ID G8TGL9_NIAKG Unreviewed; 631 AA.
AC G8TGL9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 OrderedLocusNames=Niako_2106 {ECO:0000313|EMBL:AEV98461.1};
OS Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS GR20-10).
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV98461.1, ECO:0000313|Proteomes:UP000005438};
RN [1] {ECO:0000313|EMBL:AEV98461.1, ECO:0000313|Proteomes:UP000005438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC {ECO:0000313|Proteomes:UP000005438};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Niastella koreensis GR20-10.";
RL Submitted (DEC-2011) 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; CP003178; AEV98461.1; -; Genomic_DNA.
DR AlphaFoldDB; G8TGL9; -.
DR STRING; 700598.Niako_2106; -.
DR KEGG; nko:Niako_2106; -.
DR PATRIC; fig|700598.3.peg.2160; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_10; -.
DR Proteomes; UP000005438; 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 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; 2.
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}.
FT DOMAIN 18..102
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 518..631
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REGION 451..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..147
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 631 AA; 71543 MW; 90A2C4ED47D672BD CRC64;
MVHSGKFAVQ INRMAIVPVI QQAVSEQLNK LYQVEVNPAS ITVSETKPEF EGDYTVVLFA
LLKTLKKKPE ELGNELGQAL VTDNGALFSA FNVIKGFLNL AISDSFWLNF LKENYKTTGY
GRQYRNGKRV MVEYSSPNTN KPLHLGHLRN NFLGWSVAEI YKANGYQVIK TCIANDRGIH
ICKSMIAWQL FGNGATPEST GIKGDHLVGD YYVLFGTELK KQMAPIREKK LAELLAAGKT
REQAEKILED TKQELEKEAP IMQAAQQMLV DWEAGKPDVV ELWRTMNSWV YKGFEETYRR
IGSDFDKIYY ESETYLLGKD LVEEGLQKKV FFLKEDGSAW VDLTADGLDQ KIVRRRDGTA
VYITQDIGLA EVKQNEFNCD LSVYVVGDEQ NYHFKVLKLI CQKLGIAGAD GIFHLSYGMV
ELPTGRMKTR EGTVVDADDI LDEMNREATR KRIEREEEQK AKGQHKTEEM SAEELKQLDE
MVGAGGLKFF LLRVDPQKRM IFNPEESIEL NGFTATFVQY AYARTQSVFR KELYTGGDIG
TDLLPLEKEL ILSLERYPEV LKQACAEMSP SVVAGYVFNV AQLFNTFYNK HSFLNAETPV
KKELRLQINQ MVANVLKTGM ALLGIEVPER M
//
