ID A0A1W6K228_9CREN Unreviewed; 619 AA.
AC A0A1W6K228;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123};
DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123};
DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123};
DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123};
GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123};
GN ORFNames=B6F84_11345 {ECO:0000313|EMBL:ARM76555.1};
OS Acidianus manzaensis.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=282676 {ECO:0000313|EMBL:ARM76555.1, ECO:0000313|Proteomes:UP000193404};
RN [1] {ECO:0000313|EMBL:ARM76555.1, ECO:0000313|Proteomes:UP000193404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN-25 {ECO:0000313|EMBL:ARM76555.1,
RC ECO:0000313|Proteomes:UP000193404};
RA Ma Y., Yang Y., Xia J.;
RT "Sulfur activation and transportation mechanism of thermophilic Archaea
RT Acidianus manzaensis YN-25.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|HAMAP-Rule:MF_00123};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123,
CC ECO:0000256|RuleBase:RU363038}.
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DR EMBL; CP020477; ARM76555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6K228; -.
DR STRING; 282676.B6F84_11345; -.
DR KEGG; aman:B6F84_11345; -.
DR OrthoDB; 372102at2157; -.
DR Proteomes; UP000193404; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF05746; DALR_1; 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|HAMAP-Rule:MF_00123};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00123}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00123};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00123}.
FT DOMAIN 503..619
FT /note="DALR anticodon binding"
FT /evidence="ECO:0000259|SMART:SM00836"
FT MOTIF 111..121
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ SEQUENCE 619 AA; 71206 MW; 35B5B24CCFF1D098 CRC64;
MYALAKAKEE MAEYLSKIIE VDKEKILNSI EYPKSEIADL SLPLPSVSKK RDIEVKYSGY
LIKEMTKDKI FINVRLNELN LMKEIFSNFN ENYGIIKVEK PLRIVVEHTS ANPIHPLHVG
HLRNAIIGDT LVRLLKARGH EVNSRFYVND GGRQVALLIY GLSKLDYPEP PEGQKKDEWL
GQIYAITNVI IEIRKITEEL KSASEQEYKE KISKRDELIA VASELESRNQ DYFNRILNGV
NSDKDPEAEI SKIIQLYESG DSKTKQIVRK YVNYALEGFK ESLENLHISY DNFDYESDLL
WNGDVGKILD LALESVARIS YKGTVALDLQ KFLDDKVREE LKIPKGFEIP PLVLMRSDGT
SLYTIRDIAY TLYKFSQFNA DEVINVIAEQ QSVSQMQLRA SLYLLGYPEI AKRLIHYSYG
MVTVQGLRMS GRLGRYISFD NIYDKVSEVV KTKIQEKKGV LENIKEIANA AIRYAIISVS
SNKPVSFNIA RVANFEENSG PYLQYSYARA YNILNKSTDK LDIQKIDESD LKNEKRQLLI
MIAKFPEVFM SSADYLQPEN LTMFLRFLAD TFNSWYDKER VIQEPDEKKR ITRLYIVKGV
ETVLRNGLNA LGINSLTRM
//