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Conserved domains on  [gi|1063735606|ref|NP_001331306|]
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dynamin-like protein [Arabidopsis thaliana]

Protein Classification

dynamin-like protein( domain architecture ID 10171956)

dynamin-like protein is a GTPase responsible for endocytosis in the eukaryotic cell; similar to Homo sapiens interferon-induced GTP-binding protein Mx2, which is an interferon-induced dynamin-like GTPase with potent antiviral activity against human immunodeficiency virus type 1 (HIV-1)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
33-300 5.72e-131

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: 385.06  E-value: 5.72e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  33 SLPAIAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQLQ-----KIDDGTREYAEFLHLPRKKFTDFAAVRKEI 107
Cdd:cd08771     2 DLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRrspseSDEDEKEEWGEFLHLKSKEFTDFEELREEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 108 QDETDRETGRSKAISSVPIHLSIYSPNVVNLTLIDLPGLTKVAVDGQSDSIVKDIENMVRSYIEKPNCIILAISPANQDL 187
Cdd:cd08771    82 EKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVDL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 188 ATSDAIKISREVDPSGDRTFGVLTKIDLMDKGTDA---VEILEGRSFKLKYPWVGVVNRSQADINKNVDMIAARKREREY 264
Cdd:cd08771   162 ANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAediLLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEEF 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1063735606 265 FSNTTEYRHL-ANKMGSEHLAKMLSKHLERVIKSRIP 300
Cdd:cd08771   242 FETHPWYKLLpASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
221-495 1.44e-81

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: 258.22  E-value: 1.44e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 221 DAVEILEGRSFKLKYPWVGVVNRSQADINKNVDMIAARKREREYFSNTTEYRHLANKMGSEHLAKMLSKHLERVIKSRIP 300
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 301 GIQSLINKTVLELETELSRLGKPIAADAGGKLYSIMEICRLFDQIFKEHLDGVRA-------GGEKVYNVFDNQLPAALK 373
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEistnelsGGARIRYIFNEIFPKSLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 374 RLQFDKQLAMDNIRKLVTEADGYQPHLIAPEQGYRRLIESSIVSIRGPAEASVDTVHAILKDLVHKSvneTVELKQYPAL 453
Cdd:pfam01031 161 KIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC---TPELKRFPNL 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1063735606 454 RVEVTNAAIESLDKMREGSKKATLQLVDMECSYLTV---DFFRKL 495
Cdd:pfam01031 238 RERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTnhpDFIGGL 282
GED smart00302
Dynamin GTPase effector domain;
513-606 1.20e-29

Dynamin GTPase effector domain;


:

Pssm-ID: 128597  Cd Length: 92  Bit Score: 112.33  E-value: 1.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  513 YNDSYLRRIGSNVLSYVNMVCAGLRNSIPKSIVYCQVREAKRSLLDHFFAELGtmDMKRLSSLLNEDPAIMERRSAISKR 592
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLY--KEELLDELLEEDPEIASKRKELKKR 78
                           90
                   ....*....|....
gi 1063735606  593 LELYRAAQSEIDAV 606
Cdd:smart00302  79 LELLKKARQIIAAV 92
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
33-300 5.72e-131

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: 385.06  E-value: 5.72e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  33 SLPAIAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQLQ-----KIDDGTREYAEFLHLPRKKFTDFAAVRKEI 107
Cdd:cd08771     2 DLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRrspseSDEDEKEEWGEFLHLKSKEFTDFEELREEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 108 QDETDRETGRSKAISSVPIHLSIYSPNVVNLTLIDLPGLTKVAVDGQSDSIVKDIENMVRSYIEKPNCIILAISPANQDL 187
Cdd:cd08771    82 EKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVDL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 188 ATSDAIKISREVDPSGDRTFGVLTKIDLMDKGTDA---VEILEGRSFKLKYPWVGVVNRSQADINKNVDMIAARKREREY 264
Cdd:cd08771   162 ANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAediLLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEEF 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1063735606 265 FSNTTEYRHL-ANKMGSEHLAKMLSKHLERVIKSRIP 300
Cdd:cd08771   242 FETHPWYKLLpASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
1-249 1.10e-100

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: 306.04  E-value: 1.10e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606    1 MENLISLVNKIQRACTALGDHGDSSalptlwdsLPAIAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQLQKid 80
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLD--------LPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIK-- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606   81 dGTREYAEFLHLPRKKFTDFAAVRKEIQDETDRETGRSKAISSVPIHLSIYSPNVVNLTLIDLPGLTKVAVDGQSDSIVK 160
Cdd:smart00053  71 -SKTEYAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEY 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  161 DIENMVRSYIEKPNCIILAISPANQDLATSDAIKISREVDPSGDRTFGVLTKIDLMDKGTDAVEILEGRSFKLKYPWVGV 240
Cdd:smart00053 150 QIKKMIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGV 229

                   ....*....
gi 1063735606  241 VNRSQADIN 249
Cdd:smart00053 230 VNRSQKDIE 238
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
221-495 1.44e-81

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: 258.22  E-value: 1.44e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 221 DAVEILEGRSFKLKYPWVGVVNRSQADINKNVDMIAARKREREYFSNTTEYRHLANKMGSEHLAKMLSKHLERVIKSRIP 300
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 301 GIQSLINKTVLELETELSRLGKPIAADAGGKLYSIMEICRLFDQIFKEHLDGVRA-------GGEKVYNVFDNQLPAALK 373
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEistnelsGGARIRYIFNEIFPKSLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 374 RLQFDKQLAMDNIRKLVTEADGYQPHLIAPEQGYRRLIESSIVSIRGPAEASVDTVHAILKDLVHKSvneTVELKQYPAL 453
Cdd:pfam01031 161 KIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC---TPELKRFPNL 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1063735606 454 RVEVTNAAIESLDKMREGSKKATLQLVDMECSYLTV---DFFRKL 495
Cdd:pfam01031 238 RERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTnhpDFIGGL 282
Dynamin_N pfam00350
Dynamin family;
37-213 1.47e-65

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 212.09  E-value: 1.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  37 IAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQLQK-----IDDGTREYAEFlhlpRKKFTDFAAVRKEIQDET 111
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGEspgasEGAVKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 112 DRETGRSKAISSVPIHLSIYSPNVVNLTLIDLPGLTKVAVDGQsdsivkdieNMVRSYIeKPNCIILAISPANQDLATSD 191
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146
                         170       180
                  ....*....|....*....|..
gi 1063735606 192 AIKISREVDPSGDRTFGVLTKI 213
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED smart00302
Dynamin GTPase effector domain;
513-606 1.20e-29

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 112.33  E-value: 1.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  513 YNDSYLRRIGSNVLSYVNMVCAGLRNSIPKSIVYCQVREAKRSLLDHFFAELGtmDMKRLSSLLNEDPAIMERRSAISKR 592
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLY--KEELLDELLEEDPEIASKRKELKKR 78
                           90
                   ....*....|....
gi 1063735606  593 LELYRAAQSEIDAV 606
Cdd:smart00302  79 LELLKKARQIIAAV 92
GED pfam02212
Dynamin GTPase effector domain;
514-606 6.52e-25

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 98.74  E-value: 6.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 514 NDSYLRRIGSNVLSYVNMVCAGLRNSIPKSIVYCQVREAKRSLLDHFFAELGTMDMkrLSSLLNEDPAIMERRSAISKRL 593
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSEL--LDELLKEDPEIAQKRKECKKRL 78
                          90
                  ....*....|...
gi 1063735606 594 ELYRAAQSEIDAV 606
Cdd:pfam02212  79 EALKQAREILSEV 91
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
33-300 5.72e-131

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: 385.06  E-value: 5.72e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  33 SLPAIAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQLQ-----KIDDGTREYAEFLHLPRKKFTDFAAVRKEI 107
Cdd:cd08771     2 DLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRrspseSDEDEKEEWGEFLHLKSKEFTDFEELREEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 108 QDETDRETGRSKAISSVPIHLSIYSPNVVNLTLIDLPGLTKVAVDGQSDSIVKDIENMVRSYIEKPNCIILAISPANQDL 187
Cdd:cd08771    82 EKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVDL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 188 ATSDAIKISREVDPSGDRTFGVLTKIDLMDKGTDA---VEILEGRSFKLKYPWVGVVNRSQADINKNVDMIAARKREREY 264
Cdd:cd08771   162 ANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAediLLLLQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEEF 241
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1063735606 265 FSNTTEYRHL-ANKMGSEHLAKMLSKHLERVIKSRIP 300
Cdd:cd08771   242 FETHPWYKLLpASRVGTPALRKRLSKLLQKHIRESLP 278
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
1-249 1.10e-100

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: 306.04  E-value: 1.10e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606    1 MENLISLVNKIQRACTALGDHGDSSalptlwdsLPAIAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQLQKid 80
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCDLD--------LPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIK-- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606   81 dGTREYAEFLHLPRKKFTDFAAVRKEIQDETDRETGRSKAISSVPIHLSIYSPNVVNLTLIDLPGLTKVAVDGQSDSIVK 160
Cdd:smart00053  71 -SKTEYAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEY 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  161 DIENMVRSYIEKPNCIILAISPANQDLATSDAIKISREVDPSGDRTFGVLTKIDLMDKGTDAVEILEGRSFKLKYPWVGV 240
Cdd:smart00053 150 QIKKMIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGV 229

                   ....*....
gi 1063735606  241 VNRSQADIN 249
Cdd:smart00053 230 VNRSQKDIE 238
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
221-495 1.44e-81

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: 258.22  E-value: 1.44e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 221 DAVEILEGRSFKLKYPWVGVVNRSQADINKNVDMIAARKREREYFSNTTEYRHLANKMGSEHLAKMLSKHLERVIKSRIP 300
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 301 GIQSLINKTVLELETELSRLGKPIAADAGGKLYSIMEICRLFDQIFKEHLDGVRA-------GGEKVYNVFDNQLPAALK 373
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESEistnelsGGARIRYIFNEIFPKSLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 374 RLQFDKQLAMDNIRKLVTEADGYQPHLIAPEQGYRRLIESSIVSIRGPAEASVDTVHAILKDLVHKSvneTVELKQYPAL 453
Cdd:pfam01031 161 KIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC---TPELKRFPNL 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1063735606 454 RVEVTNAAIESLDKMREGSKKATLQLVDMECSYLTV---DFFRKL 495
Cdd:pfam01031 238 RERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTnhpDFIGGL 282
Dynamin_N pfam00350
Dynamin family;
37-213 1.47e-65

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 212.09  E-value: 1.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  37 IAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQLQK-----IDDGTREYAEFlhlpRKKFTDFAAVRKEIQDET 111
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGEspgasEGAVKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 112 DRETGRSKAISSVPIHLSIYSPNVVNLTLIDLPGLTKVAVDGQsdsivkdieNMVRSYIeKPNCIILAISPANQDLATSD 191
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDLSTSE 146
                         170       180
                  ....*....|....*....|..
gi 1063735606 192 AIKISREVDPSGDRTFGVLTKI 213
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED smart00302
Dynamin GTPase effector domain;
513-606 1.20e-29

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 112.33  E-value: 1.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  513 YNDSYLRRIGSNVLSYVNMVCAGLRNSIPKSIVYCQVREAKRSLLDHFFAELGtmDMKRLSSLLNEDPAIMERRSAISKR 592
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLY--KEELLDELLEEDPEIASKRKELKKR 78
                           90
                   ....*....|....
gi 1063735606  593 LELYRAAQSEIDAV 606
Cdd:smart00302  79 LELLKKARQIIAAV 92
GED pfam02212
Dynamin GTPase effector domain;
514-606 6.52e-25

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 98.74  E-value: 6.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 514 NDSYLRRIGSNVLSYVNMVCAGLRNSIPKSIVYCQVREAKRSLLDHFFAELGTMDMkrLSSLLNEDPAIMERRSAISKRL 593
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSEL--LDELLKEDPEIAQKRKECKKRL 78
                          90
                  ....*....|...
gi 1063735606 594 ELYRAAQSEIDAV 606
Cdd:pfam02212  79 EALKQAREILSEV 91
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
38-256 1.17e-05

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 45.91  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  38 AVVGGQSSGKSSVLESIVGKDFLprgsgivtrrplvlqlqkiddgtreyaeflhlprkkftdfaavrkeiqdETDRETGR 117
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGEVG-------------------------------------------------EVSDVPGT 31
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 118 SKAISSVPIHLSIYSpnvVNLTLIDLPGLTkvavdgqsDSIVKDIENMVRSYIEKPNCIILAISPANQDLATSDAIKISR 197
Cdd:cd00882    32 TRDPDVYVKELDKGK---VKLVLVDTPGLD--------EFGGLGREELARLLLRGADLILLVVDSTDRESEEDAKLLILR 100
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 198 EVDPSGDRTFGVLTKIDLMDKGT-DAVEILEGRSFKLKYPWVGVVNRSQADINKNVDMIA 256
Cdd:cd00882   101 RLRKEGIPIILVGNKIDLLEEREvEELLRLEELAKILGVPVFEVSAKTGEGVDELFEKLI 160
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
37-243 1.27e-03

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. 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 mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 40.22  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606  37 IAVVGGQSSGKSSVLESIVGKDFLPRGSGIVTRRPLVLQ--LQKiddgtreyaeflhlprkkftdfaavrkeiqdetdre 114
Cdd:cd09912     3 LAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVITVLRygLLK------------------------------------ 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063735606 115 tgrskaissvpihlsiyspnvvNLTLIDLPGLtkvavdgqsDSIVKDIENMVRSYIEKPNCIILAISpANQDLATSDAIK 194
Cdd:cd09912    47 ----------------------GVVLVDTPGL---------NSTIEHHTEITESFLPRADAVIFVLS-ADQPLTESEREF 94
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1063735606 195 ISREVDPSGDRTFGVLTKIDLMDKGTDAVEILEGRSFKLKYPWVGVVNR 243
Cdd:cd09912    95 LKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGVLELGGGEPR 143
 
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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