SYV_PYRHO
ID SYV_PYRHO Reviewed; 891 AA.
AC O58052;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 128.
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=PH0314;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA29387.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA29387.1; ALT_INIT; Genomic_DNA.
DR PIR; D71457; D71457.
DR RefSeq; WP_048053083.1; NC_000961.1.
DR AlphaFoldDB; O58052; -.
DR SMR; O58052; -.
DR STRING; 70601.3256704; -.
DR EnsemblBacteria; BAA29387; BAA29387; BAA29387.
DR GeneID; 1444193; -.
DR KEGG; pho:PH0314; -.
DR eggNOG; arCOG00808; Archaea.
DR OMA; FATKLWN; -.
DR OrthoDB; 4914at2157; -.
DR Proteomes; UP000000752; 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_0000106252"
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; 104961 MW; 6E3924A940C217FC CRC64;
MLPKNYDPNE IEPKWQKYWL EEKIYKYRLD ENKPSYAIDT PPPFTSGTLH LGHVLSHTWI
DIIARYKRMR GYNVLFPQGF DNHGLPTELK VEKEFGITKD QPEEFLKKCV EWTWQAIEAM
RKQFIRIGYS ADWDLEYHTM DDWYKAAVQR SLLEFYKKGL IYREEHPVYW CPKCRTSLAK
AEVGYVEEEG YLYYIKLPLA DGSGYIPIAT TRPELMPACV AVFVHPDDER YKHLVGKKVK
LPIFEREVPI LADEDVDPNF GTGAVYNCTY GDEQDIVWQK RYNLPVIIVI NEDGTMNENA
GPYAGLKIEE ARKKIAEDLE KMGLLYKKEK IKHRVLRHTE RSSCMAPIEL LPKKQWFIKV
KDLIDEIIKV AKEINWYPED MFLRLKDWAE SMDWDWVISR QRVFGTPFPF WVCKNGHIIP
AREEDLPVDP RFDKPPVDKC PVCGAEIEPV TDVLDCWVDS SITPLIITKW HEAIKGDEEA
KKWFEHNFPT ALRPQGTDII RTWAFYTILR TYVLTGKKPW KDIVINGMVA GPDGRKMSKS
YGNVVSPEEV IPKYGADALR LWTALAPPGE DHPFKWETVD YNYRFLQKVW NIYRFAERHI
KDFDYEKYRD VELEPLDKWI LSRLHRIIKF ATEELERYRF NLITRELITF IWHEVADDYI
EMIKYRLYGE DEESKLKAKV ALYELLYNVM LLLAPFVPHI TEEIYHAIFK EKIGEKSVHL
LSWPEYREDR IDEEAEKIGE LARKIVSEMR KYKNSHGLPL NAKLKHVAIY ALDSYERLKL
IERDIAGTMN IERLEIVKGE PHLEERIVEV KPNYKNIGPK YGKLVPRIVQ YLRENAESIV
REIKEKGKAE FEVEGKKVEL TKEDITVRKE VFSEGEKVET SVVDDVVIVF F
