(data stored in SCRATCH zone)

SWISSPROT: E6S7M2_INTC7

ID   E6S7M2_INTC7            Unreviewed;       586 AA.
AC   E6S7M2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   16-JAN-2019, entry version 46.
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=Intca_0368 {ECO:0000313|EMBL:ADU46917.1};
OS   Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 /
OS   NBRC 12989 / 7 KIP).
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU46917.1, ECO:0000313|Proteomes:UP000008914};
RN   [1] {ECO:0000313|EMBL:ADU46917.1, ECO:0000313|Proteomes:UP000008914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC   {ECO:0000313|Proteomes:UP000008914};
RX   PubMed=21304734; DOI=10.4056/sigs.1263355;
RA   Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S.,
RA   Cheng J.F., Detter C., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Pukall R., Sikorski J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Intrasporangium calvum type strain (7
RT   KIP).";
RL   Stand. Genomic Sci. 3:294-303(2010).
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; CP002343; ADU46917.1; -; Genomic_DNA.
DR   RefSeq; WP_013491238.1; NC_014830.1.
DR   STRING; 710696.Intca_0368; -.
DR   EnsemblBacteria; ADU46917; ADU46917; Intca_0368.
DR   KEGG; ica:Intca_0368; -.
DR   eggNOG; ENOG4105C75; Bacteria.
DR   eggNOG; COG0018; LUCA.
DR   HOGENOM; HOG000247212; -.
DR   KO; K01887; -.
DR   OrthoDB; 1146366at2; -.
DR   Proteomes; UP000008914; 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; E6S7M2.
DR   SWISS-2DPAGE; E6S7M2.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:ADU46917.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008914};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00123,
KW   ECO:0000256|RuleBase:RU363038, ECO:0000313|EMBL:ADU46917.1};
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:UP000008914}.
FT   DOMAIN        6     87       Arg_tRNA_synt_N. {ECO:0000259|SMART:
FT                                SM01016}.
FT   DOMAIN      470    586       DALR_1. {ECO:0000259|SMART:SM00836}.
FT   MOTIF       122    132       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00123}.
SQ   SEQUENCE   586 AA;  63437 MW;  0EDE9214C09E92FE CRC64;
     MVSPLVALTP KVQSAIAAAL GDDFREADPV LRPSQFADVQ VNAALALGKK VGAAPRDVAA
     RIVAALDLDG VAEKVEVSGP GFVNITFSDA WLASLLADVD QDDRLGVPVE EPQNIPIDYS
     APNVAKEMHV GHLRTTIVGD SLARTLEHLG HHVIRQNHIG DWGTPFGMLI EHLLEVGEDS
     PEAELLVTDP NAFYQAARAK FDAAEQADPD GSAGDFDIRA RARVVKLQAG DPETLEHWHR
     LVGMSKVYFN KVYQALGVTL GDENLAGEST YNHLLADVCG ELEAKGLATV SDGALCVFLD
     GYTGREGKPV PLIIRKSDGG YGYPTTDLAT IKYRVGDLGA HRVLYVIGAP QALHLNMVWD
     TARLAGWLPD DVTPVHIQIG NVLGEDRKIL KTRSGSSLRL MALLDEAVAK ARGLIDETRP
     DLSEEERATI ARQVGIGAVK YADLSVAHNS EYVFDLDRMV SLTGNTGPYL QYVVARVRSI
     FRQAGLDPLT QHAPITLGTP HERALGQQLL GFGDVVTEVG AEYEPHRLCG YLFELAQAFS
     AFYENCPVLK AETPELRESR LTLSALVLRT MVTGLDLLGL ESPEQM
//

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