Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of ...
617-960
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: 667.74 E-value: 0e+00
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
287-561
1.22e-91
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: 292.23 E-value: 1.22e-91
Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of ...
617-960
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: 667.74 E-value: 0e+00
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
287-561
1.22e-91
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: 292.23 E-value: 1.22e-91
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
288-502
5.48e-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: 110.35 E-value: 5.48e-27
Dynamin-like GTPase OPA1 C-terminal; This entry represents the C-terminal domain of ...
617-960
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: 667.74 E-value: 0e+00
Dynamin_like protein family includes dynamins and Mx proteins; The dynamin family of large ...
287-561
1.22e-91
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: 292.23 E-value: 1.22e-91
Dynamin, GTPase; Large GTPases that mediate vesicle trafficking. Dynamin participates in the ...
288-502
5.48e-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: 110.35 E-value: 5.48e-27
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
292-492
1.50e-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: 46.30 E-value: 1.50e-05
Dynamin central region; This is the stalk region which lies between the GTPase domain, see ...
484-544
1.65e-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: 41.35 E-value: 1.65e-03
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
370-470
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
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
372-468
8.13e-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: 8.13e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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