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Conserved domains on  [gi|667282310|ref|XP_008574726|]
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PREDICTED: taperin [Galeopterus variegatus]

Protein Classification

Phostensin domain-containing protein( domain architecture ID 10621587)

Phostensin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phostensin pfam13914
Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 ...
 280-421 2.83e-63

Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 regulatory protein binding PP1 at the KISF motif. The domain also appears to carry an incomplete incomplete SH3-binding domain PxRxP further upstream. It is likely that Phostensin targets PP1 to the F-actin cytoskeleton. Phostensin binds to actin and decreases the elongation and depolymerization rates of actin filament pointed ends.


:

Pssm-ID: 464038 [Multi-domain]  Cd Length: 138  Bit Score: 203.25  E-value: 2.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667282310  280 PQEAKLPCSEIGAPPRYRLHPARPGHTLEPQHRGSNTFTVVPKRKPGTLQEQhlgqaANGEPQPQEAKEEED-GSLLGPR 358
Cdd:pfam13914   1 PSTAKLPSSNIGSPLQYFPHPGGPSHSSELQHRGGNTFTVVPRRKPGGLQSQ-----ANSEPPSQPTAEEEEaPSLVGPD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 667282310  359 AAPGTTPKKRYPTVHEIEVIGGYLALQKSCLTKAGSSRKKMKISFNDKSLQTTFEYPSESSLV 421
Cdd:pfam13914  76 ATLGGTLKKRYPTVHEIEVIGGYLALDKSCLVKAGSSRKKMKISFNEKSLETTFEYPSESSLL 138
 
Name Accession Description Interval E-value
Phostensin pfam13914
Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 ...
 280-421 2.83e-63

Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 regulatory protein binding PP1 at the KISF motif. The domain also appears to carry an incomplete incomplete SH3-binding domain PxRxP further upstream. It is likely that Phostensin targets PP1 to the F-actin cytoskeleton. Phostensin binds to actin and decreases the elongation and depolymerization rates of actin filament pointed ends.


Pssm-ID: 464038 [Multi-domain]  Cd Length: 138  Bit Score: 203.25  E-value: 2.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667282310  280 PQEAKLPCSEIGAPPRYRLHPARPGHTLEPQHRGSNTFTVVPKRKPGTLQEQhlgqaANGEPQPQEAKEEED-GSLLGPR 358
Cdd:pfam13914   1 PSTAKLPSSNIGSPLQYFPHPGGPSHSSELQHRGGNTFTVVPRRKPGGLQSQ-----ANSEPPSQPTAEEEEaPSLVGPD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 667282310  359 AAPGTTPKKRYPTVHEIEVIGGYLALQKSCLTKAGSSRKKMKISFNDKSLQTTFEYPSESSLV 421
Cdd:pfam13914  76 ATLGGTLKKRYPTVHEIEVIGGYLALDKSCLVKAGSSRKKMKISFNEKSLETTFEYPSESSLL 138
 
Name Accession Description Interval E-value
Phostensin pfam13914
Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 ...
 280-421 2.83e-63

Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 regulatory protein binding PP1 at the KISF motif. The domain also appears to carry an incomplete incomplete SH3-binding domain PxRxP further upstream. It is likely that Phostensin targets PP1 to the F-actin cytoskeleton. Phostensin binds to actin and decreases the elongation and depolymerization rates of actin filament pointed ends.


Pssm-ID: 464038 [Multi-domain]  Cd Length: 138  Bit Score: 203.25  E-value: 2.83e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 667282310  280 PQEAKLPCSEIGAPPRYRLHPARPGHTLEPQHRGSNTFTVVPKRKPGTLQEQhlgqaANGEPQPQEAKEEED-GSLLGPR 358
Cdd:pfam13914   1 PSTAKLPSSNIGSPLQYFPHPGGPSHSSELQHRGGNTFTVVPRRKPGGLQSQ-----ANSEPPSQPTAEEEEaPSLVGPD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 667282310  359 AAPGTTPKKRYPTVHEIEVIGGYLALQKSCLTKAGSSRKKMKISFNDKSLQTTFEYPSESSLV 421
Cdd:pfam13914  76 ATLGGTLKKRYPTVHEIEVIGGYLALDKSCLVKAGSSRKKMKISFNEKSLETTFEYPSESSLL 138
 
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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