ID J1L1B4_9EURY Unreviewed; 862 AA.
AC J1L1B4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02005};
GN ORFNames=Metli_0854 {ECO:0000313|EMBL:EJG06812.1};
OS Methanofollis liminatans DSM 4140.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanofollis.
OX NCBI_TaxID=28892 {ECO:0000313|EMBL:EJG06812.1};
RN [1] {ECO:0000313|EMBL:EJG06812.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4140 {ECO:0000313|EMBL:EJG06812.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Lu M., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schuler E., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Methanofollis liminatans DSM 4140.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC Rule:MF_02005};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02005}.
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DR EMBL; CM001555; EJG06812.1; -; Genomic_DNA.
DR RefSeq; WP_004038312.1; NZ_CM001555.1.
DR AlphaFoldDB; J1L1B4; -.
DR STRING; 28892.Metli_0854; -.
DR PATRIC; fig|28892.9.peg.914; -.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000005095; 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 CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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 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|HAMAP-Rule:MF_02005};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02005}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02005};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02005}.
FT DOMAIN 20..561
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 603..741
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 47..57
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 523..527
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 862 AA; 97709 MW; 8A073A8E319F2A16 CRC64;
MSSSHTIPKN YDFREVEDRW QRTWRDEDNY FDPSSPKPQF VIDTPPPYPT GNFHIGNALN
WCYIDFIARY KRMCGYNVMF PQGWDCHGLP TEVKVEEIHG ITKNDVSREE FRQMCRDLTI
GNIEKMRATL RRCGFSTDWS HEYITMLPEY YRKTQLSFLR MLNAGYIYQS EHPVNFCTRC
ETAIAFAEVS YEPRETKLNF FDFDGVEIAT TRPELLAACV AVAVHPEDER YRPLAGKHLK
VPLFGHDVPV LQDGAVDPSF GSGAVMICTF GDKQDVHWWK EYDLPLRKAI DRAGRMTALC
GRYQGMNAKE CREAILADME KAGILRRQET IEQRVGTCWR CKTPIEILSE RQWFIRVKSD
EILEAAHQVS WYPEHMRTRL ENWAGQMEWD WCISRQRIFA TPIPVWSCAQ CGAIVTPDEA
DLPVDPTTER PKRPCPQCGC EEFVAEHDVL DTWMDSSISV LNITGWDGSG TPPIFPAQIR
PQGHDIIRTW AFYTILRSVA LTGQKPWDSI LVNGMVLGED GFKMSKSRNN IIAPETVVVE
YGADAFRQWG AMGAATGQDI MFNWNDVVAA SRFQTKMWNI VRFVLTQIER EPVEDGPVTA
VLDRWLLAKL SETVAEVTNA LDTYQFDQGL RAIRDFTRNI LADDYIELVK GRLYSDDAER
ASACRALTTT LDALCRLLAP YVPHFAEECW AQFREGSVLV QPWPAFSCED EEAERIGDRL
VSLTAELRRY KHDLGLALNA PFGNLAIYAP EKVDDAGDVA RALNAAIAWR TGEPRLEKVP
AGVEFNMAVI GPALRKGAKG FMQAVEALPA DQLQNPPATV IVDGAEVAVP ENAFTPKFAY
QVEGEAVDVL TIGEVTVTLR RA
//
