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Reviewed, UniProtKB/Swiss-Prot Q81R81 (SYR2_BACAN)

Last modified November 3, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Arginyl-tRNA synthetase 2
    EC=6.1.1.19
Alternative name(s):
    Arginine--tRNA ligase 2
      Short name=ArgRS 2
Gene names
Name: argS2
Ordered Locus Names: BA_2175, GBAA_2175, BAS2021
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). HAMAP MF_00123

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm. HAMAP MF_00123

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 562562Arginyl-tRNA synthetase 2 HAMAP MF_00123
PRO_0000151526

Regions

Motif122 – 13211"HIGH" region HAMAP MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q81R81-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 691B4C80AA99F3BA

FASTA56264,470
        10         20         30         40         50         60 
MDYKTQFAES LSNIFTNELT QQQILDLIET PKQDEFGDAA FPCFSLAKQY KKSPAIIAKE 

        70         80         90        100        110        120 
VAEKLSDPFF TKVEAVGPYV NVFFNRDTVS DAVLKTILAE KEEYGKNYFG CEKTVVIDYS 

       130        140        150        160        170        180 
SPNIAKPFSM GHLRSTMIGN SLKHIAEKCG YEVVGINYIG DWGTQFGKLI TAYKKWGNEA 

       190        200        210        220        230        240 
VVKEDPIREL FKLYVQFHEE VKDDEELEEE GRAWFKKLEE GDEEAVELWN WFRHESLKEF 

       250        260        270        280        290        300 
SRIYELLGVE FTNFQGEAFY NNLMEDFIGI LEEHDLLEES EGALVVNLEE EGMPPCLIRK 

       310        320        330        340        350        360 
SDGATIYATR DLTAALYRQN TFGFDKALYV VGPEQSLHFN QFFTVLKKLG YTWVDGMEHV 

       370        380        390        400        410        420 
PFGFILKDGK KMSTRKGRVI LLEEVLEEAI ELAKQNIEEK NPNLKQKEEV AKQVGAGAVI 

       430        440        450        460        470        480 
FHDLKNERMH NIEFSLENML KFEGETGPYV QYTHARACSI LRKESVEFET CTFALKDDHS 

       490        500        510        520        530        540 
WSVVKLLNKF PQVIEIAFNK NEPSVISKYV LDVAQSFNKY YGNVRILEES EEKDSRLALV 

       550        560 
YAVTVVLKEG LRLLGVEAPE EM 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

AE016879 Genomic DNA. Translation: AAP26054.1.
AE017334 Genomic DNA. Translation: AAT31293.1.
AE017225 Genomic DNA. Translation: AAT54335.1.
RefSeqNP_844568.1.
YP_018818.1.
YP_028284.1.

3D structure databases

HSSPHSSP built from PDB template 1IQ0 based on UniProtKB Q93RP5.
ModBaseSearch...

Genome annotation databases

GeneID1085743.
2815868.
2848358.
GenomeReviewsGene locus BA_2175 in contig AE016879_GR.
Gene locus BAS2021 in contig AE017225_GR.
Gene locus GBAA_2175 in contig AE017334_GR.
KEGGban:BA2175.
bar:GBAA2175.
bat:BAS2021.
TIGRBA_2175.
GBAA_2175.

Phylogenomic databases

HOGENOMQ81R81.
OMAGKLITAY.

Enzyme and pathway databases

BioCycBANT260799:BAS2021-MON.
BANT261594:GBAA2175-MON.
BRENDA6.1.1.19. 267517.

Family and domain databases

HAMAPMF_00123.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-synth_Ic.
IPR015945. Arg-tRNA-synth_Ic_core.
IPR005148. Arg-tRNA-synth_Ic_N.
IPR008909. DALR_anticod_bd.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.30.1360.70. Arg-tRNA-synth_Ic_N. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11956. Arg_tRNA-synt_1c. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
TIGRFAMsTIGR00456. argS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR2_BACAN
AccessionPrimary (citable) accession number: Q81R81
Secondary accession number(s): Q6HZF4, Q6KTE3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents