ID   A0A2U1PSC8_ARTAN        Unreviewed;       852 AA.
AC   A0A2U1PSC8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN   ORFNames=CTI12_AA118600 {ECO:0000313|EMBL:PWA88622.1};
OS   Artemisia annua (Sweet wormwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA88622.1, ECO:0000313|Proteomes:UP000245207};
RN   [1] {ECO:0000313|EMBL:PWA88622.1, ECO:0000313|Proteomes:UP000245207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PWA88622.1};
RX   PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA   Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA   Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA   Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT   "The genome of Artemisia annua provides insight into the evolution of
RT   Asteraceae family and artemisinin biosynthesis.";
RL   Mol. Plant 11:776-788(2018).
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}.
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:PWA88622.1}.
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DR   EMBL; PKPP01000795; PWA88622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1PSC8; -.
DR   Proteomes; UP000245207; 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   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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; IPR046533; DUF6598.
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; PF20241; DUF6598; 1.
DR   Pfam; PF00750; tRNA-synt_1d; 2.
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.
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:UP000245207}.
FT   DOMAIN          739..852
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   852 AA;  96298 MW;  EFE0960B29ED67FB CRC64;
     MDTKTELFGE ALRFELCNVY LIYDHIVEHH KLFGTIRVAA GETASGFSPD PLLQQNGFSD
     IFNREFNNPV DVTCVGYQYL YDVRYCSLPV SSTSTVEIAA KLYVTTDEVD DVDKYPEEDH
     QREVQNNHYE VVDDVDEEDF NRMCDLFSFC DDNDNDNKTS KHRQTSWHVK YLDNHEAFQV
     CDSHEFINFL DKPNGGWGRR SIIKGIDVDA DLEVEFESPS EKSKVTGRVL AYYGKNFDYS
     SPPNDFDVVL SKTSTPDFVE PGKINLMRSV LAVPAQFSLI LEAELYDYTS RVEILSGTYE
     FPVPRDGRSS VGRIKGKDCS LKVTVKWKLP FEKEKVPSSP PAPFSSNSSV GRLAPSILSE
     RRKSGASSMA DSDDDNRWSL QEEIEKVFNS SLERTFKDLK GAGGSCSIST CTKDVDNGDY
     LCSSVLHIWP QLRDTKYKGP KHAGLAVKDD IVGSEYKDMM ERCVVCGPGF VKFKLSRKWI
     AKSIQKMLTH GIDTWAPKLP LKKAIIYFLS RNITEEMHMG HLRSTFIREA LARMLEYSGV
     VVLQRGIRDG DHLEIKGKSS DDPIKKTLDL LRETHLATFS DGDEAVFFEG RKLPLVYLTA
     LWHALHTEKA DGILYVTDVG QRDYIGTCIS AAKHAGWLTE DHSESLLSHV GFGLVQFDDF
     KRFQTLTTQV DNLLDEAKSR CKALLAGQDE WTAEDLDHAA EALGYGVVKY ADLKNNRLAN
     YTFDIDQALN KEGNTAVYIQ FTHARICSII RDSSKDIKKL KAEEFVLKND DERELGLHLL
     RFTEVLREVC TILAPHILCE YLYILCVKFN NLNVCEVGGS SDETSRLFLC EAAEMVVRKC
     FDLLGIAPIS KI
//