ID D1CEK3_THET1 Unreviewed; 601 AA.
AC D1CEK3;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=Tter_0438 {ECO:0000313|EMBL:ACZ41359.1};
OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC Bacteria; Chloroflexota; Thermobaculum.
OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41359.1, ECO:0000313|Proteomes:UP000000323};
RN [1] {ECO:0000313|EMBL:ACZ41359.1, ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX PubMed=21304745;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M., Tice H.,
RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Lu M., Brettin T., Detter J.C., Goker M.,
RA Tindall B.J., Beck B., McDermott T.R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1).";
RL Stand. Genomic Sci. 3:153-162(2010).
RN [2] {ECO:0000313|Proteomes:UP000000323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX DOI=10.4056/sigs.1153107;
RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M.,
RA Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J.,
RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.;
RT "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T).";
RL Stand. Genomic Sci. 3:153-162(2010).
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; CP001825; ACZ41359.1; -; Genomic_DNA.
DR RefSeq; WP_012874394.1; NC_013525.1.
DR AlphaFoldDB; D1CEK3; -.
DR STRING; 525904.Tter_0438; -.
DR KEGG; ttr:Tter_0438; -.
DR eggNOG; COG0018; Bacteria.
DR HOGENOM; CLU_006406_6_1_0; -.
DR OrthoDB; 9805987at2; -.
DR Proteomes; UP000000323; Chromosome 1.
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; cd07956; Anticodon_Ia_Arg; 1.
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; 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; 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.
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}; Cytoplasm {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:UP000000323}.
FT DOMAIN 487..601
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 147..157
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 601 AA; 69415 MW; D2B6CFFED0024BE7 CRC64;
MLQQEISQAK EAIREAIAQL GLPQPENIDL RQIPFSGQWG LATSVCHQLA RNEVQVDIPE
GLSKKEARKL LEAASRERAQ SLAESIANYL SRKGIFADVQ AQNGYVNMFF EPSDVALRLL
ATVHEQGDSY GRGNPKSETV MVEYGQPNTH KQFHIGHLRN TALGDSIARI LDFAGYRKVL
KASYIGDIGA HVIKWLWGYN KWHSGEQPPA DPYKIGPWLE SIYVEANSAI ESNPDYQREY
RDLFARWDRR DPEVVELWRR TREWSLNYFR RIFKELDVNF DVWFYESDFE EPGKKIVQDL
LNKGVAEIDE GAPIVRIDQK LGLEKETYRT IVLQRSDGTS LYQTKELALT RTKFDEYKVD
RILNVVDVRQ TLYFQQVFKV LELLGYEQAR NSQHIPYELV SLPTGPMSSR EGTTVGYDEF
ATEMYERALE VVREKNPEMP QEQQERIARI VSMGSMKFGM LNRDNTRVLV FDKEEALDFD
GFSAPYVQYA HARACRILEK APDIDWENLR IGELSTVETN LLEMISRLNE SVERAAREYK
PLHVVNYVYE LAKTFNEFYR VSPVLRAEEE VRNFRLAVVY ATKVCLANSL YLLGIEAPEV
M
//
