ID A0A418SDM6_9RHOB Unreviewed; 580 AA.
AC A0A418SDM6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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 ECO:0000313|EMBL:QPM89453.1};
GN ORFNames=PSAL_006720 {ECO:0000313|EMBL:QPM89453.1};
OS Pseudooceanicola algae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1537215 {ECO:0000313|EMBL:QPM89453.1, ECO:0000313|Proteomes:UP000283786};
RN [1] {ECO:0000313|EMBL:QPM89453.1, ECO:0000313|Proteomes:UP000283786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lw-13e {ECO:0000313|EMBL:QPM89453.1,
RC ECO:0000313|Proteomes:UP000283786};
RA Poehlein A., Wolter L., Daniel R., Brinkhoff T.;
RT "Genome sequence of Rhodobacteraceae bacterium Lw-13e.";
RL Submitted (AUG-2020) 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; CP060436; QPM89453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418SDM6; -.
DR KEGG; palw:PSAL_006720; -.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000283786; 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:UP000283786}.
FT DOMAIN 5..94
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 451..579
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 580 AA; 63884 MW; 8C3AE456B5822E4D CRC64;
MNLFTDIRSL VLESLTALQA RGDLPEGLVF DSVTVEPPRD PAHGDMATNA AMVLAKPAGM
KPRDIAEALA ALLIEDPRID SAEVAGPGFL NLRLAEAIWG EIVTAALHEG TGYGRSVMGE
GTRVNVEYVS ANPTGPLHVG HTRGAVFGDA LAELLAYAGY GVTREYYIND GGAQVDVLAR
SVYLRYLEAH GREVEFADGT YPGDYLIETG AALKDRVGDA YVDQPEEVWL QDIRSFATEA
MMDLIREDLA LLNVQMDVFY SEKSLYGTGR IEEAIETLRA KGLIYRGVLE PPKGKMPEDW
EPREQTLFKS TEHGDDVDRP IAKSDGAWTY FAPDIAYHYD KVSRGFDQLI DVFGADHGGY
VKRMKAAVSA LSDDRVPLDI KLCQLVKLFK NGEPFKMSKR AGTFIMLRDV VEQVGADVTR
FVMLTRKNDA PLDFDFDKVL EQSRENPVFY VQYAHARICS ALRKAEAAGI ACGDADLLAT
PTSVTHPSEL AVARKLAEWP RQVEIAARTH EPHRIAFYLY ELASDLHALY NRGNEETQLR
FVQEDAPQVS QSKLALARAV TVVISAGLGI LGVTPAKEMR
//
