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Database: UniProt
Entry: A0A091VCA2_OPIHO
LinkDB: A0A091VCA2_OPIHO
Original site: A0A091VCA2_OPIHO 
ID   A0A091VCA2_OPIHO        Unreviewed;       613 AA.
AC   A0A091VCA2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Arginine--tRNA ligase, cytoplasmic {ECO:0000256|ARBA:ARBA00022171};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
DE   AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00033033};
DE   Flags: Fragment;
GN   ORFNames=N306_11049 {ECO:0000313|EMBL:KFR00048.1};
OS   Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC   Opisthocomus.
OX   NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR00048.1, ECO:0000313|Proteomes:UP000053605};
RN   [1] {ECO:0000313|EMBL:KFR00048.1, ECO:0000313|Proteomes:UP000053605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR00048.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KK733821; KFR00048.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091VCA2; -.
DR   STRING; 30419.A0A091VCA2; -.
DR   PhylomeDB; A0A091VCA2; -.
DR   Proteomes; UP000053605; 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   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:UP000053605}.
FT   DOMAIN          64..153
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          521..611
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   COILED          450..484
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFR00048.1"
FT   NON_TER         613
FT                   /evidence="ECO:0000313|EMBL:KFR00048.1"
SQ   SEQUENCE   613 AA;  69992 MW;  518C30C909B20EF8 CRC64;
     QENEIKLLTA EIERLKNFGC LGVSPSLEGL RDENAKLKYR LNFLRKSLQE ERSKTAKSMI
     NINSCLQEIF GAAIQAAYPD LENPPLVVTP SQQPKFGDYQ CNSAMGITQI LLKTKEQKVS
     PREIAEKISK NIPANECIEK VEIAGPGFIN VHLRKDFVSK QLSSLLMNGV QPPAVGKRKK
     VVVDFSSPNI AKEMHVGHLR STIIGESMCR LFEFAGYDVL RLNHLGDWGT QFGMLIAHLQ
     DKFPDYLTVS PPIGDLQAFY KESKRRFDTE EEFKKRAYQC VVLLQSKNPD FIKAWELICD
     VSRKEFQKIY SCLDITLIER GESFYQEMMK DVVKEFEDKG FVQVDDGRKI VFVPGFPVPL
     TIMKSDGGYT YDTSDLAALR HRLYEEKADI LIYVVDSGQS VHLQTVFAAG QMIGWYDPKV
     TRVAHAAFGV VLGEDKKKFK TRSGDTVRLI DLLEEGLKRA MDKLKDKERD KVLTEEELKA
     AQTSVAFGCI KYADLSHNRL NDYVFSFDKM LDDRGNTAAY LLYAFTRIRA IARLANVDEQ
     MLRKAAGEEV LILDHEKEWK LGKCILRFPE ILQKILEDLL LHTLCDYLYE LATTFTEFYD
     NCYCVEKDRQ SGE
//
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