ID G8BTR1_TETPH Unreviewed; 679 AA.
AC G8BTR1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 Name=TPHA0E01970 {ECO:0000313|EMBL:CCE63289.1};
GN OrderedLocusNames=TPHA_0E01970 {ECO:0000313|EMBL:CCE63289.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE63289.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE63289.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE612860; CCE63289.1; -; Genomic_DNA.
DR RefSeq; XP_003685723.1; XM_003685675.1.
DR AlphaFoldDB; G8BTR1; -.
DR STRING; 1071381.G8BTR1; -.
DR GeneID; 11531290; -.
DR KEGG; tpf:TPHA_0E01970; -.
DR eggNOG; KOG1195; Eukaryota.
DR HOGENOM; CLU_006406_6_2_1; -.
DR OMA; YEFKWER; -.
DR OrthoDB; 67085at2759; -.
DR Proteomes; UP000005666; Chromosome 5.
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; cd07956; Anticodon_Ia_Arg; 1.
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 HAMAP; MF_00123; Arg_tRNA_synth; 1.
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 NCBIfam; TIGR00456; argS; 1.
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; 1.
DR PRINTS; PR01038; TRNASYNTHARG.
DR SMART; SM01016; Arg_tRNA_synt_N; 1.
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:UP000005666}.
FT DOMAIN 105..186
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 561..679
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 679 AA; 77991 MW; 3D4B6F277C2EB488 CRC64;
MIKSCSSTLL HNINSFTSVC KNKRLSNFLA NRFNYNFDLN YLHIDKNPTS IRFYSNKKLH
KPEIKREASE KYKMSTEHIS QQLTKLSLAL PAVVEGSNPD VNVVDLMRNY ISQELSKISG
VDTKLIFEAL EWTNTPERGD LLIPVPRLRI KGSNPKDLAT EWAEKFPVGD YIDKVEANGP
FLQFFFKPSA LFNIVIPDIL ERGDDYGSYK MEQKKTVVFD FSSPNIAKPF HAGHLRSTII
GGFISNLYEK LGWNVVRLNY LGDWGKQFGL LAVGFEKYGN EESLSKDPIH HLFDVYVKVN
KDIEKEGDSL PEEESSNGRA AEFFKRMEDG DEEALKIWKR FRELSIEKYI ETYARLNIQY
DVYSGESQVS KERLDEAIKI LNDKNLTHED RGALLVDLTK FNKKLGKTIV KKSNGATLYM
TRDIGAAMDR YEKYHFDKMI YVVAVQQDLH LAQLFEILKQ MGFGWSDRLS HINFGMVQGM
STRKGTVVFL DNILEETKEK MHEVMKKNEV KYAQIQNPEE VADLIGISAV MIQDMQSKRI
NNYEFKWERM LSFEGDTGPY LQYAHSRLRS VERNASEITP EKWANADLSL LTEPAAVLLI
RLLAQYPDVL RNALKTHEPA TIVTYLFKLT HQVSSCYDVL WVAGQTEELA TARLALYASA
RQTLYNGMRL LGLTPVERM
//
