ID A0A0F3NLC7_9RICK Unreviewed; 576 AA.
AC A0A0F3NLC7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:KJV68840.1};
GN ORFNames=NLO413_0206 {ECO:0000313|EMBL:KJV68840.1};
OS Candidatus Neoehrlichia lotoris str. RAC413.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neoehrlichia.
OX NCBI_TaxID=1359163 {ECO:0000313|EMBL:KJV68840.1, ECO:0000313|Proteomes:UP000033562};
RN [1] {ECO:0000313|EMBL:KJV68840.1, ECO:0000313|Proteomes:UP000033562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC413 {ECO:0000313|EMBL:KJV68840.1,
RC ECO:0000313|Proteomes:UP000033562};
RA Daugherty S.C., Su Q., Abolude K., Beier-Sexton M., Carlyon J.A.,
RA Carter R., Day N.P., Dumler S.J., Dyachenko V., Godinez A., Kurtti T.J.,
RA Lichay M., Mullins K.E., Ott S., Pappas-Brown V., Paris D.H., Patel P.,
RA Richards A.L., Sadzewicz L., Sears K., Seidman D., Sengamalay N.,
RA Stenos J., Tallon L.J., Vincent G., Fraser C.M., Munderloh U.,
RA Dunning-Hotopp J.C.;
RT "Genome Sequencing of Rickettsiales.";
RL Submitted (FEB-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJV68840.1}.
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DR EMBL; LANX01000001; KJV68840.1; -; Genomic_DNA.
DR RefSeq; WP_045808681.1; NZ_LANX01000001.1.
DR AlphaFoldDB; A0A0F3NLC7; -.
DR STRING; 1359163.NLO413_0206; -.
DR PATRIC; fig|1359163.3.peg.199; -.
DR OrthoDB; 9803211at2; -.
DR Proteomes; UP000033562; Unassembled WGS sequence.
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; 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:UP000033562}.
FT DOMAIN 13..95
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 452..575
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 132..142
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 576 AA; 66219 MW; 347B27065F6F83B6 CRC64;
MNLFSYIRDL ILQRIYSLVK KNLIRFDDSL INKLIIGPPS NNEYGDIYTN AALIIGKFEK
KNPLEVSQIL IKELRLIKEI SSIEVAPPGF INLKLEMKFL YKVLFSINVL KSEYGKVNLG
KGEKINIEFA SANPTGPLHI GHARGAIFGD VLSNLLEWVG YQVTREYYIN DAGNQIDILT
QSVYLRYKEI LGENIIIEDG LYPGEYLKAV AQGLFDLYQN NLLNMDKDEK MSIIQDFTLN
YIMNLIKNDM HCLGIKYDIF TSEKQLHSNF FIDNCITKLQ KKGLIYYGVL DKPKGKEQSD
WSSREQMLFR STKFGDDVDR ALKKKDGSWT YFANDIAYHF DKISRGFYRM ILELGSDHAG
YVTRLKSAVK ALSDGKATID IKLHNIVNFL ENGEPIKMSK RKGEFLTVKD VVEKVGRDIT
RFIMLTRRSD MVLDFDFAKV VEKSRDNPIF YVQYAHARVC SLIRRCPNLL VLDDVNFNVL
SSNEELFLIK LLARWPDIIE LSAKTFEPHR IAFYLIEVAE AFHVLWGYGN NNVNMRFIID
DDIHITSARM YLAKAVSYVI ASGLTIFSIS PIEEMS
//
