protein furry homolog-like isoform X16 [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||||||||||||||
Fry_C | pfam19421 | Furry protein C-terminal; This is the C-terminal domain of Furry (Fry) protein. Fry plays a ... |
2300-3031 | 0e+00 | ||||||||||||||||||
Furry protein C-terminal; This is the C-terminal domain of Furry (Fry) protein. Fry plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity. This domain binds to polo-like kinase 1 (Plk1) through the polo-box domain (PBD) of Plk1 in a manner dependent on the cyclin-dependent kinase 1-mediated Fry phosphorylation, promoting Plk1 activity during early mitosis. Fry also binds to Aurora A and may function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. : Pssm-ID: 466072 Cd Length: 633 Bit Score: 1010.06 E-value: 0e+00
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MOR2-PAG1_N | pfam14222 | Cell morphogenesis N-terminal; This family is the conserved N-terminal region of proteins that ... |
117-664 | 0e+00 | ||||||||||||||||||
Cell morphogenesis N-terminal; This family is the conserved N-terminal region of proteins that are involved in cell morphogenesis. : Pssm-ID: 464107 Cd Length: 554 Bit Score: 622.68 E-value: 0e+00
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MOR2-PAG1_C | pfam14225 | Cell morphogenesis C-terminal; This family is the conserved C-terminal region of proteins that ... |
2017-2270 | 8.62e-75 | ||||||||||||||||||
Cell morphogenesis C-terminal; This family is the conserved C-terminal region of proteins that are involved in cell morphogenesis. : Pssm-ID: 464109 Cd Length: 252 Bit Score: 250.08 E-value: 8.62e-75
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MOR2-PAG1_mid super family | cl20509 | Cell morphogenesis central region; This family is the conserved central region of proteins ... |
702-1875 | 2.08e-38 | ||||||||||||||||||
Cell morphogenesis central region; This family is the conserved central region of proteins that are involved in cell morphogenesis. The actual alignment was detected with superfamily member pfam14228: Pssm-ID: 433790 [Multi-domain] Cd Length: 1113 Bit Score: 158.65 E-value: 2.08e-38
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Name | Accession | Description | Interval | E-value | ||||||||||||||||||
Fry_C | pfam19421 | Furry protein C-terminal; This is the C-terminal domain of Furry (Fry) protein. Fry plays a ... |
2300-3031 | 0e+00 | ||||||||||||||||||
Furry protein C-terminal; This is the C-terminal domain of Furry (Fry) protein. Fry plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity. This domain binds to polo-like kinase 1 (Plk1) through the polo-box domain (PBD) of Plk1 in a manner dependent on the cyclin-dependent kinase 1-mediated Fry phosphorylation, promoting Plk1 activity during early mitosis. Fry also binds to Aurora A and may function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. Pssm-ID: 466072 Cd Length: 633 Bit Score: 1010.06 E-value: 0e+00
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MOR2-PAG1_N | pfam14222 | Cell morphogenesis N-terminal; This family is the conserved N-terminal region of proteins that ... |
117-664 | 0e+00 | ||||||||||||||||||
Cell morphogenesis N-terminal; This family is the conserved N-terminal region of proteins that are involved in cell morphogenesis. Pssm-ID: 464107 Cd Length: 554 Bit Score: 622.68 E-value: 0e+00
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MOR2-PAG1_C | pfam14225 | Cell morphogenesis C-terminal; This family is the conserved C-terminal region of proteins that ... |
2017-2270 | 8.62e-75 | ||||||||||||||||||
Cell morphogenesis C-terminal; This family is the conserved C-terminal region of proteins that are involved in cell morphogenesis. Pssm-ID: 464109 Cd Length: 252 Bit Score: 250.08 E-value: 8.62e-75
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MOR2-PAG1_mid | pfam14228 | Cell morphogenesis central region; This family is the conserved central region of proteins ... |
702-1875 | 2.08e-38 | ||||||||||||||||||
Cell morphogenesis central region; This family is the conserved central region of proteins that are involved in cell morphogenesis. Pssm-ID: 433790 [Multi-domain] Cd Length: 1113 Bit Score: 158.65 E-value: 2.08e-38
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Name | Accession | Description | Interval | E-value | ||||||||||||||||||
Fry_C | pfam19421 | Furry protein C-terminal; This is the C-terminal domain of Furry (Fry) protein. Fry plays a ... |
2300-3031 | 0e+00 | ||||||||||||||||||
Furry protein C-terminal; This is the C-terminal domain of Furry (Fry) protein. Fry plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity. This domain binds to polo-like kinase 1 (Plk1) through the polo-box domain (PBD) of Plk1 in a manner dependent on the cyclin-dependent kinase 1-mediated Fry phosphorylation, promoting Plk1 activity during early mitosis. Fry also binds to Aurora A and may function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylation. Pssm-ID: 466072 Cd Length: 633 Bit Score: 1010.06 E-value: 0e+00
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MOR2-PAG1_N | pfam14222 | Cell morphogenesis N-terminal; This family is the conserved N-terminal region of proteins that ... |
117-664 | 0e+00 | ||||||||||||||||||
Cell morphogenesis N-terminal; This family is the conserved N-terminal region of proteins that are involved in cell morphogenesis. Pssm-ID: 464107 Cd Length: 554 Bit Score: 622.68 E-value: 0e+00
|
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MOR2-PAG1_C | pfam14225 | Cell morphogenesis C-terminal; This family is the conserved C-terminal region of proteins that ... |
2017-2270 | 8.62e-75 | ||||||||||||||||||
Cell morphogenesis C-terminal; This family is the conserved C-terminal region of proteins that are involved in cell morphogenesis. Pssm-ID: 464109 Cd Length: 252 Bit Score: 250.08 E-value: 8.62e-75
|
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MOR2-PAG1_mid | pfam14228 | Cell morphogenesis central region; This family is the conserved central region of proteins ... |
702-1875 | 2.08e-38 | ||||||||||||||||||
Cell morphogenesis central region; This family is the conserved central region of proteins that are involved in cell morphogenesis. Pssm-ID: 433790 [Multi-domain] Cd Length: 1113 Bit Score: 158.65 E-value: 2.08e-38
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Blast search parameters | ||||
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