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Reviewed, UniProtKB/Swiss-Prot Q5PAM4 (SYR_ANAMM)

Last modified November 3, 2009. Version 32. 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
    EC=6.1.1.19
Alternative name(s):
    Arginine--tRNA ligase
      Short name=ArgRS
Gene names
Name: argS
Ordered Locus Names: AM678
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length579 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 – 579579Arginyl-tRNA synthetase HAMAP MF_00123
PRO_0000241976

Regions

Motif136 – 14611"HIGH" region HAMAP MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5PAM4-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 015D7CDA3EE81DD0

FASTA57964,676
        10         20         30         40         50         60 
MVSAGSTINL FGNFRCIVIQ KIGELWGGEV TDSLLHKLIV APPTEDRHGD VYTNAALVVG 

        70         80         90        100        110        120 
KFKRKNPMEI AEHLRQALAE VEGVDSVDVV PPGFVNLKCS NEVWYSAIRD INKAGKDYGA 

       130        140        150        160        170        180 
VNLGQGQKVN VEFVSANPTG PLHIGHARGA VFGDVLSNLL AWVGYDVTRE YYVNDAGGQI 

       190        200        210        220        230        240 
NTLVESVYLR YKEALGEQVT IGEGLYPGEY LKPIAKALVE KHGDKLLASE DRTAVIREFA 

       250        260        270        280        290        300 
LKSILDLIRE DMALLGVKHD VFTYEADLQR SRTVEKCVEF LQQKGMLYYG TLERPRGVEE 

       310        320        330        340        350        360 
EAAWQAREQL LFRSTDFGDD SDRALQKEDG SWTYFAGDIA YHFDKISRGF HDMILGLGFD 

       370        380        390        400        410        420 
HKGYVSRLKA AVHALSDGKA TIDVKLHNMV NFLENGVPVK MSKRRGEFLT ARDVVEEVGK 

       430        440        450        460        470        480 
DVARFIMMTR KNDVVLDFDF AKAKEQSKDS QIFYIQYAHA RACSLMRNAP TLLPIEDVDF 

       490        500        510        520        530        540 
SRVSSAPEIA LIKLLVRWPN IVESSAVNHE PHRIAFYLLE VAEAFHVLWG HGSRSVDMRF 

       550        560        570 
IVEGDIATTS ARIYLVKVVA LVISLGLSIF SIAPMEEMR 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000030 Genomic DNA. Translation: AAV86656.1.
RefSeqYP_153911.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5PAM4.

Genome annotation databases

GeneID3171804.
GenomeReviewsGene locus AM678 in contig CP000030_GR.
KEGGama:AM678.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PAM4.
OMAADHHGYV.

Enzyme and pathway databases

BioCycAMAR234826:AM678-MON.

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:3.40.50.620. 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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYR_ANAMM
AccessionPrimary (citable) accession number: Q5PAM4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: January 4, 2005
Last modified: November 3, 2009
This is version 32 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