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Database: UniProt
Entry: R0N2N7_STRMT
LinkDB: R0N2N7_STRMT
Original site: R0N2N7_STRMT 
ID   R0N2N7_STRMT            Unreviewed;       199 AA.
AC   R0N2N7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Arginyl-tRNA ligase {ECO:0000313|EMBL:EOB20735.1};
DE            EC=6.1.1.19 {ECO:0000313|EMBL:EOB20735.1};
DE   Flags: Fragment;
GN   Name=argS {ECO:0000313|EMBL:EOB20735.1};
GN   ORFNames=D064_09339 {ECO:0000313|EMBL:EOB20735.1};
OS   Streptococcus mitis 11/5.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1239792 {ECO:0000313|EMBL:EOB20735.1, ECO:0000313|Proteomes:UP000013365};
RN   [1] {ECO:0000313|EMBL:EOB20735.1, ECO:0000313|Proteomes:UP000013365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11/5 {ECO:0000313|EMBL:EOB20735.1,
RC   ECO:0000313|Proteomes:UP000013365};
RA   Ikryannikova L.N., Ilina E.N., Kostryukova E.S., Semashko T.A.,
RA   Karpova I.Y.U., Larin A.K., Ischenko D.S., Alekseev D.G., Klimova E.A.,
RA   Filimonova A.V., Savinova T.A., Filimonova O.Y.U., Dubovickaya V.A.,
RA   Sidorenko S.V., Govorun V.M.;
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EOB20735.1}.
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DR   EMBL; AQTT01000035; EOB20735.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0N2N7; -.
DR   Proteomes; UP000013365; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-EC.
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          5..83
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   NON_TER         199
FT                   /evidence="ECO:0000313|EMBL:EOB20735.1"
SQ   SEQUENCE   199 AA;  21979 MW;  6DB6611C11C67F81 CRC64;
     MNTKELIASE LASVIDSLDQ EAILNLLETP KNSEMGDIAF PAFSLAKVER KAPQMIAAEL
     AEKINSQAFE KVVATGPYVN FFLDKSAISA QVLQAVITEK GHYADQHIGK QENVVIDMSS
     PNIAKPFSIG HLRSTVIGDS LSHIFQKIGY QTVKVNHLGD WGKQFGMLIV AYKKWGDEEA
     VKAHPIDELL KLYVRINAE
//
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