GenomeNet

Database: UniProt
Entry: A0A1G1CLC3_9BACT
LinkDB: A0A1G1CLC3_9BACT
Original site: A0A1G1CLC3_9BACT 
ID   A0A1G1CLC3_9BACT        Unreviewed;       608 AA.
AC   A0A1G1CLC3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN   ORFNames=A2W24_02080 {ECO:0000313|EMBL:OGV95821.1};
OS   Microgenomates group bacterium RBG_16_45_19.
OC   Bacteria.
OX   NCBI_TaxID=1817747 {ECO:0000313|EMBL:OGV95821.1, ECO:0000313|Proteomes:UP000178440};
RN   [1] {ECO:0000313|EMBL:OGV95821.1, ECO:0000313|Proteomes:UP000178440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGV95821.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MHDC01000040; OGV95821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1CLC3; -.
DR   STRING; 1817747.A2W24_02080; -.
DR   Proteomes; UP000178440; 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; 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; 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.
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}.
FT   DOMAIN          7..97
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          498..608
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   608 AA;  68101 MW;  94E37474D6AB7277 CRC64;
     MATSVKTELL ETIKLALTQL KLKPVEFSLE HPANEAHGDY AANIAFVLYP QVEDQWSNPL
     QLAEAIVAAI KLKVSHQSSS IIDSVSVAGP GFINFSLKPE HFLDYLNQLI NSKQIPLTTD
     PFIKQRICVE YTDPNPFKEL HLGHLYSNII GETMARLYEA VGAKVWRADY YGDVGQHVAK
     AIWGMQQLLT QTHTTLPNLA KKSLLERQKF LGQSYAYGVK QFESDPEVKA TINRLNPLIY
     AIAQALHQAN GWQPVVEYEV HVPQSDFNRG EIRSLYQSGL AWSLEYFESL YQFLGTKFDG
     YYPESLMGEY GYRLVQHGLK QGVFTKSQGA IIFPGEKHGT HTRVFINKLN LPTYEAKELG
     LAPAKYQDFP YDQSLIVTGT EIKDYFKVVL TAMKLVSPDL GHITTVLSHG MVKLPQGKMS
     SRSGNVVTVQ GLIAEASAYA RTLFSAETHL PAKAMDQIAQ AVGLASIRYA FLKGDVTTDV
     IFDFKQSISF EGNSGPYLQY TYARCASVLS KSPLKIKNFK LKMGALNPEE LALLRWFYRY
     PEVVAAAAQN LTPHLLCTYL YELAHRFNLF YHHHLIIGSD FRLGLTTATA KILKSGLELL
     GIEAPEKM
//
DBGET integrated database retrieval system