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Conserved domains on  [gi|1820480111|ref|NP_001365818|]
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phostensin isoform 2 [Mus musculus]

Protein Classification

Phostensin_N and Phostensin domain-containing protein( domain architecture ID 10621600)

Phostensin_N and Phostensin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phostensin super family cl16473
Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 ...
 468-583 2.66e-30

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.


The actual alignment was detected with superfamily member pfam13914:

Pssm-ID: 464038 [Multi-domain]  Cd Length: 138  Bit Score: 115.81  E-value: 2.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480111 468 GDPLMSRLFYGVKPG-PG--VGAPRRSGHTFTVNPRRCAPPASP--------------APPVNPATADAAGSGSGKKRYP 530
Cdd:pfam13914   8 SSNIGSPLQYFPHPGgPShsSELQHRGGNTFTVVPRRKPGGLQSqanseppsqptaeeEEAPSLVGPDATLGGTLKKRYP 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1820480111 531 TAEEILVLGGYLRLSRSCLVKGSPERhhKQLKISFSETALETTYQYPSESSVL 583
Cdd:pfam13914  88 TVHEIEVIGGYLALDKSCLVKAGSSR--KKMKISFNEKSLETTFEYPSESSLL 138
Phostensin_N pfam13916
PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 ...
 71-160 1.15e-22

PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 regulatory protein binding protein. This domain is N-terminal to the PP1- and SH3-binding regions though may carry an additional SH3-binding motif. 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: 464039  Cd Length: 84  Bit Score: 92.21  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480111  71 AERDRLSqMPAWKRGILERRRAKLGLPPGEGSPvpGNAEagPPDPDESAVLLEAIGPVHQNRFIqQERQRQQQQQQQQRN 150
Cdd:pfam13916   1 GPGPRTA-MPAWKREILERRRAKLAALGGGAGP--GAAE--PAGPDERLVLAESLGPLHENPFM-RLESERRRQGQAPAQ 74

                          90
                  ....*....|
gi 1820480111 151 EVLGDRKAGP 160
Cdd:pfam13916  75 QLLEDYRRVP 84
 
Name Accession Description Interval E-value
Phostensin pfam13914
Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 ...
 468-583 2.66e-30

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: 115.81  E-value: 2.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480111 468 GDPLMSRLFYGVKPG-PG--VGAPRRSGHTFTVNPRRCAPPASP--------------APPVNPATADAAGSGSGKKRYP 530
Cdd:pfam13914   8 SSNIGSPLQYFPHPGgPShsSELQHRGGNTFTVVPRRKPGGLQSqanseppsqptaeeEEAPSLVGPDATLGGTLKKRYP 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1820480111 531 TAEEILVLGGYLRLSRSCLVKGSPERhhKQLKISFSETALETTYQYPSESSVL 583
Cdd:pfam13914  88 TVHEIEVIGGYLALDKSCLVKAGSSR--KKMKISFNEKSLETTFEYPSESSLL 138
Phostensin_N pfam13916
PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 ...
 71-160 1.15e-22

PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 regulatory protein binding protein. This domain is N-terminal to the PP1- and SH3-binding regions though may carry an additional SH3-binding motif. 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: 464039  Cd Length: 84  Bit Score: 92.21  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480111  71 AERDRLSqMPAWKRGILERRRAKLGLPPGEGSPvpGNAEagPPDPDESAVLLEAIGPVHQNRFIqQERQRQQQQQQQQRN 150
Cdd:pfam13916   1 GPGPRTA-MPAWKREILERRRAKLAALGGGAGP--GAAE--PAGPDERLVLAESLGPLHENPFM-RLESERRRQGQAPAQ 74

                          90
                  ....*....|
gi 1820480111 151 EVLGDRKAGP 160
Cdd:pfam13916  75 QLLEDYRRVP 84
 
Name Accession Description Interval E-value
Phostensin pfam13914
Phostensin PP1-binding and SH3-binding region; Phostensin has been identified as a PP1 ...
 468-583 2.66e-30

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: 115.81  E-value: 2.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480111 468 GDPLMSRLFYGVKPG-PG--VGAPRRSGHTFTVNPRRCAPPASP--------------APPVNPATADAAGSGSGKKRYP 530
Cdd:pfam13914   8 SSNIGSPLQYFPHPGgPShsSELQHRGGNTFTVVPRRKPGGLQSqanseppsqptaeeEEAPSLVGPDATLGGTLKKRYP 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1820480111 531 TAEEILVLGGYLRLSRSCLVKGSPERhhKQLKISFSETALETTYQYPSESSVL 583
Cdd:pfam13914  88 TVHEIEVIGGYLALDKSCLVKAGSSR--KKMKISFNEKSLETTFEYPSESSLL 138
Phostensin_N pfam13916
PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 ...
 71-160 1.15e-22

PP1-regulatory protein, Phostensin N-terminal; Phostensin has been identified as a PP1 regulatory protein binding protein. This domain is N-terminal to the PP1- and SH3-binding regions though may carry an additional SH3-binding motif. 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: 464039  Cd Length: 84  Bit Score: 92.21  E-value: 1.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820480111  71 AERDRLSqMPAWKRGILERRRAKLGLPPGEGSPvpGNAEagPPDPDESAVLLEAIGPVHQNRFIqQERQRQQQQQQQQRN 150
Cdd:pfam13916   1 GPGPRTA-MPAWKREILERRRAKLAALGGGAGP--GAAE--PAGPDERLVLAESLGPLHENPFM-RLESERRRQGQAPAQ 74

                          90
                  ....*....|
gi 1820480111 151 EVLGDRKAGP 160
Cdd:pfam13916  75 QLLEDYRRVP 84
 
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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