ID A0A0R2QUQ4_9ACTN Unreviewed; 859 AA.
AC A0A0R2QUQ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:KRO53991.1};
GN ORFNames=ABR78_05610 {ECO:0000313|EMBL:KRO53991.1};
OS Acidimicrobiia bacterium BACL6 MAG-120910-bin40.
OC Bacteria; Actinomycetota; Acidimicrobiia.
OX NCBI_TaxID=1655586 {ECO:0000313|EMBL:KRO53991.1, ECO:0000313|Proteomes:UP000050903};
RN [1] {ECO:0000313|EMBL:KRO53991.1, ECO:0000313|Proteomes:UP000050903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL6 MAG-120910-bin40 {ECO:0000313|EMBL:KRO53991.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRO53991.1}.
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DR EMBL; LIBI01000001; KRO53991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2QUQ4; -.
DR STRING; 1655586.ABR78_05610; -.
DR Proteomes; UP000050903; 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; 2.
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}.
FT DOMAIN 17..99
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 125..618
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 659..802
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 580..584
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 859 AA; 95997 MW; 6A1AC6C5FF00C59C CRC64;
MTVPDKPSLD NVESKLIAQW DALGTYAFDR KATRDNVFAI DTPPPTVSGS LHMGHVFSYT
HTDAVARFWR MRGKSVFYPM GWDDNGLPTE RRVQNYFGVS CDPSVAHDHN FVPPFRGDVP
KDHRAVAISR PNFIALCEEL THQDEKVFED LFRRLGLSVD WSLLYTTISD HARRTSQDAF
LRNLSRGEAY AQEAPTLWDV DFGTAVAQAE LEDRERPGAF HDISFQHESG GEILIATTRP
ELIPACVALV AHPDDDRYKP FFGTMVRTPL FDVAVPVLAH ELAQIDKGTG IAMVCTFGDL
TDVVWWRELN LPTRPIIGRD GRILTQAPDG MTSTAGLEQY AVLAGKSVKQ AQTAIVEMLR
TSGDLRGEPK PLMHPVKFYE KGDRPLEIVT SRQWYIRNGG RDADLRAALL TRGNQLAWHP
EFMQHRYSNW VDGLNGDWLV SRQRYFGVPV PLWYRLNTAS EPDYSNPLVP DASRLPIDPS
TDVPNEYTEA QRGVPGGFVG DADVLDTWAT SSLTPQIAGR WLDDPTMFNN VFPMDVRPQG
HDIIRTWLFA TTVRSHFEHS VAPWRNAALS GWILDPDRKK MSKSKGNVVT PIDLFEQYGS
DAVRYWAASA RPGVDTAFSE DQMKVGRKLA TKLLNATKFV LGAGDVSAEV VPTEPLDVAM
LQRLSVVIND ATSAFESFDY ARALERTESF FWWFCDDYLE LVKMRAYGIT DISASARAAL
QRALSVMQRL FAPHIPFATE EVWSWWQQDS IHLAQWPTIT EITGDTKHVD ASEMMLDSAC
NVIGVIRRTK TEAKLSQRAE VEYTSVSATD AQIALLKECI GDLQNAGVVP AIEFVAHVAG
DSVAHIATTV RLAPVVDAK
//
