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Conserved domains on  [gi|510937029|ref|NP_001265395|]
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dynamin-1-like protein isoform 7 [Homo sapiens]

Protein Classification

Dynamin_M and GED domain-containing protein( domain architecture ID 10470546)

Dynamin_M and GED domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 44-307 1.13e-123

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


:

Pssm-ID: 460033  Cd Length: 287  Bit Score: 363.76  E-value: 1.13e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029   44 RSQLDINNKKSVTDSIRDEYAFLQKK--YPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGE 121
Cdd:pfam01031  23 RSQKDINGNKSIEEALQDERAFFETHpaYRLLADKCGTPYLAKKLNQILVNHIRKSLPDLKNKINELLQKTEKELEKYGN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029  122 PVD----DKSATLLQLITKFATEYCNTIEGTAKyIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNAT 197
Cdd:pfam01031 103 GIPsdpaEKGKFLLQLITKFNQDFKNLIDGESE-ISTNELSGGARIRYIFNEIFPKSLEKIDPLENLSDEEIRTAIRNSR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029  198 GPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCsnysTQELLRFPKLHDAIVEVVTCLLRKRLPVTN 277
Cdd:pfam01031 182 GIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC----TPELKRFPNLRERIKEVVEDLLRERLEPTE 257

                         250       260       270
                  ....*....|....*....|....*....|
gi 510937029  278 EMVHNLVAIELAYINTKHPDFADACGLMNN 307
Cdd:pfam01031 258 KMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
437-527 1.08e-35

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 128.40  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029  437 EQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKA 516
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 510937029  517 LQGASQIIAEI 527
Cdd:pfam02212  81 LKQAREILSEV 91
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 44-307 1.13e-123

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


Pssm-ID: 460033  Cd Length: 287  Bit Score: 363.76  E-value: 1.13e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029   44 RSQLDINNKKSVTDSIRDEYAFLQKK--YPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGE 121
Cdd:pfam01031  23 RSQKDINGNKSIEEALQDERAFFETHpaYRLLADKCGTPYLAKKLNQILVNHIRKSLPDLKNKINELLQKTEKELEKYGN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029  122 PVD----DKSATLLQLITKFATEYCNTIEGTAKyIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNAT 197
Cdd:pfam01031 103 GIPsdpaEKGKFLLQLITKFNQDFKNLIDGESE-ISTNELSGGARIRYIFNEIFPKSLEKIDPLENLSDEEIRTAIRNSR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029  198 GPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCsnysTQELLRFPKLHDAIVEVVTCLLRKRLPVTN 277
Cdd:pfam01031 182 GIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC----TPELKRFPNLRERIKEVVEDLLRERLEPTE 257

                         250       260       270
                  ....*....|....*....|....*....|
gi 510937029  278 EMVHNLVAIELAYINTKHPDFADACGLMNN 307
Cdd:pfam01031 258 KMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
437-527 1.08e-35

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 128.40  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029  437 EQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKA 516
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 510937029  517 LQGASQIIAEI 527
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
436-527 1.10e-33

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 122.73  E-value: 1.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029   436 REQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLK 515
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 510937029   516 ALQGASQIIAEI 527
Cdd:smart00302  81 LLKKARQIIAAV 92
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 44-99 1.03e-10

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 62.65  E-value: 1.03e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 510937029  44 RSQLDINNKKSVTDSIRDEYAFLQKKYP---SLANRNGTKYLARTLNRLLMHHIRDCLP 99
Cdd:cd08771  220 RSQKDIDSGKSIEEALEAEEEFFETHPWyklLPASRVGTPALRKRLSKLLQKHIRESLP 278
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 44-307 1.13e-123

Dynamin central region; This is the stalk region which lies between the GTPase domain, see pfam00350, and the pleckstrin homology (PH) domain, see pfam00169. This region dimerizes in a cross-like fashion forming a dynamin dimer in which the two G-domains are oriented in opposite directions.


Pssm-ID: 460033  Cd Length: 287  Bit Score: 363.76  E-value: 1.13e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029   44 RSQLDINNKKSVTDSIRDEYAFLQKK--YPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGE 121
Cdd:pfam01031  23 RSQKDINGNKSIEEALQDERAFFETHpaYRLLADKCGTPYLAKKLNQILVNHIRKSLPDLKNKINELLQKTEKELEKYGN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029  122 PVD----DKSATLLQLITKFATEYCNTIEGTAKyIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNAT 197
Cdd:pfam01031 103 GIPsdpaEKGKFLLQLITKFNQDFKNLIDGESE-ISTNELSGGARIRYIFNEIFPKSLEKIDPLENLSDEEIRTAIRNSR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029  198 GPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCsnysTQELLRFPKLHDAIVEVVTCLLRKRLPVTN 277
Cdd:pfam01031 182 GIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC----TPELKRFPNLRERIKEVVEDLLRERLEPTE 257

                         250       260       270
                  ....*....|....*....|....*....|
gi 510937029  278 EMVHNLVAIELAYINTKHPDFADACGLMNN 307
Cdd:pfam01031 258 KMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
437-527 1.08e-35

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 128.40  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029  437 EQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKA 516
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 510937029  517 LQGASQIIAEI 527
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
436-527 1.10e-33

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 122.73  E-value: 1.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510937029   436 REQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLK 515
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 510937029   516 ALQGASQIIAEI 527
Cdd:smart00302  81 LLKKARQIIAAV 92
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 44-99 1.03e-10

Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206738  Cd Length: 278  Bit Score: 62.65  E-value: 1.03e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 510937029  44 RSQLDINNKKSVTDSIRDEYAFLQKKYP---SLANRNGTKYLARTLNRLLMHHIRDCLP 99
Cdd:cd08771  220 RSQKDIDSGKSIEEALEAEEEFFETHPWyklLPASRVGTPALRKRLSKLLQKHIRESLP 278
 
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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