NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24644016|ref|NP_649476|]
View 

factor interacting with poly(A) polymerase 1 [Drosophila melanogaster]

Protein Classification

FF domain-containing protein( domain architecture ID 10524461)

FF domain-containing protein is involved in protein-protein interactions, similar to mammalian PRPF40 homologs A and B that may be involved in pre-mRNA splicing

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Fip1 pfam05182
Fip1 motif; This short motif is about 40 amino acids in length. In the Fip1 protein that is a ...
 219-261 1.29e-24

Fip1 motif; This short motif is about 40 amino acids in length. In the Fip1 protein that is a component of a yeast pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase. This region of Fip1 is needed for the interaction with the Th1 subunit of the complex and for specific polyadenylation of the cleaved mRNA precursor.


:

Pssm-ID: 461573  Cd Length: 43  Bit Score: 96.47  E-value: 1.29e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 24644016   219 EFSIDSLEEKPWRKPGADITDYFNYGFNEETWRAYCERQKRFR 261
Cdd:pfam05182   1 DVDLDSFEEKPWRRPGADISDYFNYGFDEETWKEYCKKQEQLR 43
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 530-579 3.25e-12

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


:

Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 61.32  E-value: 3.25e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24644016   530 QLRKDFLDMLRErHDIERHTRWYDIKKKFEADPRYRALDS-SYREEYFEDY 579
Cdd:pfam01846   1 KAREAFKELLKE-HKITPYSTWSEIKKKIENDPRYKALLDgSEREELFEDY 50
 
Name Accession Description Interval E-value
Fip1 pfam05182
Fip1 motif; This short motif is about 40 amino acids in length. In the Fip1 protein that is a ...
 219-261 1.29e-24

Fip1 motif; This short motif is about 40 amino acids in length. In the Fip1 protein that is a component of a yeast pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase. This region of Fip1 is needed for the interaction with the Th1 subunit of the complex and for specific polyadenylation of the cleaved mRNA precursor.


Pssm-ID: 461573  Cd Length: 43  Bit Score: 96.47  E-value: 1.29e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 24644016   219 EFSIDSLEEKPWRKPGADITDYFNYGFNEETWRAYCERQKRFR 261
Cdd:pfam05182   1 DVDLDSFEEKPWRRPGADISDYFNYGFDEETWKEYCKKQEQLR 43
FIP1 COG5213
Polyadenylation factor I complex, subunit FIP1 [RNA processing and modification];
205-261 3.85e-17

Polyadenylation factor I complex, subunit FIP1 [RNA processing and modification];


Pssm-ID: 227538  Cd Length: 266  Bit Score: 82.01  E-value: 3.85e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24644016 205 DFEGAGTINGVAVHEFSIDSLEEKPWRKPGADITDYFNYGFNEETWRAYCERQKRFR 261
Cdd:COG5213 106 DEDKEETEDGQNILDIDIESFKDKPWRKPGADISDYFNYGFNEFTWKEYCHMQEKLQ 162
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 530-579 3.25e-12

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 61.32  E-value: 3.25e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24644016   530 QLRKDFLDMLRErHDIERHTRWYDIKKKFEADPRYRALDS-SYREEYFEDY 579
Cdd:pfam01846   1 KAREAFKELLKE-HKITPYSTWSEIKKKIENDPRYKALLDgSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 529-581 3.95e-08

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 50.26  E-value: 3.95e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24644016    529 DQLRKDFLDMLRERHDIERHTRWYDIKKKFEADPRYRALDS-SYREEYFEDYLH 581
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSeSEREQLFEDHIE 54
 
Name Accession Description Interval E-value
Fip1 pfam05182
Fip1 motif; This short motif is about 40 amino acids in length. In the Fip1 protein that is a ...
 219-261 1.29e-24

Fip1 motif; This short motif is about 40 amino acids in length. In the Fip1 protein that is a component of a yeast pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase. This region of Fip1 is needed for the interaction with the Th1 subunit of the complex and for specific polyadenylation of the cleaved mRNA precursor.


Pssm-ID: 461573  Cd Length: 43  Bit Score: 96.47  E-value: 1.29e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 24644016   219 EFSIDSLEEKPWRKPGADITDYFNYGFNEETWRAYCERQKRFR 261
Cdd:pfam05182   1 DVDLDSFEEKPWRRPGADISDYFNYGFDEETWKEYCKKQEQLR 43
FIP1 COG5213
Polyadenylation factor I complex, subunit FIP1 [RNA processing and modification];
205-261 3.85e-17

Polyadenylation factor I complex, subunit FIP1 [RNA processing and modification];


Pssm-ID: 227538  Cd Length: 266  Bit Score: 82.01  E-value: 3.85e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24644016 205 DFEGAGTINGVAVHEFSIDSLEEKPWRKPGADITDYFNYGFNEETWRAYCERQKRFR 261
Cdd:COG5213 106 DEDKEETEDGQNILDIDIESFKDKPWRKPGADISDYFNYGFNEFTWKEYCHMQEKLQ 162
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 530-579 3.25e-12

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 61.32  E-value: 3.25e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24644016   530 QLRKDFLDMLRErHDIERHTRWYDIKKKFEADPRYRALDS-SYREEYFEDY 579
Cdd:pfam01846   1 KAREAFKELLKE-HKITPYSTWSEIKKKIENDPRYKALLDgSEREELFEDY 50
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 529-581 3.95e-08

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 50.26  E-value: 3.95e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24644016    529 DQLRKDFLDMLRERHDIERHTRWYDIKKKFEADPRYRALDS-SYREEYFEDYLH 581
Cdd:smart00441   1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSeSEREQLFEDHIE 54
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH