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Database: UniProt
Entry: I3D456_9ARCH
LinkDB: I3D456_9ARCH
Original site: I3D456_9ARCH 
ID   I3D456_9ARCH            Unreviewed;       771 AA.
AC   I3D456;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE            EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN   Name=valS {ECO:0000313|EMBL:EIJ66499.1};
GN   ORFNames=BD31_I1245 {ECO:0000313|EMBL:EIJ66499.1};
OS   Candidatus Nitrosopumilus salaria BD31.
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC   Nitrosopumilaceae; Nitrosopumilus.
OX   NCBI_TaxID=859350 {ECO:0000313|EMBL:EIJ66499.1, ECO:0000313|Proteomes:UP000003423};
RN   [1] {ECO:0000313|EMBL:EIJ66499.1, ECO:0000313|Proteomes:UP000003423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD31 {ECO:0000313|EMBL:EIJ66499.1,
RC   ECO:0000313|Proteomes:UP000003423};
RX   PubMed=22461555; DOI=10.1128/JB.00013-12;
RA   Mosier A.C., Allen E.E., Kim M., Ferriera S., Francis C.A.;
RT   "Genome sequence of "Candidatus Nitrosopumilus salaria" BD31, an ammonia-
RT   oxidizing archaeon from the San Francisco Bay estuary.";
RL   J. Bacteriol. 194:2121-2122(2012).
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:0000256|ARBA:ARBA00001624};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIJ66499.1}.
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DR   EMBL; AEXL02000053; EIJ66499.1; -; Genomic_DNA.
DR   RefSeq; WP_008297935.1; NZ_AEXL02000053.1.
DR   AlphaFoldDB; I3D456; -.
DR   PATRIC; fig|859350.6.peg.477; -.
DR   OrthoDB; 23906at2157; -.
DR   Proteomes; UP000003423; Unassembled WGS sequence.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; IPR002303; Valyl-tRNA_ligase.
DR   NCBIfam; TIGR00422; valS; 1.
DR   PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EIJ66499.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT   DOMAIN          18..559
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          607..752
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   771 AA;  89696 MW;  0D9409D7DD893104 CRC64;
     MEPKISEKAW NPELEKNILK QWEEEKIYEF IPENENFTID TPPPYPSGRP WHIGAAAHYS
     QIDMIARTAR MAGKNVYFPI GIDRNGLPVE LYTEKKHNIR MRETQRDEFL NLCREALDDL
     EAEMILIMKN LGISGNFANY YRTDSEEYRS LTQATFIELW NRGEVYLANR PNNYDWVSGT
     TIADAEITYE DIPTKLVYMK FKIQDTDKEI IIASTRPELL CACKTIIVNP EDERYTQYIG
     KNIIVPITNA EVKLRTHHSA QQEFGSGAVM VCSYGDQNDV ALFREFEMEE IVAIGLDGKM
     TEAAGEYAGL KPKQARTKII EDLESKGFVE KIEDIVHRTP VSERSKIPIE IIPMEEYYLK
     QKDSVEKMKK LGQEIKFHPP MHKQILMNWL ESISIDWPIS RRRFYGTEIP IWYCKSCSEP
     HVPEPGKYYK PWAEEAPFDK CTKCGKSEFV GEERTFDTWM DSSVSPLFVS KFNRDKEFFD
     KVYPTTIRPQ AKDIVRTWLY YTLLRCEQLT GKKPWSEAWI MGYGLDEKGM KMSKSKGNAI
     DPLPVIEKLG ADTFRFWSAS EINHGYDFRC NEQKIESTKK FLSKLWNVSR FLSSFPVIES
     GNVNPTDKWI LAELDNLVKE CKKGYEEYNF FVPAIAIREF TWNLFAAHYI EMVKARAYGI
     GFSDEERDGA IFTLHKTLST ILKLLAPITP FITEYLWKEL YSKESIHRQL QVEPESLEDQ
     SSITKEITEF NSLVWNEKKK QNLSLKDTIS IEIPDNLKSY KNDLKSMHNL A
//
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