ID SYR_KORCO Reviewed; 632 AA.
AC B1L3E4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=Kcr_0213;
OS Korarchaeum cryptofilum (strain OPF8).
OC Archaea; Candidatus Korarchaeota; Korarchaeum.
OX NCBI_TaxID=374847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF8;
RX PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA Richardson P., Keller M., Stetter K.O.;
RT "A korarchaeal genome reveals new insights into the evolution of the
RT Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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 -!- 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; CP000968; ACB06973.1; -; Genomic_DNA.
DR RefSeq; WP_012308870.1; NC_010482.1.
DR AlphaFoldDB; B1L3E4; -.
DR SMR; B1L3E4; -.
DR STRING; 374847.Kcr_0213; -.
DR EnsemblBacteria; ACB06973; ACB06973; Kcr_0213.
DR GeneID; 6093502; -.
DR KEGG; kcr:Kcr_0213; -.
DR eggNOG; arCOG00487; Archaea.
DR HOGENOM; CLU_006406_6_1_2; -.
DR InParanoid; B1L3E4; -.
DR OrthoDB; 372102at2157; -.
DR PhylomeDB; B1L3E4; -.
DR Proteomes; UP000001686; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IBA:GO_Central.
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; IPR001278; Arg-tRNA-ligase.
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; PF05746; DALR_1; 1.
DR Pfam; PF00750; tRNA-synt_1d; 2.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..632
FT /note="Arginine--tRNA ligase"
FT /id="PRO_1000095374"
FT MOTIF 129..139
FT /note="'HIGH' region"
SQ SEQUENCE 632 AA; 71667 MW; 751ACAF493D4691C CRC64;
MIKDPLGAVK STFAEEVNRV LRDLGSATRF SPIQVSRVRK DYASYGLPVG FKVAKDLNLD
PERAAKTVLD RIDMSRIAYS SDAYAESGYL NLRIDKARFF RDILKLASSE ELGRGERKGV
VGMVEHTSAN PVHPLHVGSG RNAVIGDSFS RILNFLGWDV RRHYLVNDCN LQVAILAAGR
SKVRDLIPKG KVDHWFGLIY AISNAFLEIW RIKNGFNSES KIEEWSEVVE RIGRMEPELL
RIGELSEEEV MSLLREYQRK EGGSVQMFRE ITESVLRGFV ETLERMGITY DSFDRESELI
WDGWVDRAIE KLESSGYLKR EGKAAYVDLW EAAKGDENVR KVFELSEDDI SKLEREGKLG
EVIPRKFYLT RSDGTWLYTG TDVAYSLYKF DGLGVSFCYN VIASEQNMEQ KGVRACLALM
GHDPGKLIHL SYEMVNLVGA AMSGRRGLYI TLDEVLDEAK RRVEAILKER GIYDEEICEK
VAIGALKYGL ISVSPNKVVQ FRWERVLNLE ENSGPFIQYA YTRALNIIKK AQGVPEDFDP
NELKSDAEIT IVQMISEFPE RVWSAFNLMR PDIIASYANE LASQFNKFYE DHPVLSAARP
EERAARLNLV NAVKGTLGLA MDLIGIPRLE RM
//
