ID A0A0K1XCM8_9GAMM Unreviewed; 580 AA.
AC A0A0K1XCM8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123};
GN ORFNames=AKN88_02965 {ECO:0000313|EMBL:AKX59014.1};
OS Thiopseudomonas alkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Thiopseudomonas.
OX NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX59014.1, ECO:0000313|Proteomes:UP000063953};
RN [1] {ECO:0000313|EMBL:AKX59014.1, ECO:0000313|Proteomes:UP000063953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E5571 {ECO:0000313|EMBL:AKX59014.1,
RC ECO:0000313|Proteomes:UP000063953};
RX PubMed=26679585;
RA Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA Juieng P., Loparev V., McQuiston J.R.;
RT "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. (Proposed),
RT a Novel Bacterium of the Pseudomonadaceae Family.";
RL Genome Announc. 3:e01474-15(2015).
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 ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC ECO:0000256|RuleBase:RU363038}.
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; CP012365; AKX59014.1; -; Genomic_DNA.
DR RefSeq; WP_053100011.1; NZ_CP012365.1.
DR AlphaFoldDB; A0A0K1XCM8; -.
DR STRING; 1697053.AKN87_04970; -.
DR KEGG; pbb:AKN87_04970; -.
DR PATRIC; fig|1697053.3.peg.1009; -.
DR Proteomes; UP000063953; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07956; Anticodon_Ia_Arg; 1.
DR CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00123; Arg_tRNA_synth; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
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:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 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; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Reference proteome {ECO:0000313|Proteomes:UP000063953}.
FT DOMAIN 3..91
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 463..580
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 127..137
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 580 AA; 64848 MW; F198D6752C3E58B0 CRC64;
MKNHIRHLVQ HALNQLTEQG VLPKELTPNI QVENTRDKAH GDFACNIAMM LAKPAQMKPR
DLAEKIIQAL PQDPQISQVQ IAGPGFLNFF QNSQALAERL DAALADEHLG IAKKSPAETV
VIDLSSPNLA KEMHVGHLRS TIIGDAVARV LEFLGDHVIR QNHVGDWGTQ FGMLLAYMQE
QGADSQAELA DLEEFYRAAK QRFDESPEFA NRARQLVVAL QAGDEDCLRL WQRFNEVSLN
HCQAVYDRLD VKLSMDDVKG ESFYNPDLAT IVQELKDQGL LTEDAGAQCV FMDEFKNADN
DPLPIIVQKA DGGYLYSTTD LAAMRYRNNQ LQADRVLYFV DQRQALHFQM VFSLARLAGF
VRPAMQLEHM GFGTMNGADG RPFKTRDGGT VKLIDLLDEA EQRAYQLVKQ KNPELNEDEL
QQVAHSVGIG AVKYADLSKH RSSDYSFNFE QMLSFEGNTA PYLLYAYTRV ASVFRKAGLT
MDAALPGSMQ LEAEQELSLA SSLARFAEVL QQVADKGTPH TLCTYLYDLA GQFSSFYENC
PILTAEQEST QHSRLRLAAL TGRTLKQGLE LLGLNTLERM
//
