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Conserved domains on  [gi|970644146|gb|KUF85120|]
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Dynamin-1 protein [Phytophthora nicotianae]

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 ...
23-300 3.62e-155

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: 450.16  E-value: 3.62e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  23 INLPQIVVIGSQSSGKSSVLENIVGKDFLPRGSGIVTRRPLVLQLYNSsatiPVEGADETVEEWGEFLHLPGQKFTDFNE 102
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRS----PSESDEDEKEEWGEFLHLKSKEFTDFEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146 103 IRREIEKETDRMTGKNKGISNKSINLKVYSPHVLNLTLVDLPGITKVPVGDQPVNIEEQIRDMCTEFISNPNSIILAVTS 182
Cdd:cd08771   77 LREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146 183 ANTDLANSDALKMAREIDPNGERTIGVLTKLDLMDDGTDAMDML---QGRVIPLKKGYVGVVNRSQADINSQLSIRDSLA 259
Cdd:cd08771  157 ANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALE 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 970644146 260 KEQNFFKTHPAYR-AIASRMGTQYLSKTLNTILMHHIRDCLP 300
Cdd:cd08771  237 AEEEFFETHPWYKlLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
221-511 2.40e-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: 414.99  E-value: 2.40e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  221 DAMDMLQGRVIPLKKGYVGVVNRSQADINSQLSIRDSLAKEQNFFKTHPAYRAIASRMGTQYLSKTLNTILMHHIRDCLP 300
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  301 EIKSKISSMISDLDQELGEMGsPTEQMTPTEMGGCLLNLLSHFSSNFTNSLDGRNHqlVEMDELYGGARINYIFNEIFSK 380
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYG-NGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESE--ISTNELSGGARIRYIFNEIFPK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  381 SLREVNPFDGLSDEDIRTTIRNANGPRQSLFVPEVSFELLAKRQISRLEQPGLQCVDLVFDELQRVTSQCETiELTRFPE 460
Cdd:pfam01031 158 SLEKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTP-ELKRFPN 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 970644146  461 LRDRVMEVVNGMLRASLVPTQAMIQNLIQIELAYVNTNHPDFIGGSRAVAQ 511
Cdd:pfam01031 237 LRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
608-698 5.16e-30

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 113.38  E-value: 5.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  608 ERIETEIIKSLLASYFDIVRKNFLDLVPKAIMCFMVGHSKENIQNELVSSLYREDKLNELLAETGDIAARRSNCDEMRTL 687
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 970644146  688 LQRALEIVNEV 698
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 ...
23-300 3.62e-155

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: 450.16  E-value: 3.62e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  23 INLPQIVVIGSQSSGKSSVLENIVGKDFLPRGSGIVTRRPLVLQLYNSsatiPVEGADETVEEWGEFLHLPGQKFTDFNE 102
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRS----PSESDEDEKEEWGEFLHLKSKEFTDFEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146 103 IRREIEKETDRMTGKNKGISNKSINLKVYSPHVLNLTLVDLPGITKVPVGDQPVNIEEQIRDMCTEFISNPNSIILAVTS 182
Cdd:cd08771   77 LREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146 183 ANTDLANSDALKMAREIDPNGERTIGVLTKLDLMDDGTDAMDML---QGRVIPLKKGYVGVVNRSQADINSQLSIRDSLA 259
Cdd:cd08771  157 ANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALE 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 970644146 260 KEQNFFKTHPAYR-AIASRMGTQYLSKTLNTILMHHIRDCLP 300
Cdd:cd08771  237 AEEEFFETHPWYKlLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
221-511 2.40e-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: 414.99  E-value: 2.40e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  221 DAMDMLQGRVIPLKKGYVGVVNRSQADINSQLSIRDSLAKEQNFFKTHPAYRAIASRMGTQYLSKTLNTILMHHIRDCLP 300
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  301 EIKSKISSMISDLDQELGEMGsPTEQMTPTEMGGCLLNLLSHFSSNFTNSLDGRNHqlVEMDELYGGARINYIFNEIFSK 380
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYG-NGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESE--ISTNELSGGARIRYIFNEIFPK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  381 SLREVNPFDGLSDEDIRTTIRNANGPRQSLFVPEVSFELLAKRQISRLEQPGLQCVDLVFDELQRVTSQCETiELTRFPE 460
Cdd:pfam01031 158 SLEKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTP-ELKRFPN 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 970644146  461 LRDRVMEVVNGMLRASLVPTQAMIQNLIQIELAYVNTNHPDFIGGSRAVAQ 511
Cdd:pfam01031 237 LRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
1-251 4.24e-124

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: 369.21  E-value: 4.24e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146     1 MEQLIPIINKLQDVFSAIGQS-PINLPQIVVIGSQSSGKSSVLENIVGKDFLPRGSGIVTRRPLVLQLYNSSAtipvega 79
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQScDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKT------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146    80 detveEWGEFLHLPGQKFTDFNEIRREIEKETDRMTGKNKGISNKSINLKVYSPHVLNLTLVDLPGITKVPVGDQPVNIE 159
Cdd:smart00053  74 -----EYAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146   160 EQIRDMCTEFISNPNSIILAVTSANTDLANSDALKMAREIDPNGERTIGVLTKLDLMDDGTDAMDMLQGRVIPLKKGYVG 239
Cdd:smart00053 149 YQIKKMIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIG 228
                          250
                   ....*....|..
gi 970644146   240 VVNRSQADINSQ 251
Cdd:smart00053 229 VVNRSQKDIEGK 240
Dynamin_N pfam00350
Dynamin family;
28-213 3.06e-69

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 223.65  E-value: 3.06e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146   28 IVVIGSQSSGKSSVLENIVGKDFLPRGSGIVTRRPLVLQLYNSsatiPVEGADETVEEWGEFlhlpGQKFTDFNEIRREI 107
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGES----PGASEGAVKVEYKDG----EKKFEDFSELREEI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  108 EKETDRMTGKNKGISNKSINLKVYSPHVLNLTLVDLPGITKVPVGDQpvnieeqirDMCTEFIsNPNSIILAVTSANTDL 187
Cdd:pfam00350  73 EKETEKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDL 142
                         170       180
                  ....*....|....*....|....*.
gi 970644146  188 ANSDALKMAREIDPNGERTIGVLTKL 213
Cdd:pfam00350 143 STSEALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
608-698 5.16e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 113.38  E-value: 5.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  608 ERIETEIIKSLLASYFDIVRKNFLDLVPKAIMCFMVGHSKENIQNELVSSLYREDKLNELLAETGDIAARRSNCDEMRTL 687
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 970644146  688 LQRALEIVNEV 698
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
607-698 1.22e-25

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 101.16  E-value: 1.22e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146   607 RERIETEIIKSLLASYFDIVRKNFLDLVPKAIMCFMVGHSKENIQNELVSSLYREDKLNELLAETGDIAARRSNCDEMRT 686
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|..
gi 970644146   687 LLQRALEIVNEV 698
Cdd:smart00302  81 LLKKARQIIAAV 92
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
23-300 3.62e-155

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: 450.16  E-value: 3.62e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  23 INLPQIVVIGSQSSGKSSVLENIVGKDFLPRGSGIVTRRPLVLQLYNSsatiPVEGADETVEEWGEFLHLPGQKFTDFNE 102
Cdd:cd08771    1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRS----PSESDEDEKEEWGEFLHLKSKEFTDFEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146 103 IRREIEKETDRMTGKNKGISNKSINLKVYSPHVLNLTLVDLPGITKVPVGDQPVNIEEQIRDMCTEFISNPNSIILAVTS 182
Cdd:cd08771   77 LREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146 183 ANTDLANSDALKMAREIDPNGERTIGVLTKLDLMDDGTDAMDML---QGRVIPLKKGYVGVVNRSQADINSQLSIRDSLA 259
Cdd:cd08771  157 ANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVNRSQKDIDSGKSIEEALE 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 970644146 260 KEQNFFKTHPAYR-AIASRMGTQYLSKTLNTILMHHIRDCLP 300
Cdd:cd08771  237 AEEEFFETHPWYKlLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
221-511 2.40e-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: 414.99  E-value: 2.40e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  221 DAMDMLQGRVIPLKKGYVGVVNRSQADINSQLSIRDSLAKEQNFFKTHPAYRAIASRMGTQYLSKTLNTILMHHIRDCLP 300
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHPAYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  301 EIKSKISSMISDLDQELGEMGsPTEQMTPTEMGGCLLNLLSHFSSNFTNSLDGRNHqlVEMDELYGGARINYIFNEIFSK 380
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYG-NGIPSDPAEKGKFLLQLITKFNQDFKNLIDGESE--ISTNELSGGARIRYIFNEIFPK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  381 SLREVNPFDGLSDEDIRTTIRNANGPRQSLFVPEVSFELLAKRQISRLEQPGLQCVDLVFDELQRVTSQCETiELTRFPE 460
Cdd:pfam01031 158 SLEKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKCTP-ELKRFPN 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 970644146  461 LRDRVMEVVNGMLRASLVPTQAMIQNLIQIELAYVNTNHPDFIGGSRAVAQ 511
Cdd:pfam01031 237 LRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
1-251 4.24e-124

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: 369.21  E-value: 4.24e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146     1 MEQLIPIINKLQDVFSAIGQS-PINLPQIVVIGSQSSGKSSVLENIVGKDFLPRGSGIVTRRPLVLQLYNSSAtipvega 79
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQScDLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKT------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146    80 detveEWGEFLHLPGQKFTDFNEIRREIEKETDRMTGKNKGISNKSINLKVYSPHVLNLTLVDLPGITKVPVGDQPVNIE 159
Cdd:smart00053  74 -----EYAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146   160 EQIRDMCTEFISNPNSIILAVTSANTDLANSDALKMAREIDPNGERTIGVLTKLDLMDDGTDAMDMLQGRVIPLKKGYVG 239
Cdd:smart00053 149 YQIKKMIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDILENKLLPLRRGYIG 228
                          250
                   ....*....|..
gi 970644146   240 VVNRSQADINSQ 251
Cdd:smart00053 229 VVNRSQKDIEGK 240
Dynamin_N pfam00350
Dynamin family;
28-213 3.06e-69

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 223.65  E-value: 3.06e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146   28 IVVIGSQSSGKSSVLENIVGKDFLPRGSGIVTRRPLVLQLYNSsatiPVEGADETVEEWGEFlhlpGQKFTDFNEIRREI 107
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGES----PGASEGAVKVEYKDG----EKKFEDFSELREEI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  108 EKETDRMTGKNKGISNKSINLKVYSPHVLNLTLVDLPGITKVPVGDQpvnieeqirDMCTEFIsNPNSIILAVTSANTDL 187
Cdd:pfam00350  73 EKETEKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI-KPADIILAVTPANVDL 142
                         170       180
                  ....*....|....*....|....*.
gi 970644146  188 ANSDALKMAREIDPNGERTIGVLTKL 213
Cdd:pfam00350 143 STSEALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
608-698 5.16e-30

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 113.38  E-value: 5.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146  608 ERIETEIIKSLLASYFDIVRKNFLDLVPKAIMCFMVGHSKENIQNELVSSLYREDKLNELLAETGDIAARRSNCDEMRTL 687
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 970644146  688 LQRALEIVNEV 698
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
607-698 1.22e-25

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 101.16  E-value: 1.22e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970644146   607 RERIETEIIKSLLASYFDIVRKNFLDLVPKAIMCFMVGHSKENIQNELVSSLYREDKLNELLAETGDIAARRSNCDEMRT 686
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|..
gi 970644146   687 LLQRALEIVNEV 698
Cdd:smart00302  81 LLKKARQIIAAV 92
 
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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