ID A0A0N0TL26_9ACTN Unreviewed; 857 AA.
AC A0A0N0TL26;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:KOX10204.1};
GN ORFNames=ADL05_26410 {ECO:0000313|EMBL:KOX10204.1};
OS Nocardiopsis sp. NRRL B-16309.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX10204.1, ECO:0000313|Proteomes:UP000037694};
RN [1] {ECO:0000313|Proteomes:UP000037694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16309 {ECO:0000313|Proteomes:UP000037694};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
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:KOX10204.1}.
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DR EMBL; LGEC01000114; KOX10204.1; -; Genomic_DNA.
DR RefSeq; WP_053619705.1; NZ_LGEC01000114.1.
DR AlphaFoldDB; A0A0N0TL26; -.
DR STRING; 1519494.ADL05_26410; -.
DR PATRIC; fig|1519494.3.peg.5769; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000037694; 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 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:UP000037694}.
FT DOMAIN 22..621
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 663..807
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 466..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 52..62
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 583..587
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 586
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 857 AA; 95987 MW; 5307D43833E7D813 CRC64;
MTNGSHSFRM PDKPSLDGIE AKWVDVWDES GVYHFDRTRS REDVFSIDTP PPTVSGSLHI
GHVFSYTHTD TVARFQRMNG KAVFYPMGWD DNGLPTERRV QNYYGVRCDP SVAYDPDFRP
PAKPDPKRQV PISRRNFIEL CDELTAEDEK VFESIWRRLG LSVDWRHTYA TIDDNSRTAA
QRAFLRNLAR GEAYMSEAPT LWDVTFRTAV AQAELEDRER PSAYHKVAFH RPDGGTVHIE
TTRPELLAAC VALVAHPDDE RYQHLFGTTV RTPVFGVEVP VRAHRLADPE KGSGIAMICT
FGDTTDVTWW RELDLDTRPI IGWDGRIVAE TPSGLPEQGR EAYARLVGAT MHTARERTVE
MLRESGDLIG EPTAITHPVK FYEKGDKPLE IVTTRQWYIR NGGRDEELRA QLVRRGRELV
WHPDHMRQRY ENWVEGLNGD WLVSRQRFFG VPFPVWYPLD GDGNPRYDEP LLPSEDQLPV
DPSSQAPEGY TESQRGRPGG FMGDPDVMDT WATSSLTPQI ASGWERDQDL FERVFPMDLR
PQGQDIIRTW LFATVVRANF ENGTLPWRTT GISGWILDPD RKKMSKSKGN VVTPVALLEK
YSSDAVRYWA ASGRLGTDTA MDEGQMKVGR RLAIKILNAS KFVMSVAGEG ASVDPSQVTE
PLDRAMLAAL AEVVDEATAA FAAYDHTRAL ERTERFFWDF CDDYLELVKT RAYNAESAEG
ASARAALLVA LGALHKLFAP FLPFVTEEVW SWWQDGSVHA QAWPQAAGYR TAAADGDPAV
LASTAEVLRA VRKAKSEAKL SMRAEVEHVR VAGKQADAAR AAAGDIAAAG RAAGIDFEVT
DDGELTVEVV LPASEEQ
//
