ID Q4E397_TRYCC Unreviewed; 692 AA.
AC Q4E397;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033033};
GN ORFNames=Tc00.1047053508355.320 {ECO:0000313|EMBL:EAN99273.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN99273.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN99273.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN99273.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
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 -!- 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:EAN99273.1}.
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DR EMBL; AAHK01000025; EAN99273.1; -; Genomic_DNA.
DR RefSeq; XP_821124.1; XM_816031.1.
DR AlphaFoldDB; Q4E397; -.
DR SMR; Q4E397; -.
DR STRING; 353153.Q4E397; -.
DR PaxDb; 353153-Q4E397; -.
DR EnsemblProtists; EAN99273; EAN99273; Tc00.1047053508355.320.
DR GeneID; 3553939; -.
DR KEGG; tcr:508355.320; -.
DR eggNOG; KOG4426; Eukaryota.
DR InParanoid; Q4E397; -.
DR OMA; CKSMLAW; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000002296; 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 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: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; 2.
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|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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296}.
FT DOMAIN 12..99
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 578..692
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 692 AA; 78834 MW; 5656DC6E5EB91E54 CRC64;
MARICTGANV ELALKDIVRH AMEKAFPTIS TPEVLISLGK VTEYQCNNAM GLAKLLSKAT
PPMKMSPINV GEELRKNLEE NDLIERFEPT PQGFINIAIK QEWAATMVSR LLKMGIQPPI
IPPKKVLVDF SSPNIAKEMH VGHLRSTIIG ETICRLFEFC GFEVHRINHV GDWGTAFGML
ILYLKRQHPN FLTEMPDITD LTKFYREAKK CFDEDPKFKE EARLQVVKLQ ALENESIQAW
KIICDISRKE FSLIYDRLGT RIEERGESFY NPIIPRVLSL LQEAGKLEES SGAKLVISKE
KKLISSLNAK DMAKLIVPHL IQIWRDNTVE FHVNMITVLR EVGILTGEEG NETIMLSKKE
TKPLSKFDAR TDIDKIVPKL EPYYKNQLSP LFREVFEAAG ITDGDTIAVP RFNFPLILQK
SDGGFTYDTT DVTSMYHRFV MEKMDRVVYC TDVGQYEHFR MCAQLAKDMG WMGDATWDHA
GFGLVTGADG KKIKTRSGET AKLKDLLDEA VERSIAILEE REGGERSQGH TKEEMETLSK
IIGIGAIKYF DLKQSRVNDY AFSYDKMLDM SGNTAVFLLY QYARLCSIKR KANVSEDEFM
KAEVVINTPQ EKRLALCAFR MESVLLKTVE DLFPHHLTDF AYELVSCFSD FFQNCKVVGD
PMQNSRLCLV ELTRITLKKV FDILNIEATE RI
//
