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Conserved domains on  [gi|4505751|ref|NP_002619|]
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profilin-2 isoform b [Homo sapiens]

Protein Classification

PROF domain-containing protein (domain architecture ID 10647785)

PROF domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
2-139 3.25e-44

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


:

Pssm-ID: 214646  Cd Length: 129  Bit Score: 140.92  E-value: 3.25e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751       2 AGWQSYVDNLMCDGCCQEAAIVGYCDAkYVWAATAGGVFQSITPIEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDsly 79
Cdd:smart00392   1 MSWQAYVDNLLVGSGCVDAAAIGGKDG-SVWAASAGGNFQKITPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA--- 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751      80 vDGDCTMDIRtksqggePTYNVAVGRAGRALVIVMGKEGVHGGTLNKKAYELALYLRRSD 139
Cdd:smart00392  77 -DDRSIMGKK-------GAGGVVIVKTKQALIIGMYKEGVQPGQANKTVEKLADYLRSSG 128
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
2-139 3.25e-44

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 140.92  E-value: 3.25e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751       2 AGWQSYVDNLMCDGCCQEAAIVGYCDAkYVWAATAGGVFQSITPIEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDsly 79
Cdd:smart00392   1 MSWQAYVDNLLVGSGCVDAAAIGGKDG-SVWAASAGGNFQKITPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA--- 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751      80 vDGDCTMDIRtksqggePTYNVAVGRAGRALVIVMGKEGVHGGTLNKKAYELALYLRRSD 139
Cdd:smart00392  77 -DDRSIMGKK-------GAGGVVIVKTKQALIIGMYKEGVQPGQANKTVEKLADYLRSSG 128
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
3-139 4.99e-41

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: 132.83  E-value: 4.99e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751    3 GWQSYVD-NLMCDGCCQEAAIVGYCDaKYVWAATAGgvFQSITPIEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSly 79
Cdd:cd00148   1 SWQAYVDdNLLGTGKVDSAAIVGHDD-GSVWAASAG--GFNLTPEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRAD-- 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751   80 vdgDCTMDIRTKSQGgeptynVAVGRAGRALVIVMGKEGVHGGTLNKKAYELALYLRRSD 139
Cdd:cd00148  76 ---DRSIYGKKGAGG------VVIVKTKQALVIGMYEEGVQPGQANKVVEKLADYLRSQG 126
Profilin pfam00235
Profilin;
3-136 9.03e-33

Profilin;


Pssm-ID: 333948  Cd Length: 124  Bit Score: 111.87  E-value: 9.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751      3 GWQSYVD-NLMCDGCCQEAAIVGYcDAKYVWAATAGgvFQsITPIEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSLY 79
Cdd:pfam00235   2 SWQAYVDdNLVGTGHVDKAAIIGL-DGGSVWAASPG--FN-LTPEEIKAIVAafKDPSKLQANGITLGGEKYMVLRADDR 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505751     80 VdgdctmdIRTKSQGGeptyNVAVGRAGRALVIVMGKEGVHGGTLNKKAYELALYLR 136
Cdd:pfam00235  78 S-------IYGKKGKE----GIVIVKTKQAIVIAHYDEGVQPGNANKAVEKLADYLR 123
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
2-139 3.25e-44

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 140.92  E-value: 3.25e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751       2 AGWQSYVDNLMCDGCCQEAAIVGYCDAkYVWAATAGGVFQSITPIEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDsly 79
Cdd:smart00392   1 MSWQAYVDNLLVGSGCVDAAAIGGKDG-SVWAASAGGNFQKITPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA--- 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751      80 vDGDCTMDIRtksqggePTYNVAVGRAGRALVIVMGKEGVHGGTLNKKAYELALYLRRSD 139
Cdd:smart00392  77 -DDRSIMGKK-------GAGGVVIVKTKQALIIGMYKEGVQPGQANKTVEKLADYLRSSG 128
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
3-139 4.99e-41

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: 132.83  E-value: 4.99e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751    3 GWQSYVD-NLMCDGCCQEAAIVGYCDaKYVWAATAGgvFQSITPIEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSly 79
Cdd:cd00148   1 SWQAYVDdNLLGTGKVDSAAIVGHDD-GSVWAASAG--GFNLTPEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRAD-- 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751   80 vdgDCTMDIRTKSQGgeptynVAVGRAGRALVIVMGKEGVHGGTLNKKAYELALYLRRSD 139
Cdd:cd00148  76 ---DRSIYGKKGAGG------VVIVKTKQALVIGMYEEGVQPGQANKVVEKLADYLRSQG 126
Profilin pfam00235
Profilin;
3-136 9.03e-33

Profilin;


Pssm-ID: 333948  Cd Length: 124  Bit Score: 111.87  E-value: 9.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505751      3 GWQSYVD-NLMCDGCCQEAAIVGYcDAKYVWAATAGgvFQsITPIEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSLY 79
Cdd:pfam00235   2 SWQAYVDdNLVGTGHVDKAAIIGL-DGGSVWAASPG--FN-LTPEEIKAIVAafKDPSKLQANGITLGGEKYMVLRADDR 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505751     80 VdgdctmdIRTKSQGGeptyNVAVGRAGRALVIVMGKEGVHGGTLNKKAYELALYLR 136
Cdd:pfam00235  78 S-------IYGKKGKE----GIVIVKTKQAIVIAHYDEGVQPGNANKAVEKLADYLR 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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