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ran-binding protein 10 isoform X4 [Homo sapiens]
CTLH and CRA domain-containing protein( domain architecture ID 10652947)
protein containing domains LisH, CTLH, and CRA
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
CRA | smart00757 | CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ... |
308-405 | 2.02e-15 | |||
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) : Pssm-ID: 214806 Cd Length: 99 Bit Score: 71.56 E-value: 2.02e-15
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CTLH | smart00668 | C-terminal to LisH motif; Alpha-helical motif of unknown function. |
62-118 | 1.60e-13 | |||
C-terminal to LisH motif; Alpha-helical motif of unknown function. : Pssm-ID: 128914 Cd Length: 58 Bit Score: 64.90 E-value: 1.60e-13
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LisH super family | cl26729 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
28-50 | 2.43e-03 | |||
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex. The actual alignment was detected with superfamily member pfam08513: Pssm-ID: 474848 Cd Length: 25 Bit Score: 34.99 E-value: 2.43e-03
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Name | Accession | Description | Interval | E-value | |||
CRA | smart00757 | CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ... |
308-405 | 2.02e-15 | |||
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) Pssm-ID: 214806 Cd Length: 99 Bit Score: 71.56 E-value: 2.02e-15
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CTLH | smart00668 | C-terminal to LisH motif; Alpha-helical motif of unknown function. |
62-118 | 1.60e-13 | |||
C-terminal to LisH motif; Alpha-helical motif of unknown function. Pssm-ID: 128914 Cd Length: 58 Bit Score: 64.90 E-value: 1.60e-13
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CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
62-116 | 2.20e-13 | |||
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif. Pssm-ID: 402305 [Multi-domain] Cd Length: 143 Bit Score: 67.21 E-value: 2.20e-13
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CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
329-400 | 7.78e-12 | |||
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif. Pssm-ID: 402305 [Multi-domain] Cd Length: 143 Bit Score: 62.59 E-value: 7.78e-12
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LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
28-50 | 2.43e-03 | |||
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex. Pssm-ID: 462501 Cd Length: 25 Bit Score: 34.99 E-value: 2.43e-03
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LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
28-55 | 2.51e-03 | |||
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly. Pssm-ID: 128913 Cd Length: 34 Bit Score: 35.10 E-value: 2.51e-03
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Name | Accession | Description | Interval | E-value | |||
CRA | smart00757 | CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, ... |
308-405 | 2.02e-15 | |||
CT11-RanBPM; protein-protein interaction domain present in crown eukaryotes (plants, animals, fungi) Pssm-ID: 214806 Cd Length: 99 Bit Score: 71.56 E-value: 2.02e-15
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CTLH | smart00668 | C-terminal to LisH motif; Alpha-helical motif of unknown function. |
62-118 | 1.60e-13 | |||
C-terminal to LisH motif; Alpha-helical motif of unknown function. Pssm-ID: 128914 Cd Length: 58 Bit Score: 64.90 E-value: 1.60e-13
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CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
62-116 | 2.20e-13 | |||
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif. Pssm-ID: 402305 [Multi-domain] Cd Length: 143 Bit Score: 67.21 E-value: 2.20e-13
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CTLH | pfam10607 | CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in ... |
329-400 | 7.78e-12 | |||
CTLH/CRA C-terminal to LisH motif domain; RanBPM is a scaffolding protein and is important in regulating cellular function in both the immune system and the nervous system. This domain is at the C-terminus of the proteins and is the binding domain for the CRA motif (for CT11-RanBPM), which is comprised of approximately 100 amino acids at the C terminal of RanBPM. It was found to be important for the interaction of RanBPM with fragile X mental retardation protein (FMRP), but its functional significance has yet to be determined. This region contains CTLH and CRA domains annotated by SMART; however, these may be a single domain, and it is refereed to as a C-terminal to LisH motif. Pssm-ID: 402305 [Multi-domain] Cd Length: 143 Bit Score: 62.59 E-value: 7.78e-12
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LisH | pfam08513 | LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The ... |
28-50 | 2.43e-03 | |||
LisH; The LisH (lis homology) domain mediates protein dimerization and tetramerization. The LisH domain is found in Sif2, a component of the Set3 complex which is responsible for repressing meiotic genes. It has been shown that the LisH domain helps mediate interaction with components of the Set3 complex. Pssm-ID: 462501 Cd Length: 25 Bit Score: 34.99 E-value: 2.43e-03
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LisH | smart00667 | Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
28-55 | 2.51e-03 | |||
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly. Pssm-ID: 128913 Cd Length: 34 Bit Score: 35.10 E-value: 2.51e-03
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Blast search parameters | ||||
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