(data stored in SCRATCH zone)

SWISSPROT: Q93RP5_THETH

ID   Q93RP5_THETH            Unreviewed;       592 AA.
AC   Q93RP5;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 115.
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:CAC39622.1};
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274 {ECO:0000313|EMBL:CAC39622.1};
RN   [1] {ECO:0000313|EMBL:CAC39622.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HB8 {ECO:0000313|EMBL:CAC39622.1};
RA   Shimada A., Nureki O., Dohmae N., Takio K., Yokoyama S.;
RT   "Gene cloning, expression, crystallization and preliminary X-ray analysis
RT   of Thermus thermophilus arginyl-tRNA synthetase.";
RL   Acta Crystallogr. 50:760-763(2001).
RN   [2] {ECO:0000213|PDB:1IQ0}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
RX   PubMed=11698642; DOI=10.1073/pnas.231267998;
RA   Shimada A., Nureki O., Goto M., Takahashi S., Yokoyama S.;
RT   "Structural and mutational studies of the recognition of the arginine tRNA-
RT   specific major identity element, A20, by arginyl-tRNA synthetase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:13537-13542(2001).
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|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|HAMAP-Rule:MF_00123, ECO:0000256|RuleBase:RU363038}.
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DR   EMBL; AJ278815; CAC39622.1; -; Genomic_DNA.
DR   RefSeq; YP_143364.1; NC_006461.1.
DR   PDB; 1IQ0; X-ray; 2.30 A; A=1-592.
DR   PDBsum; 1IQ0; -.
DR   SMR; Q93RP5; -.
DR   GeneID; 3169614; -.
DR   KEGG; ttj:TTHA0098; -.
DR   PATRIC; fig|300852.9.peg.96; -.
DR   eggNOG; ENOG4105C75; Bacteria.
DR   eggNOG; COG0018; LUCA.
DR   KO; K01887; -.
DR   BRENDA; 6.1.1.19; 2305.
DR   EvolutionaryTrace; Q93RP5; -.
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; -; 1.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR11956; PTHR11956; 1.
DR   Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 1.
DR   SMART; SM00836; DALR_1; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q93RP5.
DR   SWISS-2DPAGE; Q93RP5.
KW   3D-structure {ECO:0000213|PDB:1IQ0};
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:CAC39622.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00123, ECO:0000256|RuleBase:RU363038,
KW   ECO:0000313|EMBL:CAC39622.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038}.
FT   DOMAIN          2..82
FT                   /note="Arg_tRNA_synt_N"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          473..592
FT                   /note="DALR_1"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   MOTIF           112..122
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ   SEQUENCE   592 AA;  66227 MW;  BA300E5F28F672E6 CRC64;
     MLRRALEEAI AQALKEMGVP VRLKVARAPK DKPGDYGVPL FALAKELRKP PQAIAQELKD
     RLPLPEFVEE AVPVGGYLNF RLRTEALLRE ALRPKAPFPR RPGVVLVEHT SVNPNKELHV
     GHLRNIALGD AIARILAYAG REVLVLNYID DTGRQAAETL FALRHYGLTW DGKEKYDHFA
     GRAYVRLHQD PEYERLQPAI EEVLHALERG ELREEVNRIL LAQMATMHAL NARYDLLVWE
     SDIVRAGLLQ KALALLEQSP HVFRPREGKY AGALVMDASP VIPGLEDPFF VLLRSNGTAT
     YYAKDIAFQF WKMGILEGLR FRPYENPYYP GLRTSAPEGE AYTPKAEETI NVVDVRQSHP
     QALVRAALAL AGYPALAEKA HHLAYETVLL EGRQMSGRKG LAVSVDEVLE EATRRARAIV
     EEKNPDHPDK EEAARMVALG AIRFSMVKTE PKKQIDFRYQ EALSFEGDTG PYVQYAHARA
     HSILRKAGEW GAPDLSQATP YERALALDLL DFEEAVLEAA EERTPHVLAQ YLLDLAASWN
     AYYNARENGQ PATPVLTAPE GLRELRLSLV QSLQRTLATG LDLLGIPAPE VM
//

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