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Entry: A0A0S6WVY8_9SPHN
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ID   A0A0S6WVY8_9SPHN        Unreviewed;       908 AA.
AC   A0A0S6WVY8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=MBENS4_2741 {ECO:0000313|EMBL:GAM05743.1};
OS   Novosphingobium sp. MBES04.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1206458 {ECO:0000313|EMBL:GAM05743.1};
RN   [1] {ECO:0000313|EMBL:GAM05743.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBES04 {ECO:0000313|EMBL:GAM05743.1};
RA   Ohta Y., Nishi S., Kobayashi K., Tsubouchi T., Iida K., Tanizaki A.,
RA   Kurosawa K., Adachi A., Nishihara M., Sato R., Hasegawa R., Hatada Y.;
RT   "Draft Genome Sequence of Novosphingobium sp. Strain MBES04, Isolated from
RT   Sunken Wood from Suruga Bay, Japan.";
RL   Genome Announc. 3:e01373-14(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}.
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DR   EMBL; DF850488; GAM05743.1; -; Genomic_DNA.
DR   RefSeq; WP_039391389.1; NZ_DF850488.1.
DR   AlphaFoldDB; A0A0S6WVY8; -.
DR   STRING; 1206458.MBENS4_2741; -.
DR   HOGENOM; CLU_001493_0_2_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000053513; 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   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   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   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; 1.
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          27..605
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          647..786
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          843..908
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   MOTIF           54..64
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           565..569
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   BINDING         568
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   908 AA;  101017 MW;  728CEEF923669B5E CRC64;
     MTETTPETTP ESTLDKTFDP AAIEARWYAH WEETGLFRPE RPDAQPFTIV NPPPNVTGSL
     HIGHALDNTL QDIVIRHERL KGKDALWVVG TDHAGIATQM VVERQMEASQ DKRTNYSREG
     FVEKVWEWKA ESGGTITRQL RRLGCSMDWS REQFTMDPHF TEAVVKVFVD LYNEGLIYRD
     KRLVNWDPKL KTAISDLEVE TREVKGGFWH FKYPLADGVT LDNGQDFIEV ATTRPETMLA
     DMAVAVNAED ERYKSVIGKE ILQPITGRRF QIVADEHADP ELGSGAVKIT PGHDFNDFEV
     GKRAGFKPAE MLNMFDADAN VVQTEDGLVP EKYLGMERFA AREAIVAEMK ELGFLIPHVV
     TKTTKDGETE TTEMDAEPRT IQTPYGDRGG VVIEPWLTDQ WYVDAATLAK PAIAAVQDGQ
     IEVVPKTWEK TYFNWMDNIQ PWCVSRQLWW GHRIPAWYAQ DGKVYVAETE EAAQALAGDG
     VALTRDEDVL DTWFSSALWP FATLGWPEKT DLLAKHYPND LLISGFDILF FWCARMAMQG
     LHFMDEVPWK KLYLHGLVRA ADGAKMSKSK GNVVDPLGLI DQYGADALRF FMAAMESQGR
     DIKMDDKRIE GYRNFATKLW NAARFCQSNG VVASTSVAAP AATSAVNRWI IGEVVDTVAE
     LDKAMADMRF DAAANAIYHF VWDSFCDWYI ELVKGNFDEE TRAVAGWVLD QILVMLHPFM
     PFVTEELWSK MGAREADLIV SAWPAPDASV DTAAKAEVEW LIALIGSLRG AKAELGIAPG
     ARLTAYIAQV SDATRAIIGA NATVIDRLAR LDAIHFEAAP AGPVLQVGAG DAMLAIPLEG
     VIDIAAEKSR LEKALAASQK EAKSLDGRLS NPKFVEKAKP EAVEKARADH AHHTAEAQRL
     AAALERLG
//
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