(data stored in SCRATCH zone)

SWISSPROT: D5E8N5_METMS

ID   D5E8N5_METMS            Unreviewed;       567 AA.
AC   D5E8N5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 57.
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=Mmah_0006 {ECO:0000313|EMBL:ADE35544.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35544.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35544.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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|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|HAMAP-Rule:MF_00123, ECO:0000256|RuleBase:RU363038}.
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DR   EMBL; CP001994; ADE35544.1; -; Genomic_DNA.
DR   RefSeq; WP_013036487.1; NC_014002.1.
DR   EnsemblBacteria; ADE35544; ADE35544; Mmah_0006.
DR   GeneID; 8982137; -.
DR   KEGG; mmh:Mmah_0006; -.
DR   eggNOG; arCOG00487; Archaea.
DR   eggNOG; COG0018; LUCA.
DR   HOGENOM; HOG000247213; -.
DR   KO; K01887; -.
DR   OMA; NKPLHLG; -.
DR   OrthoDB; 7046at2157; -.
DR   BioCyc; MMAH547558:G1GHT-6-MONOMER; -.
DR   Proteomes; UP000001059; 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; D5E8N5.
DR   SWISS-2DPAGE; D5E8N5.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:ADE35544.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00123, ECO:0000256|RuleBase:RU363038,
KW   ECO:0000313|EMBL:ADE35544.1};
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:UP000001059}.
FT   DOMAIN          3..86
FT                   /note="Arg_tRNA_synt_N"
FT                   /evidence="ECO:0000259|SMART:SM01016"
FT   DOMAIN          447..567
FT                   /note="DALR_1"
FT                   /evidence="ECO:0000259|SMART:SM00836"
FT   MOTIF           121..131
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00123"
SQ   SEQUENCE   567 AA;  63324 MW;  EE4A0013B414A87F CRC64;
     MYLEFVNQVV SVLENAVQRA GFEPVEIAPE PSQHADLSTR VAFKLAAVAR KSPVEVANQI
     VENIQLRENC LIESIGTTGP YINIKANRTY IDRTFETVRS KKEDFGGNFY SGKILLEHTS
     ANPNGPLHVG HIRNSIIGDT LTRILRKAGY DVDAQYYVND MGRQIAIVSW ALEHFEMDPD
     LKSDHAIANV YIKANARLEE DSQKVEYIDN LMQRVESGDE EVIKRFDDAV DLAVKGIRST
     LLRMNVHHDS FVNESGFVRS GAVSDIVDKI RKTGRVDVDD GALVVDLSDY GFEKTLVVQR
     RDGTSLYTTR DLAYHEWKTM QADRIIDILG ADHKLISGQL KATLNAVGLK EPEIVIFEFV
     SLPEGSMSTR RGQFITADEL LDKVQARAFE EVEKRRPEMS PEFMEKVAGM VGIGAVRYDI
     IKVSPEKSTV FDWKAALDFE KQGGPFIQYS HARASSILKK AGEEGIWDPA SKPNPSVLTD
     ESEITLIKQI ALFDKVLKQA ADDLKPHIIA IYGRELADAF NQFYRFSPVL GAETEELRNA
     RLGLVDCARI VLANVLETLG MGAPESM
//

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