SYV_HALMA
ID SYV_HALMA Reviewed; 901 AA.
AC Q5V1H0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=rrnAC1729;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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_02005}.
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_02005};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}.
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DR EMBL; AY596297; AAV46632.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5V1H0; -.
DR SMR; Q5V1H0; -.
DR STRING; 272569.rrnAC1729; -.
DR PRIDE; Q5V1H0; -.
DR EnsemblBacteria; AAV46632; AAV46632; rrnAC1729.
DR KEGG; hma:rrnAC1729; -.
DR PATRIC; fig|272569.17.peg.2410; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000001169; Chromosome I.
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; 3.40.50.620; -; 2.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
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 PRINTS; PR00986; TRNASYNTHVAL.
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; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..901
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224621"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 72..82
FT /note="'HIGH' region"
FT MOTIF 572..576
FT /note="'KMSKS' region"
FT BINDING 575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 901 AA; 102800 MW; 2CB25ABD10F54E88 CRC64;
MLPGCYTHRL NMSDTQDPPQ DESTTDESAD ALDGEYDPRE IEPEWQDQWV ADKTYAYDED
ADTRFSIDTP PPTVSGNLHM GHLYQFTLQD FVARFHRMRD DTVYFPFGYD DNGIASERLT
ERELDIRHQD YPRREFQEKC RDVCTQFEDE FTQDVQSLAI SIDWDNTYKT IAPDVQRVSQ
LSFLDLYEQG REYRQRAPTI WCPDCETAIS QVEQEDKDKH TKFNDIAFDL VETGEGPADE
DATFTISTTR PELLPACVAV FVHPDDDENQ HLVGGSARVP LFEQEVPVIA DERVDMETGS
GIVMCCTFGD QNDIEWYQAH DLPLRLAIDE SATMTDVAGE YEGMHTTEAR EAIIEDLREE
GSLLESRDHD HTVQVHERCE EEVEYLVTEQ WYIELLDKKE EYIEAGRQME WYPEKMATRY
EHWIEGLEWD WCISRQRDSG IPIPVWYCDD CGEPVMAERE QLPVDPLSDA PPVDSCPECG
HDSLTPEEDV FDTWATSSLT PLVNAGWDWD ADSESFTMEL PELYPFDLRP QGHDIISFWL
FHTVVKCYEH TGEVPFENVM INGMVLDENR EAMSKSKGNV IPPSEVLEEF PVDATRYWAA
GTSIGDDFPY KEGDLEAGER LLQKLWNASR LVDQLTPAAR PDEPEELAAV DEWLLAELDA
TVESVTAKFE DYEFSKARNE LRSFFWNTFC DDYLEIAKQR LSDGEAVSTE FTLLQAHRTF
LQLFAPFLPH ITEELWERCY EEDSSIHTTD WPTSGGYDAD LEAGETAMEV VSALRRYKTE
NGLPLNADLD HVEVFGHIAG FEDAVAEAMH VAQLDTYDEA PDITTEISGI DLDYSLVGPE
FGSEVGAIDA AIEDGDYEID GDTLQVAGVE LDDEMFAVEE SRTYSGEGEM TETESAVVVV
R
