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Conserved domains on  [gi|2201827613|ref|XP_046792879|]
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RNA polymerase II elongation factor ELL2 isoform X2 [Gallus gallus]

Protein Classification

ELL and Occludin_ELL domain-containing protein( domain architecture ID 12105631)

ELL and Occludin_ELL domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ELL pfam10390
RNA polymerase II elongation factor ELL; ELL is a family of RNA polymerase II elongation ...
34-274 3.33e-138

RNA polymerase II elongation factor ELL; ELL is a family of RNA polymerase II elongation factors. It is bound stably to elongation-associated factors 1 and 2, EAFs, and together these act as a strong regulator of transcription activity. by direct interaction with Pol II. ELL binds to pol II on its own but the affinity is greatly increased by the cooperation of EAF. Some members carry an Occludin domain pfam07303 just downstream. There is no S. cerevisiae member.


:

Pssm-ID: 463068  Cd Length: 281  Bit Score: 403.97  E-value: 3.33e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613  34 DLVPSQPSIQFQGRQGLIKIPKVDHPNESHTFNFYLSNVGKDNPQGSFDCVQQTASSSGASQLSSlGLIQNKITVCATND 113
Cdd:pfam10390  41 LSLSSQPTIQFQGNQGRIKIPRSDNGSEVRTFTFYLSNVGKDNPQGSFDCIQQYVSSGSEQLECL-GSIQDKITVCATDD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613 114 SYQMTKERMTQAEEELRNRSAKVIKPGGPYLGKRVQIRKAPQSIPDPVPERKRSTPINPANTIRRTHANNAVSQRPYRDR 193
Cdd:pfam10390 120 SYQKTRERMAQAEEETRSRSAIVIKPGGTYIGKKVQIRKPAPAASDAAPSRKRSSPSNPASTIRKTNSSSDVSQRPLRER 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613 194 VIHLLALKTYKKPELLARLQRDGVNLKDRNSLTAVLQQVANLNPKDNSYTLKDYLYKDIQKDWPGYNEVDKQTLELILSR 273
Cdd:pfam10390 200 VIHLLALKPYKKPELLLRLQKDGLSQKDKNSLGSILQEVANLNPKDNTYTLKDHLYKEVQKDWPGYSEGDRQLLKRILVR 279

                  .
gi 2201827613 274 K 274
Cdd:pfam10390 280 K 280
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
518-619 4.89e-47

Occludin homology domain; This domain represents a conserved region approximately 100 residues long within eukaryotic occludin proteins and the RNA polymerase II elongation factor ELL. Occludin is an integral membrane protein that localizes to tight junctions, while ELL is an elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by polymerase at multiple sites along the DNA. This shared domain is thought to mediate protein interactions.


:

Pssm-ID: 462140 [Multi-domain]  Cd Length: 101  Bit Score: 160.39  E-value: 4.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613 518 YIAIVSYEQRQSYKDDFNAEYDEYRNLHARMESITRKFMKLDEQRKQLSPGSKEYQMLHEEVLEEYRKIQQsSPNYREEK 597
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEILQEYKKKKK-DPEYQEKK 79
                          90       100
                  ....*....|....*....|..
gi 2201827613 598 HRCEYLHNKLSHIKRLIGEFDQ 619
Cdd:pfam07303  80 KRCEYLHNKLSHIKRLILEYDQ 101
 
Name Accession Description Interval E-value
ELL pfam10390
RNA polymerase II elongation factor ELL; ELL is a family of RNA polymerase II elongation ...
34-274 3.33e-138

RNA polymerase II elongation factor ELL; ELL is a family of RNA polymerase II elongation factors. It is bound stably to elongation-associated factors 1 and 2, EAFs, and together these act as a strong regulator of transcription activity. by direct interaction with Pol II. ELL binds to pol II on its own but the affinity is greatly increased by the cooperation of EAF. Some members carry an Occludin domain pfam07303 just downstream. There is no S. cerevisiae member.


Pssm-ID: 463068  Cd Length: 281  Bit Score: 403.97  E-value: 3.33e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613  34 DLVPSQPSIQFQGRQGLIKIPKVDHPNESHTFNFYLSNVGKDNPQGSFDCVQQTASSSGASQLSSlGLIQNKITVCATND 113
Cdd:pfam10390  41 LSLSSQPTIQFQGNQGRIKIPRSDNGSEVRTFTFYLSNVGKDNPQGSFDCIQQYVSSGSEQLECL-GSIQDKITVCATDD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613 114 SYQMTKERMTQAEEELRNRSAKVIKPGGPYLGKRVQIRKAPQSIPDPVPERKRSTPINPANTIRRTHANNAVSQRPYRDR 193
Cdd:pfam10390 120 SYQKTRERMAQAEEETRSRSAIVIKPGGTYIGKKVQIRKPAPAASDAAPSRKRSSPSNPASTIRKTNSSSDVSQRPLRER 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613 194 VIHLLALKTYKKPELLARLQRDGVNLKDRNSLTAVLQQVANLNPKDNSYTLKDYLYKDIQKDWPGYNEVDKQTLELILSR 273
Cdd:pfam10390 200 VIHLLALKPYKKPELLLRLQKDGLSQKDKNSLGSILQEVANLNPKDNTYTLKDHLYKEVQKDWPGYSEGDRQLLKRILVR 279

                  .
gi 2201827613 274 K 274
Cdd:pfam10390 280 K 280
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
518-619 4.89e-47

Occludin homology domain; This domain represents a conserved region approximately 100 residues long within eukaryotic occludin proteins and the RNA polymerase II elongation factor ELL. Occludin is an integral membrane protein that localizes to tight junctions, while ELL is an elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by polymerase at multiple sites along the DNA. This shared domain is thought to mediate protein interactions.


Pssm-ID: 462140 [Multi-domain]  Cd Length: 101  Bit Score: 160.39  E-value: 4.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613 518 YIAIVSYEQRQSYKDDFNAEYDEYRNLHARMESITRKFMKLDEQRKQLSPGSKEYQMLHEEVLEEYRKIQQsSPNYREEK 597
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEILQEYKKKKK-DPEYQEKK 79
                          90       100
                  ....*....|....*....|..
gi 2201827613 598 HRCEYLHNKLSHIKRLIGEFDQ 619
Cdd:pfam07303  80 KRCEYLHNKLSHIKRLILEYDQ 101
 
Name Accession Description Interval E-value
ELL pfam10390
RNA polymerase II elongation factor ELL; ELL is a family of RNA polymerase II elongation ...
34-274 3.33e-138

RNA polymerase II elongation factor ELL; ELL is a family of RNA polymerase II elongation factors. It is bound stably to elongation-associated factors 1 and 2, EAFs, and together these act as a strong regulator of transcription activity. by direct interaction with Pol II. ELL binds to pol II on its own but the affinity is greatly increased by the cooperation of EAF. Some members carry an Occludin domain pfam07303 just downstream. There is no S. cerevisiae member.


Pssm-ID: 463068  Cd Length: 281  Bit Score: 403.97  E-value: 3.33e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613  34 DLVPSQPSIQFQGRQGLIKIPKVDHPNESHTFNFYLSNVGKDNPQGSFDCVQQTASSSGASQLSSlGLIQNKITVCATND 113
Cdd:pfam10390  41 LSLSSQPTIQFQGNQGRIKIPRSDNGSEVRTFTFYLSNVGKDNPQGSFDCIQQYVSSGSEQLECL-GSIQDKITVCATDD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613 114 SYQMTKERMTQAEEELRNRSAKVIKPGGPYLGKRVQIRKAPQSIPDPVPERKRSTPINPANTIRRTHANNAVSQRPYRDR 193
Cdd:pfam10390 120 SYQKTRERMAQAEEETRSRSAIVIKPGGTYIGKKVQIRKPAPAASDAAPSRKRSSPSNPASTIRKTNSSSDVSQRPLRER 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613 194 VIHLLALKTYKKPELLARLQRDGVNLKDRNSLTAVLQQVANLNPKDNSYTLKDYLYKDIQKDWPGYNEVDKQTLELILSR 273
Cdd:pfam10390 200 VIHLLALKPYKKPELLLRLQKDGLSQKDKNSLGSILQEVANLNPKDNTYTLKDHLYKEVQKDWPGYSEGDRQLLKRILVR 279

                  .
gi 2201827613 274 K 274
Cdd:pfam10390 280 K 280
Occludin_ELL pfam07303
Occludin homology domain; This domain represents a conserved region approximately 100 residues ...
518-619 4.89e-47

Occludin homology domain; This domain represents a conserved region approximately 100 residues long within eukaryotic occludin proteins and the RNA polymerase II elongation factor ELL. Occludin is an integral membrane protein that localizes to tight junctions, while ELL is an elongation factor that can increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by polymerase at multiple sites along the DNA. This shared domain is thought to mediate protein interactions.


Pssm-ID: 462140 [Multi-domain]  Cd Length: 101  Bit Score: 160.39  E-value: 4.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201827613 518 YIAIVSYEQRQSYKDDFNAEYDEYRNLHARMESITRKFMKLDEQRKQLSPGSKEYQMLHEEVLEEYRKIQQsSPNYREEK 597
Cdd:pfam07303   1 YPPITSDEQRQRYKQEFNAEYDEYKELHAELDAVSRKFQKLDRELKSLPEGSKEYQDIAEEILQEYKKKKK-DPEYQEKK 79
                          90       100
                  ....*....|....*....|..
gi 2201827613 598 HRCEYLHNKLSHIKRLIGEFDQ 619
Cdd:pfam07303  80 KRCEYLHNKLSHIKRLILEYDQ 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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