Reviewed,
UniProtKB/Swiss-Prot Q5BH83 (DNLI4_EMENI)
Last modified
February 9, 2010.
Version 30.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: DNA ligase 4 EC=6.5.1.1 Alternative name(s): DNA ligase IV Polydeoxyribonucleotide synthase [ATP] 4 | ||||
| Gene names |
| ||||
| Organism | Emericella nidulans (Aspergillus nidulans) [Complete proteome] | ||||
| Taxonomic identifier | 162425 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella |
Protein attributes
| Sequence length | 1009 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Involved in ds DNA break repair. Has a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining By similarity. |
| Catalytic activity | ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m). |
| Cofactor | Magnesium By similarity. |
| Subcellular location | Nucleus By similarity. |
| Sequence similarities | Belongs to the ATP-dependent DNA ligase family. Contains 2 BRCT domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA recombination DNA repair DNA replication |
| Cellular component | Nucleus |
| Domain | Repeat |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repairInferred from electronic annotation. Source: UniProtKB-KW DNA replicationInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA bindingInferred from electronic annotation. Source: InterPro DNA ligase (ATP) activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1009 | 1009 | DNA ligase 4 | PRO_0000278382 | |||||
Regions | |||||||||
| Domain | 715 – 808 | 94 | BRCT 1 | ||||||
| Domain | 887 – 995 | 109 | BRCT 2 | ||||||
Sites | |||||||||
| Active site | 317 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Metal binding | 384 | 1 | Magnesium 1 Potential | ||||||
| Metal binding | 484 | 1 | Magnesium 2 Potential | ||||||
| Binding site | 315 | 1 | ATP By similarity | ||||||
| Binding site | 322 | 1 | ATP By similarity | ||||||
| Binding site | 344 | 1 | ATP By similarity | ||||||
| Binding site | 489 | 1 | ATP By similarity | ||||||
| Binding site | 500 | 1 | ATP By similarity | ||||||
| Binding site | 506 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. Birren B.W.Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / M139. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AACD01000003 Genomic DNA. Translation: EAA65275.1. |
| RefSeq | XP_657701.1. |
3D structure databases | |
| SMR | Q5BH83. Positions 718-992. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2875873. |
| KEGG | ani:AN0097.2. |
Phylogenomic databases | |
| PhylomeDB | Q5BH83. |
Enzyme and pathway databases | |
| BRENDA | 6.5.1.1. 3859. |
Family and domain databases | |
| InterPro | IPR001357. BRCT. IPR000977. DNA_ligase. IPR012309. DNA_ligase_A_C. IPR012310. DNA_ligase_A_M. IPR016059. DNA_ligase_CS. IPR012340. NA-bd_OB-fold. [Graphical view] |
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. |
| Pfam | PF00533. BRCT. 1 hit. PF04679. DNA_ligase_A_C. 1 hit. PF01068. DNA_ligase_A_M. 1 hit. [Graphical view] |
| SMART | SM00292. BRCT. 2 hits. [Graphical view] |
| TIGRFAMs | TIGR00574. dnl1. 1 hit. |
| PROSITE | PS50172. BRCT. 2 hits. PS00697. DNA_LIGASE_A1. 1 hit. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DNLI4_EMENI | ||||||||
| Accession | Primary (citable) accession number: Q5BH83 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||

Clusters with


