ID A0A0V0S7E4_9BILA Unreviewed; 1345 AA.
AC A0A0V0S7E4;
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:KRX22691.1};
GN ORFNames=T07_8064 {ECO:0000313|EMBL:KRX22691.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX22691.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX22691.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX22691.1};
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:KRX22691.1}.
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; JYDL01000029; KRX22691.1; -; Genomic_DNA.
DR Proteomes; UP000054630; 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:KRX22691.1};
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:UP000054630};
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 1123..1144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1151..1171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1212..1234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1240..1262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1269..1290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1310..1330
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 1345 AA; 152883 MW; FB887F761C1E8870 CRC64;
MADEALLQKL ENDASLLLAE GENLKRLQSN LESYEEDPEL CSMIQTNQRL RYRIGLLETA
LSELTSNKCE KEANSDSSVL QSLKLIFAKA VNDAFPNATK CPIIITETSS EKHGDYQFNS
CMAIAKFLSN SHSTKISPRK VAEEIVNVLM TTIQLEKEKS LIEKIEIAGP GFLNIFLNSN
AVHQRIFDIF INGVKPPVLP AKRVVVDFSS PNIAKEMHVG HLRSTIIGDC ICRLLEFCGF
DVLRLNHVGD WGTQFGMLIA HLKDRFPNYQ NEPPHLADLQ SFYKESKVRF DADEEFKSRA
LKEVVKLQAH EPEQIKAWTL ICQLSRHDFQ RIYDKLDVKL VERGLLEIDE GRKIVFPEGC
STPLTIVKSD GGYTYDTSDL AALKHRLFEE KADWVLYVVD AGQGLHFQQI FTVGKQLGWW
NENSHRVQHI AFGLVLGEDK RKFRTRSGET VKLSDLLEEG MRRSAATLKE KQRDQVLSPK
ELDIAQRSVA YGCIKYADLS HNRKNDYVFS FDKMLEDKGN TAVYLLYAYS RMRSISRNAN
VSRENLKEKI HCGEISFDHP KELKLMKMII KFPDIISHVV ENFLPNLICD YIYNLATVFT
EFYDECYCIE KDPATGALVK INYNRLILCE VTADLLWFSN GEMQTAGKRN VGSELDRHLS
EWIPAEDMTP FKTAFYTVAL FTFLVVVFSL LGSVCCLLAS FAQPILWAVL FGTVLFPLKK
SLANALECWL DEIQNTQTPF AVGLLVLPWR LAEFSINSLV ARVARKSNIL SVVIYVLLWS
VSRNGPLLPL FRRLWNFLDG LLLFGFNWFY ITLSLVYFIV ICVVVDMKKK EPNKYFIRAL
SVPVWYLVIC IGSNIFGKYR VLGALAFVTF IVCVALDVFK DTEKPQTEKD FEMSHFDYLE
RIIGAALLLF ILKHNYMFAL VGVLLTLASM RKICQYFDGW KTLVDFILHI YWKFHDNFSP
VLHIWFPHQM RDFFNLCFFG SPNIGDESAS LAMLSFDLLN RTWTSGNHLP VFVENALSSH
DRQAFIEDGY LKARSWLGSK ARSLLQNDDD NCEKAQMLEN QLLLILDNIY DMWKSTNRSN
LGDQSTLTTV WVHLHTDNFG ALSSGLIHYL RANFAIVSSI LEVAWNFLLL NLNAVITLAV
PLLGEIFTFG FSLFNMLLQF IMFLTTLFYL LECSRDVWKP VEMLASFVPF LSTPKGGESV
FFVAFQRSVR SVFVISFKMS TFYGLYTWLM YSLFGLSMTV LPSVIASLLA AVPVVPPSIA
CFPGCLELWL ANGESTLAVL FLICSFAPSI ESHPFLTALS VCGGVYWLGL QGAIIGPVLL
CCFLFVTVLY RSVGKSFSDS SSTIH
//
