ID A0A1A9VK15_GLOAU Unreviewed; 942 AA.
AC A0A1A9VK15;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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};
OS Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT039606-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT039606-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT039606-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A1A9VK15; -.
DR STRING; 7395.A0A1A9VK15; -.
DR EnsemblMetazoa; GAUT039606-RA; GAUT039606-PA; GAUT039606.
DR VEuPathDB; VectorBase:GAUT039606; -.
DR OrthoDB; 3642317at2759; -.
DR Proteomes; UP000078200; 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 CDD; cd00671; ArgRS_core; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
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; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; PF13857; Ank_5; 1.
DR Pfam; PF03485; Arg_tRNA_synt_N; 1.
DR Pfam; PF05746; DALR_1; 1.
DR Pfam; PF12784; PDDEXK_2; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 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.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363038};
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363038};
KW Coiled coil {ECO:0000256|SAM:Coils};
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..92
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 446..567
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT REPEAT 677..709
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 710..742
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT COILED 887..914
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 942 AA; 107316 MW; A3F8ACE359BCE46D CRC64;
MNIFKQVSSL ISSKLNELKR RGIISTNATN FIVEPPSNRA HGDIYTNVAM VLAKHEKKNS
VEIAGMLARE FKPFDEVAKV EIAGPGFINM HLKIEVWHGI LKQINELKTE FGTLDIGDNQ
AINVEFVSAN PTGPLHIGHA RGAVFGDVLA NLLKKVGYKV TKEYYINDAG AQIDTLIKSV
YLRYKEALGE KISIEKGLYP GEYLKPIGNG LAKKYGKELL EKQDNQVIRE YTLSSILEII
KEDMNLLGVS HDVFTSEYEL QKSGKIEESI KILSDKGLVY EGYLEKPKGK ESENWTSRKE
MLFRSTKFGD DVDRALKKED GSWTYFASDI AYHFDKISRD FNNMIVELGS DHGGYVKRLK
AVVSALSDDQ AKIEVKLHNI VNFFENGKPV KMSKRSGNFL TARDVVEEVG RDITRFIMLT
RKNDMVLDFD FAKVKEQSKD NPIFYVQYAH ARAHSLMRNA PKELPTADPS LLKTDGELFL
IKTLAKWLDV VEIAARLCEP HRITFYLLEV AEAFHVLWGY GKSDLNMRFI LEDNLNLTAA
RMFLVQALAH VIASGLSIFN IEPLEEMSRV MKDEQWWKIL SAIEKEKDLN RDNWEKAGFG
VNYLFEVESN VFIQCEDGSL ILFKDFEDED FEDNAFTQPK DNGLTLLYLA VYNNLGNTIN
ALLKAEGINV NAVHTSYLRT PLHCAARNGR TKIVNTLIEN EVNVNAEDEN RFTPLHLAAY
HGHTEVVKIL IANGADPLLK NKDGKTPRDL AERCTEVNTI QEVEFLSTIM DPEIASDKQS
IVDVLCRDSS GNRYIIEMQL TRDKGFEKRA QLYAAKAYSR QADKSELPKF PKSREEQLES
VVDRWLFFFK YADETTDEDL RKIAEKSPII KLAYDELDKF HWNEKDLVAY EERIMDLRKE
EAILEYRLDL AKEEGREVFT LPSPGPTPVN RPLLNASNDF VT
//
