ID A0A0V1CRK8_TRIBR Unreviewed; 1380 AA.
AC A0A0V1CRK8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 Name=rars {ECO:0000313|EMBL:KRY51762.1};
GN ORFNames=T03_5225 {ECO:0000313|EMBL:KRY51762.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY51762.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY51762.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY51762.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRY51762.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDI01000118; KRY51762.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 1.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRY51762.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 673..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 763..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 861..879
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 902..928
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 994..1017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1149..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1181..1206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1218..1240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1260..1291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1303..1323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1343..1365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..177
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 525..636
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT COILED 7..37
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1380 AA; 156780 MW; DAB2C93F84FA2DCC CRC64;
MADEALLQKL ENDASLLLAE GENLKRLQSN LESYEEDPEL SSMIQTNQRL RYRIGLLKTA
LSELTSNKCE KEANSDSSVL QSLKLIFAKA VNDAFPNATE CPIIITETSS EKHGDYQFNS
CMAIAKFLSN SHSTKISPRK VAEEIVNVLM TTVQLEKEKS LIDKIDIAGP GFLNIFLNFN
AVHQRIFDIF VNGVKPPVLP AKRVVVDFSS PNIAKEMHVG HLRSTIIGDC ICRLLEFCGF
DVLRLNHVGD WGTQFGMLIA HLKDRFPNYQ NEPPHLADLQ SFYKESKVRF DADEEFKSRA
LQEVVKLQAH EPEQIKAWTL ICQLSRHDFQ RIYDKLDVKL VERGLLELDE GRKIVFPEGC
STPLTIVKSD GGYTYDTSDL AALKHRLFEE KADWVLYVVD SGQGLHFQQI FTVGKQLGWW
NENSHRVQHI AFGLVLGEDK RKFRTRSGET VKLSDLLEEG MRRSAATLKE KQRDQVLSPK
ELDIAQRSVA YGCIKYADLS HNRKNDYVFS FDKMLEDKGN TAVYLLYAYS RMRSISRNAN
VSRENLKEKI HCGEISFDHP KELKLMKMII KFPDIISHVV ENFLPNLICD YIYNLATVFT
EFYDECYCIE KDPATGALVK INYNRLILCE VTADQLWFSN GKMQTAGKRN VGSELDRHLS
EWIPAEDMTP FKTAFYTVAL FTFLVVVFSL LGSVCCLLAS FAQPILWAVL FGTVLFPLKK
SLANALECWL DEIQNTQTPF AVGLLVLPWR LAEFSISSLV ARVARKSNIL SVVIYVLLWS
VSRNGPLLPL FRRLWNFLDG LLLFGFNWFY ITLSLVYFIV ICVVVDMKKK EPNKYFIRAL
SVPVWYLVIC IGSNIFGKYR VLGALAFVTF IVCVALDVFK DTEKPQTEKE FEMSHFDYLE
RIIGAALLLF ILKHNYMFAL VGVLLTLASM RKICQYFDGW KTLVDFILHI YWKFHDNFSP
VLHIWFPHQM RDFFNLCFFG SPNYLSKLRS CSSILSTVTV MVVMMAALIL LLFFFVVQIG
DESASLAMLS FDLLNRTWTS GNHLPVFVEN ALSSHDRQAF IEDGYLKARS WLGSKARSLL
QNDDDNCEKA QMLENQLLLI LDNIYDMWKS TNRSNLGDQS TLTTVWVHLH TDNFGALSSG
LIHYLRANFA IVSSILEVAW NFVLLNLNAV ITLAVPLLGE IFTFGFSLFN MLLQFIMFLT
TLFYLLECSR DVWKPVEMLA SFVPFLSTPK GGESVFFVAF QRSVRSVFVI SFKMSTFYGL
YTWLMYSLFG LSMTVLPSVI ASLLAAVPVV PPSIACFPGC LELWLANGES TLAVLFLICS
FAPSIESHPF LTALSVCGGV YWLGLQGAII GPVLLCCFLF VTVLYRSVGK SFSDSSSTIH
//
