ID G0QA46_NANSJ Unreviewed; 607 AA.
AC G0QA46;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00020262};
DE EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN ORFNames=J07AB56_01040 {ECO:0000313|EMBL:EGQ40858.1};
OS Nanosalinarum sp. (strain J07AB56).
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC Nanosalinarum.
OX NCBI_TaxID=889962 {ECO:0000313|EMBL:EGQ40858.1, ECO:0000313|Proteomes:UP000009382};
RN [1] {ECO:0000313|EMBL:EGQ40858.1, ECO:0000313|Proteomes:UP000009382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Narasingarao P., Podell S., Ugalde J.A., Brochier-Armanet C., Emerson J.B.,
RA Brocks J.J., Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "De novo metagenomic assembly reveals abundant novel major lineage of
RT Archaea in hypersaline microbial communities.";
RL ISME J. 0:0-0(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; GL982567; EGQ40858.1; -; Genomic_DNA.
DR AlphaFoldDB; G0QA46; -.
DR HOGENOM; CLU_006406_6_1_2; -.
DR Proteomes; UP000009382; 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; 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 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 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:UP000009382}.
FT DOMAIN 6..84
FT /note="Arginyl tRNA synthetase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01016"
FT DOMAIN 495..607
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
SQ SEQUENCE 607 AA; 68048 MW; C6186F9E77937AFE CRC64;
MKSTKDEIAQ EVSDKLGSTV DVHDIETPPV HHAAYAYPVM QEASDRDRDP MRLAKETASG
LDLSNMSHVE SVSTAPPGYL NFELDWSSYG NRLLQQAPIA PEEKDAKVVV EHTSPNPNKP
LHMGTMRCAV LGDSIARLAD YSGFDVEVQN FMNDLGRQIA KVTYGYDHLR SQLSEEELQQ
KDDFWIGLLY SKTGNYIEQN PNGEDKVDHY IQQIEAGDTH EAELKDELVS KALKGQLQTA
YRSNTFYGLL VFERSIVESG MFEEAMEKIR TLDRVYEVEE GEDEGCVVID ISDQNQLGNL
QKPYKVLQRS DGTAVYTAKD IALTMWKFGL LDSEFQCGVF DQQPNGEAVW TTDGDTERQF
GNASEVINVV GTRQSYPMHV IEASLNALGY EEEAESFHHA GFKFVYLPGK VSYSGREGNW
VGKHGDAVLD KCRELALEEV QGRHENLEPD AQEEIAEKVA VAAVRYFLLR FSRDSDIDFS
FEKALDWQGD SGPYLLYTAA RAHGILDKVD AKPEFSSVET DVEKELVRQL GELQTIAESA
YEARDPVKVA QYAKRLAENF NTFYHDCPVK GAGTHEVKSS RIALTKTYTQ VFGQALGMLG
IETTQKM
//
