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Conserved domains on  [gi|3549667|emb|CAA20578|]
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Arabidopsis dynamin-like protein ADL2 [Arabidopsis thaliana]

Protein Classification

dynamin family protein( domain architecture ID 10171943)

dynamin family protein similar to dynamins and dynamin-like proteins (DLPs), which catalyze membrane fission during clathrin-mediated endocytosis 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); contains a dynamin GTPase effector domain (GED);

EC:  3.6.5.-
Gene Ontology:  GO:0003924|GO:0005525
SCOP:  4004047|4004048

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 ...
57-330 3.08e-136

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: 404.71  E-value: 3.08e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667   57 IALPQVVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQLLQTKSRANGGSDDEWGEFRHLPETRFYDFSEIRRE 136
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLKSKEFTDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667  137 IEAETNRLVGENKGVADTQIRLKISSPNVLNITLVDLPGITKVPVGDQPSDIEARIRTMILSYIKQDTCLILAVTPANTD 216
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667  217 LANSDALQIASIVDPDGHRTIGVITKLDIMDKGTDARKLLL---GNVVPLRLGYVGVVNRCQEDILLNRTVKEALLAEEK 293
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLllqGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 3549667  294 FFRSHPVY-HGLADRLGVPQLAKKLNQILVQHIKVLLP 330
Cdd:cd08771 241 FFETHPWYkLLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
251-538 4.94e-131

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: 391.88  E-value: 4.94e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    251 DARKLLLGNVVPLRLGYVGVVNRCQEDILLNRTVKEALLAEEKFFRSHPVYHGLADRLGVPQLAKKLNQILVQHIKVLLP 330
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    331 DLKSRISNALVATAKEHQSYGE-LTESRAGQGALLLNFLSKYCEAYSSLLEGKSeEMSTSELSGGARIHYIFQSIFVKSL 409
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNgIPSDPAEKGKFLLQLITKFNQDFKNLIDGES-EISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    410 EEVDPCEDLTDDDIRTAIQNATGPRSALFVPDVPFEVLVRRQISRLLDPSLQCARFIFEELIKISHRCmMNELQRFPVLR 489
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC-TPELKRFPNLR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 3549667    490 KRMDEVIGDFLREGLEPSEAMIGDIIDMEMDYINTSHPNFIGGTKAVEA 538
Cdd:pfam01031 239 ERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
666-756 6.22e-34

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 124.93  E-value: 6.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    666 EAVEIQITKLLLRSYYDIVRKNIEDSVPKAIMHFLVNHTKRELHNVFIKKLYRENLFEEMLQEPDEIAVKRKRTQETLHV 745
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 3549667    746 LQQAYRTLDEL 756
Cdd:pfam02212  81 LKQAREILSEV 91
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
57-330 3.08e-136

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: 404.71  E-value: 3.08e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667   57 IALPQVVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQLLQTKSRANGGSDDEWGEFRHLPETRFYDFSEIRRE 136
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLKSKEFTDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667  137 IEAETNRLVGENKGVADTQIRLKISSPNVLNITLVDLPGITKVPVGDQPSDIEARIRTMILSYIKQDTCLILAVTPANTD 216
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667  217 LANSDALQIASIVDPDGHRTIGVITKLDIMDKGTDARKLLL---GNVVPLRLGYVGVVNRCQEDILLNRTVKEALLAEEK 293
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLllqGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 3549667  294 FFRSHPVY-HGLADRLGVPQLAKKLNQILVQHIKVLLP 330
Cdd:cd08771 241 FFETHPWYkLLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
251-538 4.94e-131

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: 391.88  E-value: 4.94e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    251 DARKLLLGNVVPLRLGYVGVVNRCQEDILLNRTVKEALLAEEKFFRSHPVYHGLADRLGVPQLAKKLNQILVQHIKVLLP 330
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    331 DLKSRISNALVATAKEHQSYGE-LTESRAGQGALLLNFLSKYCEAYSSLLEGKSeEMSTSELSGGARIHYIFQSIFVKSL 409
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNgIPSDPAEKGKFLLQLITKFNQDFKNLIDGES-EISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    410 EEVDPCEDLTDDDIRTAIQNATGPRSALFVPDVPFEVLVRRQISRLLDPSLQCARFIFEELIKISHRCmMNELQRFPVLR 489
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC-TPELKRFPNLR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 3549667    490 KRMDEVIGDFLREGLEPSEAMIGDIIDMEMDYINTSHPNFIGGTKAVEA 538
Cdd:pfam01031 239 ERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
36-278 2.03e-104

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: 321.06  E-value: 2.03e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667      36 SVIPIVNKLQDIFAQLGSQSTIALPQVVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQLLQTKSranggsddE 115
Cdd:smart00053   3 ELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKT--------E 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667     116 WGEFRHLPETRFYDFSEIRREIEAETNRLVGENKGVADTQIRLKISSPNVLNITLVDLPGITKVPVGDQPSDIEARIRTM 195
Cdd:smart00053  75 YAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKM 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667     196 ILSYIKQDTCLILAVTPANTDLANSDALQIASIVDPDGHRTIGVITKLDIMDKGTDARKLLLGNVVPLRLGYVGVVNRCQ 275
Cdd:smart00053 155 IKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQ 234

                   ...
gi 3549667     276 EDI 278
Cdd:smart00053 235 KDI 237
Dynamin_N pfam00350
Dynamin family;
62-243 5.10e-65

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 214.02  E-value: 5.10e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667     62 VVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQLLQTKSRANGGSDDEWGEFrhlpETRFYDFSEIRREIEAET 141
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    142 NRLVGENKGVADTQIRLKISSPNVLNITLVDLPGITKVPVGDQpsdiearirTMILSYIKQdTCLILAVTPANTDLANSD 221
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIKP-ADIILAVTPANVDLSTSE 146
                         170       180
                  ....*....|....*....|..
gi 3549667    222 ALQIASIVDPDGHRTIGVITKL 243
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
666-756 6.22e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 124.93  E-value: 6.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    666 EAVEIQITKLLLRSYYDIVRKNIEDSVPKAIMHFLVNHTKRELHNVFIKKLYRENLFEEMLQEPDEIAVKRKRTQETLHV 745
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 3549667    746 LQQAYRTLDEL 756
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
665-755 1.81e-32

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 120.80  E-value: 1.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667     665 QEAVEIQITKLLLRSYYDIVRKNIEDSVPKAIMHFLVNHTKRELHNVFIKKLYRENLFEEMLQEPDEIAVKRKRTQETLH 744
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|.
gi 3549667     745 VLQQAYRTLDE 755
Cdd:smart00302  81 LLKKARQIIAA 91
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
57-330 3.08e-136

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: 404.71  E-value: 3.08e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667   57 IALPQVVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQLLQTKSRANGGSDDEWGEFRHLPETRFYDFSEIRRE 136
Cdd:cd08771   1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDEDEKEEWGEFLHLKSKEFTDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667  137 IEAETNRLVGENKGVADTQIRLKISSPNVLNITLVDLPGITKVPVGDQPSDIEARIRTMILSYIKQDTCLILAVTPANTD 216
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667  217 LANSDALQIASIVDPDGHRTIGVITKLDIMDKGTDARKLLL---GNVVPLRLGYVGVVNRCQEDILLNRTVKEALLAEEK 293
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLllqGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALEAEEE 240
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 3549667  294 FFRSHPVY-HGLADRLGVPQLAKKLNQILVQHIKVLLP 330
Cdd:cd08771 241 FFETHPWYkLLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
251-538 4.94e-131

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: 391.88  E-value: 4.94e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    251 DARKLLLGNVVPLRLGYVGVVNRCQEDILLNRTVKEALLAEEKFFRSHPVYHGLADRLGVPQLAKKLNQILVQHIKVLLP 330
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    331 DLKSRISNALVATAKEHQSYGE-LTESRAGQGALLLNFLSKYCEAYSSLLEGKSeEMSTSELSGGARIHYIFQSIFVKSL 409
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNgIPSDPAEKGKFLLQLITKFNQDFKNLIDGES-EISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    410 EEVDPCEDLTDDDIRTAIQNATGPRSALFVPDVPFEVLVRRQISRLLDPSLQCARFIFEELIKISHRCmMNELQRFPVLR 489
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC-TPELKRFPNLR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 3549667    490 KRMDEVIGDFLREGLEPSEAMIGDIIDMEMDYINTSHPNFIGGTKAVEA 538
Cdd:pfam01031 239 ERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
36-278 2.03e-104

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: 321.06  E-value: 2.03e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667      36 SVIPIVNKLQDIFAQLGSQSTIALPQVVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQLLQTKSranggsddE 115
Cdd:smart00053   3 ELIPLVNKLQDAFSALGQSCDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKT--------E 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667     116 WGEFRHLPETRFYDFSEIRREIEAETNRLVGENKGVADTQIRLKISSPNVLNITLVDLPGITKVPVGDQPSDIEARIRTM 195
Cdd:smart00053  75 YAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKM 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667     196 ILSYIKQDTCLILAVTPANTDLANSDALQIASIVDPDGHRTIGVITKLDIMDKGTDARKLLLGNVVPLRLGYVGVVNRCQ 275
Cdd:smart00053 155 IKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIGVVNRSQ 234

                   ...
gi 3549667     276 EDI 278
Cdd:smart00053 235 KDI 237
Dynamin_N pfam00350
Dynamin family;
62-243 5.10e-65

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 214.02  E-value: 5.10e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667     62 VVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQLLQTKSRANGGSDDEWGEFrhlpETRFYDFSEIRREIEAET 141
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    142 NRLVGENKGVADTQIRLKISSPNVLNITLVDLPGITKVPVGDQpsdiearirTMILSYIKQdTCLILAVTPANTDLANSD 221
Cdd:pfam00350  77 EKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYIKP-ADIILAVTPANVDLSTSE 146
                         170       180
                  ....*....|....*....|..
gi 3549667    222 ALQIASIVDPDGHRTIGVITKL 243
Cdd:pfam00350 147 ALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
666-756 6.22e-34

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 124.93  E-value: 6.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667    666 EAVEIQITKLLLRSYYDIVRKNIEDSVPKAIMHFLVNHTKRELHNVFIKKLYRENLFEEMLQEPDEIAVKRKRTQETLHV 745
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 3549667    746 LQQAYRTLDEL 756
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
665-755 1.81e-32

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 120.80  E-value: 1.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667     665 QEAVEIQITKLLLRSYYDIVRKNIEDSVPKAIMHFLVNHTKRELHNVFIKKLYRENLFEEMLQEPDEIAVKRKRTQETLH 744
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|.
gi 3549667     745 VLQQAYRTLDE 755
Cdd:smart00302  81 LLKKARQIIAA 91
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
62-100 8.32e-04

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: 40.99  E-value: 8.32e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 3549667   62 VVVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLVLQ 100
Cdd:cd09912   3 LAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAVITVLR 41
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
63-257 5.82e-03

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: 38.21  E-value: 5.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667   63 VVVGSQSSGKSSVLEALVGRDFLPRGND-ICTRRPlvlqllqtksranggsddewgefrhlpetrfydfseirreieaet 141
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVpGTTRDP--------------------------------------------- 35
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3549667  142 nrlvgenkgvadTQIRLKISSPNVlNITLVDLPGITKVPVgdqpsdieARIRTMILSYIKQDTCLILAVTPANTDLANSD 221
Cdd:cd00882  36 ------------DVYVKELDKGKV-KLVLVDTPGLDEFGG--------LGREELARLLLRGADLILLVVDSTDRESEEDA 94
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 3549667  222 ALQIASIVDPDGHRTIGVITKLDIMDKGTDARKLLL 257
Cdd:cd00882  95 KLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRL 130
 
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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