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Conserved domains on  [gi|1058916509|ref|NP_001317309|]
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dynamin-1-like protein isoform 8 [Homo sapiens]

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 ...
23-315 1.37e-138

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: 407.79  E-value: 1.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509  23 IQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSqedkrkttgeendpatwknsrHLSKGVEAEE 102
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSP---------------------SESDEDEKEE 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 103 WGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIREL 182
Cdd:cd08771    60 WGEFLHLKSKEFTDFEELREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSM 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 183 ILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVL---MGRVIPVKLGIIGVVN 259
Cdd:cd08771   140 VKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVN 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1058916509 260 RSQLDINNKKSVTDSIRDEYAFLQKKYP---SLANRNGTKYLARTLNRLLMHHIRDCLP 315
Cdd:cd08771   220 RSQKDIDSGKSIEEALEAEEEFFETHPWyklLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
238-523 8.88e-138

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: 406.13  E-value: 8.88e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 238 DAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKK--YPSLANRNGTKYLARTLNRLLMHHIRDCLP 315
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHpaYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 316 ELKTRINVLAAQYQSLLNSYGEPVD----DKSATLLQLITKFATEYCNTIEGTAKyIETSELCGGARICYIFHETFGRTL 391
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPsdpaEKGKFLLQLITKFNQDFKNLIDGESE-ISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 392 ESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCsnysTQELLRFP 471
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC----TPELKRFP 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1058916509 472 KLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNN 523
Cdd:pfam01031 236 NLRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
GED pfam02212
Dynamin GTPase effector domain;
616-706 1.45e-35

Dynamin GTPase effector domain;


:

Pssm-ID: 460495  Cd Length: 91  Bit Score: 129.17  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 616 EQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKA 695
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1058916509 696 LQGASQIIAEI 706
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 ...
23-315 1.37e-138

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: 407.79  E-value: 1.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509  23 IQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSqedkrkttgeendpatwknsrHLSKGVEAEE 102
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSP---------------------SESDEDEKEE 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 103 WGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIREL 182
Cdd:cd08771    60 WGEFLHLKSKEFTDFEELREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSM 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 183 ILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVL---MGRVIPVKLGIIGVVN 259
Cdd:cd08771   140 VKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVN 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1058916509 260 RSQLDINNKKSVTDSIRDEYAFLQKKYP---SLANRNGTKYLARTLNRLLMHHIRDCLP 315
Cdd:cd08771   220 RSQKDIDSGKSIEEALEAEEEFFETHPWyklLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
238-523 8.88e-138

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: 406.13  E-value: 8.88e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 238 DAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKK--YPSLANRNGTKYLARTLNRLLMHHIRDCLP 315
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHpaYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 316 ELKTRINVLAAQYQSLLNSYGEPVD----DKSATLLQLITKFATEYCNTIEGTAKyIETSELCGGARICYIFHETFGRTL 391
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPsdpaEKGKFLLQLITKFNQDFKNLIDGESE-ISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 392 ESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCsnysTQELLRFP 471
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC----TPELKRFP 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1058916509 472 KLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNN 523
Cdd:pfam01031 236 NLRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
1-268 1.54e-108

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: 329.15  E-value: 1.54e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509    1 MEALIPVINKLQDVFNTVGADI-IQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEdkrktt 79
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCdLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTE------ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509   80 geendpatwknsrhlskgveaeeWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVD 159
Cdd:smart00053  75 -----------------------YAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLID 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509  160 LPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDA 239
Cdd:smart00053 132 LPGITKVAVGDQPPDIEYQIKKMIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDA 211
                          250       260
                   ....*....|....*....|....*....
gi 1058916509  240 MDVLMGRVIPVKLGIIGVVNRSQLDINNK 268
Cdd:smart00053 212 RDILENKLLPLRRGYIGVVNRSQKDIEGK 240
Dynamin_N pfam00350
Dynamin family;
28-230 4.62e-64

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 210.17  E-value: 4.62e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509  28 IVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENDPatwknsrhlskgveaeewgkfl 107
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDG---------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 108 htkNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQpkdielqirELILRFI 187
Cdd:pfam00350  59 ---EKKFEDFSELREEIEKETEKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI 126
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1058916509 188 sNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKL 230
Cdd:pfam00350 127 -KPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
616-706 1.45e-35

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 129.17  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 616 EQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKA 695
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1058916509 696 LQGASQIIAEI 706
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
615-706 6.67e-34

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 124.66  E-value: 6.67e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509  615 REQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLK 694
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|..
gi 1058916509  695 ALQGASQIIAEI 706
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 ...
23-315 1.37e-138

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: 407.79  E-value: 1.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509  23 IQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSqedkrkttgeendpatwknsrHLSKGVEAEE 102
Cdd:cd08771     1 IDLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSP---------------------SESDEDEKEE 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 103 WGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIREL 182
Cdd:cd08771    60 WGEFLHLKSKEFTDFEELREEIEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSM 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 183 ILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVL---MGRVIPVKLGIIGVVN 259
Cdd:cd08771   140 VKSYISNPRSIILAVVPANVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILlllQGKVIPLKLGYVGVVN 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1058916509 260 RSQLDINNKKSVTDSIRDEYAFLQKKYP---SLANRNGTKYLARTLNRLLMHHIRDCLP 315
Cdd:cd08771   220 RSQKDIDSGKSIEEALEAEEEFFETHPWyklLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
238-523 8.88e-138

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: 406.13  E-value: 8.88e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 238 DAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKK--YPSLANRNGTKYLARTLNRLLMHHIRDCLP 315
Cdd:pfam01031   1 DALDILRNRVIPLKLGYVGVVNRSQKDINGNKSIEEALQDERAFFETHpaYRLLADKCGTPYLAKKLNQILVNHIRKSLP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 316 ELKTRINVLAAQYQSLLNSYGEPVD----DKSATLLQLITKFATEYCNTIEGTAKyIETSELCGGARICYIFHETFGRTL 391
Cdd:pfam01031  81 DLKNKINELLQKTEKELEKYGNGIPsdpaEKGKFLLQLITKFNQDFKNLIDGESE-ISTNELSGGARIRYIFNEIFPKSL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 392 ESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCsnysTQELLRFP 471
Cdd:pfam01031 160 EKIDPLENLSDEEIRTAIRNSRGIRLPLFVPEKAFELLVKQQIKRLEEPALKCVELVYEELERIIHKC----TPELKRFP 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1058916509 472 KLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNN 523
Cdd:pfam01031 236 NLRERIKEVVEDLLRERLEPTEKMIRSLIEMELAYINTNHPDFIGGLNAVRE 287
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
1-268 1.54e-108

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: 329.15  E-value: 1.54e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509    1 MEALIPVINKLQDVFNTVGADI-IQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEdkrktt 79
Cdd:smart00053   1 MEELIPLVNKLQDAFSALGQSCdLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTE------ 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509   80 geendpatwknsrhlskgveaeeWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVD 159
Cdd:smart00053  75 -----------------------YAEFLHCKGKKFTDFDEVRNEIEAETDRVTGTNKGISGIPINLRVYSPHVLNLTLID 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509  160 LPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDA 239
Cdd:smart00053 132 LPGITKVAVGDQPPDIEYQIKKMIKQFISREECLILAVTPANTDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDA 211
                          250       260
                   ....*....|....*....|....*....
gi 1058916509  240 MDVLMGRVIPVKLGIIGVVNRSQLDINNK 268
Cdd:smart00053 212 RDILENKLLPLRRGYIGVVNRSQKDIEGK 240
Dynamin_N pfam00350
Dynamin family;
28-230 4.62e-64

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 210.17  E-value: 4.62e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509  28 IVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENDPatwknsrhlskgveaeewgkfl 107
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKDG---------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 108 htkNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQpkdielqirELILRFI 187
Cdd:pfam00350  59 ---EKKFEDFSELREEIEKETEKIAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQ---------ELTKEYI 126
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1058916509 188 sNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKL 230
Cdd:pfam00350 127 -KPADIILAVTPANVDLSTSEALFLAREVDPNGKRTIGVLTKA 168
GED pfam02212
Dynamin GTPase effector domain;
616-706 1.45e-35

Dynamin GTPase effector domain;


Pssm-ID: 460495  Cd Length: 91  Bit Score: 129.17  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509 616 EQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKA 695
Cdd:pfam02212   1 EESETEEIRSLINSYFNIVRKTIADQIPKAIMHFLVNESKESLQKELLQKLYKSELLDELLKEDPEIAQKRKECKKRLEA 80
                          90
                  ....*....|.
gi 1058916509 696 LQGASQIIAEI 706
Cdd:pfam02212  81 LKQAREILSEV 91
GED smart00302
Dynamin GTPase effector domain;
615-706 6.67e-34

Dynamin GTPase effector domain;


Pssm-ID: 128597  Cd Length: 92  Bit Score: 124.66  E-value: 6.67e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1058916509  615 REQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLK 694
Cdd:smart00302   1 YEDSELEEIKSLVKSYFTIVSKTLADQVPKAIMYLLVNESKDSLQNELLALLYKEELLDELLEEDPEIASKRKELKKRLE 80
                           90
                   ....*....|..
gi 1058916509  695 ALQGASQIIAEI 706
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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