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Database: UniProt
Entry: A0A091QV87_MERNU
LinkDB: A0A091QV87_MERNU
Original site: A0A091QV87_MERNU 
ID   A0A091QV87_MERNU        Unreviewed;       573 AA.
AC   A0A091QV87;
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 {ECO:0000256|ARBA:ARBA00012837};
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=N331_03194 {ECO:0000313|EMBL:KFQ31153.1};
OS   Merops nubicus (Northern carmine bee-eater).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX   NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ31153.1, ECO:0000313|Proteomes:UP000052967};
RN   [1] {ECO:0000313|EMBL:KFQ31153.1, ECO:0000313|Proteomes:UP000052967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ31153.1};
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; KK707255; KFQ31153.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091QV87; -.
DR   Proteomes; UP000052967; 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; 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; PF05746; DALR_1; 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; 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   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:UP000052967}.
FT   DOMAIN          458..573
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ31153.1"
FT   NON_TER         573
FT                   /evidence="ECO:0000313|EMBL:KFQ31153.1"
SQ   SEQUENCE   573 AA;  64487 MW;  80FB4C71A3BE99F4 CRC64;
     QLSKVLDLPP ENLIKSISAV PVSKKRCVAD FQLSVASLTE DSSSNCLAQD LNLQAQKLAE
     RLKCDGVVSE ISAGPGTVNF TINRELLAKA VLQQVLKDGS EYGVKSELFS AVPRQKAVIE
     FSSPNIAKKF HVGHLRSTII GNFIANLKKA LGHEVVRINY LGDWGMQFGL LGVGFQSFGD
     KEKLKSSPLQ HLFEVYVQIN KAAEDENTKK MAKDFFRKLE EHDEQTLSLW KQFRDFSIEE
     YVRIYKRLGV HFDEYSGESF YQEKSQEVLK ILEDKGLLQK TTKGTGIVDL SEKKDFSSFS
     TVMRSDGTSL YITRQVSPSV DLAAAIDRMN KHSCDTMIYV TDKSQSTHFQ HLFQILKLMG
     YNWAERCQHV SFGLVQGMKT RRGEVIFLED VLNEVRSRVL QNMASAKTTK EMEDPMETAE
     KVGLAALIIQ DFRGLLSSDY QFSWDRALQS RGDTGMFLQY THARLHSLEQ MHGNELLPDV
     NVACLQEPDA ISVLQHLLRY DEVLYRSSQD LQPKHIVSYL LTLSHLAAVA HKSLPVKGSA
     PELAQARLRL FQAARSVLAS GMRLLGITPV TRM
//
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