| Basic Information | |
|---|---|
| Species | Selaginella moellendorffii |
| Cazyme ID | 101237 |
| Family | GT47 |
| Protein Properties | Length: 466 Molecular Weight: 54085 Isoelectric Point: 8.3444 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT47 | 65 | 401 | 0 |
| SCQGRRVFMYELPRKFNLEVLEKCDKMVSWLTFCDHFINHGFGKALAGANSSWYATDPYMLEVIFHERMRRYRCLVNSPREADAFFIPYYAGLDALRFLY GADNLNRHEQGVDLVKFLEANYSWSWRRNLGHDHFMVTGRTAWDFASYRGKSSWGTSLRLLKQMENVTTLVMERRPWDRTEQAIPYPTSFHPATKSELQA WIERVKASPRTNFMSFAGAPRPQQNESIRGILFEQCRKSRSCEAVNCSKLRCAHNPLPIAEKLLSSIFCLQPQGDTSTRRSSFDSLVCGCIPVFFHADSA YTQYTWHLPRERESYSVFIPEEEIRRDGLEVEEFLRS | |||
| Full Sequence |
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| Protein Sequence Length: 466 Download |
| MSASFGTYWA FSSSYRLHPI KFLTFPEQHK SSSAFFEEVT NRDRARHPFS RGDHHEFPDG 60 QDLHSCQGRR VFMYELPRKF NLEVLEKCDK MVSWLTFCDH FINHGFGKAL AGANSSWYAT 120 DPYMLEVIFH ERMRRYRCLV NSPREADAFF IPYYAGLDAL RFLYGADNLN RHEQGVDLVK 180 FLEANYSWSW RRNLGHDHFM VTGRTAWDFA SYRGKSSWGT SLRLLKQMEN VTTLVMERRP 240 WDRTEQAIPY PTSFHPATKS ELQAWIERVK ASPRTNFMSF AGAPRPQQNE SIRGILFEQC 300 RKSRSCEAVN CSKLRCAHNP LPIAEKLLSS IFCLQPQGDT STRRSSFDSL VCGCIPVFFH 360 ADSAYTQYTW HLPRERESYS VFIPEEEIRR DGLEVEEFLR SKFSSQRIGE LQRNIRKIIP 420 RLLYTGKPWS SGDGGRDSLD GEDDAFDVSV KEMVEKSQRT QFSST* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam03016 | Exostosin | 3.0e-55 | 65 | 401 | 352 | + Exostosin family. The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear. |
| Hydropathy |
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| Sequence Alignments (This image is cropped. Click for full image.) |
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