ID A0RWH5_CENSY Unreviewed; 773 AA.
AC A0RWH5;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
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 OrderedLocusNames=CENSYa_1062 {ECO:0000313|EMBL:ABK77692.1};
OS Cenarchaeum symbiosum (strain A).
OC Archaea; Nitrososphaerota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX NCBI_TaxID=414004 {ECO:0000313|EMBL:ABK77692.1, ECO:0000313|Proteomes:UP000000758};
RN [1] {ECO:0000313|EMBL:ABK77692.1, ECO:0000313|Proteomes:UP000000758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|Proteomes:UP000000758};
RX PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT symbiosum.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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 ---------------------------------------------------------------------------
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; DP000238; ABK77692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RWH5; -.
DR STRING; 414004.CENSYa_1062; -.
DR EnsemblBacteria; ABK77692; ABK77692; CENSYa_1062.
DR KEGG; csy:CENSYa_1062; -.
DR PATRIC; fig|414004.10.peg.976; -.
DR HOGENOM; CLU_001493_0_2_2; -.
DR Proteomes; UP000000758; Chromosome.
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 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; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABK77692.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000000758}.
FT DOMAIN 23..569
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 608..750
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 773 AA; 87442 MW; F0652E775C7F716A CRC64;
MDKTEPKIAA KSWDPALEGE VRKRWNSEGL YSFKPAPNSY TIDTPPPYPS GRPWHIGAAA
HYSQIDMIAR TARMAGKNVY FPLGIDRNGL PVELYTEKKH KLRMRDINRD EFLSLCRGTL
DELEAEMLDT MEALGLSCNV RDCYRTDSDE YRTLTQSTFI HLWKKGLIYK ATRPNNYDWT
SGTTIADAEI SYEELPTKLV HMKFTAGTGQ ITIASTRPEL LCACRAVIVC EDDERYSGLV
GSEVTVPVYG NKVPVLAHPS VKRDFGSGAV MVCSYGDQND VALFRELGLS EVAAIGLDGR
MTGIAGAYTG LRPKQAREKI IHDLEEGGHL EKVEDILHRT PVSERSRTPI EIIPMEEYYL
KQVDSIPRIR ELSKDLQFHP PMHRQILENW LDSVSMDWPI SRRRYYGTEI PVWHCASCSE
PYVPEPGRYY RPWMEQCPAD SCASCGGTKF EGEQRIFDTW MDSSVSPLFI SKYGKDDKFF
ESTYPAGLRP QAKDIVRTWL YYTMLRCDQL TGKRPWSEAW IMGYGLDERG QKMSKRAGNS
IDPLPLVKRI GADAFRLWSA GEVSHGHDFR CNEDMMVSTK KFLSKLWNVS RFLSGFSSAD
AEPSAEPDRW ILSELDKLVS KCQEGYEKYD FFVPAVAIRE FTWNIFAAHY IELVKGRAYG
DPGPGRDSAI STLHRVLSTI LLLLAPITPF ITDYLWRELY SKDSIHLESA PRPSGAPDMS
SITEQLTAFN STIWNKKKEL GLSLKDSVEA EVPAGLSGFA SDLCSMHNIG EKP
//
