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Conserved domains on  [gi|18860835|ref|NP_570846|]
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dynamin-like GTPase OPA1, mitochondrial isoform 4 [Homo sapiens]

Protein Classification

dynamin family protein( domain architecture ID 17693365)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OPA1_C pfam19434
Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of ...
618-961 0e+00

Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of Dynamin-like GTPase OPA1. This protein is involved in mitochondrial fusion and inner membrane remodelling, essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Mutations in human OPA1 cause optic atrophy. This domain includes the helix bundle (HB) domains HB1 (C-terminal) and HB2 (equivalent to extreme C-terminal bundle signaling element (BSE) and to the stalk domain of dynamin-1, respectively) and the lipid-interacting stalk (LIS, equivalent to the PH domain of dynamin-1).


:

Pssm-ID: 466080  Cd Length: 345  Bit Score: 668.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   618 EEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPK-GKEHDD 696
Cdd:pfam19434   1 EEALQKKLWEKVSSHVFENIYLPAAQSENAGTFNTTVDIKLKQWADKQLPQKSVEVGWETLKEEFSRLLEKAKaGKDHDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   697 IFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRW 776
Cdd:pfam19434  81 IFDKLKEAVVEEALKRHQWDSKAEDSLRVIQLNALEDRSVPDKQQWDSAVKFMEEALKERLKEVESQLKEMVGPGFWERW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   777 LYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNL 856
Cdd:pfam19434 161 LYWKSRTPEQHKRSAVKNELEKLLKSDPKHKAELSDDELTTVRKNLEAQGVEVDPEFIRETWHLVYRQHFLKKALARAQE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   857 CRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQL 936
Cdd:pfam19434 241 CRKGFYYYQQGFLDTELDCNDVVLFWRIQRMLKATSNALRQQIMNREARRLEKEVKEVLDDISQDPEKKKKLLTGRRVQL 320
                         330       340
                  ....*....|....*....|....*
gi 18860835   937 AEDLKKVREIQEKLDAFIEALHQEK 961
Cdd:pfam19434 321 AEELKRVRQIQEKLEEFIQALNKEK 345
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
288-562 5.97e-92

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: 293.00  E-value: 5.97e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 288 HLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGeMMTRSPVKVTLSEGPHH-VALFKDSSREFDLTKEE---DLAALRHE 363
Cdd:cd08771   2 DLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSG-ICTRRPLELQLRRSPSEsDEDEKEEWGEFLHLKSKeftDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 364 IELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVD 443
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 444 AERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQiIEGKLFPMKaLGYFAVVTGKG---NSSESIEAIREYE 520
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLL-LQGKVIPLK-LGYVGVVNRSQkdiDSGKSIEEALEAE 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 18860835 521 EEFFQNSKLLKTsmLKAHQVTTRNLSLAVSDCFWKMVRESVE 562
Cdd:cd08771 239 EEFFETHPWYKL--LPASRVGTPALRKRLSKLLQKHIRESLP 278
 
Name Accession Description Interval E-value
OPA1_C pfam19434
Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of ...
618-961 0e+00

Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of Dynamin-like GTPase OPA1. This protein is involved in mitochondrial fusion and inner membrane remodelling, essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Mutations in human OPA1 cause optic atrophy. This domain includes the helix bundle (HB) domains HB1 (C-terminal) and HB2 (equivalent to extreme C-terminal bundle signaling element (BSE) and to the stalk domain of dynamin-1, respectively) and the lipid-interacting stalk (LIS, equivalent to the PH domain of dynamin-1).


Pssm-ID: 466080  Cd Length: 345  Bit Score: 668.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   618 EEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPK-GKEHDD 696
Cdd:pfam19434   1 EEALQKKLWEKVSSHVFENIYLPAAQSENAGTFNTTVDIKLKQWADKQLPQKSVEVGWETLKEEFSRLLEKAKaGKDHDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   697 IFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRW 776
Cdd:pfam19434  81 IFDKLKEAVVEEALKRHQWDSKAEDSLRVIQLNALEDRSVPDKQQWDSAVKFMEEALKERLKEVESQLKEMVGPGFWERW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   777 LYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNL 856
Cdd:pfam19434 161 LYWKSRTPEQHKRSAVKNELEKLLKSDPKHKAELSDDELTTVRKNLEAQGVEVDPEFIRETWHLVYRQHFLKKALARAQE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   857 CRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQL 936
Cdd:pfam19434 241 CRKGFYYYQQGFLDTELDCNDVVLFWRIQRMLKATSNALRQQIMNREARRLEKEVKEVLDDISQDPEKKKKLLTGRRVQL 320
                         330       340
                  ....*....|....*....|....*
gi 18860835   937 AEDLKKVREIQEKLDAFIEALHQEK 961
Cdd:pfam19434 321 AEELKRVRQIQEKLEEFIQALNKEK 345
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
288-562 5.97e-92

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: 293.00  E-value: 5.97e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 288 HLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGeMMTRSPVKVTLSEGPHH-VALFKDSSREFDLTKEE---DLAALRHE 363
Cdd:cd08771   2 DLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSG-ICTRRPLELQLRRSPSEsDEDEKEEWGEFLHLKSKeftDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 364 IELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVD 443
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 444 AERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQiIEGKLFPMKaLGYFAVVTGKG---NSSESIEAIREYE 520
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLL-LQGKVIPLK-LGYVGVVNRSQkdiDSGKSIEEALEAE 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 18860835 521 EEFFQNSKLLKTsmLKAHQVTTRNLSLAVSDCFWKMVRESVE 562
Cdd:cd08771 239 EEFFETHPWYKL--LPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_N pfam00350
Dynamin family;
292-470 1.18e-46

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 164.33  E-value: 1.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   292 VVVVGDQSAGKTSVLEMIAQARIFPRGSGeMMTRSPVKVTLSEGPH-HVALFKDSSREFdLTKEEDLAALRHEIELRMRK 370
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPG-PTTRRPTVLRLGESPGaSEGAVKVEYKDG-EKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   371 NVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMApdtketifsISKAYMqNPNAIILCIQDGSVDAERSIVT 450
Cdd:pfam00350  79 IAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQE---------LTKEYI-KPADIILAVTPANVDLSTSEAL 148
                         170       180
                  ....*....|....*....|
gi 18860835   451 DLVSQMDPHGRRTIFVLTKV 470
Cdd:pfam00350 149 FLAREVDPNGKRTIGVLTKA 168
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
289-503 4.00e-27

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: 111.12  E-value: 4.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835    289 LPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGeMMTRSPVKVTLSEGPHHVALFKdSSREFDLTkeeDLAALRHEIELRM 368
Cdd:smart00053  26 LPQIAVVGGQSAGKSSVLENFVGRDFLPRGSG-IVTRRPLILQLIKSKTEYAEFL-HCKGKKFT---DFDEVRNEIEAET 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835    369 RKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSI 448
Cdd:smart00053 101 DRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFISREECLILAVTPANTDLANSD 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 18860835    449 VTDLVSQMDPHGRRTIFVLTKVDLAEKNvaspSRIQQIIEGKLFPMKAlGYFAVV 503
Cdd:smart00053 181 ALKLAKEVDPQGLRTIGVITKLDLMDEG----TDARDILENKLLPLRR-GYIGVV 230
YeeP COG3596
Predicted GTPase [General function prediction only];
372-474 2.96e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 40.90  E-value: 2.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 372 VKEGCTVSPETISLNVkgPGLQRMVLVDLPGvintVTSGMAPDTKETIFsisKAYMQNPNAIILCI--QDGSVDAERSIV 449
Cdd:COG3596  69 VGRPCTREIQRYRLES--DGLPGLVLLDTPG----LGEVNERDREYREL---RELLPEADLILWVVkaDDRALATDEEFL 139
                        90       100
                ....*....|....*....|....*
gi 18860835 450 TDLVSQMDPHgrRTIFVLTKVDLAE 474
Cdd:COG3596 140 QALRAQYPDP--PVLVVLTQVDRLE 162
 
Name Accession Description Interval E-value
OPA1_C pfam19434
Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of ...
618-961 0e+00

Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of Dynamin-like GTPase OPA1. This protein is involved in mitochondrial fusion and inner membrane remodelling, essential for normal mitochondrial morphology by regulating the equilibrium between mitochondrial fusion and mitochondrial fission. Mutations in human OPA1 cause optic atrophy. This domain includes the helix bundle (HB) domains HB1 (C-terminal) and HB2 (equivalent to extreme C-terminal bundle signaling element (BSE) and to the stalk domain of dynamin-1, respectively) and the lipid-interacting stalk (LIS, equivalent to the PH domain of dynamin-1).


Pssm-ID: 466080  Cd Length: 345  Bit Score: 668.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   618 EEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPK-GKEHDD 696
Cdd:pfam19434   1 EEALQKKLWEKVSSHVFENIYLPAAQSENAGTFNTTVDIKLKQWADKQLPQKSVEVGWETLKEEFSRLLEKAKaGKDHDD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   697 IFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRW 776
Cdd:pfam19434  81 IFDKLKEAVVEEALKRHQWDSKAEDSLRVIQLNALEDRSVPDKQQWDSAVKFMEEALKERLKEVESQLKEMVGPGFWERW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   777 LYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNL 856
Cdd:pfam19434 161 LYWKSRTPEQHKRSAVKNELEKLLKSDPKHKAELSDDELTTVRKNLEAQGVEVDPEFIRETWHLVYRQHFLKKALARAQE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   857 CRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQL 936
Cdd:pfam19434 241 CRKGFYYYQQGFLDTELDCNDVVLFWRIQRMLKATSNALRQQIMNREARRLEKEVKEVLDDISQDPEKKKKLLTGRRVQL 320
                         330       340
                  ....*....|....*....|....*
gi 18860835   937 AEDLKKVREIQEKLDAFIEALHQEK 961
Cdd:pfam19434 321 AEELKRVRQIQEKLEEFIQALNKEK 345
DLP_1 cd08771
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
288-562 5.97e-92

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: 293.00  E-value: 5.97e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 288 HLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGeMMTRSPVKVTLSEGPHH-VALFKDSSREFDLTKEE---DLAALRHE 363
Cdd:cd08771   2 DLPQIVVVGDQSSGKSSVLEALVGRDFLPRGSG-ICTRRPLELQLRRSPSEsDEDEKEEWGEFLHLKSKeftDFEELREE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 364 IELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVD 443
Cdd:cd08771  81 IEKETDRVAGENKGISPEPIRLEIESPDVPNLTLVDLPGLIKVPVGDQPEDIEEQIRSMVKSYISNPRSIILAVVPANVD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 444 AERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQiIEGKLFPMKaLGYFAVVTGKG---NSSESIEAIREYE 520
Cdd:cd08771 161 LANSEALKLAREVDPEGERTIGVLTKLDLMDPGTDAEDILLL-LQGKVIPLK-LGYVGVVNRSQkdiDSGKSIEEALEAE 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 18860835 521 EEFFQNSKLLKTsmLKAHQVTTRNLSLAVSDCFWKMVRESVE 562
Cdd:cd08771 239 EEFFETHPWYKL--LPASRVGTPALRKRLSKLLQKHIRESLP 278
Dynamin_N pfam00350
Dynamin family;
292-470 1.18e-46

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 164.33  E-value: 1.18e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   292 VVVVGDQSAGKTSVLEMIAQARIFPRGSGeMMTRSPVKVTLSEGPH-HVALFKDSSREFdLTKEEDLAALRHEIELRMRK 370
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPG-PTTRRPTVLRLGESPGaSEGAVKVEYKDG-EKKFEDFSELREEIEKETEK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   371 NVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMApdtketifsISKAYMqNPNAIILCIQDGSVDAERSIVT 450
Cdd:pfam00350  79 IAGTGKGISSEPIVLEILSPLVPGLTLVDTPGLDSVAVGDQE---------LTKEYI-KPADIILAVTPANVDLSTSEAL 148
                         170       180
                  ....*....|....*....|
gi 18860835   451 DLVSQMDPHGRRTIFVLTKV 470
Cdd:pfam00350 149 FLAREVDPNGKRTIGVLTKA 168
DYNc smart00053
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
289-503 4.00e-27

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: 111.12  E-value: 4.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835    289 LPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGeMMTRSPVKVTLSEGPHHVALFKdSSREFDLTkeeDLAALRHEIELRM 368
Cdd:smart00053  26 LPQIAVVGGQSAGKSSVLENFVGRDFLPRGSG-IVTRRPLILQLIKSKTEYAEFL-HCKGKKFT---DFDEVRNEIEAET 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835    369 RKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSI 448
Cdd:smart00053 101 DRVTGTNKGISGIPINLRVYSPHVLNLTLIDLPGITKVAVGDQPPDIEYQIKKMIKQFISREECLILAVTPANTDLANSD 180
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 18860835    449 VTDLVSQMDPHGRRTIFVLTKVDLAEKNvaspSRIQQIIEGKLFPMKAlGYFAVV 503
Cdd:smart00053 181 ALKLAKEVDPQGLRTIGVITKLDLMDEG----TDARDILENKLLPLRR-GYIGVV 230
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
293-493 1.07e-05

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 46.68  E-value: 1.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 293 VVVGDQSAGKTSVLEMIAQARIFPRGSgemmtrspvkvtlsegphhvalfkdssrefdltkeedlaalrheielrmrknv 372
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSD----------------------------------------------------- 27
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 373 KEGCTVSPETISLNVKGPGLQrMVLVDLPGVINTVTSGMAPDTKEtifsiskaYMQNPNAIILCIQDGSVDAERSIVTDL 452
Cdd:cd00882  28 VPGTTRDPDVYVKELDKGKVK-LVLVDTPGLDEFGGLGREELARL--------LLRGADLILLVVDSTDRESEEDAKLLI 98
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 18860835 453 VSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQIIEGKLFP 493
Cdd:cd00882  99 LRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAKILGV 139
Dynamin_M pfam01031
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
485-545 1.52e-03

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: 41.74  E-value: 1.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18860835   485 QIIEGKLFPMKaLGYFAVVTgKG----NSSESIEAIREYEEEFFQNSKLLKtsmLKAHQVTTRNL 545
Cdd:pfam01031   4 DILRNRVIPLK-LGYVGVVN-RSqkdiNGNKSIEEALQDERAFFETHPAYR---LLADKCGTPYL 63
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
371-471 1.88e-03

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 39.63  E-value: 1.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 371 NVKEGCTVSPETISLnvkGPGLQRMVLVDLPGVintvtsGMAPDTKETIFSISKAYMQNPNAIILCI--QDGSVDAERsi 448
Cdd:cd11383  26 GDRRPTTRAAQAYVW---QTGGDGLVLLDLPGV------GERGRRDREYEELYRRLLPEADLVLWLLdaDDRALAADH-- 94
                        90       100
                ....*....|....*....|...
gi 18860835 449 vTDLVSQMDPHGRRTIFVLTKVD 471
Cdd:cd11383  95 -DFYLLPLAGHDAPLLFVLNQVD 116
YeeP COG3596
Predicted GTPase [General function prediction only];
372-474 2.96e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 40.90  E-value: 2.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835 372 VKEGCTVSPETISLNVkgPGLQRMVLVDLPGvintVTSGMAPDTKETIFsisKAYMQNPNAIILCI--QDGSVDAERSIV 449
Cdd:COG3596  69 VGRPCTREIQRYRLES--DGLPGLVLLDTPG----LGEVNERDREYREL---RELLPEADLILWVVkaDDRALATDEEFL 139
                        90       100
                ....*....|....*....|....*
gi 18860835 450 TDLVSQMDPHgrRTIFVLTKVDLAE 474
Cdd:COG3596 140 QALRAQYPDP--PVLVVLTQVDRLE 162
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
373-469 6.97e-03

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 37.21  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18860835   373 KEGCTVSPETISLNVKGPglqRMVLVDLPGVINTVTSGMapDTKETIFSISKAymqnpNAIILCIQdgSVDAERSIVTDL 452
Cdd:pfam01926  29 YPGTTRDPNEGRLELKGK---QIILVDTPGLIEGASEGE--GLGRAFLAIIEA-----DLILFVVD--SEEGITPLDEEL 96
                          90
                  ....*....|....*..
gi 18860835   453 VSQMDPHGRRTIFVLTK 469
Cdd:pfam01926  97 LELLRENKKPIILVLNK 113
 
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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