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Database: UniProt
Entry: D0MG64_RHOM4
LinkDB: D0MG64_RHOM4
Original site: D0MG64_RHOM4 
ID   D0MG64_RHOM4            Unreviewed;       895 AA.
AC   D0MG64;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 94.
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   OrderedLocusNames=Rmar_0722 {ECO:0000313|EMBL:ACY47620.1};
OS   Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS   obamensis).
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC   Rhodothermus.
OX   NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY47620.1, ECO:0000313|Proteomes:UP000002221};
RN   [1] {ECO:0000313|EMBL:ACY47620.1, ECO:0000313|Proteomes:UP000002221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43812 / DSM 4252 / R-10
RC   {ECO:0000313|Proteomes:UP000002221};
RX   PubMed=21304669; DOI=10.4056/sigs.46736;
RA   Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA   Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Detter J.C.;
RT   "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL   Stand. Genomic Sci. 1:283-291(2009).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR   EMBL; CP001807; ACY47620.1; -; Genomic_DNA.
DR   RefSeq; WP_012843232.1; NC_013501.1.
DR   AlphaFoldDB; D0MG64; -.
DR   STRING; 518766.Rmar_0722; -.
DR   KEGG; rmr:Rmar_0722; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_10; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002221; 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; 3.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002221}.
FT   DOMAIN          25..573
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          623..768
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          830..894
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   COILED          828..895
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   BINDING         536
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   895 AA;  104617 MW;  544CBC3C43E0B252 CRC64;
     MAGEPLLKTE RVRKVYDPQE IEPRWYAYWE ANNFFRAEIR PDRTPFVIMM PPPNVTGRLH
     MGHALQDTIQ DALTRIRRMQ GYEALWLPGI DHAGIATQNV VERELREKEG KTRHDLGREA
     FLQRVWQWKE EYGDIILQQK RRLGDSCDWS RTRFTMDEGF TRAVQEAFIR LYNEGLIYRG
     DYLVNWCPVD QTALSDEEVD NVEQDGHLWY IRYPLVDGSG YITIATTRPE TMLGDTAVAV
     HPEDERYRHL IGKKVRLPLI GREIPIIADE HVKRDFGAGA LKITPGHDKN DFEIGQRHGL
     PIINIMNPDG TINENGGPYA GLDRFEARKR IVEDLRAQGL LEKVEPYRHT VPISSRSKAI
     IEPMLSRQWF VRMKPLAEPA IEAVRRGEIR FYPERWANEY FRWMENIRDW CISRQIWWGH
     RIPVWYYTDE NGQIDESKGF VVSIEQPEPG MVQDEDVLDT WFSSWLWPFA TLGWPDQTPD
     LEYFYPTTVL VSGYDILFFW IARMIMAGIH FTGKIPFRDV FITGMVKDKY GRWMSKSLGN
     GIDPLEMIDQ YGADAVRYSL TVLCTQGQDI KLDPSKFEMG RNFANKIWNA FNVFGQFMET
     DDEGRPLRDY RRQRRFEELS LVERWMVTRL NQTIATVNEA IDRYRLNEAL LTIYDLFWGD
     YCDWYLELIK PPRGQAMDDE TIALAVELYE KMIQLLHPFM PFITEALWWR LRPRGEREAC
     IVSRWPEQNP DEIDETALVR FGRIQEMISG IRNVRSTYGV PPGREIRALI NVPEAEAEEV
     AHLEAHRDYF ARLARVSELT VGVGLERPKA SATVVVGRYE VYVPLADVID LEQERARLEK
     EIAQKERFLE SVRKKLQNPQ FLEKAPAEVV ARERQKEQDA RAELERLQAN LAALS
//
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