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Conserved domains on  [gi|568910454|ref|XP_006496712|]
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protein enabled homolog isoform X12 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 693-727 7.19e-15

VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerization domain which forms a right handed alpha helical coiled coil structure.


:

Pssm-ID: 462599  Cd Length: 35  Bit Score: 68.83  E-value: 7.19e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568910454  693 LDYDRLKQDILDEMRKELAKLKEELIDAIRQELSK 727
Cdd:pfam08776   1 SDLERLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
WH2_hVASP-like cd22185
Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human ...
 525-551 2.86e-07

Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human Vasodilator-stimulated phosphoprotein and related proteins; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of Ena/VASP family members including Protein enabled homolog (also known as Mena, mammalian enabled), VASP (vasodilator-stimulated phosphoprotein) and EVL (Ena-VASP-like or Enabled VASP or Ena/VASP). These are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells, platelet activation and cell migration. Ena/VASP proteins processively elongate F-actin barbed ends, promoting dissociation of barbed end assembly antagonists (uncapping). WH2 domains are small, widespread intrinsically disordered actin-binding peptides displaying significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. WH2 domains are identified by a central consensus actin-binding motif LKKT/V flanked by variable N-terminal and C-terminal extensions.


:

Pssm-ID: 409225  Cd Length: 27  Bit Score: 46.90  E-value: 2.86e-07
                         10        20
                 ....*....|....*....|....*..
gi 568910454 525 DNRPLTGLAAAIAGAKLRKVSRVEDGS 551
Cdd:cd22185    1 GGSGAPGLAAAIAGAKLRKVSKQEEAS 27
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 227-447 3.56e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454  227 AATRFATSLGSAFHPVLPHYATVPRPLNKNSRPSSPvntPSSQPPAAKSCAWPTSNFSPLPPSPpimiSSPPGKATGPRP 306
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAA 2816

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454  307 VLPVcVSSPVPQMPPSPTA-------PNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHC 379
Cdd:PHA03247 2817 ALPP-AASPAGPLPPPTSAqptapppPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST 2895

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568910454  380 GSQASPPPGTPLASTPSSKPSVLPSPSAAAPASAETPLNPElgdsSASEPGLQAASQPAESPTPQGLV 447
Cdd:PHA03247 2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP----PRPQPPLAPTTDPAGAGEPSGAV 2959
 
Name Accession Description Interval E-value
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 693-727 7.19e-15

VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerization domain which forms a right handed alpha helical coiled coil structure.


Pssm-ID: 462599  Cd Length: 35  Bit Score: 68.83  E-value: 7.19e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568910454  693 LDYDRLKQDILDEMRKELAKLKEELIDAIRQELSK 727
Cdd:pfam08776   1 SDLERLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
WH2_hVASP-like cd22185
Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human ...
 525-551 2.86e-07

Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human Vasodilator-stimulated phosphoprotein and related proteins; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of Ena/VASP family members including Protein enabled homolog (also known as Mena, mammalian enabled), VASP (vasodilator-stimulated phosphoprotein) and EVL (Ena-VASP-like or Enabled VASP or Ena/VASP). These are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells, platelet activation and cell migration. Ena/VASP proteins processively elongate F-actin barbed ends, promoting dissociation of barbed end assembly antagonists (uncapping). WH2 domains are small, widespread intrinsically disordered actin-binding peptides displaying significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. WH2 domains are identified by a central consensus actin-binding motif LKKT/V flanked by variable N-terminal and C-terminal extensions.


Pssm-ID: 409225  Cd Length: 27  Bit Score: 46.90  E-value: 2.86e-07
                         10        20
                 ....*....|....*....|....*..
gi 568910454 525 DNRPLTGLAAAIAGAKLRKVSRVEDGS 551
Cdd:cd22185    1 GGSGAPGLAAAIAGAKLRKVSKQEEAS 27
PHA03247 PHA03247
large tegument protein UL36; Provisional
 227-447 3.56e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454  227 AATRFATSLGSAFHPVLPHYATVPRPLNKNSRPSSPvntPSSQPPAAKSCAWPTSNFSPLPPSPpimiSSPPGKATGPRP 306
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAA 2816

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454  307 VLPVcVSSPVPQMPPSPTA-------PNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHC 379
Cdd:PHA03247 2817 ALPP-AASPAGPLPPPTSAqptapppPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST 2895

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568910454  380 GSQASPPPGTPLASTPSSKPSVLPSPSAAAPASAETPLNPElgdsSASEPGLQAASQPAESPTPQGLV 447
Cdd:PHA03247 2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP----PRPQPPLAPTTDPAGAGEPSGAV 2959
 
Name Accession Description Interval E-value
VASP_tetra pfam08776
VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin ...
 693-727 7.19e-15

VASP tetramerization domain; Vasodilator-stimulated phosphoprotein (VASP) is an actin cytoskeletal regulatory protein. This region corresponds to the tetramerization domain which forms a right handed alpha helical coiled coil structure.


Pssm-ID: 462599  Cd Length: 35  Bit Score: 68.83  E-value: 7.19e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 568910454  693 LDYDRLKQDILDEMRKELAKLKEELIDAIRQELSK 727
Cdd:pfam08776   1 SDLERLKQEILEEVRKELQKVKEEIIDAIRQELNR 35
WH2_hVASP-like cd22185
Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human ...
 525-551 2.86e-07

Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of human Vasodilator-stimulated phosphoprotein and related proteins; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) of Ena/VASP family members including Protein enabled homolog (also known as Mena, mammalian enabled), VASP (vasodilator-stimulated phosphoprotein) and EVL (Ena-VASP-like or Enabled VASP or Ena/VASP). These are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells, platelet activation and cell migration. Ena/VASP proteins processively elongate F-actin barbed ends, promoting dissociation of barbed end assembly antagonists (uncapping). WH2 domains are small, widespread intrinsically disordered actin-binding peptides displaying significant sequence variability and different regulations of actin self-assembly in motile and morphogenetic processes. WH2 domains are identified by a central consensus actin-binding motif LKKT/V flanked by variable N-terminal and C-terminal extensions.


Pssm-ID: 409225  Cd Length: 27  Bit Score: 46.90  E-value: 2.86e-07
                         10        20
                 ....*....|....*....|....*..
gi 568910454 525 DNRPLTGLAAAIAGAKLRKVSRVEDGS 551
Cdd:cd22185    1 GGSGAPGLAAAIAGAKLRKVSKQEEAS 27
PHA03247 PHA03247
large tegument protein UL36; Provisional
 227-447 3.56e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454  227 AATRFATSLGSAFHPVLPHYATVPRPLNKNSRPSSPvntPSSQPPAAKSCAWPTSNFSPLPPSPpimiSSPPGKATGPRP 306
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP---PRRLTRPAVASLSESRESLPSPWDP----ADPPAAVLAPAA 2816

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454  307 VLPVcVSSPVPQMPPSPTA-------PNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHC 379
Cdd:PHA03247 2817 ALPP-AASPAGPLPPPTSAqptapppPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRST 2895

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568910454  380 GSQASPPPGTPLASTPSSKPSVLPSPSAAAPASAETPLNPElgdsSASEPGLQAASQPAESPTPQGLV 447
Cdd:PHA03247 2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP----PRPQPPLAPTTDPAGAGEPSGAV 2959
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 264-447 1.98e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.45  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454 264 NTPSSQPPAAKSCAW------PTSNFSPLPPSPPIMISSPPGKATGPRPVLPVCV-------SSPVPQMPPSPTAPNGSL 330
Cdd:PLN03209 322 KIPSQRVPPKESDAAdgpkpvPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAyedlkppTSPIPTPPSSSPASSKSV 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454 331 DSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHcGSQASPPPGTPLASTPSSKPSV-LPSPSAAA 409
Cdd:PLN03209 402 DAVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKP-PTSPSPTAPTGVSPSVSSTSSVpAVPDTAPA 480

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568910454 410 PASAETPLNPELGDSSASEPGLQAASQPAESPTPQGLV 447
Cdd:PLN03209 481 TAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPV 518
PHA03247 PHA03247
large tegument protein UL36; Provisional
 189-443 5.17e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454  189 PPSYakviSAPVSDATPDYAVVTALPPTSTPPTPPLRHAATRFATSLGSAFHPVLPHYATVPR-------PLNKNSRPSS 261
Cdd:PHA03247 2628 PPSP----SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRaarptvgSLTSLADPPP 2703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454  262 PVNTPSSQP------------PAAKSCAWPTSNFSPLPPSPPIMISSPPGKATGPRPvlpvcvssPVPQMPPSPTAPNGs 329
Cdd:PHA03247 2704 PPPTPEPAPhalvsatplppgPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP--------PTTAGPPAPAPPAA- 2774

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568910454  330 ldsvtyPVSPPPTSGPAAPPPPPPPPPPPPPPPPPLPPPPLPPLASLSHCGSQASPPPGTPLASTPSSKPSVLPSPSAAA 409
Cdd:PHA03247 2775 ------PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPP 2848

                         250       260       270
                  ....*....|....*....|....*....|....
gi 568910454  410 PASAETPLNPElGDSSASEPGLQAASQPAESPTP 443
Cdd:PHA03247 2849 SLPLGGSVAPG-GDVRRRPPSRSPAAKPAAPARP 2881
 
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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