ID D2VG96_NAEGR Unreviewed; 536 AA.
AC D2VG96;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=NAEGRDRAFT_33778 {ECO:0000313|EMBL:EFC44232.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC44232.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC44232.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-
CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA-
CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215;
CC EC=6.1.1.19; Evidence={ECO:0000256|ARBA:ARBA00001766};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363038}.
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DR EMBL; GG738869; EFC44232.1; -; Genomic_DNA.
DR AlphaFoldDB; D2VG96; -.
DR STRING; 5762.D2VG96; -.
DR EnsemblProtists; EFC44232; EFC44232; NAEGRDRAFT_33778.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_33778; -.
DR eggNOG; KOG1195; Eukaryota.
DR InParanoid; D2VG96; -.
DR OMA; WFRRMEN; -.
DR OrthoDB; 5472958at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00456; argS; 1.
DR PANTHER; PTHR11956:SF11; ARGININE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|RuleBase:RU363038};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363038};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU363038};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 420..536
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 536 AA; 60500 MW; 9944A32265E195C7 CRC64;
MNIASDLAKE ISRIVKEKTD VVVENCVGEG PYVNFFYQPA HLGKAIEEVH NGNFLSVRES
KNENVMIEYS QPNTHKTFHV GHMRNAALGN SLVLLYEWCG YNVHAVNYIG DVVDKQGVIS
QGFILSQAEL GSSENKEKIH IFPADSPVGI ELTELGRKAD CNVDASINIG QEFKKRESQC
KTLLRAMEDH KKNISMLWEI TRTWSIEDFK SIYKWSDCRF DHFFHESDVG DESKEIVLKA
YEEGKLIKSD GAIGADLGKL GFCVLLTSAG TGLYATKDLA LAKRKFEEFK VDRSVYVVDV
SQSLHFQQVF KTLEVLGFEQ AKKCKHLAYG MVVLPDGKMS SRKGNIIYFS TLQKSLTQNI
TDNFMSKYEG EWPKEEIEET TRKIAISAIK YGMLNQDNNK DITFVLKEWA SKSGNTGPYL
MYAYARAVSV VNKIGLDSSV TIDYSLLTDE TERKLLSTIL QYSIVVERAA EQYKPQLLCI
FLYNLCKQYS KMYEAVSIRD AATPELKQTR LRLVAGFAKV LKHGLGLLGI STAERM
//