GenomeNet

Database: UniProt
Entry: R1G9Y5_NANST
LinkDB: R1G9Y5_NANST
Original site: R1G9Y5_NANST 
ID   R1G9Y5_NANST            Unreviewed;       744 AA.
AC   R1G9Y5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE            EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN   ORFNames=Nst1_391 {ECO:0000313|EMBL:EOD42659.1};
OS   Nanobsidianus stetteri.
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanopusillaceae; Nanobsidianus.
OX   NCBI_TaxID=1294122 {ECO:0000313|EMBL:EOD42659.1, ECO:0000313|Proteomes:UP000053279};
RN   [1] {ECO:0000313|EMBL:EOD42659.1, ECO:0000313|Proteomes:UP000053279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Podar M., Makarova K.S., Graham D.E., Wolf Y.I., Koonin E.V.,
RA   Reysenbach A.-L.;
RT   "Insights into archaeal evolution and symbiosis from the genomes of a
RT   Nanoarchaeon and its crenarchaeal host from Yellowstone National Park.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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};
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:EOD42659.1}.
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; APJZ01000002; EOD42659.1; -; Genomic_DNA.
DR   AlphaFoldDB; R1G9Y5; -.
DR   PATRIC; fig|1294122.7.peg.377; -.
DR   Proteomes; UP000053279; Unassembled WGS sequence.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; 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; 1.
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.
PE   4: Predicted;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000313|EMBL:EOD42659.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EOD42659.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053279}.
FT   DOMAIN          14..597
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          637..734
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
SQ   SEQUENCE   744 AA;  89082 MW;  669E5826D6370363 CRC64;
     MDKRPDYKII EKEILNLWNK NKEIFKFDIN KDKRYIIDTP PPFTSGEAHM GHALEFIWID
     FLARYKRLEG YNVYFPLGFD CHGLPTELKV INKLKISKEN KEQFIKACID WTNKMIESMY
     KTFERLGSSF DRDKVYKTID RKYEAFVQYT LIKMFNDNLI ERKRYPIMWC PKCQTAISMQ
     EAGYLEKEGY LIYIKLPTNN GKYILIATTR PELINSCSLI LIAKNKYVET ENNLIISKAY
     AEKNNLKIIR EYDYKELENL EVTIPLINRK AKIISDNDVD YNFGTGIVWI CTYGDPYDIK
     WKEKYNLPEI ISISEDGRII SNINEINGLK VEEAREKMKE ILKDYIYKIE KINHNVLSHT
     ERSDCLSPLE FIPKEQFFIK IKDLKEKILE WQKDIKIIPE SEVKRLIDWI NNIDQDWNIS
     RTKMLWGLTF PFYEKDGKIY PVNIEDLPID PRIEKEKVKK YNGKFFEDET VDVWIESSIT
     PLVILYYALT ENKEFNPKEL PELFNKIKEY LPVDLRQQGY EIIRTWLFDT IVRVNLLTNK
     NPWKYALIHG MVLDEKGRKM SKSLGNAINP NEIMDKYSPD ALRYWALLAA PGNDYRFNIK
     DIESGQAFII KLWNIGRYIE MNIKEKPEKV LELKDEDREI IKILEENIKE SKEYVDQFRY
     SEYVKLWRKF TWEDFANNYL EKIKERIKND DKTAKYLLYT IYKIILIMLH PILPYITEYI
     YQQLYKENKL IIENKIDEIM KLIL
//
DBGET integrated database retrieval system