ID A0A1F5EII4_9BACT Unreviewed; 566 AA.
AC A0A1F5EII4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=A2Z61_01535 {ECO:0000313|EMBL:OGD67218.1};
OS Candidatus Campbellbacteria bacterium RIFCSPLOWO2_02_35_12.
OC Bacteria; Candidatus Campbellbacteria.
OX NCBI_TaxID=1797580 {ECO:0000313|EMBL:OGD67218.1, ECO:0000313|Proteomes:UP000186029};
RN [1] {ECO:0000313|EMBL:OGD67218.1, ECO:0000313|Proteomes:UP000186029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD67218.1}.
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DR EMBL; MFAC01000011; OGD67218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5EII4; -.
DR STRING; 1797580.A2Z61_01535; -.
DR Proteomes; UP000186029; 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 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; 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.
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}.
FT DOMAIN 4..87
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 454..566
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 124..134
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 566 AA; 64040 MW; 8B53702138B46D66 CRC64;
MVRDILKNTI KETISDLSLE ADDIHLEHPS DFAYGDYSTN VAMRIAKQIG ENPKELAREI
TDKIREIKIK EIEKVKVAGA GFINFYLSRE FFTQSIKEIL KIGEKWGSGN SLKNQKIIIE
YTDPNPFKEF HIGHLMSNAI GESISRIIEF SGAEAKRANY QGDVGLHTAK AIWALMRRKQ
RGSTPLFTGD EVLGVLGEAY AEGAKAYDGD DIAKEEIKKI NKKIYDKNDN EINSLYENGR
KISLEHFEEI YKKLGTKFDY YFFESETGPI GKELVKKNIG KIFEESNGAI IFRGEKAGLH
TRVFVNSEGL PTYEAKDLAL AKIKNERYDY EKSIVITANE QKEYYKVVLE AMKQIYPELA
KKTKHISHGI LRLSSGKMSS RTGLVITSES LIGEVKTKVL DKMKDADIAD KEGVAEQIAV
GAIKYSILKQ SAGKDIVFDF DKSISFEGDS GPYLQYAYAR ASSVLEKARR QNIKSDTKKV
IAETTELEKL LYRFPEVIER ANNEFEPHYI TTYLTELAGV FNSFYSREKI VEESGSSPYK
IALTEVFKIT IKNGLWLLGI KAPENM
//
