myocardin-related transcription factor B isoform 5 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| SAP | pfam02037 | SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ... |
329-362 | 2.70e-10 | ||||
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins. : Pssm-ID: 460424 [Multi-domain] Cd Length: 35 Bit Score: 56.25 E-value: 2.70e-10
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| RPEL | smart00707 | Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; |
68-93 | 8.74e-06 | ||||
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; : Pssm-ID: 128947 Cd Length: 26 Bit Score: 43.23 E-value: 8.74e-06
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| RPEL | pfam02755 | RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ... |
25-48 | 1.18e-04 | ||||
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin. : Pssm-ID: 460677 Cd Length: 24 Bit Score: 39.95 E-value: 1.18e-04
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| PHA03247 super family | cl33720 | large tegument protein UL36; Provisional |
126-339 | 1.52e-04 | ||||
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247: Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 1.52e-04
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| DUF2130 super family | cl38307 | Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ... |
497-532 | 2.27e-04 | ||||
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various hypothetical prokaryotic proteins, has no known function. The actual alignment was detected with superfamily member pfam09903: Pssm-ID: 430914 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 2.27e-04
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| SP1-4_N super family | cl41773 | N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ... |
578-755 | 1.51e-03 | ||||
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4. The actual alignment was detected with superfamily member cd22540: Pssm-ID: 425404 [Multi-domain] Cd Length: 511 Bit Score: 42.22 E-value: 1.51e-03
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| DUF4482 super family | cl20732 | Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
499-582 | 8.59e-03 | ||||
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam11365. The actual alignment was detected with superfamily member pfam14818: Pssm-ID: 464333 [Multi-domain] Cd Length: 138 Bit Score: 37.74 E-value: 8.59e-03
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| Name | Accession | Description | Interval | E-value | ||||
| SAP | pfam02037 | SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ... |
329-362 | 2.70e-10 | ||||
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins. Pssm-ID: 460424 [Multi-domain] Cd Length: 35 Bit Score: 56.25 E-value: 2.70e-10
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| SAP | smart00513 | Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation; |
329-360 | 7.15e-09 | ||||
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation; Pssm-ID: 128789 [Multi-domain] Cd Length: 35 Bit Score: 52.10 E-value: 7.15e-09
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| RPEL | smart00707 | Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; |
68-93 | 8.74e-06 | ||||
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; Pssm-ID: 128947 Cd Length: 26 Bit Score: 43.23 E-value: 8.74e-06
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| RPEL | pfam02755 | RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ... |
69-92 | 2.31e-05 | ||||
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin. Pssm-ID: 460677 Cd Length: 24 Bit Score: 41.88 E-value: 2.31e-05
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| RPEL | pfam02755 | RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ... |
25-48 | 1.18e-04 | ||||
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin. Pssm-ID: 460677 Cd Length: 24 Bit Score: 39.95 E-value: 1.18e-04
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
126-339 | 1.52e-04 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 1.52e-04
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| DUF2130 | pfam09903 | Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ... |
497-532 | 2.27e-04 | ||||
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various hypothetical prokaryotic proteins, has no known function. Pssm-ID: 430914 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 2.27e-04
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| COG4487 | COG4487 | Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
493-532 | 2.27e-04 | ||||
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 44.94 E-value: 2.27e-04
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| SP2_N | cd22540 | N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ... |
578-755 | 1.51e-03 | ||||
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2. Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 42.22 E-value: 1.51e-03
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| GBP_C | cd16269 | Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
500-546 | 1.58e-03 | ||||
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines. Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 1.58e-03
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| RPEL | smart00707 | Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; |
25-48 | 2.12e-03 | ||||
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; Pssm-ID: 128947 Cd Length: 26 Bit Score: 36.30 E-value: 2.12e-03
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| DUF4482 | pfam14818 | Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
499-582 | 8.59e-03 | ||||
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam11365. Pssm-ID: 464333 [Multi-domain] Cd Length: 138 Bit Score: 37.74 E-value: 8.59e-03
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| Name | Accession | Description | Interval | E-value | ||||
| SAP | pfam02037 | SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ... |
329-362 | 2.70e-10 | ||||
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins. Pssm-ID: 460424 [Multi-domain] Cd Length: 35 Bit Score: 56.25 E-value: 2.70e-10
|
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| SAP | smart00513 | Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation; |
329-360 | 7.15e-09 | ||||
Putative DNA-binding (bihelical) motif predicted to be involved in chromosomal organisation; Pssm-ID: 128789 [Multi-domain] Cd Length: 35 Bit Score: 52.10 E-value: 7.15e-09
|
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| RPEL | smart00707 | Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; |
68-93 | 8.74e-06 | ||||
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; Pssm-ID: 128947 Cd Length: 26 Bit Score: 43.23 E-value: 8.74e-06
|
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| RPEL | pfam02755 | RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ... |
69-92 | 2.31e-05 | ||||
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin. Pssm-ID: 460677 Cd Length: 24 Bit Score: 41.88 E-value: 2.31e-05
|
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| RPEL | pfam02755 | RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL ... |
25-48 | 1.18e-04 | ||||
RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin. Pssm-ID: 460677 Cd Length: 24 Bit Score: 39.95 E-value: 1.18e-04
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
126-339 | 1.52e-04 | ||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 1.52e-04
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| DUF2130 | pfam09903 | Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various ... |
497-532 | 2.27e-04 | ||||
Uncharacterized protein conserved in bacteria (DUF2130); This domain, found in various hypothetical prokaryotic proteins, has no known function. Pssm-ID: 430914 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 2.27e-04
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| COG4487 | COG4487 | Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
493-532 | 2.27e-04 | ||||
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 44.94 E-value: 2.27e-04
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| SP2_N | cd22540 | N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ... |
578-755 | 1.51e-03 | ||||
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2. Pssm-ID: 411776 [Multi-domain] Cd Length: 511 Bit Score: 42.22 E-value: 1.51e-03
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| GBP_C | cd16269 | Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
500-546 | 1.58e-03 | ||||
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines. Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 1.58e-03
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| PRK14971 | PRK14971 | DNA polymerase III subunit gamma/tau; |
114-252 | 1.81e-03 | ||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 42.07 E-value: 1.81e-03
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| RPEL | smart00707 | Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; |
25-48 | 2.12e-03 | ||||
Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2; Pssm-ID: 128947 Cd Length: 26 Bit Score: 36.30 E-value: 2.12e-03
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| ERM_helical | pfam20492 | Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
494-546 | 3.62e-03 | ||||
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins. Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 3.62e-03
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| DUF4482 | pfam14818 | Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately ... |
499-582 | 8.59e-03 | ||||
Domain of unknown function (DUF4482); This family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam11365. Pssm-ID: 464333 [Multi-domain] Cd Length: 138 Bit Score: 37.74 E-value: 8.59e-03
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| PTZ00449 | PTZ00449 | 104 kDa microneme/rhoptry antigen; Provisional |
122-224 | 8.68e-03 | ||||
104 kDa microneme/rhoptry antigen; Provisional Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 8.68e-03
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| Blast search parameters | ||||
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