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Conserved domains on  [gi|767914467|ref|XP_011531125|]
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profilin-4 isoform X1 [Homo sapiens]

Protein Classification

profilin( domain architecture ID 10066278)

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 cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
 14-129 1.01e-45

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: 144.39  E-value: 1.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914467  14 GTKHVDSAALIKIQERSLCVASPG-FNVTPSDVRTLVNGFaKNPLQARREGLYFKGKDYRCVRADEYSLYAKNENTGVVV 92
Cdd:cd00148   12 GTGKVDSAAIVGHDDGSVWAASAGgFNLTPEEVGTLVAGF-KDPDGVFSTGLTLGGQKYMVIRADDRSIYGKKGAGGVVI 90

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767914467  93 VKTHLYLLVATYTEGMYPSICVEATESLGDYLRKKGS 129
Cdd:cd00148   91 VKTKQALVIGMYEEGVQPGQANKVVEKLADYLRSQGY 127
 
Name Accession Description Interval E-value
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
 14-129 1.01e-45

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: 144.39  E-value: 1.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914467  14 GTKHVDSAALIKIQERSLCVASPG-FNVTPSDVRTLVNGFaKNPLQARREGLYFKGKDYRCVRADEYSLYAKNENTGVVV 92
Cdd:cd00148   12 GTGKVDSAAIVGHDDGSVWAASAGgFNLTPEEVGTLVAGF-KDPDGVFSTGLTLGGQKYMVIRADDRSIYGKKGAGGVVI 90

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767914467  93 VKTHLYLLVATYTEGMYPSICVEATESLGDYLRKKGS 129
Cdd:cd00148   91 VKTKQALVIGMYEEGVQPGQANKVVEKLADYLRSQGY 127
Profilin pfam00235
Profilin;
14-126 4.56e-45

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 142.69  E-value: 4.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914467   14 GTKHVDSAALIKIQERSLCVASPGFNVTPSDVRTLVNGFaKNPLQARREGLYFKGKDYRCVRADEYSLYAKNENTGVVVV 93
Cdd:pfam00235  13 GTGHVDKAAIIGLDGGSVWASSPGFNLSPEEIKAIVAAF-KDPSKLQANGITLGGKKYMVIRADDRSIYGKKGKEGIVIV 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767914467   94 KTHLYLLVATYTEGMYPSICVEATESLGDYLRK 126
Cdd:pfam00235  92 KTKQAIIIGHYDEGVQPGNANKAVEKLADYLRS 124
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
 14-128 3.00e-17

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 71.97  E-value: 3.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914467    14 GTKHVDSAALIKIQErSLCVASPGFNV---TPSDVRTLVNGFaKNPLQARREGLYFKGKDYRCVRADEYSLYAKNENTGV 90
Cdd:smart00392  13 GSGCVDAAAIGGKDG-SVWAASAGGNFqkiTPEEIAAIAALF-NSLAAVFSNGLTLGGQKYMVIRADDRSIMGKKGAGGV 90

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767914467    91 VVVKTHLYLLVATYTEGMYPSICVEATESLGDYLRKKG 128
Cdd:smart00392  91 VIVKTKQALIIGMYKEGVQPGQANKTVEKLADYLRSSG 128
 
Name Accession Description Interval E-value
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
 14-129 1.01e-45

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: 144.39  E-value: 1.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914467  14 GTKHVDSAALIKIQERSLCVASPG-FNVTPSDVRTLVNGFaKNPLQARREGLYFKGKDYRCVRADEYSLYAKNENTGVVV 92
Cdd:cd00148   12 GTGKVDSAAIVGHDDGSVWAASAGgFNLTPEEVGTLVAGF-KDPDGVFSTGLTLGGQKYMVIRADDRSIYGKKGAGGVVI 90

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767914467  93 VKTHLYLLVATYTEGMYPSICVEATESLGDYLRKKGS 129
Cdd:cd00148   91 VKTKQALVIGMYEEGVQPGQANKVVEKLADYLRSQGY 127
Profilin pfam00235
Profilin;
14-126 4.56e-45

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 142.69  E-value: 4.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914467   14 GTKHVDSAALIKIQERSLCVASPGFNVTPSDVRTLVNGFaKNPLQARREGLYFKGKDYRCVRADEYSLYAKNENTGVVVV 93
Cdd:pfam00235  13 GTGHVDKAAIIGLDGGSVWASSPGFNLSPEEIKAIVAAF-KDPSKLQANGITLGGKKYMVIRADDRSIYGKKGKEGIVIV 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 767914467   94 KTHLYLLVATYTEGMYPSICVEATESLGDYLRK 126
Cdd:pfam00235  92 KTKQAIIIGHYDEGVQPGNANKAVEKLADYLRS 124
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
 14-128 3.00e-17

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 71.97  E-value: 3.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914467    14 GTKHVDSAALIKIQErSLCVASPGFNV---TPSDVRTLVNGFaKNPLQARREGLYFKGKDYRCVRADEYSLYAKNENTGV 90
Cdd:smart00392  13 GSGCVDAAAIGGKDG-SVWAASAGGNFqkiTPEEIAAIAALF-NSLAAVFSNGLTLGGQKYMVIRADDRSIMGKKGAGGV 90

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 767914467    91 VVVKTHLYLLVATYTEGMYPSICVEATESLGDYLRKKG 128
Cdd:smart00392  91 VIVKTKQALIIGMYKEGVQPGQANKTVEKLADYLRSSG 128
 
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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