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Q5PAM4 (SYR_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginine--tRNA ligase

EC=6.1.1.19
Alternative name(s):
Arginyl-tRNA synthetase
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.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00123

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

arginine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000241976

Regions

Motif136 – 14611"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q5PAM4 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86656.1.
RefSeqYP_153911.1. NC_004842.2.

3D structure databases

ProteinModelPortalQ5PAM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234826.AM678.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV86656; AAV86656; AM678.
GeneID3171804.
KEGGama:AM678.
PATRIC20947351. VBIAnaMar46146_0592.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247214.
KOK01887.
OMALCNVLAK.
OrthoDBEOG6JB13C.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00123. Arg_tRNA_synth.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR11956. PTHR11956. 1 hit.
PfamPF03485. Arg_tRNA_synt_N. 1 hit.
PF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSPR01038. TRNASYNTHARG.
SMARTSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
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: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries