ID G0QGM3_NANS0 Unreviewed; 331 AA.
AC G0QGM3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00020262};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=J07AB43_14350 {ECO:0000313|EMBL:EGQ43444.1};
OS Nanosalina sp. (strain J07AB43).
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC Nanosalina.
OX NCBI_TaxID=889948 {ECO:0000313|EMBL:EGQ43444.1, ECO:0000313|Proteomes:UP000009379};
RN [1] {ECO:0000313|EMBL:EGQ43444.1, ECO:0000313|Proteomes:UP000009379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07AB43 {ECO:0000313|Proteomes:UP000009379};
RA Narasingarao P., Podell S., Ugalde J.A., Brochier-Armanet C., Emerson J.B.,
RA Brocks J.J., Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "De novo metagenomic assembly reveals abundant novel major lineage of
RT Archaea in hypersaline microbial communities.";
RL ISME J. 0:0-0(2011).
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; GL982576; EGQ43444.1; -; Genomic_DNA.
DR AlphaFoldDB; G0QGM3; -.
DR HOGENOM; CLU_006406_4_0_2; -.
DR Proteomes; UP000009379; 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 PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
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 ECO:0000313|EMBL:EGQ43444.1}; ATP-binding {ECO:0000256|RuleBase:RU363038};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|RuleBase:RU363038};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363038};
KW Protein biosynthesis {ECO:0000256|RuleBase:RU363038};
KW Reference proteome {ECO:0000313|Proteomes:UP000009379}.
FT DOMAIN 219..331
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 154..181
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 331 AA; 37992 MW; 56C2C301365A7DB6 CRC64;
MEEGEDEGCV VIDLSEYEEQ IGEMKKPYKI LFRSDGTATY TAKDIALTMW KFGIIESSFQ
YKKFDHQPND ETLWSTGGDK DKCFGDADQV INVIGAPQKY PMKVIKYSLK ALGYEEEAEN
FSHCHFKFVY LPGKVSYSGR KGNWVGKHGD AVLGKCKELA LEEVEKRHEE LSDEKKQKIA
NKVGVAAVRY FLLKFTREKD IDFSFEKALS WEGDSGPYLL YSTARAHEIL DKTKIEPDFT
EYEEEIEFEL IRELDKFESV VKQGYHSQEP AKLIHYLKGL AEKFNSFYHK CPVKDAETEK
LAISRAAITE AYVDVMEEGL NLLGIEPLEE M
//
