SYR_MANSM
ID SYR_MANSM Reviewed; 576 AA.
AC Q65SX3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=MS1330;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(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; AE016827; AAU37937.1; -; Genomic_DNA.
DR RefSeq; WP_011200504.1; NC_006300.1.
DR AlphaFoldDB; Q65SX3; -.
DR SMR; Q65SX3; -.
DR STRING; 221988.MS1330; -.
DR EnsemblBacteria; AAU37937; AAU37937; MS1330.
DR KEGG; msu:MS1330; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_5_1_6; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
DR Proteomes; UP000000607; 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.
FT CHAIN 1..576
FT /note="Arginine--tRNA ligase"
FT /id="PRO_0000242041"
FT MOTIF 122..132
FT /note="'HIGH' region"
SQ SEQUENCE 576 AA; 64648 MW; BFD98DD1CE1474DC CRC64;
MNIQWILSDK IKRAMIAAGA EQNAEPLVRQ SGKPQFGDYQ ANGIMGAAKK LGLNPREFAQ
KVLEQVDLSD IAEKTEIAGP GFINIFLNKN WVAQQADTAL NTPNFGIKTA HPQTVVIDYS
SPNVAKEMHV GHLRSTIIGD AVARALEFMG NHVIRANHVG DWGTQFGMLI AYLEKMENEH
ADAMQLSDLE AFYRAAKETY DNDEEFAVKA RSYVVKLQSG DEYCRTMWKK LVDMTMQQNQ
RNYERLNVTL TEKDVMGESL YNPMLPAIVE DLKKQGLAVE DDGALVVYLD EFKNKDGDPM
GVIVQKKDGG FLYTTTDIAA AKYRYHTLHA DRALVFSDTR QSQHMQQAWL ITRKAGYVPD
SFSLEHHNFG MMLGKDGKPF KTRSGGTVKL ADLLDEAVER ATLLINEKNT ALSEQEKAAV
IEAVAIGSVK YADLSKNRTT DYVFDWDNML SFEGNTAPYM QYAYTRIRSI FNKTDVNPTA
LSAAHIEIRN DKERALAIKL LQFEEAVQTV AKDGTPHILC NYLYELAGVF SSFYEHCPIL
NAEEPVKLSR LKLAKLTEKT LKQGLDLLGI KTVEKM