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O14133 (ATE1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arginyl-tRNA--protein transferase 1

Short name=Arginyltransferase 1
Short name=R-transferase 1
EC=2.3.2.8
Alternative name(s):
Arginine-tRNA--protein transferase 1
Gene names
ORF Names:SPAC3C7.07c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Does not arginylate cysteine residues By similarity.

Catalytic activity

L-arginyl-tRNA + protein = tRNA + L-arginyl-protein.

Subcellular location

Cytoplasm. Nucleus Ref.2.

Sequence similarities

Belongs to the R-transferase family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processprotein arginylation

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionarginyltransferase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Arginyl-tRNA--protein transferase 1
PRO_0000351080

Sequences

Sequence LengthMass (Da)Tools
O14133 [UniParc].

Last modified May 1, 1999. Version 2.
Checksum: B0944019596EAD52

FASTA36141,727
        10         20         30         40         50         60 
MVLDKLLYTG YNRLIDLGWR RSGHYLYKPN GKTSCCSLYT IRLDSYNFKI AKEQKKAIKK 

        70         80         90        100        110        120 
WVKYVNGKPL KPMKSEISTD YLNNAFQTIE SLGAEKYSVT MEPCTYTDEK FEVFKKYQMQ 

       130        140        150        160        170        180 
VHLEKEEEIT KKGFSRFLCN SPLFNEDKGI KYGSYHQMYR FQGRLVAVGV LDLLPHGVSS 

       190        200        210        220        230        240 
VYLFYDPDMS KFSLGRISAC REIWLALECG YRYYYMGYYI HTCPKMKYKA TYSPSYLLNP 

       250        260        270        280        290        300 
GTNKWIPIEN FTSLWNTGAP KYISFGDENN SDIQTAVDYD SSEDSSQNED DYTLFNRQLP 

       310        320        330        340        350        360 
GILSVNVAES LVSENFANIG NSTFPTRHVL SYFPQVKHWF VEINAAVGEE VAKSYTLVLS 


S 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB16746.1.
PIRT38693.
RefSeqNP_593608.1. NM_001019039.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2542941.
KEGGspo:SPAC3C7.07c.
NMPDRfig|4896.1.peg.3578.

Organism-specific databases

GeneDB_SpombeSPAC3C7.07c.

Phylogenomic databases

eggNOGfuNOG07956.
GeneTreeEFGT00050000003257.
OrthoDBEOG46HKK8.

Gene expression databases

ArrayExpressO14133.

Family and domain databases

InterProIPR016181. Acyl_CoA_acyltransferase.
IPR017137. Arg-tRNA-P_Trfase_1_euk.
IPR007472. Arg-tRNA-P_Trfase_C.
IPR007471. Arg_tRNA_PTrfase_N.
[Graphical view]
KOK00685.
PfamPF04377. ATE_C. 1 hit.
PF04376. ATE_N. 1 hit.
[Graphical view]
PIRSFPIRSF037207. ATE1_euk. 1 hit.
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameATE1_SCHPO
AccessionPrimary (citable) accession number: O14133
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: May 1, 1999
Last modified: December 14, 2011
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families