serum response factor isoform X2 [Mus musculus]
MADS-box domain-containing protein( domain architecture ID 734)
MADS (MCM1, AGAMOUS, DEFICIENS, and SRF, serum response factor)-box domain-containing protein functions as a transcription factor and may be involved in various important aspects of development and differentiation
List of domain hits
Name | Accession | Description | Interval | E-value | ||
MADS super family | cl00109 | MADS: MCM1, Agamous, Deficiens, and SRF (serum response factor) box family of eukaryotic ... |
16-67 | 1.51e-08 | ||
MADS: MCM1, Agamous, Deficiens, and SRF (serum response factor) box family of eukaryotic transcriptonal regulators. Binds DNA and exists as hetero and homo-dimers. Composed of 2 main subgroups: SRF-like/Type I and MEF2-like (myocyte enhancer factor 2)/ Type II. These subgroups differ mainly in position of the alpha 2 helix responsible for the dimerization interface; Important in homeotic regulation in plants and in immediate-early development in animals. Also found in fungi. The actual alignment was detected with superfamily member cd00266: Pssm-ID: 469617 [Multi-domain] Cd Length: 83 Bit Score: 51.11 E-value: 1.51e-08
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Name | Accession | Description | Interval | E-value | ||
MADS_SRF_like | cd00266 | SRF-like/Type I subfamily of MADS (MCM1, Agamous, Deficiens, and SRF (serum response factor) ... |
16-67 | 1.51e-08 | ||
SRF-like/Type I subfamily of MADS (MCM1, Agamous, Deficiens, and SRF (serum response factor) box family of eukaryotic transcriptional regulators. Binds DNA and exists as hetero- and homo-dimers. Differs from the MEF-like/Type II subgroup mainly in position of the alpha 2 helix responsible for the dimerization interface. Important in homeotic regulation in plants and in immediate-early development in animals. Also found in fungi. Pssm-ID: 238166 [Multi-domain] Cd Length: 83 Bit Score: 51.11 E-value: 1.51e-08
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ARG80 | COG5068 | Regulator of arginine metabolism and related MADS box-containing transcription factors ... |
16-74 | 2.90e-08 | ||
Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription]; Pssm-ID: 227400 [Multi-domain] Cd Length: 412 Bit Score: 55.02 E-value: 2.90e-08
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SRF-TF | pfam00319 | SRF-type transcription factor (DNA-binding and dimerization domain); |
16-41 | 6.37e-07 | ||
SRF-type transcription factor (DNA-binding and dimerization domain); Pssm-ID: 459760 [Multi-domain] Cd Length: 48 Bit Score: 45.50 E-value: 6.37e-07
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MADS | smart00432 | MADS domain; |
16-44 | 5.65e-06 | ||
MADS domain; Pssm-ID: 197721 [Multi-domain] Cd Length: 59 Bit Score: 43.31 E-value: 5.65e-06
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Name | Accession | Description | Interval | E-value | ||
MADS_SRF_like | cd00266 | SRF-like/Type I subfamily of MADS (MCM1, Agamous, Deficiens, and SRF (serum response factor) ... |
16-67 | 1.51e-08 | ||
SRF-like/Type I subfamily of MADS (MCM1, Agamous, Deficiens, and SRF (serum response factor) box family of eukaryotic transcriptional regulators. Binds DNA and exists as hetero- and homo-dimers. Differs from the MEF-like/Type II subgroup mainly in position of the alpha 2 helix responsible for the dimerization interface. Important in homeotic regulation in plants and in immediate-early development in animals. Also found in fungi. Pssm-ID: 238166 [Multi-domain] Cd Length: 83 Bit Score: 51.11 E-value: 1.51e-08
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ARG80 | COG5068 | Regulator of arginine metabolism and related MADS box-containing transcription factors ... |
16-74 | 2.90e-08 | ||
Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription]; Pssm-ID: 227400 [Multi-domain] Cd Length: 412 Bit Score: 55.02 E-value: 2.90e-08
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SRF-TF | pfam00319 | SRF-type transcription factor (DNA-binding and dimerization domain); |
16-41 | 6.37e-07 | ||
SRF-type transcription factor (DNA-binding and dimerization domain); Pssm-ID: 459760 [Multi-domain] Cd Length: 48 Bit Score: 45.50 E-value: 6.37e-07
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MADS | smart00432 | MADS domain; |
16-44 | 5.65e-06 | ||
MADS domain; Pssm-ID: 197721 [Multi-domain] Cd Length: 59 Bit Score: 43.31 E-value: 5.65e-06
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Blast search parameters | ||||
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