ID   A0A183JFK2_9TREM        Unreviewed;       433 AA.
AC   A0A183JFK2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Arginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033033};
GN   ORFNames=SCUD_LOCUS1470 {ECO:0000313|EMBL:VDO67882.1};
OS   Schistosoma curassoni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0000146901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SCUD_0000146901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO67882.1, ECO:0000313|Proteomes:UP000279833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dakar {ECO:0000313|EMBL:VDO67882.1}, and Dakar, Senegal
RC   {ECO:0000313|Proteomes:UP000279833};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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   EMBL; UZAK01001191; VDO67882.1; -; Genomic_DNA.
DR   STRING; 6186.A0A183JFK2; -.
DR   WBParaSite; SCUD_0000146901-mRNA-1; SCUD_0000146901-mRNA-1; SCUD_0000146901.
DR   Proteomes; UP000050789; Unplaced.
DR   Proteomes; UP000279833; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00456; argS; 1.
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; PF00750; tRNA-synt_1d; 1.
DR   PRINTS; PR01038; TRNASYNTHARG.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279833};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..433
FT                   /note="Arginyl-tRNA synthetase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041047717"
FT   DOMAIN          33..70
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03485"
FT   DOMAIN          80..425
FT                   /note="Arginyl-tRNA synthetase catalytic core"
FT                   /evidence="ECO:0000259|Pfam:PF00750"
FT   COILED          368..402
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   433 AA;  49408 MW;  93451E6A5D467EE4 CRC64;
     MFPLSAVLGI ISATLLLAFE KYVLNNVTIA QESNSDQNPF DIAKSIVAAL PVNDLIERVD
     VVLPGFINIW IKQQFISAEV RKILLHGVTP PFIPHKYSVI VDMSSPNIAK EMHVGHLRST
     IIGESISRLL SFLGHKVLKL NHLGDWGTQF GMLITHLKEI YPDHKTAPPI SDLQAFYKTS
     KTRFDEEKDF NQRAHVAVVK LQQNDPEYVH AWKQICDISR KEFDDVYRRL GIENLIERGE
     SFYQSRMEEF VNDLKSQNVL QEDEGRLILW PPKCEVPLTV VKSDGGFTYD TSDLTALLQR
     LHEEKADWVL YVVDMGQSVH LNTVFAGAEM LGYYNPNVHR VQHIGFGVVL GEDKKKFKTR
     SGDTVRLVDL LDEGLERAKN RLLEKERNKE LTEAEFERAQ KAVAYGCIKY ADLSHSRTID
     YVFSFDRVSN GDM
//