histone acetyltransferase p300-like isoform X2 [Carcharodon carcharias]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| HAT_KAT11 | pfam08214 | Histone acetylation protein; Histone acetylation is required in many cellular processes ... |
1349-1656 | 2.06e-94 | |||||||
Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11. : Pssm-ID: 400497 Cd Length: 348 Bit Score: 310.10 E-value: 2.06e-94
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| Bromo_cbp_like | cd05495 | Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ... |
1094-1201 | 2.88e-76 | |||||||
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. : Pssm-ID: 99927 Cd Length: 108 Bit Score: 248.13 E-value: 2.88e-76
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| KIX | pfam02172 | KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ... |
592-672 | 2.00e-47 | |||||||
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun. : Pssm-ID: 366953 Cd Length: 81 Bit Score: 164.59 E-value: 2.00e-47
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| RING_CBP-p300 | cd15802 | atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ... |
1213-1285 | 1.93e-33 | |||||||
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902. : Pssm-ID: 276805 Cd Length: 73 Bit Score: 124.32 E-value: 1.93e-33
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| Creb_binding | pfam09030 | Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ... |
2042-2151 | 6.07e-30 | |||||||
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery. : Pssm-ID: 462659 [Multi-domain] Cd Length: 111 Bit Score: 115.70 E-value: 6.07e-30
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
369-436 | 3.38e-28 | |||||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. : Pssm-ID: 460457 Cd Length: 72 Bit Score: 109.40 E-value: 3.38e-28
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| ZZ_CBP | cd02337 | Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ... |
1712-1752 | 1.04e-27 | |||||||
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear. : Pssm-ID: 239077 Cd Length: 41 Bit Score: 106.88 E-value: 1.04e-27
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
1777-1845 | 1.77e-23 | |||||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. : Pssm-ID: 460457 Cd Length: 72 Bit Score: 95.92 E-value: 1.77e-23
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| PHD_SF super family | cl22851 | PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ... |
1286-1320 | 1.76e-18 | |||||||
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies. The actual alignment was detected with superfamily member cd15646: Pssm-ID: 473978 Cd Length: 40 Bit Score: 80.68 E-value: 1.76e-18
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| Med15 super family | cl26621 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
2038-2448 | 2.31e-13 | |||||||
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development. The actual alignment was detected with superfamily member pfam09606: Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 75.82 E-value: 2.31e-13
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| Atrophin-1 super family | cl38111 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
679-1063 | 7.27e-10 | |||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. The actual alignment was detected with superfamily member pfam03154: Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 64.79 E-value: 7.27e-10
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| Med15 super family | cl26621 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
1873-2192 | 1.36e-06 | |||||||
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development. The actual alignment was detected with superfamily member pfam09606: Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 53.86 E-value: 1.36e-06
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| Name | Accession | Description | Interval | E-value | |||||||
| HAT_KAT11 | pfam08214 | Histone acetylation protein; Histone acetylation is required in many cellular processes ... |
1349-1656 | 2.06e-94 | |||||||
Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11. Pssm-ID: 400497 Cd Length: 348 Bit Score: 310.10 E-value: 2.06e-94
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| Bromo_cbp_like | cd05495 | Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ... |
1094-1201 | 2.88e-76 | |||||||
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99927 Cd Length: 108 Bit Score: 248.13 E-value: 2.88e-76
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| KIX | pfam02172 | KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ... |
592-672 | 2.00e-47 | |||||||
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun. Pssm-ID: 366953 Cd Length: 81 Bit Score: 164.59 E-value: 2.00e-47
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| RING_CBP-p300 | cd15802 | atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ... |
1213-1285 | 1.93e-33 | |||||||
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902. Pssm-ID: 276805 Cd Length: 73 Bit Score: 124.32 E-value: 1.93e-33
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| BROMO | smart00297 | bromo domain; |
1091-1199 | 2.12e-33 | |||||||
bromo domain; Pssm-ID: 197636 [Multi-domain] Cd Length: 107 Bit Score: 125.47 E-value: 2.12e-33
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| Creb_binding | pfam09030 | Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ... |
2042-2151 | 6.07e-30 | |||||||
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery. Pssm-ID: 462659 [Multi-domain] Cd Length: 111 Bit Score: 115.70 E-value: 6.07e-30
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
369-436 | 3.38e-28 | |||||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. Pssm-ID: 460457 Cd Length: 72 Bit Score: 109.40 E-value: 3.38e-28
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| ZZ_CBP | cd02337 | Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ... |
1712-1752 | 1.04e-27 | |||||||
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear. Pssm-ID: 239077 Cd Length: 41 Bit Score: 106.88 E-value: 1.04e-27
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
1777-1845 | 1.77e-23 | |||||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. Pssm-ID: 460457 Cd Length: 72 Bit Score: 95.92 E-value: 1.77e-23
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
1771-1849 | 3.28e-23 | |||||||
TAZ zinc finger, present in p300 and CBP; Pssm-ID: 214717 Cd Length: 79 Bit Score: 95.51 E-value: 3.28e-23
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| RING_CBP-p300 | pfam06001 | CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ... |
1199-1238 | 3.87e-23 | |||||||
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902. Pssm-ID: 399179 Cd Length: 40 Bit Score: 93.92 E-value: 3.87e-23
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
369-439 | 6.79e-21 | |||||||
TAZ zinc finger, present in p300 and CBP; Pssm-ID: 214717 Cd Length: 79 Bit Score: 88.58 E-value: 6.79e-21
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| Bromodomain | pfam00439 | Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ... |
1111-1187 | 4.74e-20 | |||||||
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 425683 [Multi-domain] Cd Length: 84 Bit Score: 86.60 E-value: 4.74e-20
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| PHD_p300 | cd15646 | PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ... |
1286-1320 | 1.76e-18 | |||||||
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CREB-binding protein (CBP). It is involved in E1A function in cell cycle progression and cellular differentiation. It functions as an intrinsic HAT, as well as a factor acetyltransferase (FAT) for many transcription regulators. And thus, p300 serves as a scaffold or bridge for transcription factors and other components of the basal transcription machinery to facilitate chromatin remodeling and to activate gene transcription. p300 contains a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain. Pssm-ID: 277116 Cd Length: 40 Bit Score: 80.68 E-value: 1.76e-18
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1708-1750 | 3.04e-17 | |||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 77.09 E-value: 3.04e-17
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| NCBD_CREBBP-p300_like | cd20910 | Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ... |
2103-2145 | 1.82e-16 | |||||||
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) binding protein (CREBBP, also known as CBP) and its paralog p300; CREBBP (also called CBP) and its paralog p300, generally referred to as CREBBP/p300, are universal transcriptional coactivators that interact with many important transcription factors and comodulators to activate transcription. The NCBD domain [nuclear coactivator binding domain, also known as IRF-3 binding domain (IBiD) or SRC1 interaction domain (SID)] of CREBBP/p300 behaves as an intrinsically disordered domain in isolation, but folds into helical structures with different topologies upon binding to different ligands such as nuclear receptor coactivator p160, CREBBP interaction domain (CID) from nuclear receptor coactivator 1 (NCOA1 or Src1), NCOA2 (Tif2), and NCOA3 (ACTR), or interferon regulatory factor 3 (IRF-3). In Drosophila, there is only one CREB-binding protein ortholog and it is called nejire, dCBP, CBP/p300, or CBP. Pssm-ID: 411021 [Multi-domain] Cd Length: 43 Bit Score: 75.00 E-value: 1.82e-16
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
1708-1749 | 5.25e-16 | |||||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 73.67 E-value: 5.25e-16
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| COG5076 | COG5076 | Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ... |
1105-1204 | 5.13e-15 | |||||||
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription]; Pssm-ID: 227408 [Multi-domain] Cd Length: 371 Bit Score: 79.46 E-value: 5.13e-15
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| Med15 | pfam09606 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
2038-2448 | 2.31e-13 | |||||||
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development. Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 75.82 E-value: 2.31e-13
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| Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
679-1063 | 7.27e-10 | |||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 64.79 E-value: 7.27e-10
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| Med15 | pfam09606 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
1873-2192 | 1.36e-06 | |||||||
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development. Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 53.86 E-value: 1.36e-06
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
619-1007 | 2.50e-05 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 2.50e-05
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| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
855-908 | 8.86e-04 | |||||||
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide. Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 42.47 E-value: 8.86e-04
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| PABP-1234 | TIGR01628 | polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
1978-2135 | 3.69e-03 | |||||||
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range. Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 42.49 E-value: 3.69e-03
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| PABP-1234 | TIGR01628 | polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
726-891 | 5.28e-03 | |||||||
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range. Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 42.10 E-value: 5.28e-03
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| PRK10263 | PRK10263 | DNA translocase FtsK; Provisional |
2302-2405 | 7.20e-03 | |||||||
DNA translocase FtsK; Provisional Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.99 E-value: 7.20e-03
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| PABP-1234 | TIGR01628 | polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
2126-2259 | 7.49e-03 | |||||||
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range. Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 41.33 E-value: 7.49e-03
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| Name | Accession | Description | Interval | E-value | |||||||
| HAT_KAT11 | pfam08214 | Histone acetylation protein; Histone acetylation is required in many cellular processes ... |
1349-1656 | 2.06e-94 | |||||||
Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11. Pssm-ID: 400497 Cd Length: 348 Bit Score: 310.10 E-value: 2.06e-94
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| Bromo_cbp_like | cd05495 | Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ... |
1094-1201 | 2.88e-76 | |||||||
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99927 Cd Length: 108 Bit Score: 248.13 E-value: 2.88e-76
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| KIX | pfam02172 | KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP ... |
592-672 | 2.00e-47 | |||||||
KIX domain; CBP and P300 bind to the CREB via a domain known as KIX. The KIX domain of CBP also binds to transactivation domains of other nuclear factors including Myb and Jun. Pssm-ID: 366953 Cd Length: 81 Bit Score: 164.59 E-value: 2.00e-47
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| RING_CBP-p300 | cd15802 | atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ... |
1213-1285 | 1.93e-33 | |||||||
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902. Pssm-ID: 276805 Cd Length: 73 Bit Score: 124.32 E-value: 1.93e-33
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| BROMO | smart00297 | bromo domain; |
1091-1199 | 2.12e-33 | |||||||
bromo domain; Pssm-ID: 197636 [Multi-domain] Cd Length: 107 Bit Score: 125.47 E-value: 2.12e-33
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| Bromodomain | cd04369 | Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ... |
1097-1193 | 4.50e-30 | |||||||
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine. Pssm-ID: 99922 [Multi-domain] Cd Length: 99 Bit Score: 115.55 E-value: 4.50e-30
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| Creb_binding | pfam09030 | Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices ... |
2042-2151 | 6.07e-30 | |||||||
Creb binding; The Creb binding domain assumes a structure comprising of three alpha-helices which pack in a bundle, exposing a hydrophobic groove between alpha-1 and alpha-3 within which complimentary domains found in the protein 'activator for thyroid hormone and retinoid receptors' (ACTR) can dock. Docking of these domains is required for the recruitment of RNA polymerase II and the basal transcription machinery. Pssm-ID: 462659 [Multi-domain] Cd Length: 111 Bit Score: 115.70 E-value: 6.07e-30
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| Bromo_Brdt_II_like | cd05498 | Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ... |
1117-1193 | 1.52e-29 | |||||||
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99930 Cd Length: 102 Bit Score: 114.30 E-value: 1.52e-29
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
369-436 | 3.38e-28 | |||||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. Pssm-ID: 460457 Cd Length: 72 Bit Score: 109.40 E-value: 3.38e-28
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| ZZ_CBP | cd02337 | Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ... |
1712-1752 | 1.04e-27 | |||||||
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear. Pssm-ID: 239077 Cd Length: 41 Bit Score: 106.88 E-value: 1.04e-27
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| Bromo_gcn5_like | cd05509 | Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ... |
1096-1193 | 6.17e-27 | |||||||
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99941 [Multi-domain] Cd Length: 101 Bit Score: 106.87 E-value: 6.17e-27
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| Bromo_plant1 | cd05506 | Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ... |
1110-1193 | 8.62e-26 | |||||||
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99938 Cd Length: 99 Bit Score: 103.56 E-value: 8.62e-26
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| Bromo_BDF1_2_I | cd05500 | Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ... |
1104-1193 | 1.81e-24 | |||||||
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99932 Cd Length: 103 Bit Score: 99.70 E-value: 1.81e-24
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| zf-TAZ | pfam02135 | TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ... |
1777-1845 | 1.77e-23 | |||||||
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC. Pssm-ID: 460457 Cd Length: 72 Bit Score: 95.92 E-value: 1.77e-23
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
1771-1849 | 3.28e-23 | |||||||
TAZ zinc finger, present in p300 and CBP; Pssm-ID: 214717 Cd Length: 79 Bit Score: 95.51 E-value: 3.28e-23
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| RING_CBP-p300 | pfam06001 | CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also ... |
1199-1238 | 3.87e-23 | |||||||
CREB-binding protein/p300, atypical RING domain; CBP (CREB-binding protein) and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This RING domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902. Pssm-ID: 399179 Cd Length: 40 Bit Score: 93.92 E-value: 3.87e-23
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| Bromo_Brdt_I_like | cd05497 | Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ... |
1099-1192 | 3.44e-22 | |||||||
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99929 Cd Length: 107 Bit Score: 93.64 E-value: 3.44e-22
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| Bromo_tif1_like | cd05502 | Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ... |
1092-1193 | 6.68e-22 | |||||||
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99934 [Multi-domain] Cd Length: 109 Bit Score: 92.74 E-value: 6.68e-22
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| Bromo_WDR9_II | cd05496 | Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ... |
1114-1199 | 3.97e-21 | |||||||
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99928 Cd Length: 119 Bit Score: 90.98 E-value: 3.97e-21
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| ZnF_TAZ | smart00551 | TAZ zinc finger, present in p300 and CBP; |
369-439 | 6.79e-21 | |||||||
TAZ zinc finger, present in p300 and CBP; Pssm-ID: 214717 Cd Length: 79 Bit Score: 88.58 E-value: 6.79e-21
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| Bromo_Acf1_like | cd05504 | Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ... |
1095-1195 | 1.18e-20 | |||||||
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99936 Cd Length: 115 Bit Score: 89.38 E-value: 1.18e-20
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| Bromodomain | pfam00439 | Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ... |
1111-1187 | 4.74e-20 | |||||||
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 425683 [Multi-domain] Cd Length: 84 Bit Score: 86.60 E-value: 4.74e-20
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| Bromo_BDF1_2_II | cd05499 | Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ... |
1117-1193 | 4.91e-20 | |||||||
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99931 Cd Length: 102 Bit Score: 86.96 E-value: 4.91e-20
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| PHD_p300 | cd15646 | PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated ... |
1286-1320 | 1.76e-18 | |||||||
PHD finger found in histone acetyltransferase p300; p300, also termed KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CREB-binding protein (CBP). It is involved in E1A function in cell cycle progression and cellular differentiation. It functions as an intrinsic HAT, as well as a factor acetyltransferase (FAT) for many transcription regulators. And thus, p300 serves as a scaffold or bridge for transcription factors and other components of the basal transcription machinery to facilitate chromatin remodeling and to activate gene transcription. p300 contains a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain. Pssm-ID: 277116 Cd Length: 40 Bit Score: 80.68 E-value: 1.76e-18
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| Bromo_SPT7_like | cd05510 | Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ... |
1095-1185 | 1.93e-17 | |||||||
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99942 [Multi-domain] Cd Length: 112 Bit Score: 80.18 E-value: 1.93e-17
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1708-1750 | 3.04e-17 | |||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 77.09 E-value: 3.04e-17
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| NCBD_CREBBP-p300_like | cd20910 | Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) ... |
2103-2145 | 1.82e-16 | |||||||
Nuclear Coactivator Binding Domain (NCBD) of CREB (cyclic AMP response element binding protein) binding protein (CREBBP, also known as CBP) and its paralog p300; CREBBP (also called CBP) and its paralog p300, generally referred to as CREBBP/p300, are universal transcriptional coactivators that interact with many important transcription factors and comodulators to activate transcription. The NCBD domain [nuclear coactivator binding domain, also known as IRF-3 binding domain (IBiD) or SRC1 interaction domain (SID)] of CREBBP/p300 behaves as an intrinsically disordered domain in isolation, but folds into helical structures with different topologies upon binding to different ligands such as nuclear receptor coactivator p160, CREBBP interaction domain (CID) from nuclear receptor coactivator 1 (NCOA1 or Src1), NCOA2 (Tif2), and NCOA3 (ACTR), or interferon regulatory factor 3 (IRF-3). In Drosophila, there is only one CREB-binding protein ortholog and it is called nejire, dCBP, CBP/p300, or CBP. Pssm-ID: 411021 [Multi-domain] Cd Length: 43 Bit Score: 75.00 E-value: 1.82e-16
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| PHD_CBP_p300 | cd15557 | PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300 ... |
1287-1318 | 1.90e-16 | |||||||
PHD finger found in CREB-binding protein (CBP) and histone acetyltransferase p300; This p300/CBP family includes two highly homologous histone acetyltransferases (HATs), CREB-binding protein (CBP) and p300. CBP is also known as KAT3A or CREBBP. It specifically interacts with the phosphorylated form of cyclic adenosine monophosphate-responsive element-binding protein (CREB). p300, also termed as KAT3B, or E1A-associated protein p300 (EP300), is a paralog of CBP. and is involved in E1A function in cell cycle progression and cellular differentiation. Both CBP and p300 are co-activator proteins that have been implicated in cell cycle regulation, apoptosis, embryonic development, cellular differentiation and cancer. They associate with a number of DNA-binding transcription activators as well as general transcription factors (GTFs), thus mediating recruitment of basal transcription machinery to the promoter. They contain a cysteine-histidine rich region, KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain. Pssm-ID: 277032 Cd Length: 37 Bit Score: 74.61 E-value: 1.90e-16
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| Bromo_brd1_like | cd05512 | Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ... |
1100-1190 | 4.54e-16 | |||||||
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99944 Cd Length: 98 Bit Score: 75.51 E-value: 4.54e-16
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
1708-1749 | 5.25e-16 | |||||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 73.67 E-value: 5.25e-16
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| PHD_CBP | cd15647 | PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an ... |
1287-1320 | 3.87e-15 | |||||||
PHD finger found in CREB-binding protein (CBP); CBP, also termed as KAT3A, is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CBP is also known as CREBBP, since it specifically interacts with the phosphorylated form of cyclic adenosine monophosphate-responsive element-binding protein (CREB). It augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. CBP contains a cysteine-histidine rich region, a KIX (CREB interaction) domain, a plant homeodomain (PHD) finger, a HAT domain, followed by a SRC interaction domain. Pssm-ID: 277117 Cd Length: 40 Bit Score: 71.17 E-value: 3.87e-15
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| Bromo_BAZ2A_B_like | cd05503 | Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ... |
1113-1181 | 4.68e-15 | |||||||
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99935 Cd Length: 97 Bit Score: 72.79 E-value: 4.68e-15
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| Bromo_AAA | cd05528 | Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ... |
1111-1198 | 4.87e-15 | |||||||
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver Pssm-ID: 99957 Cd Length: 112 Bit Score: 73.16 E-value: 4.87e-15
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| COG5076 | COG5076 | Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ... |
1105-1204 | 5.13e-15 | |||||||
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription]; Pssm-ID: 227408 [Multi-domain] Cd Length: 371 Bit Score: 79.46 E-value: 5.13e-15
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| Bromo_TFIID | cd05511 | Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ... |
1110-1218 | 1.24e-14 | |||||||
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99943 [Multi-domain] Cd Length: 112 Bit Score: 71.91 E-value: 1.24e-14
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| Bromo_polybromo_V | cd05515 | Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ... |
1130-1183 | 7.73e-14 | |||||||
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine. Pssm-ID: 99946 Cd Length: 105 Bit Score: 69.64 E-value: 7.73e-14
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| Bromo_polybromo_I | cd05524 | Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ... |
1130-1202 | 1.41e-13 | |||||||
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine. Pssm-ID: 99954 [Multi-domain] Cd Length: 113 Bit Score: 69.28 E-value: 1.41e-13
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| PHD_HAC_like | cd15614 | PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ... |
1243-1318 | 1.82e-13 | |||||||
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. Pssm-ID: 277086 Cd Length: 73 Bit Score: 67.38 E-value: 1.82e-13
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| Med15 | pfam09606 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
2038-2448 | 2.31e-13 | |||||||
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development. Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 75.82 E-value: 2.31e-13
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| Bromo_brd8_like | cd05507 | Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ... |
1098-1183 | 4.76e-13 | |||||||
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with the thyroid hormone receptor in a ligand-dependent fashion and enhances thyroid hormone-dependent activation from thyroid response elements. Brd8 is thought to be a nuclear receptor coactivator. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99939 Cd Length: 104 Bit Score: 67.39 E-value: 4.76e-13
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| Bromo_WSTF_like | cd05505 | Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ... |
1093-1181 | 1.63e-12 | |||||||
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99937 Cd Length: 97 Bit Score: 65.64 E-value: 1.63e-12
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| ZZ | cd02249 | Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
1712-1752 | 2.08e-12 | |||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins. Pssm-ID: 239069 [Multi-domain] Cd Length: 46 Bit Score: 63.61 E-value: 2.08e-12
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| Bromo_Rsc1_2_I | cd05521 | Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ... |
1096-1184 | 2.09e-11 | |||||||
Bromodomain, repeat I in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99952 Cd Length: 106 Bit Score: 62.73 E-value: 2.09e-11
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| Bromo_SNF2L2 | cd05516 | Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ... |
1117-1192 | 2.78e-11 | |||||||
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99947 Cd Length: 107 Bit Score: 62.45 E-value: 2.78e-11
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| Bromo_brd7_like | cd05513 | Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ... |
1097-1188 | 3.68e-11 | |||||||
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown to inhibit cell growth and the progression of the cell cycle by regulating cell-cycle genes at the transcriptional level. BRD7 has been identified as a gene involved in nasopharyngeal carcinoma. The protein interacts with acetylated histone H3 via its bromodomain. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99945 Cd Length: 98 Bit Score: 61.66 E-value: 3.68e-11
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| Bromo_polybromo_III | cd05520 | Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ... |
1130-1188 | 8.52e-11 | |||||||
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine. Pssm-ID: 99951 Cd Length: 103 Bit Score: 60.82 E-value: 8.52e-11
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| Bromo_Rsc1_2_II | cd05522 | Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ... |
1130-1188 | 1.98e-10 | |||||||
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99953 [Multi-domain] Cd Length: 104 Bit Score: 59.95 E-value: 1.98e-10
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| Bromo_polybromo_IV | cd05518 | Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ... |
1119-1182 | 4.26e-10 | |||||||
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine. Pssm-ID: 99949 [Multi-domain] Cd Length: 103 Bit Score: 59.00 E-value: 4.26e-10
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| Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
679-1063 | 7.27e-10 | |||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 64.79 E-value: 7.27e-10
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| Bromo_SNF2 | cd05519 | Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ... |
1097-1193 | 1.40e-09 | |||||||
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99950 Cd Length: 103 Bit Score: 57.35 E-value: 1.40e-09
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| Med15 | pfam09606 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
1984-2367 | 1.82e-09 | |||||||
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development. Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 63.10 E-value: 1.82e-09
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| Bromo_WDR9_I_like | cd05529 | Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ... |
1095-1192 | 9.76e-09 | |||||||
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99958 Cd Length: 128 Bit Score: 55.81 E-value: 9.76e-09
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| Bromo_ASH1 | cd05525 | Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ... |
1124-1193 | 5.48e-08 | |||||||
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99955 [Multi-domain] Cd Length: 106 Bit Score: 52.78 E-value: 5.48e-08
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| Bromo_polybromo_II | cd05517 | Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ... |
1124-1194 | 8.29e-08 | |||||||
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine. Pssm-ID: 99948 Cd Length: 103 Bit Score: 52.44 E-value: 8.29e-08
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| ZZ_NBR1_like | cd02340 | Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ... |
1713-1752 | 1.03e-07 | |||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain. Pssm-ID: 239080 Cd Length: 43 Bit Score: 49.95 E-value: 1.03e-07
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| Bromodomain_1 | cd05494 | Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ... |
1095-1152 | 9.97e-07 | |||||||
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine. Pssm-ID: 99926 [Multi-domain] Cd Length: 114 Bit Score: 49.75 E-value: 9.97e-07
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| Med15 | pfam09606 | ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
1873-2192 | 1.36e-06 | |||||||
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development. Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 53.86 E-value: 1.36e-06
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| Bromo_SP100C_like | cd05501 | Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ... |
1129-1193 | 5.30e-06 | |||||||
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major component of PML-SP100 nuclear bodies (NBs), which are poorly understood. It is covalently modified by SUMO-1 and may play a role in processes at the chromatin level. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99933 Cd Length: 102 Bit Score: 47.04 E-value: 5.30e-06
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| Glutenin_hmw | pfam03157 | High molecular weight glutenin subunit; Members of this family include high molecular weight ... |
1988-2436 | 1.40e-05 | |||||||
High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm. Pssm-ID: 367362 [Multi-domain] Cd Length: 786 Bit Score: 50.72 E-value: 1.40e-05
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
619-1007 | 2.50e-05 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 2.50e-05
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| ZZ_ADA2 | cd02335 | Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ... |
1712-1748 | 2.75e-05 | |||||||
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239075 [Multi-domain] Cd Length: 49 Bit Score: 43.44 E-value: 2.75e-05
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| PAT1 | pfam09770 | Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
2296-2447 | 3.61e-05 | |||||||
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division. Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 49.26 E-value: 3.61e-05
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| PAT1 | pfam09770 | Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
1976-2143 | 5.70e-05 | |||||||
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division. Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 48.49 E-value: 5.70e-05
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| ZZ_Mind_bomb | cd02339 | Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ... |
1714-1751 | 7.66e-05 | |||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster. Pssm-ID: 239079 Cd Length: 45 Bit Score: 42.06 E-value: 7.66e-05
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| Bromo_RACK7 | cd05508 | Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ... |
1095-1191 | 2.00e-04 | |||||||
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) was identified as a potential tumor suppressor genes, it shares domain architecture with BS69/ZMYND11; both have been implicated in the regulation of cellular proliferation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. Pssm-ID: 99940 Cd Length: 99 Bit Score: 42.76 E-value: 2.00e-04
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| ZZ_dah | cd02345 | Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ... |
1713-1749 | 2.06e-04 | |||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila. Pssm-ID: 239085 Cd Length: 49 Bit Score: 41.04 E-value: 2.06e-04
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| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
769-1007 | 2.38e-04 | |||||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 46.45 E-value: 2.38e-04
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| PAT1 | pfam09770 | Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
783-903 | 2.40e-04 | |||||||
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division. Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 46.57 E-value: 2.40e-04
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| PHA03269 | PHA03269 | envelope glycoprotein C; Provisional |
779-905 | 4.60e-04 | |||||||
envelope glycoprotein C; Provisional Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 45.49 E-value: 4.60e-04
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| ZZ_ZZZ3 | cd02341 | Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ... |
1712-1751 | 5.07e-04 | |||||||
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239081 Cd Length: 48 Bit Score: 39.72 E-value: 5.07e-04
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| ZZ_HERC2 | cd02344 | Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ... |
1713-1748 | 7.73e-04 | |||||||
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239084 Cd Length: 45 Bit Score: 39.10 E-value: 7.73e-04
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| Amelogenin | smart00818 | Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ... |
855-908 | 8.86e-04 | |||||||
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide. Pssm-ID: 197891 [Multi-domain] Cd Length: 165 Bit Score: 42.47 E-value: 8.86e-04
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| Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
818-1012 | 1.72e-03 | |||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 43.99 E-value: 1.72e-03
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| PAT1 | pfam09770 | Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
2114-2219 | 2.91e-03 | |||||||
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division. Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 43.10 E-value: 2.91e-03
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| PABP-1234 | TIGR01628 | polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
1978-2135 | 3.69e-03 | |||||||
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range. Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 42.49 E-value: 3.69e-03
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| ZZ_PCMF_like | cd02338 | Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ... |
1713-1743 | 5.22e-03 | |||||||
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination. Pssm-ID: 239078 Cd Length: 49 Bit Score: 36.94 E-value: 5.22e-03
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| PABP-1234 | TIGR01628 | polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
726-891 | 5.28e-03 | |||||||
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range. Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 42.10 E-value: 5.28e-03
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| DUF4175 | pfam13779 | Domain of unknown function (DUF4175); |
1979-2196 | 5.70e-03 | |||||||
Domain of unknown function (DUF4175); Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 41.90 E-value: 5.70e-03
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| Cytadhesin_P30 | pfam07271 | Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ... |
2114-2221 | 5.75e-03 | |||||||
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat. Pssm-ID: 429374 [Multi-domain] Cd Length: 275 Bit Score: 41.11 E-value: 5.75e-03
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| PRK10263 | PRK10263 | DNA translocase FtsK; Provisional |
2302-2405 | 7.20e-03 | |||||||
DNA translocase FtsK; Provisional Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.99 E-value: 7.20e-03
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| PABP-1234 | TIGR01628 | polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
2126-2259 | 7.49e-03 | |||||||
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range. Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 41.33 E-value: 7.49e-03
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