SYV_PYRFU
ID SYV_PYRFU Reviewed; 891 AA.
AC Q8U409;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, 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=PF0290;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; AE009950; AAL80414.1; -; Genomic_DNA.
DR RefSeq; WP_011011404.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U409; -.
DR SMR; Q8U409; -.
DR STRING; 186497.PF0290; -.
DR EnsemblBacteria; AAL80414; AAL80414; PF0290.
DR GeneID; 41712080; -.
DR KEGG; pfu:PF0290; -.
DR PATRIC; fig|186497.12.peg.302; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 4914at2157; -.
DR PhylomeDB; Q8U409; -.
DR Proteomes; UP000001013; 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; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
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..891
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000224632"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 536..540
FT /note="'KMSKS' region"
FT BINDING 539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02005"
SQ SEQUENCE 891 AA; 104933 MW; 56E70FD7627F5D9C CRC64;
MLPKNYDPNE IEPKWQKYWL EEKIYKYKLE PDKPSYAIDT PPPFTSGTLH LGHVLSHTWI
DIIARYKRMR GYNVLFPQGF DNHGLPTELK VEKEFGISKD QPEEFLKKCI EWTWQAIEKM
RAQFIRIGYS ADWDLEYHTM DDWYKAAVQK SLLDFYKKGL IYREEHPVYW CPRCRTSLAK
AEVGYVEEEG YLYYIKLPLA DGSGYIPIAT TRPELMPACV AVFVHPDDER YKHLVGKKVK
LPIYEREVPI LADEDVDPNF GTGAVYNCTY GDEQDIVWQK RYNLPVIIAI NEDGTMNENA
GPYAGLKIEE ARKKIAEDLE KMGLLYKKEK ITHRVLRHTE RSSCMAPIEL LPKKQWFIKV
REFTDDIVEV AKKINWYPED MFLRLKDWAE SMDWDWVISR QRVFGTPIPF WICKNGHIIP
AREEDLPVDP RFDKPPVEKC PVCGAEIEPV TDVLDCWVDS SITPLIITKW HEAIKGDEEA
KKWFEHNFPT ALRPQGTDII RTWAFYTIFR TYMLTGEKPW NDIVINGMVA GPDGRKMSKS
YGNVVSPEEV IPKYGADALR LWTALAPPGE DHPFKWEIVD YNFRFLQKLW NIYRFAERHI
KDFDYEKYKH IELEPLDRWI LSRLHRIIKF ATEELEKYRF NLITRELMTF IWHEVADDYI
EMIKHRLYGE DEESKLKAKV ALYELLYNIM LLLAPFVPHI TEELYHHIFK EKIGEKSVHL
LQWPEYREDR IDEEAEKIGE LAREIVSAMR KYKNSHGMPL NAKLKHVAIY ATDSYEMLKV
IEKDIAGTMN IERLEIVKGE PQLEEKVVEI KPIYKRIGPR YGKLVPKIVK HLQENAEEIG
RRIKEEGKVE FEVEGQKVVL EKEDIEIKKA VFSEGEEVET AVVRDATILF F
