ID A0A0M8V7E1_9ACTN Unreviewed; 850 AA.
AC A0A0M8V7E1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ECO:0000313|EMBL:KOV57647.1};
GN ORFNames=ADL00_26800 {ECO:0000313|EMBL:KOV57647.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV57647.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV57647.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV57647.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-2015) 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 -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-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}.
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:KOV57647.1}.
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DR EMBL; LGDU01000319; KOV57647.1; -; Genomic_DNA.
DR RefSeq; WP_053760735.1; NZ_LGDU01000319.1.
DR AlphaFoldDB; A0A0M8V7E1; -.
DR PATRIC; fig|1519489.3.peg.6025; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000037758; Unassembled WGS sequence.
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; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 InterPro; IPR048044; Valyl-tRNA_ligase_actino.
DR NCBIfam; NF000540; alt_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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000037758}.
FT DOMAIN 22..620
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 658..804
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 52..62
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 582..586
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 585
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 850 AA; 95247 MW; 0C6234D8C6D28825 CRC64;
MTTPSSRSTT PDKPTLDGLE AKWIKNWEER GVYAFDRSAT RDHVYSIDTP PPTVSGSLHV
GHVFSYTQTD AIARFQRMQG KQIFYPMGWD DNGLPTERRV QNYFGVRCDP SLPYDPDYTP
PAAPDKRQVP VSRRNFIELC ERLTLEDEKV FEDLWRRLGL SVDWRQTYQT IGLRARAVSQ
RAFLRNLARD EAYRAEAPTL WDVTFQTAVA QAELEDRERP SAYHHIAFQG AGERVLEVAT
TRPELLPACV ALVAHPDDER FQDLFGTTAR TPVFDVEVPV LPHRLADPEK GSGLVMVCTF
GDTTDVIWWR ELDLPTRAVI GRDGRFGAQG PAVLDSQQAQ DAYARLAGAT PHTARERILE
LLDQANALLA EPRPFNHMVK FYEKGDKPLE IVTSRQWYLR NGGRDTALRE QLIGRGQELS
WHPESMRSRY QSWVEGLNGD WLISRQRFFG VPIPVWYRLD DSGNPTDEMI LPAEDTLPID
PSSDAPPGFT AEQRDVPGGF TGDPDVMDTW ATSSLTPQIA GGWGHDDDLF ARVFPMDLRP
QAHEIIRTWL FSSAVRAELE HGVLPWKHAA ISGWILDPDR KKMSKSKGNV VTPVDLLDQY
GSDAVRYWAV SARPGTDTAF EVGQMKIGRR LAVKVLNASK FVLGFGTGTN TEVTRPLDQA
MLARIAEVVV EATEHLEGYD YARALETIER CFWSFCDHYV ELVKNRAYGA LAEADADSAR
ATLTTALSVL LRTLAPFLPF TTEEAWSWHQ TGSIHRATWP TPQELQTLVP HGDPRLLTLA
MEVTAAIRKA KSTAQLSMRA EVKNLIATGP PTLLTALGEV LPDVTAAGHV LNVEFRPADT
DNLAYEVVLL
//
