ID   H2C8C2_9CREN            Unreviewed;       815 AA.
AC   H2C8C2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
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   ORFNames=MetMK1DRAFT_00028300 {ECO:0000313|EMBL:EHP68398.1};
OS   Metallosphaera yellowstonensis MK1.
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=671065 {ECO:0000313|EMBL:EHP68398.1, ECO:0000313|Proteomes:UP000003980};
RN   [1] {ECO:0000313|EMBL:EHP68398.1, ECO:0000313|Proteomes:UP000003980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MK1 {ECO:0000313|EMBL:EHP68398.1,
RC   ECO:0000313|Proteomes:UP000003980};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Cheng J.-F., Goodwin L., Pitluck S., Peters L.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Kozubal M., Macur R.E., Jay Z., Inskeep W., Woyke T.;
RT   "Improved High-Quality Draft sequence of Metallosphaera yellowstonensis
RT   MK1.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; JH597770; EHP68398.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2C8C2; -.
DR   STRING; 671065.MetMK1DRAFT_00028300; -.
DR   eggNOG; arCOG00808; Archaea.
DR   HOGENOM; CLU_001493_0_2_2; -.
DR   Proteomes; UP000003980; 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; 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; 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.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003980}.
FT   DOMAIN          27..580
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          623..766
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   815 AA;  94437 MW;  C8B01003A59A92A0 CRC64;
     MSSQGDILKK MEEWPKHYNP KEIEPRWQNK WLSREFWEKV IRFQDSDTRP VFFIDTPPPF
     TSGELHMGHA YWVTIADAMT RFKILQGYNV LIPQGWDTQG LPTELKVQYR LGIPKENREL
     FLKKCVEWTE EMIGKMKSAM MRLGYRPNWE QFEYRTYSAE YRAIIQRSLL DMFNKGMIKM
     RKGPVYWCPK CETAVAQSEV GYLEKQGILA YISFPLKEGG EIVIATTRPE LLGATQAVAV
     NPEDERYKNL VGKVAIIPIF NKEVRIISDP AVDKEFGTGA VMISTYGDPQ DIKWQLKYDL
     PVDEMIDERG RMKGTGFLDG LKVEEARKKI VEMLKQQGFL KKLEGLTHNV LSHTERSDCQ
     SPIEFLVKDQ VYISVLEFKD RLLSEMKKMT FKPSRMAYYL QEWINNMEWD WNISRQRVYG
     TPLPFWHCEN LHLVPADPSS LPVDPTKSSP PLEKCPHCGL PLKPVTHVAD VWVDSSVTVL
     YLAGFYNNKE RFAKAFPADV RLQGTDIIRT WLFYTFFRTL MLAGDVPFKR VLVHGQVLGP
     DGTRMSKSKG NVVSPMDRIE EYGADAIRMT LLDAAIGDDF PFKWDTVRGK KLLLQKLWNA
     SRLAYPFISK RKVERPEKPH VLDVWVLNEH RNFVERAISA YENQDFYVVL SMLYNYFWEI
     IADEYLELIK HRLFSDDQSA IYTLSRILKD IVIILHPIAP HITEEIYSKL FGDKESVLME
     KLPSVSDIPS DQEAVRIGNE VKEINSAIRT KKVSMRLSMN SPVKVKLIGS LSFVEDIRKV
     EEDLKKTLKI TQMTYEINDS SRPIIEVEPD QPMGV
//