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Database: UniProt
Entry: A0A087H9C9_ARAAL
LinkDB: A0A087H9C9_ARAAL
Original site: A0A087H9C9_ARAAL 
ID   A0A087H9C9_ARAAL        Unreviewed;       514 AA.
AC   A0A087H9C9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
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};
GN   OrderedLocusNames=AALP_Aa3g153100 {ECO:0000313|EMBL:KFK38731.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK38731.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(2015).
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; CM002871; KFK38731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087H9C9; -.
DR   EnsemblPlants; KFK38731; KFK38731; AALP_AA3G153100.
DR   Gramene; KFK38731; KFK38731; AALP_AA3G153100.
DR   eggNOG; KOG4426; Eukaryota.
DR   OMA; WLPEQNG; -.
DR   OrthoDB; 67085at2759; -.
DR   Proteomes; UP000029120; Chromosome 3.
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   GO; GO:0009791; P:post-embryonic development; IEA:UniProt.
DR   GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
DR   Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
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   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; 2.
DR   PRINTS; PR01038; TRNASYNTHARG.
DR   SMART; SM01016; Arg_tRNA_synt_N; 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:UP000029120}.
FT   DOMAIN          13..101
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
SQ   SEQUENCE   514 AA;  58542 MW;  67020F841757E340 CRC64;
     MAVNEEFTGN LIQKLEELFD VSLKLTVPDE PSVDPMITVG KFGDYQCDNT MKPWSKLKGK
     STTTQFTNSL AIGQAIVTNL PTSEMVESCS VTGPGYINVV LSTKWIAKSI ESMLINGIHT
     WAPTLSVKRA VVDFSSPNIA KKMHVGHLRS TIIGDTIARM LEYSKVEVLR RNHVGDWGTQ
     FGMIIEYLFE EFPDSDSVPR HQLKIFSCFT DNQMQNVKRI QTLRKRHKRL WSVFRVEILF
     TARFGLRFEK PAEKNVPRFI NAFKSSLKKR LQDPSDACKD RWWCFTYDTT DMAALWYRLN
     EEKAEWIIYV TDAGQQEHFA RFFKVARNAG WLPENDKTYP RASNVTFGVV NGEDGKRFRG
     RGKEAVSLTD LLDEAKTRSK AALIERGKVK EWTPKKLDQT AEAVGYGAVK YADLKNNRST
     SYVFNFDKML DDKGDTAVYL LYAYARICSV IEKSGKDMDE LKKIGKLALD HAEERALGLH
     LIRFAETVNV GHIFGGPNPP LMTRPIRSLK PNIY
//
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