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Database: UniProt
Entry: A0A1W6K228_9CREN
LinkDB: A0A1W6K228_9CREN
Original site: A0A1W6K228_9CREN 
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
//
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