ID G8XA90_FLACA Unreviewed; 592 AA.
AC G8XA90;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ECO:0000313|EMBL:AEW85948.1};
GN OrderedLocusNames=FCOL_05615 {ECO:0000313|EMBL:AEW85948.1};
OS Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1041826 {ECO:0000313|EMBL:AEW85948.1, ECO:0000313|Proteomes:UP000005638};
RN [1] {ECO:0000313|Proteomes:UP000005638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC {ECO:0000313|Proteomes:UP000005638};
RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D., Benton N.R., Zaitshik J.,
RA Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA Lawrence M.L.;
RT "Complete genome sequence of Flavobacterium columnare ATCC 49512.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEW85948.1, ECO:0000313|Proteomes:UP000005638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC {ECO:0000313|Proteomes:UP000005638};
RX PubMed=22535941; DOI=10.1128/JB.00281-12;
RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D.W., Benton N.R., Zaitshik J.,
RA Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA Lawrence M.L.;
RT "Genome Sequence of the Fish Pathogen Flavobacterium columnare ATCC
RT 49512.";
RL J. Bacteriol. 194:2763-2764(2012).
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; CP003222; AEW85948.1; -; Genomic_DNA.
DR RefSeq; WP_014165227.1; NC_016510.2.
DR AlphaFoldDB; G8XA90; -.
DR STRING; 1041826.FCOL_05615; -.
DR GeneID; 60757492; -.
DR KEGG; fco:FCOL_05615; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_10; -.
DR Proteomes; UP000005638; 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; 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 {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}; Reference proteome {ECO:0000313|Proteomes:UP000005638}.
FT DOMAIN 5..86
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 477..592
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 123..133
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 592 AA; 67171 MW; 1848BA4228A9E10B CRC64;
MTLQQILTEK IKIAVEQLFE VSLDKVEFQA TRREFEGDIT MVVFPLLKLI KGNPVEIGSK
IGDYLVQNVA EIEKFNVVQG FLNLVVADRY YVDFFNAART IEQFGFKAPI EGDKAVMVEY
SSPNTNKPLH LGHIRNNLLG HAVAEIVKAS GKKVYKTQII NDRGIHICKS MLAWQKEGKN
QTPESTGLKG DKLVGHFYVE FDKQYKNEIK ELIAAGHTEE EAKKIAPSIL EAQEMLRKWE
AGDAEVVALW KKMNQWVYDG FSVTYKNLGV DFDSYYYESN TYLLGKDVIE EGLQKGVFYK
KEDGSVWIDL TSEGLDEKLV LRADGTSVYI TQDIGTAIQR VKDTPDVGGM VYTVGNEQDY
HFKVLFLILK KLGFDWAEQL YHLSYGMVEL PSGKMKSREG TVVDADDLMA EMTSTAQSIS
EELGKLDGYT DQEKADLYKI IGLGALKYYM LKVDPKKTMM FNPEESVDFN GNTGPFIQYT
YARIQSILRK ADFDCSENIL LKELHEKEKE LIKQIALFPE AIQNAAVNHS PALVANYTYD
LVKEFNSFYQ NVSILGEENT DKKIFRVQLA KLVGETIQRA FSLLGIQVPE RM
//
