UniProt: A0A249SVU7

Database: UniProt
Entry: A0A249SVU7_9BACT

LinkDB:  A0A249SVU7_9BACT 
Original site:  A0A249SVU7_9BACT

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (1)   
   SMART (2)   
All databases (19)   

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ID   A0A249SVU7_9BACT        Unreviewed;       641 AA.
AC   A0A249SVU7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=arginine--tRNA ligase {ECO:0000256|ARBA:ARBA00012837};
DE            EC=6.1.1.19 {ECO:0000256|ARBA:ARBA00012837};
GN   ORFNames=CK934_12750 {ECO:0000313|EMBL:ASZ11766.1};
OS   Chitinophaga sp. MD30.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=2033437 {ECO:0000313|EMBL:ASZ11766.1, ECO:0000313|Proteomes:UP000217148};
RN   [1] {ECO:0000313|EMBL:ASZ11766.1, ECO:0000313|Proteomes:UP000217148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD30 {ECO:0000313|EMBL:ASZ11766.1,
RC   ECO:0000313|Proteomes:UP000217148};
RA   Wan X., Darris M., Hou S., Donachie S.P.;
RT   "Draft genome sequence of a novel Chitinophaga sp., MD30, isolated from a
RT   biofilm in an air conditioner condensate pipe.";
RL   Submitted (AUG-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   -!- 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; CP023254; ASZ11766.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A249SVU7; -.
DR   OrthoDB; 9805987at2; -.
DR   Proteomes; UP000217148; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   NCBIfam; TIGR00456; argS; 1.
DR   PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 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; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000217148}.
FT   DOMAIN          5..89
FT                   /note="Arginyl tRNA synthetase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          517..641
FT                   /note="DALR anticodon binding"
FT                   /evidence="ECO:0000259|SMART:SM00836"
SQ   SEQUENCE   641 AA;  72969 MW;  5C888C6080D3EDDE CRC64;
     MSVVQTIRTA AVQAIKALYQ QEMSIQDIAI NSTKPEFEGE YTIVVFAFTR FSRQKPEETG
     QQLGQYLVTH FSELIAGFNV VKGFLNLRIN DAFWNNFLRK EFTNPQPGIK APNGKKIMVE
     FSSPNTNKPL HLGHLRNNFL GFSISEILKA NGNEVIKTNL VNDRGIHICK SMLAWQLYAH
     GDTPASTGIK GDHLVGDYYV KFESILKEQA EPIIANVLEN NFQDFDGAEL ERIEKLATAL
     HKPEVQQDED KEAKIMDEIK ELARNKTEIM QQARIMLEQW EAGNPEVRAL WATMNSWVYQ
     GFDETYRKLG VSFDKMYYES DTYLLGKELV EKGLRKEVLF RKNDNSVWID LTADGLDEKL
     LLRGNGTSVY MTQDLGTFRI KYDDYHMDQS IVVVADEQNY HFKVLKLILE KLQEPCADGI
     FHLSYGMVEL PHGRMKSREG TVVDADDMVT EMVTTAAEHT KDSNKLKDFP EEELQQLYNM
     IGLGAMKFFL LRVDPKKKMI FNPEESIDLH GFTGPFIQYA HARIKSILRE AGPQQGIDNF
     VASSPLLPLE KELIILNEQF GTILEDAQKE MSPAVVANYA FQLAQKFNSF YAEKVEGKYT
     YSVLGAESEE KKILRIQLIT LTASTIAQAM QLLGIAVPER M
//

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