Reviewed,
UniProtKB/Swiss-Prot O96539 (ATE1_DROME)
Last modified
November 3, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
| ||||
| Organism | Drosophila melanogaster (Fruit fly) [Complete proteome] | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora |
Protein attributes
| Sequence length | 484 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. |
| 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 process | Ubl conjugation pathway |
| Coding sequence diversity | Alternative splicing |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | protein arginylation Inferred from electronic annotation. Source: InterPro |
| Molecular function | acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW arginyltransferase activityInferred 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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 484 | 484 | Arginyl-tRNA--protein transferase 1 | PRO_0000195090 | |||||
Natural variations | |||||||||
| Alternative sequence | 175 – 181 | 7 | Missing in isoform A and isoform C. | VSP_000339 | |||||
| Alternative sequence | 239 – 288 | 50 | LRLIH…ATPLQ → IVLVASSDTERTCADAVIAL YRKYQITVHNDNPARLTLAS MQRFLVKSPLK in isoform C and isoform D. | VSP_011157 | |||||
Sequences
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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. 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. 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. 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. | |
| RefSeq | NP_477394.3. NP_725939.2. NP_725940.2. |
| UniGene | Dm.4513 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | FBtr0086318; FBpp0085627; FBgn0025720; Drosophila melanogaster. [Genome view] |
| GeneID | 37288. |
| KEGG | dme:Dmel_CG9204. |
| UCSC | CG9204-RA. d. melanogaster. |
Organism-specific databases | |
| CTD | 37288. |
| FlyBase | FBgn0025720. Ate1. |
Phylogenomic databases | |
| OMA | TERTCAD. |
Enzyme and pathway databases | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-005615-MON. |
| BRENDA | 2.3.2.8. 48. |
Gene expression databases | |
| GermOnline | CG9204. Drosophila melanogaster. |
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... |
Other Resources | |
| NextBio | 802931. |
Entry information
| Entry name | ATE1_DROME | ||||||||
| Accession | Primary (citable) accession number: O96539 Secondary accession number(s): Q7KRL0 Q9V907 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with


