NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1197663886|ref|XP_021154223|]
View 

profilin-2, partial [Columba livia]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 1-97 2.47e-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: 469622  Cd Length: 129  Bit Score: 83.91  E-value: 2.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197663886    1 QPVEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDslyvDGDCTMDIRtksqggePTYNVAVGRAGRVLVFVMGKEGVHG 78
Cdd:smart00392  42 TPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA----DDRSIMGKK-------GAGGVVIVKTKQALIIGMYKEGVQP 110

                           90
                   ....*....|....*....
gi 1197663886   79 GGLNKKAYSMAKYLRDSGF 97
Cdd:smart00392 111 GQANKTVEKLADYLRSSGY 129
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
 1-97 2.47e-22

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 83.91  E-value: 2.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197663886    1 QPVEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDslyvDGDCTMDIRtksqggePTYNVAVGRAGRVLVFVMGKEGVHG 78
Cdd:smart00392  42 TPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA----DDRSIMGKK-------GAGGVVIVKTKQALIIGMYKEGVQP 110

                           90
                   ....*....|....*....
gi 1197663886   79 GGLNKKAYSMAKYLRDSGF 97
Cdd:smart00392 111 GQANKTVEKLADYLRSSGY 129
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
 1-97 1.18e-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: 81.99  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197663886   1 QPVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSlyvdgDCTMDIRTKSQGgeptynVAVGRAGRVLVFVMGKEGVHG 78
Cdd:cd00148    40 TPEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRAD-----DRSIYGKKGAGG------VVIVKTKQALVIGMYEEGVQP 108

                          90
                  ....*....|....*....
gi 1197663886  79 GGLNKKAYSMAKYLRDSGF 97
Cdd:cd00148   109 GQANKVVEKLADYLRSQGY 127
Profilin pfam00235
Profilin;
1-94 2.55e-16

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 68.34  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197663886   1 QPVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSLYVdgdctmdIRTKSQGGeptyNVAVGRAGRVLVFVMGKEGVHG 78
Cdd:pfam00235  40 SPEEIKAIVAafKDPSKLQANGITLGGKKYMVIRADDRS-------IYGKKGKE----GIVIVKTKQAIIIGHYDEGVQP 108

                          90
                  ....*....|....*.
gi 1197663886  79 GGLNKKAYSMAKYLRD 94
Cdd:pfam00235 109 GNANKAVEKLADYLRS 124
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
 1-97 2.47e-22

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 83.91  E-value: 2.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197663886    1 QPVEIDMIVGKDRE--GFFTNGLTLGAKKCSVIRDslyvDGDCTMDIRtksqggePTYNVAVGRAGRVLVFVMGKEGVHG 78
Cdd:smart00392  42 TPEEIAAIAALFNSlaAVFSNGLTLGGQKYMVIRA----DDRSIMGKK-------GAGGVVIVKTKQALIIGMYKEGVQP 110

                           90
                   ....*....|....*....
gi 1197663886   79 GGLNKKAYSMAKYLRDSGF 97
Cdd:smart00392 111 GQANKTVEKLADYLRSSGY 129
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
 1-97 1.18e-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: 81.99  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197663886   1 QPVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSlyvdgDCTMDIRTKSQGgeptynVAVGRAGRVLVFVMGKEGVHG 78
Cdd:cd00148    40 TPEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRAD-----DRSIYGKKGAGG------VVIVKTKQALVIGMYEEGVQP 108

                          90
                  ....*....|....*....
gi 1197663886  79 GGLNKKAYSMAKYLRDSGF 97
Cdd:cd00148   109 GQANKVVEKLADYLRSQGY 127
Profilin pfam00235
Profilin;
1-94 2.55e-16

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 68.34  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197663886   1 QPVEIDMIVG--KDREGFFTNGLTLGAKKCSVIRDSLYVdgdctmdIRTKSQGGeptyNVAVGRAGRVLVFVMGKEGVHG 78
Cdd:pfam00235  40 SPEEIKAIVAafKDPSKLQANGITLGGKKYMVIRADDRS-------IYGKKGKE----GIVIVKTKQAIIIGHYDEGVQP 108

                          90
                  ....*....|....*.
gi 1197663886  79 GGLNKKAYSMAKYLRD 94
Cdd:pfam00235 109 GNANKAVEKLADYLRS 124
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH