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Conserved domains on  [gi|442619618|ref|NP_001262672|]
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splicing factor 1, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SF1-HH super family cl37905
Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is ...
 274-334 1.41e-22

Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is mainly found in splicing factor 1 from yeast to human. It is a helix-hairpin domain, which forms a secondary, hydrophobic interface with U2AF65(UHM) to lock the orientation of the two subunits, which is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex. In this domain, it contains a highly conserved SPSP motif in its C terminal and phophorylation of SPSP motif induces a disorder-to-order transition within a novel SF1/U2AF65 interface, indicating a phosphorylation-dependent control of pre-mRNA splicing factors.


The actual alignment was detected with superfamily member pfam16275:

Pssm-ID: 465080  Cd Length: 114  Bit Score: 91.13  E-value: 1.41e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619618  274 RKSRWGG--SENDKTFIPGMPTILPSTLDPAQQEAYLVQFQIEEISRKLRTGDLGITQNPEER 334
Cdd:pfam16275   1 RKSRWGGepEKTDKPPIPGLPTAIPGGLTPEQLDAYLLQFRIEEITRKLRTGDLGVPPSPEER 63
 
Name Accession Description Interval E-value
SF1-HH pfam16275
Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is ...
 274-334 1.41e-22

Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is mainly found in splicing factor 1 from yeast to human. It is a helix-hairpin domain, which forms a secondary, hydrophobic interface with U2AF65(UHM) to lock the orientation of the two subunits, which is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex. In this domain, it contains a highly conserved SPSP motif in its C terminal and phophorylation of SPSP motif induces a disorder-to-order transition within a novel SF1/U2AF65 interface, indicating a phosphorylation-dependent control of pre-mRNA splicing factors.


Pssm-ID: 465080  Cd Length: 114  Bit Score: 91.13  E-value: 1.41e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619618  274 RKSRWGG--SENDKTFIPGMPTILPSTLDPAQQEAYLVQFQIEEISRKLRTGDLGITQNPEER 334
Cdd:pfam16275   1 RKSRWGGepEKTDKPPIPGLPTAIPGGLTPEQLDAYLLQFRIEEITRKLRTGDLGVPPSPEER 63
 
Name Accession Description Interval E-value
SF1-HH pfam16275
Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is ...
 274-334 1.41e-22

Splicing factor 1 helix-hairpin domain; This domain, approximately 100 residues in length, is mainly found in splicing factor 1 from yeast to human. It is a helix-hairpin domain, which forms a secondary, hydrophobic interface with U2AF65(UHM) to lock the orientation of the two subunits, which is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex. In this domain, it contains a highly conserved SPSP motif in its C terminal and phophorylation of SPSP motif induces a disorder-to-order transition within a novel SF1/U2AF65 interface, indicating a phosphorylation-dependent control of pre-mRNA splicing factors.


Pssm-ID: 465080  Cd Length: 114  Bit Score: 91.13  E-value: 1.41e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442619618  274 RKSRWGG--SENDKTFIPGMPTILPSTLDPAQQEAYLVQFQIEEISRKLRTGDLGITQNPEER 334
Cdd:pfam16275   1 RKSRWGGepEKTDKPPIPGLPTAIPGGLTPEQLDAYLLQFRIEEITRKLRTGDLGVPPSPEER 63
 
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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