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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747472  97 MKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTN--CFLRVGgtdgheaflltegseekksvktvnqlahalhqdeqlh 174
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAviTVLRYG------------------------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747472 175 agslvsvmwpnskcplLKDDLVLMDSPGIDVTTE-LDSWIDKFCLDADVFVLVANSESTLMQTEKQFFHKVSERlSRPNI 253
Cdd:cd09912   44 ----------------LLKGVVLVDTPGLNSTIEhHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKI 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747472 254 FILNNRWDASASEPEYMEEVRRQHmerctsflvdELGVVDRAQAGDRIFFVSAKEVLSARVQKAQGMPEGggalaegfqv 333
Cdd:cd09912  107 FFVLNKIDLLSEEELEEVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQ---------- 166

                        250
                 ....*....|....*.
gi 148747472 334 rmFEFQNFERRFEECI 349
Cdd:cd09912  167 --SGFEELEEHLEEFL 180

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747472  97 MKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTN--CFLRVGgtdgheaflltegseekksvktvnqlahalhqdeqlh 174
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAviTVLRYG------------------------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747472 175 agslvsvmwpnskcplLKDDLVLMDSPGIDVTTE-LDSWIDKFCLDADVFVLVANSESTLMQTEKQFFHKVSERlSRPNI 253
Cdd:cd09912   44 ----------------LLKGVVLVDTPGLNSTIEhHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKI 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747472 254 FILNNRWDASASEPEYMEEVRRQHmerctsflvdELGVVDRAQAGDRIFFVSAKEVLSARVQKAQGMPEGggalaegfqv 333
Cdd:cd09912  107 FFVLNKIDLLSEEELEEVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQ---------- 166

                        250
                 ....*....|....*.
gi 148747472 334 rmFEFQNFERRFEECI 349
Cdd:cd09912  167 --SGFEELEEHLEEFL 180

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747472  97 MKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTN--CFLRVGgtdgheaflltegseekksvktvnqlahalhqdeqlh 174
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLGEEVLPTGVTPTTAviTVLRYG------------------------------------- 43

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747472 175 agslvsvmwpnskcplLKDDLVLMDSPGIDVTTE-LDSWIDKFCLDADVFVLVANSESTLMQTEKQFFHKVSERlSRPNI 253
Cdd:cd09912   44 ----------------LLKGVVLVDTPGLNSTIEhHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKI 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148747472 254 FILNNRWDASASEPEYMEEVRRQHmerctsflvdELGVVDRAQAGDRIFFVSAKEVLSARVQKAQGMPEGggalaegfqv 333
Cdd:cd09912  107 FFVLNKIDLLSEEELEEVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQ---------- 166

                        250
                 ....*....|....*.
gi 148747472 334 rmFEFQNFERRFEECI 349
Cdd:cd09912  167 --SGFEELEEHLEEFL 180

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.

                         10        20        30
                 ....*....|....*....|....*....|..
gi 148747472 100 AFFGRTSNGKSTVINAMLWDKVLP-SGIGHTT 130
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIvSPIPGTT 32