active breakpoint cluster region-related protein isoform g [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Bcr-Abl_Oligo super family | cl07596 | Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain ... |
3-65 | 5.38e-14 | ||
Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerization domain is essential for the oncogenicity of the Bcr-Abl protein. The actual alignment was detected with superfamily member pfam09036: Pssm-ID: 430380 Cd Length: 73 Bit Score: 66.04 E-value: 5.38e-14
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| Name | Accession | Description | Interval | E-value | ||
| Bcr-Abl_Oligo | pfam09036 | Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain ... |
3-65 | 5.38e-14 | ||
Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerization domain is essential for the oncogenicity of the Bcr-Abl protein. Pssm-ID: 430380 Cd Length: 73 Bit Score: 66.04 E-value: 5.38e-14
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| Name | Accession | Description | Interval | E-value | ||
| Bcr-Abl_Oligo | pfam09036 | Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain ... |
3-65 | 5.38e-14 | ||
Bcr-Abl oncoprotein oligomerization domain; The Bcr-Abl oncoprotein oligomerization domain consists of a short N-terminal helix (alpha-1), a flexible loop and a long C-terminal helix (alpha-2). Together these form an N-shaped structure, with the loop allowing the two helices to assume a parallel orientation. The monomeric domains associate into a dimer through the formation of an antiparallel coiled coil between the alpha-2 helices and domain swapping of two alpha-1 helices, where one alpha-1 helix swings back and packs against the alpha-2 helix from the second monomer. Two dimers then associate into a tetramer. The oligomerization domain is essential for the oncogenicity of the Bcr-Abl protein. Pssm-ID: 430380 Cd Length: 73 Bit Score: 66.04 E-value: 5.38e-14
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| Blast search parameters | ||||
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