P74750 (DPO3A_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 107.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: DNA polymerase III subunit alpha EC=2.7.7.7 Cleaved into the following chain: | |||||||||
| Gene names |
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| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP] | |||||||||
| Taxonomic identifier | 1111708 [NCBI] | |||||||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › ![]() |
Protein attributes
| Sequence length | 1355 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase By similarity. |
| Catalytic activity | Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). |
| Subunit structure | DNA polymerase III contains a core (composed of alpha, epsilon and theta chains) that associates with a tau subunit. This core dimerizes to form the PolIII' complex. PolIII' associates with the gamma complex (composed of gamma, delta, delta', psi and chi chains) and with the beta chain to form the complete DNA polymerase III complex By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Post-translational modification | This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation. |
| Miscellaneous | The intein is a split intein capable of protein trans-splicing. The N- and C-terminal halves of dnaE are encoded by two separate genes located 745 kb apart in the genome and on opposite DNA strands. The dnaE-N product consists of a N-extein sequence followed by a 123-aa intein sequence (Ssp dnaE1), whereas the dnaE-C product consists of a 36-aa intein sequence (Ssp dnaE2) followed by a C-extein sequence. The N- and C-extein sequences together reconstitute a complete DnaE sequence that is interrupted by the intein sequences inside the beta- and tau-binding domains. |
| Sequence similarities | Belongs to the DNA polymerase type-C family. DnaE subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA replication |
| Cellular component | Cytoplasm |
| Molecular function | DNA-directed DNA polymerase Nucleotidyltransferase Transferase |
| PTM | Autocatalytic cleavage Protein splicing |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA replication Inferred from electronic annotation. Source: UniProtKB-KW intein-mediated protein splicingInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | 3'-5' exonuclease activity Inferred from electronic annotation. Source: InterPro DNA bindingInferred from electronic annotation. Source: InterPro DNA-directed DNA polymerase activityInferred 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 – 774 | 774 | DNA polymerase III subunit alpha, 1st part | PRO_0000007364 | ||||||||||||||||||||||||||||||||||||||||
| Chain | 775 – 897 | 123 | Ssp dnaE intein, 1st part | PRO_0000007365 | ||||||||||||||||||||||||||||||||||||||||
| Chain | 898 – 933 | 36 | Ssp dnaE intein, 2nd part | PRO_0000007366 | ||||||||||||||||||||||||||||||||||||||||
| Chain | 934 – 1355 | 422 | DNA polymerase III subunit alpha, 2nd part | PRO_0000007367 | ||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||
| Non-adjacent residues | 897 – 898 | 2 | ||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 781 – 784 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Turn | 785 – 787 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 788 – 791 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 792 – 797 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 803 – 807 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 811 – 817 | 7 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 820 – 834 | 15 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 839 – 842 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 847 – 850 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 855 – 857 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 858 – 864 | 7 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 868 – 871 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 877 – 879 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Turn | 883 – 885 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 887 – 889 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 890 – 893 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 896 – 899 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 901 – 916 | 16 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 923 – 925 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 928 – 932 | 5 | ||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa. |
| [2] | "Protein trans-splicing by a split intein encoded in a split DnaE gene of Synechocystis sp. PCC6803." Wu H., Hu Z., Liu X.-Q. Proc. Natl. Acad. Sci. U.S.A. 95:9226-9231(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF SPLIT INTEIN. |
| [3] | "Protein trans-splicing and cyclization by a naturally split intein from the dnaE gene of Synechocystis species PCC6803." Evans T.C. Jr., Martin D., Kolly R., Panne D., Sun L., Ghosh I., Chen L., Benner J., Liu X.-Q., Xu M.-Q. J. Biol. Chem. 275:9091-9094(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF SPLIT INTEIN. |
| [4] | "Characterization of a naturally occurring trans-splicing intein from Synechocystis sp. PCC6803." Martin D.D., Xu M.-Q., Evans T.C. Jr. Biochemistry 40:1393-1402(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF SPLIT INTEIN. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | BA000022 Genomic DNA. Translation: BAA18870.1. Sequence problems. BA000022 Genomic DNA. Translation: BAA17242.1. Sequence problems. | ||||||||||||||||||||||||||||||
| PIR | A59016. S75328. S76958. | ||||||||||||||||||||||||||||||
| RefSeq | NP_440562.1. NC_000911.1. NP_443058.1. NC_000911.1. YP_005650620.1. NC_017277.1. YP_005653117.1. NC_017277.1. YP_007450445.1. NC_020286.1. YP_007452933.1. NC_020286.1. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P74750. | ||||||||||||||||||||||||||||||
| SMR | P74750. Positions 775-933. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| IntAct | P74750. 2 interactions. | ||||||||||||||||||||||||||||||
| STRING | 1148.sll1572. | ||||||||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||||||||
| MEROPS | N10.003. | ||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||
| PRIDE | P74750. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| EnsemblBacteria | BAA17242; BAA17242; BAA17242. BAA18870; BAA18870; BAA18870. | ||||||||||||||||||||||||||||||
| GeneID | 12255728. 12256312. 14616095. 14618625. 951978. 953863. | ||||||||||||||||||||||||||||||
| KEGG | syn:sll1572. syn:slr0603. syy:SYNGTS_0667. syy:SYNGTS_3164. | ||||||||||||||||||||||||||||||
| PATRIC | 23838310. VBISynSp132158_0722. | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| eggNOG | COG0587. | ||||||||||||||||||||||||||||||
| HOGENOM | HOG000021784. | ||||||||||||||||||||||||||||||
| KO | K02337. | ||||||||||||||||||||||||||||||
| ProtClustDB | PRK09532. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| Gene3D | 2.40.50.140. 1 hit. | ||||||||||||||||||||||||||||||
| InterPro | IPR011708. DNA_pol3_alpha. IPR003587. Hint_dom_N. IPR006141. Intein_splice_site. IPR012340. NA-bd_OB-fold. IPR004365. NA-bd_OB_tRNA-helicase. IPR004013. PHP_C. IPR003141. Pol/His_phosphatase_N. IPR016195. Pol/histidinol_Pase-like. IPR004805. PolC_alpha. [Graphical view] | ||||||||||||||||||||||||||||||
| Pfam | PF07733. DNA_pol3_alpha. 1 hit. PF02811. PHP. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| SMART | SM00306. HintN. 1 hit. SM00481. POLIIIAc. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| SUPFAM | SSF89550. PHP-like. 1 hit. | ||||||||||||||||||||||||||||||
| TIGRFAMs | TIGR01443. intein_Cterm. 1 hit. TIGR01445. intein_Nterm. 1 hit. TIGR00594. polc. 1 hit. | ||||||||||||||||||||||||||||||
| PROSITE | PS50818. INTEIN_C_TER. 1 hit. PS50817. INTEIN_N_TER. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Other | |||||||||||||||||||||||||||||||
| EvolutionaryTrace | P74750. | ||||||||||||||||||||||||||||||
Entry information
| Entry name | DPO3A_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: P74750 Secondary accession number(s): P73215 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Recent format changes Overview of recent format changes |
| Intein-containing proteins List of intein-containing protein entries |
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
