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Database: UniProt
Entry: A0A0G0PW38_9BACT
LinkDB: A0A0G0PW38_9BACT
Original site: A0A0G0PW38_9BACT 
ID   A0A0G0PW38_9BACT        Unreviewed;       403 AA.
AC   A0A0G0PW38;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Arginine-tRNA ligase {ECO:0000313|EMBL:KKR32103.1};
GN   ORFNames=UT65_C0008G0003 {ECO:0000313|EMBL:KKR32103.1};
OS   Parcubacteria group bacterium GW2011_GWF2_39_8b.
OC   Bacteria.
OX   NCBI_TaxID=1618963 {ECO:0000313|EMBL:KKR32103.1, ECO:0000313|Proteomes:UP000034884};
RN   [1] {ECO:0000313|EMBL:KKR32103.1, ECO:0000313|Proteomes:UP000034884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, 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:KKR32103.1}.
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DR   EMBL; LBXP01000008; KKR32103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0PW38; -.
DR   Proteomes; UP000034884; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; IPR014729; Rossmann-like_a/b/a_fold.
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; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 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|RuleBase:RU363038};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363038};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363038};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363038}.
FT   DOMAIN          3..86
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
SQ   SEQUENCE   403 AA;  45704 MW;  EF5616F607E3DDD4 CRC64;
     MKDILQKEIE KLLKAIGVKN PKVTFEYPTR MDFGDLSTNV AMVYAKELSK NPLELSNEIK
     EILAHTQCAQ VWKIEAVAPG FINFYFDAEY FGKNIEKILK DGPAFAKGFS LAKQKVIIEY
     TVTNVLKPMH IGHLLGNVIG ESISRIIENS GAEVKRNNYQ GDSGLHVAKA VWGILKLGGK
     KEGSTVEKSD YIGNSYVKGA QAYDDDKQSK TEIKEINKKL FEKSDSELLD LYQWGRQVSL
     NHFEELYKKL GTKFNFYFFE SEVTESALQV VREFVKKGLF EESDGAVVFH GEKYDPKLHT
     RVFITSEGFP TYEAKDIAHA LRKYEKYPFD TAIIVTANEQ DEYFKVMFRA LQEISPEIAS
     KTQHISHGLL KLSSGKMSSR TGSVISAESL IEQVKEKIRD KMN
//
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