SYV_PYRAB
ID SYV_PYRAB Reviewed; 891 AA.
AC Q9UY55; G8ZK14;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=PYRAB16530;
GN ORFNames=PAB1255;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50557.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71121.1; -; Genomic_DNA.
DR PIR; G75014; G75014.
DR RefSeq; WP_010868771.1; NC_000868.1.
DR AlphaFoldDB; Q9UY55; -.
DR SMR; Q9UY55; -.
DR STRING; 272844.PAB1255; -.
DR EnsemblBacteria; CAB50557; CAB50557; PAB1255.
DR GeneID; 1495950; -.
DR KEGG; pab:PAB1255; -.
DR PATRIC; fig|272844.11.peg.1767; -.
DR eggNOG; arCOG00808; Archaea.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 4914at2157; -.
DR PhylomeDB; Q9UY55; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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.
FT CHAIN 1..891
FT /note="Valine--tRNA ligase"
FT /id="PRO_0000106251"
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; 104985 MW; D88339B05981A956 CRC64;
MLPKKYDPNE IEPKWQKYWL EEKIYKYRLD ENKPSYAIDT PPPFTSGTLH LGHVLSHTWI
DIIARYKRMR GYNVLFPQGF DNHGLPTELK VEKEFGITKD QPEEFLKKCV EWTWQAIEAM
RKQFIRIGYS ADWDLEYHTM DDWYKAAVQK SLLEFYKKGL IYREEHPVYW CPKCRTSLAK
AEVGYVEEEG YLYYIKLPLA DGSGYIPIAT TRPELMPACV AVFVHPDDER YKHLVGKKVK
LPIYEREVPI LADEDVDPNF GTGAVYNCTY GDEQDIVWQK RYNLPVIIAI NEDGTMNENA
GPYAGLKVEE ARKKIAEDLE KMGLLYKKEK IKHRVLRHTE RSSCMAPIEL LPKKQWFIRV
KDFTDEIVKV AKEINWYPED MFLRLKDWAE SMDWDWVISR QRVFGTPFPF WVCKNGHIIP
AREEDLPVDP RFDKPPVEKC PVCGAEIEPV TDVLDCWVDS SITPLIITRW HEAIKGDEEA
KKWFEHNFPT ALRPQGTDII RTWAFYTIFR TFKLTGKKPW KDIVINGMVA GPDGRKMSKS
YGNVVAPDEV IPKYGADALR LWTALAPPGE DHPFKWETVD YNFRFLQKVW NIYRFAERHI
KDFDYEKYKD IELEPLDRWI LSRLHRIIKF ATEELERYRF NLITRELMTF IWHEVADDYI
EMVKYRLYGD DEESKLKAKV ALYELLYNVM LLLAPFVPHI TEEIYHAMFK DKIGEKSVHL
LSWPEYREDR IDEKAEKLGE LARKVVSEMR KYKNSHGMPL NAKLEHVAIY ALESYDDLKL
IEKDIAGTMN IEKLEIFKGE PQLEERIVEV KPNYKRIGPR YGKLVPRIVE HLKNNAESIA
REIKENGKVE FEIDGEKVEL TKEDVMIKKE VFSEGERVET AVVDDIVILF F
