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Conserved domains on  [gi|307776548|pdb|3NEC|B]
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Chain B, Inflammatory profilin

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 ...
7-166 4.05e-13

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: 62.34  E-value: 4.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B           7 WDPVVKEWLVDTGyCCAGGIANAEDGVVfaaaaddddgWSKLYKDDHEEDTIGEdgnacgKVSINEASTIKAAVddgsAP 86
Cdd:smart00392   3 WQAYVDNLLVGSG-CVDAAAIGGKDGSV----------WAASAGGNFQKITPEE------IAAIAALFNSLAAV----FS 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B          87 NGVWIGGQKYKVVRpekgfEYNDCTFDIt*caRSKGGAHLIKTpNGSIVIALYDEekEQDKGNSRTSALAFAEYLHQSGY 166
Cdd:smart00392  62 NGLTLGGQKYMVIR-----ADDRSIMGK----KGAGGVVIVKT-KQALIIGMYKE--GVQPGQANKTVEKLADYLRSSGY 129
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
7-166 4.05e-13

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 62.34  E-value: 4.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B           7 WDPVVKEWLVDTGyCCAGGIANAEDGVVfaaaaddddgWSKLYKDDHEEDTIGEdgnacgKVSINEASTIKAAVddgsAP 86
Cdd:smart00392   3 WQAYVDNLLVGSG-CVDAAAIGGKDGSV----------WAASAGGNFQKITPEE------IAAIAALFNSLAAV----FS 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B          87 NGVWIGGQKYKVVRpekgfEYNDCTFDIt*caRSKGGAHLIKTpNGSIVIALYDEekEQDKGNSRTSALAFAEYLHQSGY 166
Cdd:smart00392  62 NGLTLGGQKYMVIR-----ADDRSIMGK----KGAGGVVIVKT-KQALIIGMYKE--GVQPGQANKTVEKLADYLRSSGY 129
Profilin pfam00235
Profilin;
7-161 3.32e-11

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 57.17  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B          7 WDPVVKEWLVDTGYCCAGGIANAEDGVVfaaaaddddgWSKlykddheedtigeDGNAcgKVSINEASTIKAAVDDGS-- 84
Cdd:pfam00235   3 WQAYVDDNLLGTGHVDKAAIIGLDGGSV----------WAS-------------SPGF--NLSPEEIKAIVAAFKDPSkl 57
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3NEC_B         85 APNGVWIGGQKYKVVRpekgfeYNDCTFdit*CARSKGGAHLIKTpNGSIVIALYDEEKEQdkGNSRTSALAFAEYL 161
Cdd:pfam00235  58 QANGITLGGKKYMVIR------ADDRSI---YGKKGKEGIVIVKT-KQAIIIGHYDEGVQP--GNANKAVEKLADYL 122
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
67-166 2.05e-10

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: 55.41  E-value: 2.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B       67 KVSINEASTIKAAVDD--GSAPNGVWIGGQKYKVVRPEkgfeynDCTFDit*cARSK-GGAHLIKTpNGSIVIALYDEek 143
Cdd:cd00148  38 NLTPEEVGTLVAGFKDpdGVFSTGLTLGGQKYMVIRAD------DRSIY----GKKGaGGVVIVKT-KQALVIGMYEE-- 104
                        90       100
                ....*....|....*....|...
3NEC_B      144 EQDKGNSRTSALAFAEYLHQSGY 166
Cdd:cd00148 105 GVQPGQANKVVEKLADYLRSQGY 127
 
Name Accession Description Interval E-value
PROF smart00392
Profilin; Binds actin monomers, membrane polyphosphoinositides and poly-L-proline.
7-166 4.05e-13

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


Pssm-ID: 214646  Cd Length: 129  Bit Score: 62.34  E-value: 4.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B           7 WDPVVKEWLVDTGyCCAGGIANAEDGVVfaaaaddddgWSKLYKDDHEEDTIGEdgnacgKVSINEASTIKAAVddgsAP 86
Cdd:smart00392   3 WQAYVDNLLVGSG-CVDAAAIGGKDGSV----------WAASAGGNFQKITPEE------IAAIAALFNSLAAV----FS 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B          87 NGVWIGGQKYKVVRpekgfEYNDCTFDIt*caRSKGGAHLIKTpNGSIVIALYDEekEQDKGNSRTSALAFAEYLHQSGY 166
Cdd:smart00392  62 NGLTLGGQKYMVIR-----ADDRSIMGK----KGAGGVVIVKT-KQALIIGMYKE--GVQPGQANKTVEKLADYLRSSGY 129
Profilin pfam00235
Profilin;
7-161 3.32e-11

Profilin;


Pssm-ID: 459724  Cd Length: 124  Bit Score: 57.17  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B          7 WDPVVKEWLVDTGYCCAGGIANAEDGVVfaaaaddddgWSKlykddheedtigeDGNAcgKVSINEASTIKAAVDDGS-- 84
Cdd:pfam00235   3 WQAYVDDNLLGTGHVDKAAIIGLDGGSV----------WAS-------------SPGF--NLSPEEIKAIVAAFKDPSkl 57
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3NEC_B         85 APNGVWIGGQKYKVVRpekgfeYNDCTFdit*CARSKGGAHLIKTpNGSIVIALYDEEKEQdkGNSRTSALAFAEYL 161
Cdd:pfam00235  58 QANGITLGGKKYMVIR------ADDRSI---YGKKGKEGIVIVKT-KQAIIIGHYDEGVQP--GNANKAVEKLADYL 122
PROF cd00148
Profilin binds actin monomers, membrane polyphosphoinositides such as PI(4,5)P2, and ...
67-166 2.05e-10

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: 55.41  E-value: 2.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3NEC_B       67 KVSINEASTIKAAVDD--GSAPNGVWIGGQKYKVVRPEkgfeynDCTFDit*cARSK-GGAHLIKTpNGSIVIALYDEek 143
Cdd:cd00148  38 NLTPEEVGTLVAGFKDpdGVFSTGLTLGGQKYMVIRAD------DRSIY----GKKGaGGVVIVKT-KQALVIGMYEE-- 104
                        90       100
                ....*....|....*....|...
3NEC_B      144 EQDKGNSRTSALAFAEYLHQSGY 166
Cdd:cd00148 105 GVQPGQANKVVEKLADYLRSQGY 127
 
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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