ID A0A0V0VA60_9BILA Unreviewed; 619 AA.
AC A0A0V0VA60;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE Flags: Fragment;
GN ORFNames=T09_13845 {ECO:0000313|EMBL:KRX60141.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX60141.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX60141.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX60141.1};
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 -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000256|ARBA:ARBA00009451, ECO:0000256|RuleBase:RU004005}.
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:KRX60141.1}.
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DR EMBL; JYDN01000063; KRX60140.1; -; Genomic_DNA.
DR EMBL; JYDN01000063; KRX60141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VA60; -.
DR STRING; 181606.A0A0V0VA60; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; 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:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.470.10; Ribosomal protein L22/L17; 1.
DR InterPro; IPR001278; Arg-tRNA-ligase.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR008909; DALR_anticod-bd.
DR InterPro; IPR001063; Ribosomal_uL22.
DR InterPro; IPR036394; Ribosomal_uL22_sf.
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; PF05746; DALR_1; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR Pfam; PF00750; tRNA-synt_1d; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM00836; DALR_1; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF54843; Ribosomal protein L22; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KRX60141.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU004005};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU004005}.
FT DOMAIN 302..421
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX60141.1"
FT NON_TER 619
FT /evidence="ECO:0000313|EMBL:KRX60141.1"
SQ SEQUENCE 619 AA; 70827 MW; 9E7285DDFA691DD9 CRC64;
LLKSAGHDVI SVNYLGDWGT QFGMIASGLR KIGKSSTAFS LADYANAYVA ANHDSLSDNE
ITEFARHFVT ALESGESEET ALWRSICSAS MAELKQTYST LNVHFDIWQR ESQFFQNAKE
LIHTLTKNGL ITVNKEGVRG IVSKGHFIPL CKSDNTTLYL TRDLAATILR FQQYQPDCIY
YVVDSGQHQH FENLKVVLSA AGYPSFAERV KHIKFGRILN TSTRQGKGVK ADELLKQGQL
KAKTVLENAS TTKVLPFEYE SVCQQLVLTA LIVNDFKLRR IIDYKFCWDS VLNVKGATGY
SLQATYARLS SLVDGGQNDP LDADCNDFQS LHESEAKCLA EILAPEFLAQ SLRRCLDEFE
PYPLVHYLFR LCKSANVAHK RLHVANAPAD VARARLLLFK TAQLTLHHCL HILGIQPLNK
VHFFLNIQQP PIRLKHEFVA PEWDLTRKTN GISIDEWQYY DNVIWPPHCE SKVGEVFHHR
ENVRYSAKRM WYVCQMIQGL RIDDALLQLH YTPRKGATIM KEILLEAQEK ASSEHCIEQK
ANLWIAEAFA RNSLIVKGVR RHALERWGIV KYRYSNVFVR LQEGDPPQQV TRFPKKLCGW
KTVEKYMEEI RNRKIMYNP
//
