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Conserved domains on  [gi|1776945285|ref|NP_001363709|]
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pre-mRNA 3'-end-processing factor FIP1 isoform 39 [Homo sapiens]

Protein Classification

pre-mRNA polyadenylation factor Fip1 domain-containing protein( domain architecture ID 10524433)

pre-mRNA polyadenylation factor Fip1 domain-containing protein such as human FIP1, which is a component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition

Gene Ontology:  GO:0006397
PubMed:  11238938

Graphical summary

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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 ...
 139-181 2.98e-28

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: 106.10  E-value: 2.98e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1776945285 139 EVDLDSFEDKPWRKPGADLSDYFNYGFNEDTWKAYCEKQKRIR 181
Cdd:pfam05182   1 DVDLDSFEEKPWRRPGADISDYFNYGFDEETWKEYCKKQEQLR 43
 
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 ...
 139-181 2.98e-28

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: 106.10  E-value: 2.98e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1776945285 139 EVDLDSFEDKPWRKPGADLSDYFNYGFNEDTWKAYCEKQKRIR 181
Cdd:pfam05182   1 DVDLDSFEEKPWRRPGADISDYFNYGFDEETWKEYCKKQEQLR 43
FIP1 COG5213
Polyadenylation factor I complex, subunit FIP1 [RNA processing and modification];
120-181 1.13e-21

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


Pssm-ID: 227538  Cd Length: 266  Bit Score: 94.72  E-value: 1.13e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776945285 120 KVKGVDLDAPGSINGVPLLEVDLDSFEDKPWRKPGADLSDYFNYGFNEDTWKAYCEKQKRIR 181
Cdd:COG5213   101 KTPEIDEDKEETEDGQNILDIDIESFKDKPWRKPGADISDYFNYGFNEFTWKEYCHMQEKLQ 162
 
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 ...
 139-181 2.98e-28

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: 106.10  E-value: 2.98e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1776945285 139 EVDLDSFEDKPWRKPGADLSDYFNYGFNEDTWKAYCEKQKRIR 181
Cdd:pfam05182   1 DVDLDSFEEKPWRRPGADISDYFNYGFDEETWKEYCKKQEQLR 43
FIP1 COG5213
Polyadenylation factor I complex, subunit FIP1 [RNA processing and modification];
120-181 1.13e-21

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


Pssm-ID: 227538  Cd Length: 266  Bit Score: 94.72  E-value: 1.13e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776945285 120 KVKGVDLDAPGSINGVPLLEVDLDSFEDKPWRKPGADLSDYFNYGFNEDTWKAYCEKQKRIR 181
Cdd:COG5213   101 KTPEIDEDKEETEDGQNILDIDIESFKDKPWRKPGADISDYFNYGFNEFTWKEYCHMQEKLQ 162
 
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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