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Conserved domains on  [gi|578807554|ref|XP_005247653|]
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mitofusin-1 isoform X1 [Homo sapiens]

Protein Classification

Fzo-like mitofusin( domain architecture ID 10177731)

Fzo-like mitofusin such as Homo sapien mitofusin 2 (MFN2), a homolog of the Drosophila protein fuzzy onion (Fzo), is a dynamin-like GTPase that plays a central role in regulating mitochondrial fusion and cell metabolism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Fzo_mitofusin pfam04799
fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a ...
577-735 5.78e-88

fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a mediator of mitochondrial fusion. This conserved region is also found in the human mitofusin protein.


:

Pssm-ID: 461432  Cd Length: 159  Bit Score: 273.42  E-value: 5.78e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  577 QEELMITLVTGLASVTSRTSMGIIIVGGVIWKTIGWKLLSVSLTMYGALYLYERLSWTTHAKERAFKQQFVNYATEKLRM 656
Cdd:pfam04799   1 QEELMLSLRLGLASVTSRGSLGVLVVGGVVWRTVGWRLIALSGALYGLLYLYERLTWTTKAKERAFKRQFVDHATQKLRL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578807554  657 IVSSTSANCSHQVKQQIATTFARLCQQVDITQKQLEEEIARLPKEIDQLEKIQNNSKLLRNKAVQLENELENFTKQFLP 735
Cdd:pfam04799  81 IVSFTSANCSHQVQQELSSTFARLCQQVDETQNELEEEIARLEREIQQLESVQSRSKTLRNKATFLENELDDFQETYLK 159
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
76-328 3.46e-44

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


:

Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 156.94  E-value: 3.46e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  76 MKVAFFGRTSSGKSSVINAMLWDKVLPSGIGHITN--CFLSVEgtdgdkaylmtegsdekksvktvnqlahalhmdkdlk 153
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAviTVLRYG------------------------------------- 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554 154 agclvrvfwpkakcalLRDDLVLVDSPGTDVTTE-LDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERlSKPNI 232
Cdd:cd09912   44 ----------------LLKGVVLVDTPGLNSTIEhHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKI 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554 233 FILNNRWDASASEPEYMEDVRRQHmerclhflveELKVVNALEAQNRIFFVSAKEVLSARKQKAQGMPESgvalaegfha 312
Cdd:cd09912  107 FFVLNKIDLLSEEELEEVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQ---------- 166
                        250
                 ....*....|....*.
gi 578807554 313 rlQEFQNFEQIFEECI 328
Cdd:cd09912  167 --SGFEELEEHLEEFL 180
 
Name Accession Description Interval E-value
Fzo_mitofusin pfam04799
fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a ...
577-735 5.78e-88

fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a mediator of mitochondrial fusion. This conserved region is also found in the human mitofusin protein.


Pssm-ID: 461432  Cd Length: 159  Bit Score: 273.42  E-value: 5.78e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  577 QEELMITLVTGLASVTSRTSMGIIIVGGVIWKTIGWKLLSVSLTMYGALYLYERLSWTTHAKERAFKQQFVNYATEKLRM 656
Cdd:pfam04799   1 QEELMLSLRLGLASVTSRGSLGVLVVGGVVWRTVGWRLIALSGALYGLLYLYERLTWTTKAKERAFKRQFVDHATQKLRL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578807554  657 IVSSTSANCSHQVKQQIATTFARLCQQVDITQKQLEEEIARLPKEIDQLEKIQNNSKLLRNKAVQLENELENFTKQFLP 735
Cdd:pfam04799  81 IVSFTSANCSHQVQQELSSTFARLCQQVDETQNELEEEIARLEREIQQLESVQSRSKTLRNKATFLENELDDFQETYLK 159
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
76-328 3.46e-44

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 156.94  E-value: 3.46e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  76 MKVAFFGRTSSGKSSVINAMLWDKVLPSGIGHITN--CFLSVEgtdgdkaylmtegsdekksvktvnqlahalhmdkdlk 153
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAviTVLRYG------------------------------------- 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554 154 agclvrvfwpkakcalLRDDLVLVDSPGTDVTTE-LDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERlSKPNI 232
Cdd:cd09912   44 ----------------LLKGVVLVDTPGLNSTIEhHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKI 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554 233 FILNNRWDASASEPEYMEDVRRQHmerclhflveELKVVNALEAQNRIFFVSAKEVLSARKQKAQGMPESgvalaegfha 312
Cdd:cd09912  107 FFVLNKIDLLSEEELEEVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQ---------- 166
                        250
                 ....*....|....*.
gi 578807554 313 rlQEFQNFEQIFEECI 328
Cdd:cd09912  167 --SGFEELEEHLEEFL 180
Dynamin_N pfam00350
Dynamin family;
78-237 3.51e-27

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 108.47  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554   78 VAFFGRTSSGKSSVINAMLWDKVLPSGIGHITNCFLSV---EGTDGDKAYLMTEGSDEKKSVKTVNQLAHALHMDKDLKA 154
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLrlgESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  155 GCLVRV---FWPKAKCALLRDDLVLVDSPG-TDVTTELDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERLSKP 230
Cdd:pfam00350  81 GTGKGIssePIVLEILSPLVPGLTLVDTPGlDSVAVGDQELTKEYIKPADIILAVTPANVDLSTSEALFLAREVDPNGKR 160

                  ....*..
gi 578807554  231 NIFILNN 237
Cdd:pfam00350 161 TIGVLTK 167
YeeP COG3596
Predicted GTPase [General function prediction only];
69-287 1.11e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 41.68  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  69 EVLSRRHMKVAFFGRTSSGKSSVINAMLWDKVlpSGIGHITNCflsvegTDGDKAYLMTEGSDekksvktvnqlahalhm 148
Cdd:COG3596   33 LLVELPPPVIALVGKTGAGKSSLINALFGAEV--AEVGVGRPC------TREIQRYRLESDGL----------------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554 149 dkdlkagclvrvfwpkakcallrDDLVLVDSPGTDVT---TELDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNE 225
Cdd:COG3596   88 -----------------------PGLVLLDTPGLGEVnerDREYRELRELLPEADLILWVVKADDRALATDEEFLQALRA 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578807554 226 RLS-KPNIFILN--------NRWDASAS--EPEYMEDVRRQHMERCLHFLVeelkvvnaleAQNRIFFVSAKE 287
Cdd:COG3596  145 QYPdPPVLVVLTqvdrlepeREWDPPYNwpSPPKEQNIRRALEAIAEQLGV----------PIDRVIPVSAAE 207
 
Name Accession Description Interval E-value
Fzo_mitofusin pfam04799
fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a ...
577-735 5.78e-88

fzo-like conserved region; Family of putative transmembrane GTPase. The fzo protein is a mediator of mitochondrial fusion. This conserved region is also found in the human mitofusin protein.


Pssm-ID: 461432  Cd Length: 159  Bit Score: 273.42  E-value: 5.78e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  577 QEELMITLVTGLASVTSRTSMGIIIVGGVIWKTIGWKLLSVSLTMYGALYLYERLSWTTHAKERAFKQQFVNYATEKLRM 656
Cdd:pfam04799   1 QEELMLSLRLGLASVTSRGSLGVLVVGGVVWRTVGWRLIALSGALYGLLYLYERLTWTTKAKERAFKRQFVDHATQKLRL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578807554  657 IVSSTSANCSHQVKQQIATTFARLCQQVDITQKQLEEEIARLPKEIDQLEKIQNNSKLLRNKAVQLENELENFTKQFLP 735
Cdd:pfam04799  81 IVSFTSANCSHQVQQELSSTFARLCQQVDETQNELEEEIARLEREIQQLESVQSRSKTLRNKATFLENELDDFQETYLK 159
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
76-328 3.46e-44

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 156.94  E-value: 3.46e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  76 MKVAFFGRTSSGKSSVINAMLWDKVLPSGIGHITN--CFLSVEgtdgdkaylmtegsdekksvktvnqlahalhmdkdlk 153
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAviTVLRYG------------------------------------- 43
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554 154 agclvrvfwpkakcalLRDDLVLVDSPGTDVTTE-LDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERlSKPNI 232
Cdd:cd09912   44 ----------------LLKGVVLVDTPGLNSTIEhHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKI 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554 233 FILNNRWDASASEPEYMEDVRRQHmerclhflveELKVVNALEAQNRIFFVSAKEVLSARKQKAQGMPESgvalaegfha 312
Cdd:cd09912  107 FFVLNKIDLLSEEELEEVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQ---------- 166
                        250
                 ....*....|....*.
gi 578807554 313 rlQEFQNFEQIFEECI 328
Cdd:cd09912  167 --SGFEELEEHLEEFL 180
Dynamin_N pfam00350
Dynamin family;
78-237 3.51e-27

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 108.47  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554   78 VAFFGRTSSGKSSVINAMLWDKVLPSGIGHITNCFLSV---EGTDGDKAYLMTEGSDEKKSVKTVNQLAHALHMDKDLKA 154
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRDILPRGPGPTTRRPTVLrlgESPGASEGAVKVEYKDGEKKFEDFSELREEIEKETEKIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  155 GCLVRV---FWPKAKCALLRDDLVLVDSPG-TDVTTELDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERLSKP 230
Cdd:pfam00350  81 GTGKGIssePIVLEILSPLVPGLTLVDTPGlDSVAVGDQELTKEYIKPADIILAVTPANVDLSTSEALFLAREVDPNGKR 160

                  ....*..
gi 578807554  231 NIFILNN 237
Cdd:pfam00350 161 TIGVLTK 167
YeeP COG3596
Predicted GTPase [General function prediction only];
69-287 1.11e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 41.68  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554  69 EVLSRRHMKVAFFGRTSSGKSSVINAMLWDKVlpSGIGHITNCflsvegTDGDKAYLMTEGSDekksvktvnqlahalhm 148
Cdd:COG3596   33 LLVELPPPVIALVGKTGAGKSSLINALFGAEV--AEVGVGRPC------TREIQRYRLESDGL----------------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578807554 149 dkdlkagclvrvfwpkakcallrDDLVLVDSPGTDVT---TELDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNE 225
Cdd:COG3596   88 -----------------------PGLVLLDTPGLGEVnerDREYRELRELLPEADLILWVVKADDRALATDEEFLQALRA 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578807554 226 RLS-KPNIFILN--------NRWDASAS--EPEYMEDVRRQHMERCLHFLVeelkvvnaleAQNRIFFVSAKE 287
Cdd:COG3596  145 QYPdPPVLVVLTqvdrlepeREWDPPYNwpSPPKEQNIRRALEAIAEQLGV----------PIDRVIPVSAAE 207
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
77-96 4.18e-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: 37.60  E-value: 4.18e-03
                          10        20
                  ....*....|....*....|
gi 578807554   77 KVAFFGRTSSGKSSVINAML 96
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALT 20
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
79-101 5.77e-03

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that 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. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 38.38  E-value: 5.77e-03
                         10        20
                 ....*....|....*....|...
gi 578807554  79 AFFGRTSSGKSSVINAMLWDKVL 101
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVG 23
 
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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