ID L0KY51_METHD Unreviewed; 866 AA.
AC L0KY51;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 OrderedLocusNames=Metho_1867 {ECO:0000313|EMBL:AGB50046.1};
OS Methanomethylovorans hollandica (strain DSM 15978 / NBRC 107637 / DMS1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanomethylovorans.
OX NCBI_TaxID=867904 {ECO:0000313|EMBL:AGB50046.1, ECO:0000313|Proteomes:UP000010866};
RN [1] {ECO:0000313|Proteomes:UP000010866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15978 / NBRC 107637 / DMS1
RC {ECO:0000313|Proteomes:UP000010866};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Methanomethylovorans hollandica DSM
RT 15978.";
RL Submitted (FEB-2012) 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; CP003362; AGB50046.1; -; Genomic_DNA.
DR RefSeq; WP_015325211.1; NC_019977.1.
DR AlphaFoldDB; L0KY51; -.
DR STRING; 867904.Metho_1867; -.
DR GeneID; 14406380; -.
DR KEGG; mhz:Metho_1867; -.
DR HOGENOM; CLU_001493_0_2_2; -.
DR OrthoDB; 23906at2157; -.
DR Proteomes; UP000010866; 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; 3.30.720.200; -; 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}; Reference proteome {ECO:0000313|Proteomes:UP000010866}.
FT DOMAIN 16..555
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 602..745
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 44..54
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 519..523
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 866 AA; 99040 MW; AC80566FE9F5E0EA CRC64;
MTVPKEYIPH EVEPKWKEAW DMSMYHFDWE DHNRPQFIID TPPPYPTGNF HIGNSLNWCY
IDFVARYKRM CGYNVMFPQG WDCHGLPTEV KVEEIHNITK NQVPREEFRR MCRELTTNNI
AKMRNTMMNL GFSVDWSNEF VTMEPAYYSK TQRSFRRMYD MGRIYQSEHP VNWCPRCETA
IAFAEVEYEG RSTQLNYLNF DKLKIATTRP ELMAACVAVA INPEDARYNA HIGSKVKVPL
FGHEVPVISD SVVDPAFGTG VVMICTFGDK QDVRWWVEHK LPLRKAIDKN GRMTKIAGKY
ADMTIPECKE AVITDLKAEG YLYEQKELEQ NVGMCWRCDT PIEILSEKQW FVKIDTNDVK
KAADEINWTP EHMKVRLENW LGTMEWDWCI SRQRIFATPI PVWYCKDCGE VMVAKEEWMP
IDPTRESPKE PCSKCGSTNF EPEEDVLDTW MDSSITVQHV TGWLTDHKSR LPAQLRPQGH
DIIRTWAFYT ILRSMALAGK RPWDSILVNG MVLGEDGHKM SKSLGNIIPP EEVIEKYSAD
SFRQWAAIGG APGSDVMFRW KDVVSASRFF AKMWSIYRFS VSHFNDRDTS YVPTKEELHI
VDRWLLDKLY ELITSVTLNM DACQFDEAFK SIRGFAWEVV ADNYIELVKS RLYGTNATDR
KAAQYTLYAT IEVLAKLLAP FAPFFAEEMY SRLGTGSVHM QSWPKADALW KDEEAGKAGE
LVKEIVSSVR RYKSEHGIAL NAPLKGLEIY GALTDVMDIT GATNTPVEVM VGNPDFEHVP
VNVKPNMGVI GPKFKGQAKA IIDALTEANP KKLVSEMEQN GKISLQTKSG IIDLAPESVE
IEKEVISAGR AVDVLDVKGI PVVVIR
//
