SYR_CHLPB
ID SYR_CHLPB Reviewed; 553 AA.
AC B3EQ83;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
GN OrderedLocusNames=Cphamn1_2487;
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) 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: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; CP001101; ACE05381.1; -; Genomic_DNA.
DR RefSeq; WP_012475837.1; NC_010831.1.
DR AlphaFoldDB; B3EQ83; -.
DR SMR; B3EQ83; -.
DR STRING; 331678.Cphamn1_2487; -.
DR KEGG; cpb:Cphamn1_2487; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_0_1_10; -.
DR OMA; NKPLHLG; -.
DR OrthoDB; 1146366at2; -.
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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..553
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000095350"
FT MOTIF 123..133
FT /note="'HIGH' region"
SQ SEQUENCE 553 AA; 62250 MW; AFAF0CD8BEE61E60 CRC64;
MREYLTEHIK QALHKASIPA SRAIKIEKPS DSRFGDFSTN IALVLAGECG MNPRQLAQKI
TENLSFSETT VSKTEIAGPG FINFYLEPAF IMKQVEQIIT SSDRFGRGAA GEGKNAIVEY
VSANPTGPLT IGRGRGGVLG DCIANILEAH GYTVTREYYF NDAGRQMSIL SESVRLRYIE
LCGIAVEFPE THYQGDYIRE IAAAILEKHG EKLVESDSTE LFKQTAETHI FTHIKNTLHR
LDITHDSYFN EHRLYQEDES GISPNQQVID ALRQKGFIDH YDGATWFMTT RLGQEKDKVL
VKSSGEPSYR LPDIAYHVTK FERGFDEIVN IFGADHIDEY PDVIEALKIL GYDTDRIRVA
INQFVTTTVN GETVKMSTRK GNADLLDDLI DDVGADATRL FFIMRSKDSH LNFDIDLAKK
QSKDNPVFYL QYAHARICSL LRIAENEAGF SLEEGSADAH LMGKLTSAHE IQLGFTLLDY
PDVIQTCARI LEPQKMVEYL HSVAELYHRF YQECPILKAD PDIRSARLIL SLATRQVLRN
GFRILGISAP KSM