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Reviewed, UniProtKB/Swiss-Prot O96539 (ATE1_DROME)

Last modified November 3, 2009. Version 68. 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 · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
Name: Ate1
ORF Names: CG9204
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Sequence similarities

Belongs to the R-transferase family.

Sequence caution

The sequence AAO25000.1 differs from that shown. Reason: Frameshift at position 106.

The sequence AAO25000.1 differs from that shown. Reason: Miscellaneous discrepancy. Deletion of many residues.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein arginylation

Inferred from electronic annotation. Source: InterPro

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

arginyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: O96539-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform A (identifier: O96539-2)

The sequence of this isoform differs from the canonical sequence as follows:
     175-181: Missing.
Isoform C (identifier: O96539-4)

The sequence of this isoform differs from the canonical sequence as follows:
     175-181: Missing.
     239-288: LRLIHVYDDE...KEHLQATPLQ → IVLVASSDTE...QRFLVKSPLK
Isoform D (identifier: O96539-5)

The sequence of this isoform differs from the canonical sequence as follows:
     239-288: LRLIHVYDDE...KEHLQATPLQ → IVLVASSDTE...QRFLVKSPLK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Arginyl-tRNA--protein transferase 1
PRO_0000195090

Natural variations

Alternative sequence175 – 1817Missing in isoform A and isoform C.
VSP_000339
Alternative sequence239 – 28850LRLIH…ATPLQ → IVLVASSDTERTCADAVIAL YRKYQITVHNDNPARLTLAS MQRFLVKSPLK in isoform C and isoform D.
VSP_011157

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified August 16, 2004. Version 3.
Checksum: 38677BF50672AC6D

FASTA48455,317
        10         20         30         40         50         60 
MSLSIVSYYG SQQSKCGYCA GANCSLSHGM HAYQLDCRDY QDLIDRGWRR CGYYCYKLRN 

        70         80         90        100        110        120 
QETCCPCYTI KCNGLEFKLS KSNKRILRRI NRFLRDGKRE SKPEAGDGDG EADADYAIVA 

       130        140        150        160        170        180 
PEVTASEPQP QLPDKSPPVI NVEQVASLAT AQRKPTKQAT AAAVEAPTLG SNKSSLLSSS 

       190        200        210        220        230        240 
AAAPISNKPC KKAKQMRLDR RLAKLGDSAS YSTKSLTQEK TLRDFLNTDS ETNKHRLKLR 

       250        260        270        280        290        300 
LIHVYDDEFR RTLPQSFALY KKYQISIHND PPKDQDAYKE HLQATPLQNE KPWDGPEMGY 

       310        320        330        340        350        360 
GSFHQQYWLD DKLIAVGVID ILPGCVSSVY FFYDPDYSFL SLGTYGSLRE IELVQSLAEK 

       370        380        390        400        410        420 
VPSLKYYYMG FYIHSCPKMR YKGKLSPSYL LCPETYEWLP LTDVIRAKLD EHKYQRLNED 

       430        440        450        460        470        480 
PAARDVNEFL MEHLDEVKLL LGGRTRTDYK HFRQLRGTVS DDDIIIEYSK LVGKECARRM 


LYVK 

« Hide

Isoform A.

Checksum: B32B8200D1CC4CE8
Show »

FASTA47754,671
Isoform C.

Checksum: 0ED47DA90616B696
Show »

FASTA47854,348
Isoform D.

Checksum: D12F3150F3C10876
Show »

FASTA48554,994

References

« Hide 'large scale' references
[1]"Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway."
Kwon Y.T., Kashina A.S., Varshavsky A.
Mol. Cell. Biol. 19:182-193(1999) [PubMed: 9858543] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
Strain: Berkeley.
Tissue: Embryo.
[5]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
Strain: Berkeley.
Tissue: Embryo.
[6]"Independent emergence of alternative splicing of arginyl-tRNA-protein transferase in Drosophila melanogaster and mammals."
Picaud F., Petit D., Maftah A.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-484 (ISOFORM C).
+Additional computationally mapped references.

Cross-references

Sequence databases

AF079101 mRNA. Translation: AAD12369.1.
AE013599 Genomic DNA. Translation: AAF57496.3.
AE013599 Genomic DNA. Translation: AAF57497.3.
AE013599 Genomic DNA. Translation: AAF57498.2.
AY051688 mRNA. Translation: AAK93112.1.
BT001498 mRNA. Translation: AAN71253.1.
BT003243 mRNA. Translation: AAO25000.1. Sequence problems.
AF354710 mRNA. Translation: AAL83965.1.
RefSeqNP_477394.3.
NP_725939.2.
NP_725940.2.
UniGeneDm.4513

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblFBtr0086318; FBpp0085627; FBgn0025720; Drosophila melanogaster. [Genome view]
GeneID37288.
KEGGdme:Dmel_CG9204.
UCSCCG9204-RA. d. melanogaster.

Organism-specific databases

CTD37288.
FlyBaseFBgn0025720. Ate1.

Phylogenomic databases

OMATERTCAD.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-005615-MON.
BRENDA2.3.2.8. 48.

Gene expression databases

GermOnlineCG9204. Drosophila melanogaster.

Family and domain databases

InterProIPR017137. Arg-tRNA-P_Trfase_1_euk.
IPR007472. Arg-tRNA-P_Trfase_C.
IPR007471. Arg_tRNA_PTrfase_N.
[Graphical view]
PfamPF04377. ATE_C. 1 hit.
PF04376. ATE_N. 1 hit.
[Graphical view]
PIRSFPIRSF037207. ATE1_euk. 1 hit.
ProtoNetSearch...

Other Resources

NextBio802931.

Entry information

Entry nameATE1_DROME
AccessionPrimary (citable) accession number: O96539
Secondary accession number(s): Q7KRL0 expand/collapse secondary AC list , Q86PB1, Q8IH08, Q8N0R9, Q8T7L5, Q9V906, Q9V907
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 16, 2004
Last modified: November 3, 2009
This is version 68 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents