ID D7LQ31_ARALL Unreviewed; 388 AA.
AC D7LQ31;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Arginyl tRNA synthetase N-terminal domain-containing protein {ECO:0000259|SMART:SM01016};
GN ORFNames=ARALYDRAFT_904472 {ECO:0000313|EMBL:EFH51384.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
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; GL348717; EFH51384.1; -; Genomic_DNA.
DR RefSeq; XP_002875125.1; XM_002875079.1.
DR AlphaFoldDB; D7LQ31; -.
DR STRING; 81972.D7LQ31; -.
DR EnsemblPlants; scaffold_500176.1; scaffold_500176.1; scaffold_500176.1.
DR Gramene; scaffold_500176.1; scaffold_500176.1; scaffold_500176.1.
DR eggNOG; KOG4426; Eukaryota.
DR HOGENOM; CLU_712401_0_0_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
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; IPR005148; Arg-tRNA-synth_N.
DR InterPro; IPR036695; Arg-tRNA-synth_N_sf.
DR InterPro; IPR035684; ArgRS_core.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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; PF00750; tRNA-synt_1d; 2.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 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:UP000008694}.
FT DOMAIN 37..126
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
SQ SEQUENCE 388 AA; 44291 MW; 51D46621B0087DDA CRC64;
MDRYSREDDV TNALAVDLSS EIEAEKKNEE FTGNLKRQLA KLLVVCLKLT VPDEPSFEPL
VAASAAGKFG DYQCNNAMGL WSIIKGKGTQ FKGPPAVGLA LVKSLPTSEM VESCSVARPG
YINVVLSAKW MAKLIFPLPT LQNKYMLVIL RSTIIGDMLA RMLEYSKVEV LRRNHVDDWG
TKFGMLIEYL FEKFPDTDSV IETDVVFDRC FTRHQKKKFD LDEDFKERAQ QAVVRLQAQG
GDPVYRKAWA KICEISRTEF AKVYQRLRVE LEERYWLDEE KAQWMIYNTA AGQEQHLSTF
FKKEGWLPGN EKTYPRVNHV GFGLVLGEDG KRFRTRATDV VRLVDLVDEA KTRSKLALIE
RGKDKEWTPE ELDQTTEAVG YGAVNEFS
//
