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Database: UniProt
Entry: D2VG96_NAEGR
LinkDB: D2VG96_NAEGR
Original site: D2VG96_NAEGR 
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
//
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