Dynamin family;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950876  127 IALFGSTGAGKSSLINAIIQQAmFLPvSGESICTSCIVQVSSGccvQYEAKIHLLSDQEWREELKNLTKLLHRTEELSRE 206
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRD-ILP-RGPGPTTRRPTVLRLG---ESPGASEGAVKVEYKDGEKKFEDFSELREEIEKE 75

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950876 308 EGVVLVDIPGTGDFNSKRDEMWKKTIDKCSVIWVISDIERVsggQAHEDLlnESIKACQRGFCRDVALVVTKMDKL 383
Cdd:cd09912   46 KGVVLVDTPGLNSTIEHHTEITESFLPRADAVIFVLSADQP---LTESER--EFLKEILKWSGKKIFFVLNKIDLL 116

Dynamin family;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950876  127 IALFGSTGAGKSSLINAIIQQAmFLPvSGESICTSCIVQVSSGccvQYEAKIHLLSDQEWREELKNLTKLLHRTEELSRE 206
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRD-ILP-RGPGPTTRRPTVLRLG---ESPGASEGAVKVEYKDGEKKFEDFSELREEIEKE 75

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950876  71 LIPDEKLESRTRRVLSNTYQKL---IQSVFLDDSiPNGvkYLINRLLALIEKPTVDPIYIALFGSTGAGKSSLINAIIQQ 147
Cdd:cd01855   72 LLPKDVKPNRLKQWVKKRLKIGglkIKDVILVSA-KKG--WGVEELIEEIKKLAKYRGDVYVVGATNVGKSTLINALLKS 148

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950876 308 EGVVLVDIPGTGDFNSKRDEMWKKTIDKCSVIWVISDIERVsggQAHEDLlnESIKACQRGFCRDVALVVTKMDKL 383
Cdd:cd09912   46 KGVVLVDTPGLNSTIEHHTEITESFLPRADAVIFVLSADQP---LTESER--EFLKEILKWSGKKIFFVLNKIDLL 116

ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli. [Protein synthesis, Other]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 767950876  107 KYLINRLLALIEK--PTVDpIYIalFGSTGAGKSSLINAIIQQ 147
Cdd:TIGR03597 138 GNGIDELLDKIKKarNKKD-VYV--VGVTNVGKSSLINKLLKQ 177

Dynamin family;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950876  127 IALFGSTGAGKSSLINAIIQQAmFLPvSGESICTSCIVQVSSGccvQYEAKIHLLSDQEWREELKNLTKLLHRTEELSRE 206
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRD-ILP-RGPGPTTRRPTVLRLG---ESPGASEGAVKVEYKDGEKKFEDFSELREEIEKE 75

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950876  71 LIPDEKLESRTRRVLSNTYQKL---IQSVFLDDSiPNGvkYLINRLLALIEKPTVDPIYIALFGSTGAGKSSLINAIIQQ 147
Cdd:cd01855   72 LLPKDVKPNRLKQWVKKRLKIGglkIKDVILVSA-KKG--WGVEELIEEIKKLAKYRGDVYVVGATNVGKSTLINALLKS 148

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.

                         10        20        30
                 ....*....|....*....|....*....|....
gi 767950876 128 ALFGSTGAGKSSLINAIIQQAMfLPVSGESICTS 161
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEV-AAVGDRRPTTR 33

conjugal transfer ATPase TrbB; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950876 127 IALFGSTGAGKSSLINAIIQQaMFLPVSGESIC----TSCIvQVSSGCCVQYEAKIHLlsdqewreelkNLTKLLHRT-- 200
Cdd:PRK13894 151 ILVIGGTGSGKTTLVNAIINE-MVIQDPTERVFiiedTGEI-QCAAENYVQYHTSIDV-----------NMTALLKTTlr 217

                         90       100
                 ....*....|....*....|....
gi 767950876 201 --------EELSREEA----DAWN 212
Cdd:PRK13894 218 mrpdrilvGEVRGPEAldllMAWN 241

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.

                          10        20
                  ....*....|....*....|.
gi 767950876  127 IALFGSTGAGKSSLINAIIQQ 147
Cdd:pfam01926   2 VALVGRPNVGKSTLINALTGA 22

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950876 127 IALFGSTGAGKSSLINAIIqQAMFLPVsGESICTSCIVQVSsgcCVQYEAKIHLLSDQEWREELKNLTKLLHRTEELSRE 206
Cdd:cd08771    6 IVVVGDQSSGKSSVLEALV-GRDFLPR-GSGICTRRPLELQ---LRRSPSESDEDEKEEWGEFLHLKSKEFTDFEELREE 80

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
                 ....*....|....*....|
gi 767950876 128 ALFGSTGAGKSSLINAIIQQ 147
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQ 20