDKENKQS LPSKYNPKEV EEGRYQFWLD GKFFEATGDP DKEPYSIVIP PPNVTGRLHL
GHAWDTSMQD TITRMKRMQG YDVLWLPGMD HAGIATQAKV EARLKESGTN RYELGREKFL
EKAWEWKEEY AAFIRSQWEK LGLGLDYSRE RFTLDEGLSD AVREVFVKLY EKGLIYRGEY
IINWDPSTKT ALSDIEVIYE EIQGKFYHMR YPIKGSDETI EIATTRPETM LGDTAVAVHP
KDERYQHLIG KTVILPIVGR EIEIVADDYV DMELGSGAVK ITPAHDPNDF EIGNRHQLER
ILVMNEDGSM NENAGKYQGL DRFECRKQIV KDLKEQGVMF NIEERTHQVG HSERSGAVVE
PYLSTQWFVK MDPLAKSALD MQADADEKVN FVPDRFERTY FNWMDNIRDW CISRQLWWGH
RIPAWYHKET KEIYVGKEAP ADIENWEQDE DVLDTWFSSA LWPFSTMGWP NEDSADLKRY
FPTNVLVTGY DIIFFWVSRM IFQSKEFMNE KPFEDTLLHG LIRDADGRKM SKSLGNGVDP
MDVIEKYGAD SLRYFLMTGS TPGQDLRFHW EKVESTWNFA NKVWNASRFS IMNMEGFTYE
DIDLTGELSL PDRWILARLN ETIEQVTRNS NKYEFGEAGR HLYNFIWDEF CDWYIEMAKL
SLYGEDENKK KTTRSVLAHV LDQTMRMLHP FMPFITEEIW QQLPHEGPSI TVSKWPEVNS
EFDNPQAVQE MQRLVSIIRS VRNSRAEVDT PMSKQIKMLI KTENEQLTAE LEKNRDYLER
FCNPSELSIS TVIEAPDKAM TSVVTGAEIF LPLEGLIDFD KEIKRLENEL AKWTKEVERV
QKKLSNQGFV SKAPESVVEE EKRKEKDYLD KQAKVKTRLS ELK
