ID A0A2K8KAZ5_9RHOB Unreviewed; 581 AA.
AC A0A2K8KAZ5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=BG454_12965 {ECO:0000313|EMBL:ATX66612.1};
OS Rhodobaca barguzinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobaca.
OX NCBI_TaxID=441209 {ECO:0000313|EMBL:ATX66612.1, ECO:0000313|Proteomes:UP000228948};
RN [1] {ECO:0000313|EMBL:ATX66612.1, ECO:0000313|Proteomes:UP000228948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alga05 {ECO:0000313|Proteomes:UP000228948};
RA Kopejtka K., Tomasch J.M., Bunk B., Koblizek M.;
RT "Revised Sequence and Annotation of the Rhodobaca barguzinensis strain
RT alga05 Genome.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP024899; ATX66612.1; -; Genomic_DNA.
DR RefSeq; WP_071481103.1; NZ_SODJ01000002.1.
DR AlphaFoldDB; A0A2K8KAZ5; -.
DR STRING; 441209.GCA_001870665_02375; -.
DR KEGG; rbg:BG454_12965; -.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000228948; 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; 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:UP000228948}.
FT DOMAIN 5..94
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 451..580
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 131..141
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 581 AA; 63447 MW; 17C4F006D3D099F6 CRC64;
MNLFSDIRTL VIACLDAMVR DGALPAGLDF ANVAVEPPRD AAHGDMATNA AMVLAKPAGL
KPREIADALV AQLLNDDRIA AAEVAGPGFL NLRLAPSVWQ GIVATALAQG NDFGRSAMGQ
NLRVNVEFVS ANPTGPMHVG HTRGAVVGDA LSNLLAFAGY DVTREYYIND GGAQVDVLAR
SAYERYREAH GMSPEIAEGL YPGEYLIEVG EALKAEFGDR FLDKPESVWL ETVRNFATER
MMIMIREDLA ALGVRMDVYS SEKALYGTGE IEAAIERLSA QGLIYEGVLE PPKGKTPEDW
EPREQTLFRS TAHGDDVDRP IKKSDGAWTY FAPDIAYHYN KITRGFDMLI DIFGADHGGY
VKRMKAAVSA LSDGQVPLDI KLIQLVKLYK NGEPFKMSKR AGTFVTLRDV VEEVGADVTR
FVMLTRKNDA TLDFDFDKVL EQSKDNPVFY VQYAHARVCS VLRKAAESGI DTSDAALSQA
TIARLDHEAE LAMMRKLAEW PRIVELAART QEPHRIAAYL SELAAEFHGL WNRGNDIPAL
RFVQEGDPAT TSAKLALARA TGVAISAGLA ILGVTPVEEM R
//
