Reviewed,
UniProtKB/Swiss-Prot Q01513 (CYAA_PODAN)
Last modified
June 16, 2009.
Version 59.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Adenylate cyclase EC=4.6.1.1 Alternative name(s): ATP pyrophosphate-lyase Adenylyl cyclase |
| Organism | Podospora anserina |
| Taxonomic identifier | 5145 [NCBI] |
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Lasiosphaeriaceae › Podospora |
Protein attributes
| Sequence length | 2145 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. |
| Catalytic activity | ATP = 3',5'-cyclic AMP + diphosphate. |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Sequence similarities | Belongs to the adenylyl cyclase class-3 family. Contains 1 guanylate cyclase domain. Contains 21 LRR (leucine-rich) repeats. Contains 1 PP2C-like domain. Contains 1 Ras-associating domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | cAMP biosynthesis |
| Domain | Leucine-rich repeat Repeat |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Lyase |
| Gene Ontology (GO) | |
| Biological process | cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascadeInferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2145 | 2145 | Adenylate cyclase | PRO_0000195729 | |||||
Regions | |||||||||
| Domain | 637 – 727 | 91 | Ras-associating | ||||||
| Repeat | 751 – 776 | 26 | LRR 1 | ||||||
| Repeat | 778 – 800 | 23 | LRR 2 | ||||||
| Repeat | 801 – 824 | 24 | LRR 3 | ||||||
| Repeat | 826 – 847 | 22 | LRR 4 | ||||||
| Repeat | 848 – 870 | 23 | LRR 5 | ||||||
| Repeat | 872 – 894 | 23 | LRR 6 | ||||||
| Repeat | 895 – 917 | 23 | LRR 7 | ||||||
| Repeat | 919 – 940 | 22 | LRR 8 | ||||||
| Repeat | 941 – 965 | 25 | LRR 9 | ||||||
| Repeat | 983 – 1005 | 23 | LRR 10 | ||||||
| Repeat | 1006 – 1027 | 22 | LRR 11 | ||||||
| Repeat | 1028 – 1051 | 24 | LRR 12 | ||||||
| Repeat | 1053 – 1074 | 22 | LRR 13 | ||||||
| Repeat | 1075 – 1097 | 23 | LRR 14 | ||||||
| Repeat | 1099 – 1120 | 22 | LRR 15 | ||||||
| Repeat | 1233 – 1256 | 24 | LRR 16 | ||||||
| Repeat | 1257 – 1280 | 24 | LRR 17 | ||||||
| Repeat | 1282 – 1304 | 23 | LRR 18 | ||||||
| Repeat | 1305 – 1328 | 24 | LRR 19 | ||||||
| Repeat | 1357 – 1380 | 24 | LRR 20 | ||||||
| Repeat | 1394 – 1419 | 26 | LRR 21 | ||||||
| Domain | 1445 – 1710 | 266 | PP2C-like | ||||||
| Domain | 1773 – 1910 | 138 | Guanylate cyclase | ||||||
| Compositional bias | 36 – 41 | 6 | Poly-Ser | ||||||
Sites | |||||||||
| Metal binding | 1778 | 1 | Magnesium By similarity | ||||||
| Metal binding | 1821 | 1 | Magnesium By similarity | ||||||
Sequences
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References
| [1] | "An additional copy of the adenylate cyclase-encoding gene relieves developmental defects produced by a mutation in a vegetative incompatibility-controlling gene in Podospora anserina." Loubradou G., Begueret J., Turcq B. Gene 170:119-123(1996) [PubMed: 8621071] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| L43413 Genomic DNA. Translation: AAB05642.1. | |
| PIR | JC4747. |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 4.6.1.1. 142554. |
Family and domain databases | |
| InterPro | IPR001054. A/G_cyclase. IPR013716. Adenylate_cyclase_G-a-bd. IPR001611. Leu-rich_rpt. IPR003591. Leu-rich_rpt_typical-subtyp. IPR001932. PP2C-related. IPR014045. PP2C_N. IPR000159. Ras-assoc. [Graphical view] |
| Gene3D | G3DSA:3.30.70.1230. A/G_cyclase. 1 hit. G3DSA:3.60.40.10. PP2C-related. 1 hit. |
| Pfam | PF08509. Ad_cyc_g-alpha. 1 hit. PF00211. Guanylate_cyc. 1 hit. PF00560. LRR_1. 8 hits. PF00481. PP2C. 1 hit. PF00788. RA. 1 hit. [Graphical view] |
| SMART | SM00789. Ad_cyc_g-alpha. 1 hit. SM00044. CYCc. 1 hit. SM00369. LRR_TYP. 1 hit. SM00332. PP2Cc. 1 hit. SM00314. RA. 1 hit. [Graphical view] |
| PROSITE | PS50125. GUANYLATE_CYCLASE_2. 1 hit. PS50200. RA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYAA_PODAN | ||||||||
| Accession | Primary (citable) accession number: Q01513 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
