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Conserved domains on  [gi|24586214|ref|NP_724547|]
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ELL-associated factor, isoform A [Drosophila melanogaster]

Protein Classification

ELL-associated factor( domain architecture ID 10561279)

EAF family ELL-associated factor acts as a transcriptional transactivator of ELL and ELL2 elongation activities

Gene Ontology:  GO:0006355|GO:0003711|GO:0008023|GO:0006368

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EAF pfam09816
RNA polymerase II transcription elongation factor; Members of this family act as ...
 23-122 5.62e-28

RNA polymerase II transcription elongation factor; Members of this family act as transcriptional transactivators of ELL and ELL2 elongation activities.3]. Eaf proteins form a stable heterodimer complex with ELL proteins to facilitate the binding of RNA polymerase II to activate transcription elongation. The N-terminus of approx 120 residues is globular and highly conserved.


:

Pssm-ID: 462913  Cd Length: 101  Bit Score: 106.99  E-value: 5.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586214    23 LKLGATF--NPKNTSTAFHTIKYDFKPASVDTSRMASVDVG--SNNQVTVTVPNSEssgvPHTVYKGNQREY-AKECLMI 97
Cdd:pfam09816   1 IVLGDSLanLGKSSSSEFTTIRYNFKPASVDASKPGTLTVSssDNDEVSYELPIND----GTYVFEGSRDPYkEKDCVLI 76

                          90       100
                  ....*....|....*....|....*
gi 24586214    98 YDKETGAITIEKLNHNIQVKKTRNE 122
Cdd:pfam09816  77 FDPETKTFVLERLDSTLRFNLTRAP 101
 
Name Accession Description Interval E-value
EAF pfam09816
RNA polymerase II transcription elongation factor; Members of this family act as ...
 23-122 5.62e-28

RNA polymerase II transcription elongation factor; Members of this family act as transcriptional transactivators of ELL and ELL2 elongation activities.3]. Eaf proteins form a stable heterodimer complex with ELL proteins to facilitate the binding of RNA polymerase II to activate transcription elongation. The N-terminus of approx 120 residues is globular and highly conserved.


Pssm-ID: 462913  Cd Length: 101  Bit Score: 106.99  E-value: 5.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586214    23 LKLGATF--NPKNTSTAFHTIKYDFKPASVDTSRMASVDVG--SNNQVTVTVPNSEssgvPHTVYKGNQREY-AKECLMI 97
Cdd:pfam09816   1 IVLGDSLanLGKSSSSEFTTIRYNFKPASVDASKPGTLTVSssDNDEVSYELPIND----GTYVFEGSRDPYkEKDCVLI 76

                          90       100
                  ....*....|....*....|....*
gi 24586214    98 YDKETGAITIEKLNHNIQVKKTRNE 122
Cdd:pfam09816  77 FDPETKTFVLERLDSTLRFNLTRAP 101
 
Name Accession Description Interval E-value
EAF pfam09816
RNA polymerase II transcription elongation factor; Members of this family act as ...
 23-122 5.62e-28

RNA polymerase II transcription elongation factor; Members of this family act as transcriptional transactivators of ELL and ELL2 elongation activities.3]. Eaf proteins form a stable heterodimer complex with ELL proteins to facilitate the binding of RNA polymerase II to activate transcription elongation. The N-terminus of approx 120 residues is globular and highly conserved.


Pssm-ID: 462913  Cd Length: 101  Bit Score: 106.99  E-value: 5.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586214    23 LKLGATF--NPKNTSTAFHTIKYDFKPASVDTSRMASVDVG--SNNQVTVTVPNSEssgvPHTVYKGNQREY-AKECLMI 97
Cdd:pfam09816   1 IVLGDSLanLGKSSSSEFTTIRYNFKPASVDASKPGTLTVSssDNDEVSYELPIND----GTYVFEGSRDPYkEKDCVLI 76

                          90       100
                  ....*....|....*....|....*
gi 24586214    98 YDKETGAITIEKLNHNIQVKKTRNE 122
Cdd:pfam09816  77 FDPETKTFVLERLDSTLRFNLTRAP 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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