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Conserved domains on  [gi|332642758|gb|AEE76279|]
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P-loop containing nucleoside triphosphate hydrolases superfamily protein [Arabidopsis thaliana]

Protein Classification

dynamin family protein( domain architecture ID 10171807)

dynamin family protein similar to dynamins and dynamin-like proteins (DLPs), which catalyze membrane fission during clathrin-mediated endocytosis

EC:  3.6.5.5
Gene Ontology:  GO:0005525|GO:0003924
SCOP:  4004047

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 ...
49-343 1.17e-61

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: 208.64  E-value: 1.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758  49 PAVLVVGQQTDGKSALVEALMGFQFNHVGGGTKTRRPITLHMKYDPQCQFPlchlGSDDDPSVSLPKS------LSQIQA 122
Cdd:cd08771    4 PQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDE----DEKEEWGEFLHLKskeftdFEELRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758 123 YIEAENMRLEQEPCSpFSAKEIIVKVQYKYCPNLTIIDTPGLIAPAPGLKNRALQVQaraVEALVRAKMQHKEFIILCLE 202
Cdd:cd08771   80 EIEKETDRVAGENKG-ISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQ---IRSMVKSYISNPRSIILAVV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758 203 D-SSDWSIATTRRIVMQVDPELSRTIVVSTKLDTKIPQFSCSSDVEVFLSPpasaldssLLGDSPFFTSVPSGRvgygqd 281
Cdd:cd08771  156 PaNVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLLLQGK--------VIPLKLGYVGVVNRS------ 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332642758 282 svYKSNDEFKQAVSLREMEdiASLEKKlGRLLTKQEKSRIGISKLRLFLEELLWKRYKESVP 343
Cdd:cd08771  222 --QKDIDSGKSIEEALEAE--EEFFET-HPWYKLLPASRVGTPALRKRLSKLLQKHIRESLP 278
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
49-343 1.17e-61

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: 208.64  E-value: 1.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758  49 PAVLVVGQQTDGKSALVEALMGFQFNHVGGGTKTRRPITLHMKYDPQCQFPlchlGSDDDPSVSLPKS------LSQIQA 122
Cdd:cd08771    4 PQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDE----DEKEEWGEFLHLKskeftdFEELRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758 123 YIEAENMRLEQEPCSpFSAKEIIVKVQYKYCPNLTIIDTPGLIAPAPGLKNRALQVQaraVEALVRAKMQHKEFIILCLE 202
Cdd:cd08771   80 EIEKETDRVAGENKG-ISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQ---IRSMVKSYISNPRSIILAVV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758 203 D-SSDWSIATTRRIVMQVDPELSRTIVVSTKLDTKIPQFSCSSDVEVFLSPpasaldssLLGDSPFFTSVPSGRvgygqd 281
Cdd:cd08771  156 PaNVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLLLQGK--------VIPLKLGYVGVVNRS------ 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332642758 282 svYKSNDEFKQAVSLREMEdiASLEKKlGRLLTKQEKSRIGISKLRLFLEELLWKRYKESVP 343
Cdd:cd08771  222 --QKDIDSGKSIEEALEAE--EEFFET-HPWYKLLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_N pfam00350
Dynamin family;
51-233 6.01e-38

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 139.29  E-value: 6.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758   51 VLVVGQQTDGKSALVEALMGFQFNHVGGGTKTRRPITLHMKYDPQCQ--FPLCHLGSDddpsVSLPKSLSQIQAYIEAEN 128
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASegAVKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758  129 MRLEQEpCSPFSAKEIIVKVQYKYCPNLTIIDTPGLIAPAPGLKNralqvqaraveaLVRAKMqHKEFIILCLED-SSDW 207
Cdd:pfam00350  77 EKIAGT-GKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQE------------LTKEYI-KPADIILAVTPaNVDL 142
                         170       180
                  ....*....|....*....|....*.
gi 332642758  208 SIATTRRIVMQVDPELSRTIVVSTKL 233
Cdd:pfam00350 143 STSEALFLAREVDPNGKRTIGVLTKA 168
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
37-234 6.14e-14

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: 72.22  E-value: 6.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758    37 ALAQELEtpFEAPAVLVVGQQTDGKSALVEALMGFQFNHVGGGTKTRRPITLHMKYDPQCQFPLCHLGSDDdpsvslPKS 116
Cdd:smart00053  17 ALGQSCD--LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLHCKGKK------FTD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758   117 LSQIQAYIEAENMRLEQEPcSPFSAKEIIVKVQYKYCPNLTIIDTPGLIAPAPGLKNRALQVQaraVEALVRAKMQHKEF 196
Cdd:smart00053  89 FDEVRNEIEAETDRVTGTN-KGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQ---IKKMIKQFISREEC 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 332642758   197 IILCLEdSSDWSIATTRRIVM--QVDPELSRTIVVSTKLD 234
Cdd:smart00053 165 LILAVT-PANTDLANSDALKLakEVDPQGLRTIGVITKLD 203
 
Name Accession Description Interval E-value
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
49-343 1.17e-61

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: 208.64  E-value: 1.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758  49 PAVLVVGQQTDGKSALVEALMGFQFNHVGGGTKTRRPITLHMKYDPQCQFPlchlGSDDDPSVSLPKS------LSQIQA 122
Cdd:cd08771    4 PQIVVVGDQSSGKSSVLEALVGRDFLPRGSGICTRRPLELQLRRSPSESDE----DEKEEWGEFLHLKskeftdFEELRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758 123 YIEAENMRLEQEPCSpFSAKEIIVKVQYKYCPNLTIIDTPGLIAPAPGLKNRALQVQaraVEALVRAKMQHKEFIILCLE 202
Cdd:cd08771   80 EIEKETDRVAGENKG-ISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQ---IRSMVKSYISNPRSIILAVV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758 203 D-SSDWSIATTRRIVMQVDPELSRTIVVSTKLDTKIPQFSCSSDVEVFLSPpasaldssLLGDSPFFTSVPSGRvgygqd 281
Cdd:cd08771  156 PaNVDLANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLLLQGK--------VIPLKLGYVGVVNRS------ 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332642758 282 svYKSNDEFKQAVSLREMEdiASLEKKlGRLLTKQEKSRIGISKLRLFLEELLWKRYKESVP 343
Cdd:cd08771  222 --QKDIDSGKSIEEALEAE--EEFFET-HPWYKLLPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_N pfam00350
Dynamin family;
51-233 6.01e-38

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 139.29  E-value: 6.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758   51 VLVVGQQTDGKSALVEALMGFQFNHVGGGTKTRRPITLHMKYDPQCQ--FPLCHLGSDddpsVSLPKSLSQIQAYIEAEN 128
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLRLGESPGASegAVKVEYKDG----EKKFEDFSELREEIEKET 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758  129 MRLEQEpCSPFSAKEIIVKVQYKYCPNLTIIDTPGLIAPAPGLKNralqvqaraveaLVRAKMqHKEFIILCLED-SSDW 207
Cdd:pfam00350  77 EKIAGT-GKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQE------------LTKEYI-KPADIILAVTPaNVDL 142
                         170       180
                  ....*....|....*....|....*.
gi 332642758  208 SIATTRRIVMQVDPELSRTIVVSTKL 233
Cdd:pfam00350 143 STSEALFLAREVDPNGKRTIGVLTKA 168
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
37-234 6.14e-14

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: 72.22  E-value: 6.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758    37 ALAQELEtpFEAPAVLVVGQQTDGKSALVEALMGFQFNHVGGGTKTRRPITLHMKYDPQCQFPLCHLGSDDdpsvslPKS 116
Cdd:smart00053  17 ALGQSCD--LDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIKSKTEYAEFLHCKGKK------FTD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332642758   117 LSQIQAYIEAENMRLEQEPcSPFSAKEIIVKVQYKYCPNLTIIDTPGLIAPAPGLKNRALQVQaraVEALVRAKMQHKEF 196
Cdd:smart00053  89 FDEVRNEIEAETDRVTGTN-KGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQ---IKKMIKQFISREEC 164
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 332642758   197 IILCLEdSSDWSIATTRRIVM--QVDPELSRTIVVSTKLD 234
Cdd:smart00053 165 LILAVT-PANTDLANSDALKLakEVDPQGLRTIGVITKLD 203
 
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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