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Database: UniProt
Entry: A0A195CVZ5_9HYME
LinkDB: A0A195CVZ5_9HYME
Original site: A0A195CVZ5_9HYME 
ID   A0A195CVZ5_9HYME        Unreviewed;       552 AA.
AC   A0A195CVZ5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=ALC62_04189 {ECO:0000313|EMBL:KYN04805.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN04805.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYN04805.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYN04805.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN04805.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) 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; KQ977220; KYN04805.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195CVZ5; -.
DR   STRING; 456900.A0A195CVZ5; -.
DR   Proteomes; UP000078542; Unassembled WGS sequence.
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; cd07956; Anticodon_Ia_Arg; 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; 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; 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:UP000078542}.
FT   DOMAIN          437..552
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KYN04805.1"
SQ   SEQUENCE   552 AA;  63315 MW;  62B8A2E591B9481A CRC64;
     IAESLSNDNN INISNVASYL YLKTCKTERI YSFLLPLKTL QYNISKEAQN IINHEPNSIF
     DNINIKNNAI SFNISRDRCV KEVLEHNCST VSAPTFVNNK KNIIVEFSSP NIAKPFHVGH
     FRSTIIGNYV ANINSFVNNK VKKINYLGDW GTQYGLVHLG INVTDISEDE MRRNPMKALY
     TAYVNANKLA ETDSSILDHA RKIFNDLEIG IGVTHKQWNI FKQYTIEELK RVYSRIGITF
     DEYHLESMYN AKNIEKIVTL MEEMQLLKRD EQNRKVVNLS NEKNVPIIKS DGSTLYIARD
     IAAAIDRFEK NDFDCMYYVV DNTQASHFSN LLEILKRMQM SWAERLKHVK FGRLHGMRTR
     KGNVMFLEDI LDTARDIIKQ KQINSHTTKV HLNSSNSSDI LGISAIIVND LKRKRGRDYT
     FDWNAALDLK GDTGVKLQYT HCRLVSLERN CGAILTSKCE PSLLQEEVVD DLVILIAKFE
     EVVLRSYEEI EPCILTVYLF NLSNAINKAF NSLRVKDELP DVASQRLLLF HTARNVLAQG
     MKLLGLIPLE EM
//
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