P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927102  23 LRDDLVLVDSPGTDVTTE-LDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERlSKPNIFILNNRWDASASEPEY 101
Cdd:cd09912   44 LLKGVVLVDTPGLNSTIEhHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKIFFVLNKIDLLSEEELE 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927102 102 MEDVRRQHmerclhflveELKVVNALEAQNRIFFVSAKEVLSARKQKAQGMPESgvalaegfharlQEFQNFEQIFEECI 181
Cdd:cd09912  123 EVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQ------------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 767927102  23 LRDDLVLVDSPGTDVTTE-LDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERlSKPNIFILNNRWDASASEPEY 101
Cdd:cd09912   44 LLKGVVLVDTPGLNSTIEhHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKIFFVLNKIDLLSEEELE 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927102 102 MEDVRRQHmerclhflveELKVVNALEAQNRIFFVSAKEVLSARKQKAQGMPESgvalaegfharlQEFQNFEQIFEECI 181
Cdd:cd09912  123 EVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQ------------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 767927102  23 LRDDLVLVDSPGTDVTTE-LDSWIDKFCLDADVFVLVANSESTLMNTEKHFFHKVNERlSKPNIFILNNRWDASASEPEY 101
Cdd:cd09912   44 LLKGVVLVDTPGLNSTIEhHTEITESFLPRADAVIFVLSADQPLTESEREFLKEILKW-SGKKIFFVLNKIDLLSEEELE 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927102 102 MEDVRRQHmerclhflveELKVVNALEAQNRIFFVSAKEVLSARKQKAQGMPESgvalaegfharlQEFQNFEQIFEECI 181
Cdd:cd09912  123 EVLEYSRE----------ELGVLELGGGEPRIFPVSAKEALEARLQGDEELLEQ------------SGFEELEEHLEEFL 180