ID A0A0C1IZZ4_9RHOB Unreviewed; 1052 AA.
AC A0A0C1IZZ4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=RA27_11915 {ECO:0000313|EMBL:KIC41322.1};
OS Ruegeria sp. ANG-R.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577903 {ECO:0000313|EMBL:KIC41322.1, ECO:0000313|Proteomes:UP000031318};
RN [1] {ECO:0000313|Proteomes:UP000031318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-R {ECO:0000313|Proteomes:UP000031318};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(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 -!- 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:KIC41322.1}.
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DR EMBL; JWLJ01000003; KIC41322.1; -; Genomic_DNA.
DR RefSeq; WP_039538975.1; NZ_JWLJ01000003.1.
DR AlphaFoldDB; A0A0C1IZZ4; -.
DR STRING; 1577903.RA27_11915; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000031318; 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; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing 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 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}.
FT DOMAIN 16..515
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 611..724
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 780..921
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 984..1048
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 1024..1051
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 694..698
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 697
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1052 AA; 117711 MW; 52C670DE3BBC6D6A CRC64;
MAMEKTFNAA EAEARIYEAW EQAGAFKAGA NRSRDESFTI MIPPPNVTGA LHVGHAFNNT
LQDILTRWHR MRGFDTLWQP GQDHAGIATQ MQVEKMLAAT QQPGRTELGR EAFLDKVWEW
KGEYGGTIIE QLKRLGSSCD WSRNAFTMAG APRDPRTGHE NSANFHDAVI KVFVDMYEKG
LIYRGKRLVN WDPHFETAIS DLEVENIEVA GHMWHFKYPL AGGETYTYVE KDEDGNVILE
EERDYISIAT TRPETMLGDG AVAVHPSDER YAPIVGKLCE IPVGPKEHRR QIPIITDEYP
DPDFGSGAVK ITGAHDFNDN MVAKRGSIPM YRLMDTKGAM RADGAPYADE ADKAQKYARG
KAFTENEIDA INLIPDHLRG LDRFEARAKV VEEITADGLA VMTRADDPRL GSTALKPDHE
GAEKLVPLVE SKPIMQPFGD RSKVVIEPMF TDQWFVDAEK VVGPALDAVK DGTVKIIPES
GEKTYYHWLE NIEPWCISRQ LWWGHQIPVW YGLDLSVENF KDDENDGDLD LVELGRLLNE
GGMLHRGNVM ECAANLEAVT EKFLDDNANI PNPLSHATVI EVAGKQEAIH QFAESLAQYA
VEQDPTKLVY PVWRDPDVLD TWFSSGLWPI GTLGWPEQTE ELERYFPTDV LITGADILFF
WVARMMMMQL AVVDQIPFHT VYLHQLVRDE KGKKMSKTTG NVIDPLEIVD EFGADALRFT
NASMAAIGGV LKLSRDRITG YRNFGTKLWN AVRFAEMNEV FTDTVPQLDV ADLKPKAAVN
RWIIGETARV REEVDAALES YRFNDAANGL YAFVWGKVCD WYVELSKPLL QGDDVEAQAE
TRATMRWVLD QCMVLLHPIM PFITEELWGL TGDRAKMVVH ANWPTYGTEL VDADADREMN
WVISVIENTR SARAQMRVPA GLYVPMLVTE IDSNGQAAWD RNEALIKRLA RIDSLTKADE
LPKGTISIAA PGASFGLPLA DIIDIGAEKE RLEKAKGKLA KELGGLRGRL NNPKFVASAP
EDVVAEAKAN LAAREEEEAK LNEALARLAE IA
//
