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Conserved domains on  [gi|2462529190|ref|XP_054226691|]
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dynamin-1-like protein isoform X2 [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 ...
 6-291 1.54e-141

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: 408.83  E-value: 1.54e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190   6 DAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKK--YPSLANRNGTKYLARTLNRLLMHHIRDCLP 83
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHpaYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190  84 ELKTRINVLAAQYQSLLNSYGEPVD----DKSATLLQLITKFATEYCNTIEGTAKyIETSELCGGARICYIFHETFGRTL 159
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPsdpaEKGKFLLQLITKFNQDFKNLIDGESE-ISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190 160 ESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCsnysTQELLRFP 239
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC----TPELKRFP 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462529190 240 KLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNN 291
Cdd:pfam01031 236 NLRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
421-511 5.82e-36

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 128.78  E-value: 5.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190 421 EQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKA 500
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 2462529190 501 LQGASQIIAEI 511
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 ...
 6-291 1.54e-141

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: 408.83  E-value: 1.54e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190   6 DAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKK--YPSLANRNGTKYLARTLNRLLMHHIRDCLP 83
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHpaYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190  84 ELKTRINVLAAQYQSLLNSYGEPVD----DKSATLLQLITKFATEYCNTIEGTAKyIETSELCGGARICYIFHETFGRTL 159
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPsdpaEKGKFLLQLITKFNQDFKNLIDGESE-ISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190 160 ESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCsnysTQELLRFP 239
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC----TPELKRFP 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462529190 240 KLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNN 291
Cdd:pfam01031 236 NLRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
421-511 5.82e-36

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 128.78  E-value: 5.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190 421 EQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKA 500
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 2462529190 501 LQGASQIIAEI 511
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
420-511 5.52e-34

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 123.50  E-value: 5.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190  420 REQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLK 499
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 2462529190  500 ALQGASQIIAEI 511
Cdd:smart00302  81 LLKKARQIIAAV 92
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 1-83 6.29e-21

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: 92.69  E-value: 6.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190   1 MDAGTDAMDVL---MGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYP---SLANRNGTKYLARTLNRLL 74
Cdd:cd08771   190 MDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEEFFETHPWyklLPASRVGTPALRKRLSKLL 269


                  ....*....
gi 2462529190  75 MHHIRDCLP 83
Cdd:cd08771   270 QKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 1-36 9.04e-07

Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.


Pssm-ID: 197491  Cd Length: 240  Bit Score: 50.26  E-value: 9.04e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462529190    1 MDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNK 36
Cdd:smart00053 205 MDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
 
Name Accession Description Interval E-value
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
 6-291 1.54e-141

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: 408.83  E-value: 1.54e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190   6 DAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKK--YPSLANRNGTKYLARTLNRLLMHHIRDCLP 83
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHpaYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190  84 ELKTRINVLAAQYQSLLNSYGEPVD----DKSATLLQLITKFATEYCNTIEGTAKyIETSELCGGARICYIFHETFGRTL 159
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPsdpaEKGKFLLQLITKFNQDFKNLIDGESE-ISTNELSGGARIRYIFNEIFPKSL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190 160 ESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCsnysTQELLRFP 239
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC----TPELKRFP 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462529190 240 KLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNN 291
Cdd:pfam01031 236 NLRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
421-511 5.82e-36

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 128.78  E-value: 5.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190 421 EQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKA 500
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80

                          90
                  ....*....|.
gi 2462529190 501 LQGASQIIAEI 511
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
420-511 5.52e-34

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 123.50  E-value: 5.52e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190  420 REQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLK 499
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80

                           90
                   ....*....|..
gi 2462529190  500 ALQGASQIIAEI 511
Cdd:smart00302  81 LLKKARQIIAAV 92
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
 1-83 6.29e-21

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: 92.69  E-value: 6.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462529190   1 MDAGTDAMDVL---MGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYP---SLANRNGTKYLARTLNRLL 74
Cdd:cd08771   190 MDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEEFFETHPWyklLPASRVGTPALRKRLSKLL 269


                  ....*....
gi 2462529190  75 MHHIRDCLP 83
Cdd:cd08771   270 QKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
 1-36 9.04e-07

Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.


Pssm-ID: 197491  Cd Length: 240  Bit Score: 50.26  E-value: 9.04e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2462529190    1 MDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNK 36
Cdd:smart00053 205 MDEGTDARDILENKLLPLRRGYIGVVNRSQKDIEGK 240
 
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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