NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|71274140|ref|NP_001025057|]
View 

profilin-3 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
3-136 9.51e-34

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: 114.34  E-value: 9.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274140   3 DWKVYISAVLR-DQRIDDVAIVGHaDNSCVWASRPGGLlaAISPQEVGVLTG--PDRHTFLQAGLSVGGRRCCVIRDhll 79
Cdd:cd00148   1 SWQAYVDDNLLgTGKVDSAAIVGH-DDGSVWAASAGGF--NLTPEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRA--- 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71274140  80 aeGDGVLDARTKgldARAVCVGRAPRALLVLMGRRGVHGGILNKTVHELIRGLRMQG 136
Cdd:cd00148  75 --DDRSIYGKKG---AGGVVIVKTKQALVIGMYEEGVQPGQANKVVEKLADYLRSQG 126
 
Name Accession Description Interval E-value
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
3-136 9.51e-34

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: 114.34  E-value: 9.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274140   3 DWKVYISAVLR-DQRIDDVAIVGHaDNSCVWASRPGGLlaAISPQEVGVLTG--PDRHTFLQAGLSVGGRRCCVIRDhll 79
Cdd:cd00148   1 SWQAYVDDNLLgTGKVDSAAIVGH-DDGSVWAASAGGF--NLTPEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRA--- 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71274140  80 aeGDGVLDARTKgldARAVCVGRAPRALLVLMGRRGVHGGILNKTVHELIRGLRMQG 136
Cdd:cd00148  75 --DDRSIYGKKG---AGGVVIVKTKQALVIGMYEEGVQPGQANKVVEKLADYLRSQG 126
Profilin pfam00235
Profilin;
4-133 1.14e-22

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 86.06  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274140     4 WKVYI-SAVLRDQRIDDVAIVGHADNScVWASRPGgllAAISPQEVGVLTG--PDRHTFLQAGLSVGGRRCCVIRDHlla 80
Cdd:pfam00235   3 WQAYVdDNLLGTGHVDKAAIIGLDGGS-VWASSPG---FNLSPEEIKAIVAafKDPSKLQANGITLGGKKYMVIRAD--- 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71274140    81 egDGVLDARTkglDARAVCVGRAPRALLVLMGRRGVHGGILNKTVHELIRGLR 133
Cdd:pfam00235  76 --DRSIYGKK---GKEGIVIVKTKQAIIIGHYDEGVQPGNANKAVEKLADYLR 123
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
1-136 2.83e-15

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 67.35  E-value: 2.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274140      1 MGdWKVYISAVLRDQRIDDVAIVGHADNScVWASRPGGLLAAISPQEVGVLTGPDR--HTFLQAGLSVGGRRCCVIRdhl 78
Cdd:smart00392   1 MS-WQAYVDNLLVGSGCVDAAAIGGKDGS-VWAASAGGNFQKITPEEIAAIAALFNslAAVFSNGLTLGGQKYMVIR--- 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 71274140     79 lAEGDGVLDARtkglDARAVCVGRAPRALLVLMGRRGVHGGILNKTVHELIRGLRMQG 136
Cdd:smart00392  76 -ADDRSIMGKK----GAGGVVIVKTKQALIIGMYKEGVQPGQANKTVEKLADYLRSSG 128
 
Name Accession Description Interval E-value
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
3-136 9.51e-34

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: 114.34  E-value: 9.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274140   3 DWKVYISAVLR-DQRIDDVAIVGHaDNSCVWASRPGGLlaAISPQEVGVLTG--PDRHTFLQAGLSVGGRRCCVIRDhll 79
Cdd:cd00148   1 SWQAYVDDNLLgTGKVDSAAIVGH-DDGSVWAASAGGF--NLTPEEVGTLVAgfKDPDGVFSTGLTLGGQKYMVIRA--- 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71274140  80 aeGDGVLDARTKgldARAVCVGRAPRALLVLMGRRGVHGGILNKTVHELIRGLRMQG 136
Cdd:cd00148  75 --DDRSIYGKKG---AGGVVIVKTKQALVIGMYEEGVQPGQANKVVEKLADYLRSQG 126
Profilin pfam00235
Profilin;
4-133 1.14e-22

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 86.06  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274140     4 WKVYI-SAVLRDQRIDDVAIVGHADNScVWASRPGgllAAISPQEVGVLTG--PDRHTFLQAGLSVGGRRCCVIRDHlla 80
Cdd:pfam00235   3 WQAYVdDNLLGTGHVDKAAIIGLDGGS-VWASSPG---FNLSPEEIKAIVAafKDPSKLQANGITLGGKKYMVIRAD--- 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71274140    81 egDGVLDARTkglDARAVCVGRAPRALLVLMGRRGVHGGILNKTVHELIRGLR 133
Cdd:pfam00235  76 --DRSIYGKK---GKEGIVIVKTKQAIIIGHYDEGVQPGNANKAVEKLADYLR 123
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
1-136 2.83e-15

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 67.35  E-value: 2.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71274140      1 MGdWKVYISAVLRDQRIDDVAIVGHADNScVWASRPGGLLAAISPQEVGVLTGPDR--HTFLQAGLSVGGRRCCVIRdhl 78
Cdd:smart00392   1 MS-WQAYVDNLLVGSGCVDAAAIGGKDGS-VWAASAGGNFQKITPEEIAAIAALFNslAAVFSNGLTLGGQKYMVIR--- 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 71274140     79 lAEGDGVLDARtkglDARAVCVGRAPRALLVLMGRRGVHGGILNKTVHELIRGLRMQG 136
Cdd:smart00392  76 -ADDRSIMGKK----GAGGVVIVKTKQALIIGMYKEGVQPGQANKTVEKLADYLRSSG 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH