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Conserved domains on  [gi|586555659|ref|XP_006926274|]
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profilin-2 isoform X3 [Pteropus alecto]

Protein Classification

profilin( domain architecture ID 735)

profilin binds to actin and affects the structure of the cytoskeleton

CATH:  3.30.450.30
Gene Ontology:  GO:0003779
PubMed:  17682948|28509986
SCOP:  4001840

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PROF super family cl00123
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
 2-109 4.36e-29

Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and poly-L-proline. Profilin can inhibit actin polymerization into F-actin by binding to monomeric actin (G-actin) and terminal F-actin subunits, but - as a regulator of the cytoskeleton - it may also promote actin polymerization. It plays a role in the assembly of branched actin filament networks, by activating WASP via binding to WASP's proline rich domain. Profilin may link the cytoskeleton with major signalling pathways by interacting with components of the phosphatidylinositol cycle and Ras pathway.


The actual alignment was detected with superfamily member smart00392:

Pssm-ID: 469622  Cd Length: 129  Bit Score: 102.02  E-value: 4.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586555659     2 AGWQSYVDNLMCDGCCQEAAIVGYCDAkYVWAATAGGVFQSITPVEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDsly 79
Cdd:smart00392   1 MSWQAYVDNLLVGSGCVDAAAIGGKDG-SVWAASAGGNFQKITPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA--- 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 586555659    80 vDGDCTMDIRtksqggePTYNVAVGRAGRA 109
Cdd:smart00392  77 -DDRSIMGKK-------GAGGVVIVKTKQA 98
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
 2-109 4.36e-29

Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.


Pssm-ID: 214646  Cd Length: 129  Bit Score: 102.02  E-value: 4.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586555659     2 AGWQSYVDNLMCDGCCQEAAIVGYCDAkYVWAATAGGVFQSITPVEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDsly 79
Cdd:smart00392   1 MSWQAYVDNLLVGSGCVDAAAIGGKDG-SVWAASAGGNFQKITPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA--- 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 586555659    80 vDGDCTMDIRtksqggePTYNVAVGRAGRA 109
Cdd:smart00392  77 -DDRSIMGKK-------GAGGVVIVKTKQA 98
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
 3-109 4.10e-26

Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and poly-L-proline. Profilin can inhibit actin polymerization into F-actin by binding to monomeric actin (G-actin) and terminal F-actin subunits, but - as a regulator of the cytoskeleton - it may also promote actin polymerization. It plays a role in the assembly of branched actin filament networks, by activating WASP via binding to WASP's proline rich domain. Profilin may link the cytoskeleton with major signalling pathways by interacting with components of the phosphatidylinositol cycle and Ras pathway.


Pssm-ID: 238085  Cd Length: 127  Bit Score: 94.31  E-value: 4.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586555659   3 GWQSYVD-NLMCDGCCQEAAIVGYCDaKYVWAATAGgvFQSITPVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSly 79
Cdd:cd00148    1 SWQAYVDdNLLGTGKVDSAAIVGHDD-GSVWAASAG--GFNLTPEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRAD-- 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 586555659  80 vdgDCTMDIRTKSQGgeptynVAVGRAGRA 109
Cdd:cd00148   76 ---DRSIYGKKGAGG------VVIVKTKQA 96
Profilin pfam00235
Profilin;
3-109 4.18e-20

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 79.13  E-value: 4.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586555659    3 GWQSYVD-NLMCDGCCQEAAIVGYcDAKYVWAATAGgvFQsITPVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSLY 79
Cdd:pfam00235   2 SWQAYVDdNLLGTGHVDKAAIIGL-DGGSVWASSPG--FN-LSPEEIKAIVAafKDPSKLQANGITLGGKKYMVIRADDR 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 586555659   80 VdgdctmdIRTKSQGGeptyNVAVGRAGRA 109
Cdd:pfam00235  78 S-------IYGKKGKE----GIVIVKTKQA 96
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
 2-109 4.36e-29

Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.


Pssm-ID: 214646  Cd Length: 129  Bit Score: 102.02  E-value: 4.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586555659     2 AGWQSYVDNLMCDGCCQEAAIVGYCDAkYVWAATAGGVFQSITPVEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDsly 79
Cdd:smart00392   1 MSWQAYVDNLLVGSGCVDAAAIGGKDG-SVWAASAGGNFQKITPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA--- 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 586555659    80 vDGDCTMDIRtksqggePTYNVAVGRAGRA 109
Cdd:smart00392  77 -DDRSIMGKK-------GAGGVVIVKTKQA 98
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
 3-109 4.10e-26

Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and poly-L-proline. Profilin can inhibit actin polymerization into F-actin by binding to monomeric actin (G-actin) and terminal F-actin subunits, but - as a regulator of the cytoskeleton - it may also promote actin polymerization. It plays a role in the assembly of branched actin filament networks, by activating WASP via binding to WASP's proline rich domain. Profilin may link the cytoskeleton with major signalling pathways by interacting with components of the phosphatidylinositol cycle and Ras pathway.


Pssm-ID: 238085  Cd Length: 127  Bit Score: 94.31  E-value: 4.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586555659   3 GWQSYVD-NLMCDGCCQEAAIVGYCDaKYVWAATAGgvFQSITPVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSly 79
Cdd:cd00148    1 SWQAYVDdNLLGTGKVDSAAIVGHDD-GSVWAASAG--GFNLTPEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRAD-- 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 586555659  80 vdgDCTMDIRTKSQGgeptynVAVGRAGRA 109
Cdd:cd00148   76 ---DRSIYGKKGAGG------VVIVKTKQA 96
Profilin pfam00235
Profilin;
3-109 4.18e-20

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 79.13  E-value: 4.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586555659    3 GWQSYVD-NLMCDGCCQEAAIVGYcDAKYVWAATAGgvFQsITPVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSLY 79
Cdd:pfam00235   2 SWQAYVDdNLLGTGHVDKAAIIGL-DGGSVWASSPG--FN-LSPEEIKAIVAafKDPSKLQANGITLGGKKYMVIRADDR 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 586555659   80 VdgdctmdIRTKSQGGeptyNVAVGRAGRA 109
Cdd:pfam00235  78 S-------IYGKKGKE----GIVIVKTKQA 96
 
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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