(data stored in ACNUC7421 zone)

SWISSPROT: C8VVE6_DESAS

ID   C8VVE6_DESAS            Unreviewed;       570 AA.
AC   C8VVE6;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
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   OrderedLocusNames=Dtox_0052 {ECO:0000313|EMBL:ACV61015.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61015.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61015.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-
CC         arginyl-tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658,
CC         Rhea:RHEA-COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78513,
CC         ChEBI:CHEBI:456215; EC=6.1.1.19; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00123};
CC   -!- SUBUNIT: Monomer. {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
CC       family. {ECO:0000256|HAMAP-Rule:MF_00123,
CC       ECO:0000256|RuleBase:RU363038}.
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DR   EMBL; CP001720; ACV61015.1; -; Genomic_DNA.
DR   RefSeq; WP_012813467.1; NC_013216.1.
DR   STRING; 485916.Dtox_0052; -.
DR   EnsemblBacteria; ACV61015; ACV61015; Dtox_0052.
DR   KEGG; dae:Dtox_0052; -.
DR   eggNOG; ENOG4105C75; Bacteria.
DR   eggNOG; COG0018; LUCA.
DR   HOGENOM; HOG000247214; -.
DR   KO; K01887; -.
DR   OMA; HGMSTRQ; -.
DR   OrthoDB; 1146366at2; -.
DR   BioCyc; DACE485916:G1GFV-56-MONOMER; -.
DR   Proteomes; UP000002217; 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; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00123; Arg_tRNA_synth; 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; PTHR11956; 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; SSF47323; 1.
DR   SUPFAM; SSF55190; SSF55190; 1.
DR   TIGRFAMs; TIGR00456; argS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VVE6.
DR   SWISS-2DPAGE; C8VVE6.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:ACV61015.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:ACV61015.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN       10    108       Arg_tRNA_synt_N. {ECO:0000259|SMART:
FT                                SM01016}.
FT   DOMAIN      450    570       DALR_1. {ECO:0000259|SMART:SM00836}.
FT   MOTIF       145    155       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00123}.
SQ   SEQUENCE   570 AA;  64109 MW;  37CF79F3DB69176C CRC64;
     MGGMVNEVRV NLKRILECAF KDINNNGIFH ADKLPEFVVE VPREKGHGDF ASNLAMMLAK
     PARMAPRRIA EIFVEHLNEE IKSDKQDGSF ILLDRVEVAG PGFINFYLNP AWVYETLRII
     ETEGNDYGRV MLGSGKKVQV EFVSANPTGL LHMGNARGAA LGDCLASLLD FAGYQVTREF
     YVNDAGNQIE NFGLTLEARY LQLLGQDCPV PEDGYHGLDI IQTMQGFVDK YGNKFLSAPG
     KVRRMVMINY ALEEKLREIR NTLFDFGVRY DVWFSEKDLH ESGAVNEAVA ILKEKGHIYE
     KEGALWFKAT EFGVEKDEVV VRSNGVPTYF AADIAYHKNK FDRGFDRVIN IWGADHHGHV
     SRVKGAVEAI GYDPESLDII LMQLVRLFRG TEIVRMSKRT GQFVTLDELI EEVGRDVARY
     FFVMRSADSH LDFDLELAKS QSNENPVYYI QYAHARICSI LRQLDEQGGR LPQAGAVDLA
     LLKEEIELDL IRKMADFPEE IASAAESLAP HRLARYVHEL AGLLHSFYNS HRVIVDDAAL
     SEARLVLVMS VKTVIKNALS LLGIAAPEKM
//

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