Reviewed,
UniProtKB/Swiss-Prot Q1SGF1 (PARP3_MEDTR)
Last modified
June 16, 2009.
Version 19.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative poly [ADP-ribose] polymerase 3 Short name=PARP-3 EC=2.4.2.30 Alternative name(s): ADPRT 3 NAD(+) ADP-ribosyltransferase 3 Poly[ADP-ribose] synthetase 3 | ||
| Gene names |
| ||
| Organism | Medicago truncatula (Barrel medic) | ||
| Taxonomic identifier | 3880 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago |
Protein attributes
| Sequence length | 799 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks By similarity. |
| Catalytic activity | NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. |
| Subcellular location | Nucleus Potential. |
| Sequence similarities | Contains 1 BRCT domain. Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain. Contains 1 SAP domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Nucleus |
| Ligand | DNA-binding NAD |
| Molecular function | Glycosyltransferase Transferase |
| PTM | ADP-ribosylation |
| Gene Ontology (GO) | |
| Biological process | protein amino acid ADP-ribosylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW NAD+ ADP-ribosyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | The International Medicago Genome Annotation Group Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AC144515 Genomic DNA. No translation available. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.4.2.30. 266820. |
Family and domain databases | |
| InterPro | IPR001357. BRCT. IPR012982. PADR1. IPR012317. PARP_catalytic. IPR004102. PARP_reg. IPR008893. WGR. [Graphical view] |
| Gene3D | G3DSA:1.20.142.10. PARP_reg. 1 hit. |
| Pfam | PF00533. BRCT. 1 hit. PF08063. PADR1. 1 hit. PF00644. PARP. 1 hit. PF05406. WGR. 1 hit. [Graphical view] |
| SMART | SM00773. WGR. 1 hit. [Graphical view] |
| PROSITE | PS50172. BRCT. 1 hit. PS51060. PARP_ALPHA_HD. 1 hit. PS51059. PARP_CATALYTIC. 1 hit. PS50800. SAP. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PARP3_MEDTR | ||||||||
| Accession | Primary (citable) accession number: Q1SGF1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


