hypothetical protein NDA17_003267 [Ustilago hordei]
Protein Classification
POB3 family protein( domain architecture ID 710202)
POB3 family protein such as FACT complex subunit POB3, a component of the FACT complex, which is a general chromatin factor that acts to reorganize nucleosomes
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| POB3 super family | cl28543 | Nucleosome-binding factor SPN, POB3 subunit [Transcription / DNA replication, recombination, ... |
4-475 | 3.44e-143 | |||||||
Nucleosome-binding factor SPN, POB3 subunit [Transcription / DNA replication, recombination, and repair / Chromatin structure and dynamics]; The actual alignment was detected with superfamily member COG5165: Pssm-ID: 227494 [Multi-domain] Cd Length: 508 Bit Score: 422.87 E-value: 3.44e-143
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| Name | Accession | Description | Interval | E-value | |||||||
| POB3 | COG5165 | Nucleosome-binding factor SPN, POB3 subunit [Transcription / DNA replication, recombination, ... |
4-475 | 3.44e-143 | |||||||
Nucleosome-binding factor SPN, POB3 subunit [Transcription / DNA replication, recombination, and repair / Chromatin structure and dynamics]; Pssm-ID: 227494 [Multi-domain] Cd Length: 508 Bit Score: 422.87 E-value: 3.44e-143
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| PH1_SSRP1-like | cd13230 | Structure Specific Recognition protein 1 (SSRP1) Pleckstrin homology (PH) domain, repeat 1; ... |
233-368 | 9.40e-78 | |||||||
Structure Specific Recognition protein 1 (SSRP1) Pleckstrin homology (PH) domain, repeat 1; SSRP1 is a component of FACT (facilitator of chromatin transcription), an essential chromatin reorganizing factor. In yeast FACT (yFACT) is composed of three proteins: Spt16/Cdc68, Pob3, and Nhp6. In metazoans the Pob3 and Nhp6 orthologs are fused to form SSRP1/T160 in human and mouse, respectively. The middle domain of the Pob3 subunit (Pob3-M) has an unusual double pleckstrin homology (PH) architecture. yFACT interacts in a physiologically important way with the central single-strand DNA binding factor RPA to promote a step in DNA Replication. Coordinated function by yFACT and RPA is important during nucleosome deposition. These results support the model that the FACT family has an essential role in constructing nucleosomes during DNA replication, and suggest that RPA contributes to this process. Members of this cd are composed of the first PH-like repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270050 Cd Length: 137 Bit Score: 241.28 E-value: 9.40e-78
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| POB3_N | pfam17292 | POB3-like N-terminal PH domain; This domain is found at the N-terminus of POB3 and related ... |
5-109 | 3.21e-26 | |||||||
POB3-like N-terminal PH domain; This domain is found at the N-terminus of POB3 and related proteins. Pssm-ID: 465400 [Multi-domain] Cd Length: 93 Bit Score: 102.26 E-value: 3.21e-26
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| Name | Accession | Description | Interval | E-value | |||||||
| POB3 | COG5165 | Nucleosome-binding factor SPN, POB3 subunit [Transcription / DNA replication, recombination, ... |
4-475 | 3.44e-143 | |||||||
Nucleosome-binding factor SPN, POB3 subunit [Transcription / DNA replication, recombination, and repair / Chromatin structure and dynamics]; Pssm-ID: 227494 [Multi-domain] Cd Length: 508 Bit Score: 422.87 E-value: 3.44e-143
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| PH1_SSRP1-like | cd13230 | Structure Specific Recognition protein 1 (SSRP1) Pleckstrin homology (PH) domain, repeat 1; ... |
233-368 | 9.40e-78 | |||||||
Structure Specific Recognition protein 1 (SSRP1) Pleckstrin homology (PH) domain, repeat 1; SSRP1 is a component of FACT (facilitator of chromatin transcription), an essential chromatin reorganizing factor. In yeast FACT (yFACT) is composed of three proteins: Spt16/Cdc68, Pob3, and Nhp6. In metazoans the Pob3 and Nhp6 orthologs are fused to form SSRP1/T160 in human and mouse, respectively. The middle domain of the Pob3 subunit (Pob3-M) has an unusual double pleckstrin homology (PH) architecture. yFACT interacts in a physiologically important way with the central single-strand DNA binding factor RPA to promote a step in DNA Replication. Coordinated function by yFACT and RPA is important during nucleosome deposition. These results support the model that the FACT family has an essential role in constructing nucleosomes during DNA replication, and suggest that RPA contributes to this process. Members of this cd are composed of the first PH-like repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270050 Cd Length: 137 Bit Score: 241.28 E-value: 9.40e-78
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| PH2_SSRP1-like | cd13231 | Structure Specific Recognition protein 1 (SSRP1) Pleckstrin homology (PH) domain, repeat 2; ... |
371-470 | 6.12e-46 | |||||||
Structure Specific Recognition protein 1 (SSRP1) Pleckstrin homology (PH) domain, repeat 2; SSRP1 is a component of FACT (facilitator of chromatin transcription), an essential chromatin reorganizing factor. In yeast FACT (yFACT) is composed of three proteins: Spt16/Cdc68, Pob3, and Nhp6. In metazoans the Pob3 and Nhp6 orthologs are fused to form SSRP1/T160 in human and mouse, respectively.The middle domain of the Pob3 subunit (Pob3-M) has an unusual double pleckstrin homology (PH) architecture. yFACT interacts in a physiologically important way with the central single-strand DNA binding factor RPA to promote a step in DNA Replication. Coordinated function by yFACT and RPA is important during nucleosome deposition. These results support the model that the FACT family has an essential role in constructing nucleosomes during DNA replication, and suggest that RPA contributes to this process. Members of this cd are composed of the second PH-like repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270051 Cd Length: 100 Bit Score: 156.50 E-value: 6.12e-46
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| POB3_N | pfam17292 | POB3-like N-terminal PH domain; This domain is found at the N-terminus of POB3 and related ... |
5-109 | 3.21e-26 | |||||||
POB3-like N-terminal PH domain; This domain is found at the N-terminus of POB3 and related proteins. Pssm-ID: 465400 [Multi-domain] Cd Length: 93 Bit Score: 102.26 E-value: 3.21e-26
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| Rtt106 | pfam08512 | Histone chaperone Rttp106-like; This family includes Rttp106, a histone chaperone involved in ... |
380-460 | 8.98e-25 | |||||||
Histone chaperone Rttp106-like; This family includes Rttp106, a histone chaperone involved in heterochromatin-mediated silencing. This domain belongs to the Pleckstrin homology domain superfamily. Pssm-ID: 462500 Cd Length: 84 Bit Score: 97.89 E-value: 8.98e-25
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| SSrecog | pfam03531 | Structure-specific recognition protein (SSRP1); SSRP1 has been implicated in transcriptional ... |
116-192 | 4.04e-24 | |||||||
Structure-specific recognition protein (SSRP1); SSRP1 has been implicated in transcriptional initiation and elongation and in DNA replication and repair. This domain belongs to the Pleckstrin homology fold superfamily. Pssm-ID: 460959 Cd Length: 69 Bit Score: 95.70 E-value: 4.04e-24
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| PH_TFIIH | cd13229 | Transcription Factor II H (TFIIH) Pleckstrin homology (PH) domain; The transcription factor II ... |
377-463 | 1.34e-04 | |||||||
Transcription Factor II H (TFIIH) Pleckstrin homology (PH) domain; The transcription factor II H (TFIIH) is one of the general transcription factors (GTFs) known to be a target of the transactivation domain (TAD) of p53. Human TFIIH and its homologous yeast counterpart (factor b) are composed of ten subunits that can be divided into two groups, the core TFIIH (XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and TTDA/Tfb5 in human/yeast) and the CAK complex (cdk7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3). These two complexes are linked by the XPD/Rad3 subunit. The helicase activities of XPB and XPD are essential to the formation of the open complex during transcription initiation and the kinase activity of cdk7 phosphorylates the C-terminal domain (CTD) of the RNA Pol II largest subunit, enabling RNA Pol II to progress from the initiation phase to the elongation phase of transcription. The PH domain of p62/Tfb1 has been shown to interact with herpes simplex virus protein 16 (VP16) TAD and the binding of p53 TAD is mediated by the TAD2 subdomain. TFIIE recruits TFIIH to complete the preinitiation complex (PIC) formation and regulates enzymatic activities of TFIIH. The PH domain of the human TFIIH p62 subunit binds to the C-terminal acidic (AC) domain of the human TFIIEalpha subunit. This interaction could be a switch to replace p53 with TFIIE on TFIIH in transcription. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270049 Cd Length: 93 Bit Score: 41.10 E-value: 1.34e-04
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| PH_TFIIH | cd13229 | Transcription Factor II H (TFIIH) Pleckstrin homology (PH) domain; The transcription factor II ... |
18-105 | 9.30e-04 | |||||||
Transcription Factor II H (TFIIH) Pleckstrin homology (PH) domain; The transcription factor II H (TFIIH) is one of the general transcription factors (GTFs) known to be a target of the transactivation domain (TAD) of p53. Human TFIIH and its homologous yeast counterpart (factor b) are composed of ten subunits that can be divided into two groups, the core TFIIH (XPB/Ssl2, p62/Tfb1, p52/Tfb2, p44/Ssl1, p34/Tfb4, and TTDA/Tfb5 in human/yeast) and the CAK complex (cdk7/Kin28, cyclin H/Ccl1, and MAT1/Tfb3). These two complexes are linked by the XPD/Rad3 subunit. The helicase activities of XPB and XPD are essential to the formation of the open complex during transcription initiation and the kinase activity of cdk7 phosphorylates the C-terminal domain (CTD) of the RNA Pol II largest subunit, enabling RNA Pol II to progress from the initiation phase to the elongation phase of transcription. The PH domain of p62/Tfb1 has been shown to interact with herpes simplex virus protein 16 (VP16) TAD and the binding of p53 TAD is mediated by the TAD2 subdomain. TFIIE recruits TFIIH to complete the preinitiation complex (PIC) formation and regulates enzymatic activities of TFIIH. The PH domain of the human TFIIH p62 subunit binds to the C-terminal acidic (AC) domain of the human TFIIEalpha subunit. This interaction could be a switch to replace p53 with TFIIE on TFIIH in transcription. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 270049 Cd Length: 93 Bit Score: 38.41 E-value: 9.30e-04
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