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Q7V396 (SYR_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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:PMM0187
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length603 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 – 603603Arginine--tRNA ligase HAMAP-Rule MF_00123
PRO_0000151591

Regions

Motif141 – 15111"HIGH" region HAMAP-Rule MF_00123

Sequences

Sequence LengthMass (Da)Tools
Q7V396 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 0457AA70B1F5A62B

FASTA60369,644
        10         20         30         40         50         60 
MQTIFKELTK SFEETLLESL IKNEKKEEFE KIRKNLINQA SKEEFGDYQC NICLVLSKIY 

        70         80         90        100        110        120 
KSNPREIAIA FIETLKENKK ISNLCENLEI AGPGFINIKL KNKVLIEAIK SNIKCPRAGV 

       130        140        150        160        170        180 
PLSHKNNIYS KKKVIVDFSS PNIAKEMHVG HLRSTIIGDS ISKIFEFRGY IVLRLNHIGD 

       190        200        210        220        230        240 
WGTQFGMLIT QLKDLYSSDL KEIDRIKISD LVEFYKASKK RFDNETEFQK RSREEVVQLQ 

       250        260        270        280        290        300 
SGDKKSIEAW KLLCNQSRKE FDQIYKTLNI KIKERGESFY NPFLKSIIED LNYKKILIED 

       310        320        330        340        350        360 
QGAKCVFLDG MTNKEGNPLP LIIQKKDGGF NYATTDLAAL RYRFTKEPYG DNAARIIYVT 

       370        380        390        400        410        420 
DHGQSNHFAG VFQVAKRANW IPKDCEVNHV PFGLVQGIDG KKLKTREGDT IKLKDLLSES 

       430        440        450        460        470        480 
VKRAKEDLLK RLENESRFEN DDFVLNTSKV IGIGAVKYAD LSQNRITNYQ FSFEKMLSLN 

       490        500        510        520        530        540 
GNTAPYLLYT LVRISGINRK NNMTEEAINL ESISYSHDLE WKLIRKLLKF DEVIISIEKD 

       550        560        570        580        590        600 
LMPNRLCNYL FELCKTFNRF YDQVPILKGE IDTKISRLTL CALTEKTLKL SLELLGIETL 


ERM 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE18646.1.
RefSeqNP_892308.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM0187.

Proteomic databases

PRIDEQ7V396.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE18646; CAE18646; PMM0187.
GeneID1726465.
KEGGpmm:PMM0187.
PATRIC23031020. VBIProMar68066_0194.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0018.
HOGENOMHOG000247212.
KOK01887.
OMADGTAVYM.
OrthoDBEOG6JB13C.
ProtClustDBPRK01611.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-192-MONOMER.

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_PROMP
AccessionPrimary (citable) accession number: Q7V396
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 69 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