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Conserved domains on  [gi|1390124057|ref|XP_025009186|]
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profilin-2 isoform X2 [Gallus gallus]

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 ...
15-117 1.50e-22

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: 444704  Cd Length: 129  Bit Score: 85.07  E-value: 1.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390124057   15 GNVLLREPVEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDslyvDGDCTMDIRtksqggePTYNVAVGRAGRVLVFVMG 92
Cdd:smart00392  36 GNFQKITPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA----DDRSIMGKK-------GAGGVVIVKTKQALIIGMY 104
                           90       100
                   ....*....|....*....|....*
gi 1390124057   93 KEGVHGGGLNKKAYSMAKYLRDSGF 117
Cdd:smart00392 105 KEGVQPGQANKTVEKLADYLRSSGY 129
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
15-117 1.50e-22

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 85.07  E-value: 1.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390124057   15 GNVLLREPVEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDslyvDGDCTMDIRtksqggePTYNVAVGRAGRVLVFVMG 92
Cdd:smart00392  36 GNFQKITPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA----DDRSIMGKK-------GAGGVVIVKTKQALIIGMY 104
                           90       100
                   ....*....|....*....|....*
gi 1390124057   93 KEGVHGGGLNKKAYSMAKYLRDSGF 117
Cdd:smart00392 105 KEGVQPGQANKTVEKLADYLRSSGY 129
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
22-117 1.53e-21

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: 82.37  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390124057  22 PVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSlyvdgDCTMDIRTKSQGgeptynVAVGRAGRVLVFVMGKEGVHGG 99
Cdd:cd00148    41 PEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRAD-----DRSIYGKKGAGG------VVIVKTKQALVIGMYEEGVQPG 109
                          90
                  ....*....|....*...
gi 1390124057 100 GLNKKAYSMAKYLRDSGF 117
Cdd:cd00148   110 QANKVVEKLADYLRSQGY 127
Profilin pfam00235
Profilin;
22-114 2.41e-16

Profilin;


Pssm-ID: 425544  Cd Length: 124  Bit Score: 69.12  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390124057  22 PVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSLYVdgdctmdIRTKSQGGeptyNVAVGRAGRVLVFVMGKEGVHGG 99
Cdd:pfam00235  41 PEEIKAIVAafKDPSKLQANGITLGGKKYMVIRADDRS-------IYGKKGKE----GIVIVKTKQAIIIGHYDEGVQPG 109
                          90
                  ....*....|....*
gi 1390124057 100 GLNKKAYSMAKYLRD 114
Cdd:pfam00235 110 NANKAVEKLADYLRS 124
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
15-117 1.50e-22

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 85.07  E-value: 1.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390124057   15 GNVLLREPVEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDslyvDGDCTMDIRtksqggePTYNVAVGRAGRVLVFVMG 92
Cdd:smart00392  36 GNFQKITPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA----DDRSIMGKK-------GAGGVVIVKTKQALIIGMY 104
                           90       100
                   ....*....|....*....|....*
gi 1390124057   93 KEGVHGGGLNKKAYSMAKYLRDSGF 117
Cdd:smart00392 105 KEGVQPGQANKTVEKLADYLRSSGY 129
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
22-117 1.53e-21

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: 82.37  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390124057  22 PVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSlyvdgDCTMDIRTKSQGgeptynVAVGRAGRVLVFVMGKEGVHGG 99
Cdd:cd00148    41 PEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRAD-----DRSIYGKKGAGG------VVIVKTKQALVIGMYEEGVQPG 109
                          90
                  ....*....|....*...
gi 1390124057 100 GLNKKAYSMAKYLRDSGF 117
Cdd:cd00148   110 QANKVVEKLADYLRSQGY 127
Profilin pfam00235
Profilin;
22-114 2.41e-16

Profilin;


Pssm-ID: 425544  Cd Length: 124  Bit Score: 69.12  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390124057  22 PVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSLYVdgdctmdIRTKSQGGeptyNVAVGRAGRVLVFVMGKEGVHGG 99
Cdd:pfam00235  41 PEEIKAIVAafKDPSKLQANGITLGGKKYMVIRADDRS-------IYGKKGKE----GIVIVKTKQAIIIGHYDEGVQPG 109
                          90
                  ....*....|....*
gi 1390124057 100 GLNKKAYSMAKYLRD 114
Cdd:pfam00235 110 NANKAVEKLADYLRS 124
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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