SYV_COXBU
ID SYV_COXBU Reviewed; 920 AA.
AC Q83DD0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=CBU_0808;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90342.1; -; Genomic_DNA.
DR RefSeq; NP_819828.1; NC_002971.3.
DR RefSeq; WP_010957818.1; NC_002971.4.
DR AlphaFoldDB; Q83DD0; -.
DR SMR; Q83DD0; -.
DR STRING; 227377.CBU_0808; -.
DR PRIDE; Q83DD0; -.
DR DNASU; 1208701; -.
DR EnsemblBacteria; AAO90342; AAO90342; CBU_0808.
DR GeneID; 1208701; -.
DR KEGG; cbu:CBU_0808; -.
DR PATRIC; fig|227377.7.peg.793; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_6; -.
DR OMA; FATKLWN; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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..920
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224469"
FT COILED 642..668
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT COILED 849..920
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT MOTIF 522..526
FT /note="'KMSKS' region"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 920 AA; 106648 MW; BB8C96202FF28D33 CRC64;
MEKTYDPKAI EKKWADYWEK RQLSKPTAQG SPYCIMLPPP NVTGTLHMGH GFQQTLMDTL
IRYHRMKGER TLWQGGTDHA GIATQMVVEQ QLAQEDLTRE DLGRQAFIKR VWEWRERSGG
KITHQMRRLG VSIDWSRERF SMDEGLSRAT TEAFIRLHHE GLIYRGKRLV NWDPKLNTAI
SDLEVVTEEV EGHLWHIRYP LAEGSGHLII ATTRPETLLG DVAIAVHPQD ERYQPFVGKK
VRLPLTDRTI PVIADEAVDK EFGTGSLKIT PGHDFNDYEI GQRHQLPLIN ILTSEGYLNE
NVPEPYRGLE RFEARKKIIA DLQRENLLEK TEPYRVPVPR GERSGVIIEP LLTDQWFIKM
EALAKPAMEA VESGELKFIP KNWEKTYLQW LSNIQDWCIS RQLWWGHRLP VWYDEEKNSY
VGRSREEILK KYHLSPDVKL QQETDVLDTW FSASLWPFAT LGWPEKTESF KTFYPTQVLV
TGFDIIFFWV ARMVMMGLKL THKIPFHSVY IHGLIRDSQG RKMSKSKGNV IDPIDIIDGI
SLDALIEKRT HALLQPKMAK TIEKMTRKEF PNGIASFGTD ALRFTFCALA SRGRDINFDM
GRIDGYRNFC NKIWNAARFV TMNTQEKDLN PEKPLSYSAA DEWIRTRLQQ TIKNAEEALS
QYRFDLLAQT LYEFTWNEYC DWYVEFAKCI LYDKQAKPAQ LRGTRVALLE VLEILLRLLH
PVMPFITEEI WQTVAPLAGK EGKSIMVEHW PQFNIHEMNY DAKVEIEWVK NVITAIRTLR
AEIGISPAKR IPVIFGKGDE KDKKRIAKMK SYIKTLGKVS QLRFAKHDDC FSATATGIVE
RLEIHIPLAG VIDKQTEIAR LKKEISKLQK EEEKSLKKLD NPNYLQRAPQ EVVEKERLSL
EKTQNALKKL QSQYASIESL
