Reviewed, UniProtKB/Swiss-Prot O14133 (ATE1_SCHPO)

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein arginylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe nucleus Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW arginyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 361	361	Arginyl-tRNA--protein transferase 1		PRO_0000351080

Sequences

	Sequence		Length	Mass (Da)
	O14133-1 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: B0944019596EAD52	FASTA	361	41,727
	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

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. , 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: ATCC 38366 / 972.

[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
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB16746.1.
PIR	T38693.
RefSeq	NP_593608.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2542941.
KEGG	spo:SPAC3C7.07c.
NMPDR	fig|4896.1.peg.3578.
Organism-specific databases
GeneDB_Spombe	SPAC3C7.07c.
Gene expression databases
ArrayExpress	O14133.
Family and domain databases
InterPro	IPR017137. Arg-tRNA-P_Trfase_1_euk. IPR007472. Arg-tRNA-P_Trfase_C. IPR007471. Arg_tRNA_PTrfase_N. [Graphical view]
Pfam	PF04377. ATE_C. 1 hit. PF04376. ATE_N. 1 hit. [Graphical view]
PIRSF	PIRSF037207. ATE1_euk. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ATE1_SCHPO

Accession

Primary (citable) accession number: O14133

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)