| Gene ID | Annotation | Scaffold | Start | End | Strand |
|---|---|---|---|---|---|
| CAI8046384.1 | S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE | contig_6565_pilon | 20095 | 21306 | - |
| CDS | |||||
| CAI8046384.1 | |||||
| Transcript |
| - |
| Protein |
| CAI8046384.1 |
| Gene family | Subfamily |
|---|---|
| - | - |
| Pfam accession | Pfam name | Description | Type | Source |
|---|---|---|---|---|
| PF00581 | Rhodanese | Rhodanese-like domain | Domain | Interproscan |
| PF01048 | PNP_UDP_1 | Phosphorylase superfamily | Domain | Interproscan |
| InterPro term | Type | Description | Source |
|---|---|---|---|
| IPR000845 | Domain | Nucleoside phosphorylase domain | Interproscan |
| IPR001763 | Domain | Rhodanese-like domain | Interproscan |
| IPR010044 | Family | Methylthioadenosine phosphorylase (MTAP) | Interproscan |
| IPR018099 | Conserved_site | Purine phosphorylase, family 2, conserved site | Interproscan |
| IPR035994 | Homologous_superfamily | Nucleoside phosphorylase superfamily | Interproscan |
| IPR036873 | Homologous_superfamily | Rhodanese-like domain superfamily | Interproscan |
| PANTHER term | Description | Source |
|---|---|---|
| PTHR42679 | S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE | Interproscan |
| GO terms | Category | Description | Source |
|---|---|---|---|
| GO:0003824 | Molecular Function | catalytic activity | Interproscan |
| GO:0005829 | Cellular Component | cytosol | Interproscan |
| GO:0009116 | Biological Process | nucleoside metabolic process | Interproscan |
| GO:0016763 | Molecular Function | pentosyltransferase activity | Interproscan |
| GO:0017061 | Molecular Function | S-methyl-5-thioadenosine phosphorylase activity | Interproscan |
| GO:0019509 | Biological Process | L-methionine salvage from methylthioadenosine | Interproscan |
| KO | Enzyme | Enzyme ID | pathway | mapID | Source |
|---|---|---|---|---|---|
| - | - | - | - | - | - |
Maintained by Dr. Jiajie She in Longjun Wu's Lab & Pei-yuan Qian's Lab and supported by Southern Marine Science and Engineering Guangdong Laboratory (Guangzhou) & The Hong Kong University of Science and Technology
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