SYR_NOCFA
ID SYR_NOCFA Reviewed; 552 AA.
AC Q5Z0Z9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=NFA_10470;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD55892.1; -; Genomic_DNA.
DR RefSeq; WP_011207577.1; NC_006361.1.
DR AlphaFoldDB; Q5Z0Z9; -.
DR SMR; Q5Z0Z9; -.
DR STRING; 247156.NFA_10470; -.
DR EnsemblBacteria; BAD55892; BAD55892; NFA_10470.
DR GeneID; 61131869; -.
DR KEGG; nfa:NFA_10470; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_11; -.
DR OMA; NKPLHLG; -.
DR Proteomes; UP000006820; 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; -; 1.
DR Gene3D; 3.40.50.620; -; 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 PANTHER; PTHR11956; PTHR11956; 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; SSF47323; 1.
DR SUPFAM; SSF55190; SSF55190; 1.
DR TIGRFAMs; TIGR00456; argS; 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; Reference proteome.
FT CHAIN 1..552
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242058"
FT MOTIF 130..140
FT /note="'HIGH' region"
SQ SEQUENCE 552 AA; 59065 MW; FCE2A0FCFC6A59AA CRC64;
MTPADLADLL RATAAKVLAE RGLDPAVLPD EVTVERPRNP EHGDYATNLA MKVAKKAGTN
PRDLAGWLAE ALGAADGITS AEVAGPGFLN IRLAAAAQGA VLEQVLAAGS GYGTADTLRG
TKINLEFVSA NPTGPIHLGG TRWASVGDAL GRILAAQGAD VTREYYFNDH GAQIDRFANS
LVAAATGQPT PDDGYAGAYI GEIAEQIVAE HPEAPTLPAD QRHELFRAEG VELMFAHIKR
TLHEFGTDFD VYFNESTLFA SGAVEQAVET LKASGDLYEK DGAWWIASSE YGDDQDRVVI
KSDGNAAYIA GDIAYFQNKR SRGFDLCIYM LGADHHGYIG RLKAAAAAFG DDPATVEVLI
GQMVNLVRDG QAVKMSKRAG TVVTLDDLVE AIGVDAARYA LVRWSVNSSV DIDLNLWTSQ
KNENPVYYVQ YAHARTASIG RNAAAFDYAS VTPDLSQLTA EEEGELIRTI GEYPRVVASA
ASLREPHRVA RYLEELAGAY HRFQTNSKLR VLPLGDDPVS PLNAARLVLV NATRQVLANG
LALLGVSAPE QM