SYV_CERS4
ID SYV_CERS4 Reviewed; 987 AA.
AC Q3J4Z5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=RHOS4_05710;
GN ORFNames=RSP_1989;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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: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; CP000143; ABA78139.1; -; Genomic_DNA.
DR RefSeq; WP_011337139.1; NZ_CP030271.1.
DR RefSeq; YP_352040.1; NC_007493.2.
DR AlphaFoldDB; Q3J4Z5; -.
DR SMR; Q3J4Z5; -.
DR STRING; 272943.RSP_1989; -.
DR EnsemblBacteria; ABA78139; ABA78139; RSP_1989.
DR KEGG; rsp:RSP_1989; -.
DR PATRIC; fig|272943.9.peg.878; -.
DR eggNOG; COG0525; Bacteria.
DR OMA; FATKLWN; -.
DR PhylomeDB; Q3J4Z5; -.
DR Proteomes; UP000002703; Chromosome 1.
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; -; 3.
DR Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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..987
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224546"
FT COILED 917..985
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT MOTIF 634..638
FT /note="'KMSKS' region"
FT BINDING 637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ SEQUENCE 987 AA; 110509 MW; 49C36DB6CFF3C00F CRC64;
MPMDKTFNAA EAEARLYDAW EKAGAFRAGA NASRPETFCI MIPPPNVTGS LHMGHAFNNT
LQDILTRWHR MRGFDTLWQP GQDHAGIATQ MVVERELAKS GQPGRREMGR EAFLEKVWEW
KEQSGGTIVN QLKRLGASCD WSRNAFTMDP NFQRAVLKVF VDLYEKGFIY RGKRLVNWDP
HFETAISDLE VEQVEVNGNM WRLRYQLADG ATYRHPVAFD EEGRPTEWEE RDYLTVATTR
PETMLGDTGI AVNPADERYA HLIGKEVVLP LVGRRIPIVA DDYADPSKGT GAVKITPAHD
FNDWGVGQRT GLRAINVMSG RATMFLIENP DFTEGCAPSE EALALDGLDR YEARKRVVAL
AEEQGWLDGI DQDRHMVPHG DRSKVAIEPM LTDQWFVDTA QIVQPAIDAV RTGRTEILPE
RDAKTYFHWL ENIEPWCISR QLWWGHQIPV WYGLDIWPAR FEDDGDDTLD EVEIFELLED
GAFNHADPTH HCAFDFEGVS EKFLDDLASL PHPLNNARVV EVASRAEAID RLAQALADYN
LNEDPTHLVY PVWRDPDVLD TWFSSGLWPI GTLGWPEETP ELARYFPTNV LITGFDIIFF
WVARMMMMQL AVVNEVPFKT VYVHALVRDE KGKKMSKSLG NVLDPLELID EFGADAVRFT
LTAMAAMGRD LKLSTARIQG YRNFGTKLWN ACRFAEMNGV WEGHATQAAP PAATATVNRW
IIGETGRVRE EVDAALAAYR FDSAANALYA FVWGKVCDWY VEFSKPLFDT EAAAETRATM
GWVLDQCMVL LHPIMPFITE DLWATTGSRT KMLVHSDWPS FGAELVDPAA DREMSWVISL
IEEIRSARAQ VHVPAGLKLP VVQLALDAAG REALARNEAL ILRLARLEGF TEAASAPKGA
LTIAVEGGSF AIPLEGVIDI GAEKARLAKT LEKLEKDMAG LRGRLGNPNF VASAPEEVVD
EARTRLEQGE EEGAKLSAAL ARLSEIA
