UniProt: A0A0R3WNF5

Database: UniProt
Entry: A0A0R3WNF5_HYDTA

LinkDB:  A0A0R3WNF5_HYDTA 
Original site:  A0A0R3WNF5_HYDTA

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
   SMART (2)   
All databases (20)   

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ID   A0A0R3WNF5_HYDTA        Unreviewed;       642 AA.
AC   A0A0R3WNF5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=TTAC_LOCUS2280 {ECO:0000313|EMBL:VDM19495.1};
OS   Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX   NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000229301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TTAC_0000229301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM19495.1, ECO:0000313|Proteomes:UP000274429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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, ECO:0000256|RuleBase:RU363038}.
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DR   EMBL; UYWX01000923; VDM19495.1; -; Genomic_DNA.
DR   STRING; 6205.A0A0R3WNF5; -.
DR   WBParaSite; TTAC_0000229301-mRNA-1; TTAC_0000229301-mRNA-1; TTAC_0000229301.
DR   Proteomes; UP000046396; Unplaced.
DR   Proteomes; UP000274429; 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; 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   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; 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   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:UP000274429}.
FT   DOMAIN          61..149
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          518..642
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   COILED          24..58
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   642 AA;  73249 MW;  2BF54D6237D63E0E CRC64;
     MLKQVDDLAS RFEEVINKPR FKQLNQLVEE HSKLTYQKEQ LEKAIDNIQK LLMSHQVSIL
     NALIATFDLA TKKAFPQLTS VSTVVTQSSH PNFGDYQCNN GLSLAKQFST DGTKLSPFSI
     ATKICEHLVK GSMIEKVEIA GPGFINIFIS RCFVEAEVTK LVRLGFSLPP PQRSLKCIVD
     MSSPNIAKEM HVGHLRSTII GESISRLLKF MGHNVLKLNH LGDWGTQFGM LIAHLKDTFK
     DLGDRPLPVT DLQKFYQEAK IRFDDDEDFK KRSYDAVVKL QAFDPEHIKN WEKICDVSKQ
     EFYDIYRRLD IEDLIPRGES FYQSRMITLV KDLDNSGLLN LDNGRLILWV PTSNVPLTIV
     KSDGGFTYDT SDLTAVRQRV IEEGGERIIY VVDSGQSLHL QNIYSAAEVC GFVDPARTKL
     EHIPFGVVLG EDKKKFKTRT GDVVKLIDLL NEGVDRAKAK LVEKGRDKEL TPEEQQTAAE
     SIAYGCIKYA DLSHNRINDY VFSFDKMLDD KGNTAAYLLY AYTRIQSIIR KTNWSEEKLA
     EVCKTFDVSL EHPAEFKLGK ILCRLPEVLY KLEEDLFFHK LCDYLYEVSC VFTEFYDACY
     CIEREGDKIV KIHESRILLC LATAKIMKTC FDLLGIRTVE KM
//

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