ID A0A0M3UBU6_9PSEU Unreviewed; 878 AA.
AC A0A0M3UBU6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02004};
GN ORFNames=XF36_17180 {ECO:0000313|EMBL:ALE84659.1};
OS Pseudonocardia sp. HH130629-09.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE84659.1, ECO:0000313|Proteomes:UP000062082};
RN [1] {ECO:0000313|EMBL:ALE84659.1, ECO:0000313|Proteomes:UP000062082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE84659.1,
RC ECO:0000313|Proteomes:UP000062082};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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_02004}.
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_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000256|HAMAP-Rule:MF_02004}.
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_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011868; ALE84659.1; -; Genomic_DNA.
DR RefSeq; WP_060712782.1; NZ_CP011868.1.
DR AlphaFoldDB; A0A0M3UBU6; -.
DR KEGG; pseh:XF36_17180; -.
DR PATRIC; fig|1641402.3.peg.3686; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000062082; 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 Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 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; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
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; 2.
DR Pfam; PF10458; Val_tRNA-synt_C; 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; SSF46589; tRNA-binding arm; 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_02004};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000062082}.
FT DOMAIN 25..434
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 445..567
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 610..752
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 811..875
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 809..836
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 528..532
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 878 AA; 96875 MW; 8BE2F9C744DBDE5D CRC64;
MTETLPARTA DLPAKWTPGE VEGDMYRRWV DAGYFRADPS SDADPFCIVI PPPNVTGSLH
LGHAMDHTLI DVLTRRARMQ GRDALWLPGV DHAGIATQSV VERRMAAAGE PDRHAIGRAA
FVEKVWQWKA ESGGSILGQM ERLGDGVDWS RERFTLDEGL SRAVATVFKK MFDDGLIYRA
ERLVNWSPAL RSAISDIEVD HIETEGELVS MRYGDGDASV VVATTRIETM LGDTAVAVHP
DDERYRHLVG TEIEMPITGR MIPVVADDYV DPEFGSGAVK ITPAHDPNDF EVGRRHDLPM
PTIMDETGTI AGTGTRFDGM DRFEARTAIR EELRAQGRIV AEKRPYLHSV GHCSRTGVPI
EPRLSLQWFV KVEPLARSAG DAVRSGETVL HPKEQAKRYF DWVDNMHDWT ISRQLWWGHR
IPVWYGPAGE VVCVGLDEQP PSGEGWRQDP DVLDTWFSSG LWPFSTLGWP EETPDLAKYY
PNSVLVTGYD ILFFWVVRMM MFGTYVMGKA PFRDVYLHGL IRDEHGKKMS KSKGNVIDPL
ALIDTYGADA LRFTIARGSN PGTDMSLSEE WVAGSRNFTT KLWNITRFAL SKGADPALPL
PAEADRTDAD RWILGRLAEV RAQTDELLDG YQFAKATEGL YHFAWDELAD WYVELCKTQL
DDPATEPGTR AILGHVLDAL LRMLHPIAPF VTEALWTALT GGETVVTAAW PTAGDTGAPV
DAAATARVTD AQKVITEVRR FRTEQGLPDR KAVAARLTGL GDSGLAAHER ALRFLTRLDP
AGDGFSTTAS LEVATSGGPV TVELDTSGAI DVAAERARLR RDLAAAEKER DQAEKKLGNP
KFTEKAPAEV VDGIRARHAT AVADIDRITA RLAALPEA
//
