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Conserved domains on  [gi|1844084131|ref|NP_001350470|]
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drebrin isoform c [Homo sapiens]

Protein Classification

drebrin-like protein( domain architecture ID 10181581)

drebrin-like protein such as Mus musculus drebrin, which is an actin cytoskeleton-organizing protein that plays a role in the formation of cell projections

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
ADF_drebrin_like cd11281
ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization ...
4-139 9.12e-67

ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. Abp1 and drebrin (developmentally regulated brain protein) are multidomain proteins with an N-terminal ADF homology domain and one or more C-terminal SH3 domains. They have been shown to interact with polymeric F-actin, but not with monomeric G-actin, and do not appear to promote the disassembly of actin filaments. Drebrin rather stabilizes actin filaments by inducing changes in the helical twist and may promote or interfere with the interactions of other proteins with actin filaments.


:

Pssm-ID: 200437  Cd Length: 136  Bit Score: 215.58  E-value: 9.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131   4 VSFSGHRLELLAAYEEVIREESAADWALYTYEDGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDSQAALPKYVLI 83
Cdd:cd11281     1 IDLSTNSPEILAAYEDVVDGKSSTDWALFTYEGKSNDLKVADTGDGGLEELVEEFSDGKVQYGFARVKDPNSGLPKFVLI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1844084131  84 NWVGEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLSNGLAR 139
Cdd:cd11281    81 NWCGEGVPDARKGSFASHVAAVANFLKGAHVQINARSEDDLDEDAILKKVSKASGA 136
PHA03247 super family cl33720
large tegument protein UL36; Provisional
277-606 9.88e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  277 EEAAAIIAQRPDNPREffKQQERVASASAGSCDVPSPFNHRPGRPYCPFIKASDSGPSSSSSSSSSPPRTPFPyitchRT 356
Cdd:PHA03247  2579 EPAVTSRARRPDAPPQ--SARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP-----ER 2651
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  357 PNLSSSLPcsHLDSHRRmapTPIPTRSPSDSSTASTPVAEQIERALDEVTSSQPPPLPpppppaQETQEPSPILDSEETR 436
Cdd:PHA03247  2652 PRDDPAPG--RVSRPRR---ARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP------PPTPEPAPHALVSATP 2720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  437 AA-APQAWAGPMEEPPQAQAPPRGPGSPAEDLMFMESAEQAVLAAPVEPATADATEIHDAADTIETDTATADTTVANNVP 515
Cdd:PHA03247  2721 LPpGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS 2800
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  516 PAATSLIDLWPGNGEGASTLQGEPRAPTPPSGTEVTLAevPLLDEVAPEPLLPAGEGCATLLNFDELP---EPPATFCDP 592
Cdd:PHA03247  2801 PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA--PPPPPGPPPPSLPLGGSVAPGGDVRRRPpsrSPAAKPAAP 2878
                          330
                   ....*....|....
gi 1844084131  593 EEVEGESLAAPQTP 606
Cdd:PHA03247  2879 ARPPVRRLARPAVS 2892
 
Name Accession Description Interval E-value
ADF_drebrin_like cd11281
ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization ...
4-139 9.12e-67

ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. Abp1 and drebrin (developmentally regulated brain protein) are multidomain proteins with an N-terminal ADF homology domain and one or more C-terminal SH3 domains. They have been shown to interact with polymeric F-actin, but not with monomeric G-actin, and do not appear to promote the disassembly of actin filaments. Drebrin rather stabilizes actin filaments by inducing changes in the helical twist and may promote or interfere with the interactions of other proteins with actin filaments.


Pssm-ID: 200437  Cd Length: 136  Bit Score: 215.58  E-value: 9.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131   4 VSFSGHRLELLAAYEEVIREESAADWALYTYEDGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDSQAALPKYVLI 83
Cdd:cd11281     1 IDLSTNSPEILAAYEDVVDGKSSTDWALFTYEGKSNDLKVADTGDGGLEELVEEFSDGKVQYGFARVKDPNSGLPKFVLI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1844084131  84 NWVGEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLSNGLAR 139
Cdd:cd11281    81 NWCGEGVPDARKGSFASHVAAVANFLKGAHVQINARSEDDLDEDAILKKVSKASGA 136
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
9-134 1.65e-25

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 101.98  E-value: 1.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131    9 HRLELLAAYEEViREESAADWALYTYEDgSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDS--QAALPKYVLINWV 86
Cdd:smart00102   2 DCKEAFNELKKK-RKHSAIIFKIDKDNE-EIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTteESKKSKIVFIFWS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1844084131   87 GEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLS 134
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
13-125 5.42e-24

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 97.64  E-value: 5.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  13 LLAAYEEViREESAADWALYTYEDGSDDLKLAASGEGGL--QELSGHFENQKVMYGFCSVK---DSQAALPKYVLINWVG 87
Cdd:pfam00241   1 CKEAYQEL-RSDKKTNWIIFKIDDDKEEIVVEETGEGGLsyDEFLEELPDDEPRYAVYRFEythDDGSKRSKLVFITWCP 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1844084131  88 EDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDID 125
Cdd:pfam00241  80 DGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELT 117
PHA03247 PHA03247
large tegument protein UL36; Provisional
277-606 9.88e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  277 EEAAAIIAQRPDNPREffKQQERVASASAGSCDVPSPFNHRPGRPYCPFIKASDSGPSSSSSSSSSPPRTPFPyitchRT 356
Cdd:PHA03247  2579 EPAVTSRARRPDAPPQ--SARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP-----ER 2651
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  357 PNLSSSLPcsHLDSHRRmapTPIPTRSPSDSSTASTPVAEQIERALDEVTSSQPPPLPpppppaQETQEPSPILDSEETR 436
Cdd:PHA03247  2652 PRDDPAPG--RVSRPRR---ARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP------PPTPEPAPHALVSATP 2720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  437 AA-APQAWAGPMEEPPQAQAPPRGPGSPAEDLMFMESAEQAVLAAPVEPATADATEIHDAADTIETDTATADTTVANNVP 515
Cdd:PHA03247  2721 LPpGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS 2800
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  516 PAATSLIDLWPGNGEGASTLQGEPRAPTPPSGTEVTLAevPLLDEVAPEPLLPAGEGCATLLNFDELP---EPPATFCDP 592
Cdd:PHA03247  2801 PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA--PPPPPGPPPPSLPLGGSVAPGGDVRRRPpsrSPAAKPAAP 2878
                          330
                   ....*....|....
gi 1844084131  593 EEVEGESLAAPQTP 606
Cdd:PHA03247  2879 ARPPVRRLARPAVS 2892
 
Name Accession Description Interval E-value
ADF_drebrin_like cd11281
ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization ...
4-139 9.12e-67

ADF homology domain of drebrin and actin-binding protein 1 (abp1); Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. Abp1 and drebrin (developmentally regulated brain protein) are multidomain proteins with an N-terminal ADF homology domain and one or more C-terminal SH3 domains. They have been shown to interact with polymeric F-actin, but not with monomeric G-actin, and do not appear to promote the disassembly of actin filaments. Drebrin rather stabilizes actin filaments by inducing changes in the helical twist and may promote or interfere with the interactions of other proteins with actin filaments.


Pssm-ID: 200437  Cd Length: 136  Bit Score: 215.58  E-value: 9.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131   4 VSFSGHRLELLAAYEEVIREESAADWALYTYEDGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDSQAALPKYVLI 83
Cdd:cd11281     1 IDLSTNSPEILAAYEDVVDGKSSTDWALFTYEGKSNDLKVADTGDGGLEELVEEFSDGKVQYGFARVKDPNSGLPKFVLI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1844084131  84 NWVGEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLSNGLAR 139
Cdd:cd11281    81 NWCGEGVPDARKGSFASHVAAVANFLKGAHVQINARSEDDLDEDAILKKVSKASGA 136
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
9-134 1.65e-25

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 101.98  E-value: 1.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131    9 HRLELLAAYEEViREESAADWALYTYEDgSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDS--QAALPKYVLINWV 86
Cdd:smart00102   2 DCKEAFNELKKK-RKHSAIIFKIDKDNE-EIVVEEVGSTEDSYDEFVEELPEDECRYALYDYKFTteESKKSKIVFIFWS 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1844084131   87 GEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLS 134
Cdd:smart00102  80 PDGAPVKSKMLYASSKDTLKKELGGIQVEVQATDEDDLDEEALKEKLK 127
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
13-125 5.42e-24

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 97.64  E-value: 5.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  13 LLAAYEEViREESAADWALYTYEDGSDDLKLAASGEGGL--QELSGHFENQKVMYGFCSVK---DSQAALPKYVLINWVG 87
Cdd:pfam00241   1 CKEAYQEL-RSDKKTNWIIFKIDDDKEEIVVEETGEGGLsyDEFLEELPDDEPRYAVYRFEythDDGSKRSKLVFITWCP 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1844084131  88 EDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDID 125
Cdd:pfam00241  80 DGAPIKRKMLYASSKAALKRELKGIHVEIQATDPSELT 117
ADF_coactosin_like cd11282
Coactosin-like members of the ADF homology domain family; Actin depolymerization factor ...
12-124 4.48e-18

Coactosin-like members of the ADF homology domain family; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Many of these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments. The function of coactosins is not well understood. They appear to interfere with the capping of actin filaments in Dictyostelium, and may not be able to bind monomeric globular actin. A role for coactosins as chaperones stabilizing 5-lipoxygenase (5LO) has been suggested; 5LO plays a crucial role in leukotriene synthesis.


Pssm-ID: 200438  Cd Length: 114  Bit Score: 80.37  E-value: 4.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  12 ELLAAYEEVIREESAADWALYTYEdGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDSQAAL--PKYVLINWVGED 89
Cdd:cd11282     1 EIREAYNDVRSDVSDTNWVLLGYE-SSNTLVLRGSGSGGIDELKAQLPDDEVLFGYVRITLGDGESkrSKFVFITWIGEN 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1844084131  90 VPDARKCACASHVAKVAEFFQGVDVIVNASSVEDI 124
Cdd:cd11282    80 VSVLRRAKVSVHKGDVKEVLSPFHVELTASSKDEL 114
ADF_gelsolin cd00013
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
28-119 8.01e-16

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


Pssm-ID: 200435  Cd Length: 97  Bit Score: 73.27  E-value: 8.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  28 DWALYTYEDGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVK--DSQAALPKYVLINWVGEDVPDARKCACASHVAKV 105
Cdd:cd00013     1 DWVLFKVDAKKEEIVVGSTGAGFLDEFLEELPEDDPRYAFYRFKypHSDDKRSKFVFISWIPDGVSIKQKMVYATNKQTL 80
                          90
                  ....*....|....
gi 1844084131 106 AEFFQGVDVIVNAS 119
Cdd:cd00013    81 KEALFGLAVPVQIR 94
PHA03247 PHA03247
large tegument protein UL36; Provisional
277-606 9.88e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  277 EEAAAIIAQRPDNPREffKQQERVASASAGSCDVPSPFNHRPGRPYCPFIKASDSGPSSSSSSSSSPPRTPFPyitchRT 356
Cdd:PHA03247  2579 EPAVTSRARRPDAPPQ--SARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPP-----ER 2651
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  357 PNLSSSLPcsHLDSHRRmapTPIPTRSPSDSSTASTPVAEQIERALDEVTSSQPPPLPpppppaQETQEPSPILDSEETR 436
Cdd:PHA03247  2652 PRDDPAPG--RVSRPRR---ARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPP------PPTPEPAPHALVSATP 2720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  437 AA-APQAWAGPMEEPPQAQAPPRGPGSPAEDLMFMESAEQAVLAAPVEPATADATEIHDAADTIETDTATADTTVANNVP 515
Cdd:PHA03247  2721 LPpGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS 2800
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844084131  516 PAATSLIDLWPGNGEGASTLQGEPRAPTPPSGTEVTLAevPLLDEVAPEPLLPAGEGCATLLNFDELP---EPPATFCDP 592
Cdd:PHA03247  2801 PWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTA--PPPPPGPPPPSLPLGGSVAPGGDVRRRPpsrSPAAKPAAP 2878
                          330
                   ....*....|....
gi 1844084131  593 EEVEGESLAAPQTP 606
Cdd:PHA03247  2879 ARPPVRRLARPAVS 2892
 
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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