ID SYR_MARN8 Reviewed; 561 AA.
AC A1TYU8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=Maqu_0820;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(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:0000255|HAMAP-Rule:MF_00123};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00123}.
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DR EMBL; CP000514; ABM17917.1; -; Genomic_DNA.
DR RefSeq; WP_011784339.1; NC_008740.1.
DR AlphaFoldDB; A1TYU8; -.
DR SMR; A1TYU8; -.
DR STRING; 351348.Maqu_0820; -.
DR KEGG; maq:Maqu_0820; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_6; -.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000000998; 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; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..561
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000018055"
FT MOTIF 128..138
FT /note="'HIGH' region"
SQ SEQUENCE 561 AA; 62130 MW; C04EF72CB9611219 CRC64;
MKETVSELLQ SALATLQSDG TLPADQSFTP QVGNTKDKSH GDYACNIALV ASKAAGCPPR
KLAEALVAAL PENSAVEKVE IAGPGFINFF MSTASAFGIV NTILDEAQQF GRNNSGNGER
VQVEFVSANP TGPLHVGHGR GAAIGDCLCR LLEANGYDVT REFYYNDAGA QINNLALSVQ
SRVKGLTPED ESWPEDGYRG DYIVDVANAY LAGETVVADD REVTAKADPE DRDAIREFAV
AYLRREQDLD LKAFGVQFDV YFLESSLYED GKVEATVERL KANGYTYEQD GAMWLKTTEF
GDDKDRVMRK KDGGYTYFLP DVAYHLDKWQ RGFTTVINEQ GADHHSTVTR VRAGLQALKA
DIPQGWPDYV LHQMVMVTRS GQEVKISKRA GSYVTVRDLI DEVGRDATRF FLAARRVDSQ
LTFDIDLARS QTNENPVYYI QYAHARICSV LRKLAAEGVQ RGMNECVGEL SLLTLDEEKE
LANQLAKYPE LIANSAAQRE PHHLTHYLRE LAGQFHTYYN AHKVLIEDTA LRDARVSLYL
AVRQVIANGL DLLGVSAPEE M
//
