MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
41-115
1.04e-45
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.
The actual alignment was detected with superfamily member cd02680:
Pssm-ID: 469712 Cd Length: 75 Bit Score: 156.70 E-value: 1.04e-45
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
1-32
1.73e-07
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.
The actual alignment was detected with superfamily member cd02681:
Pssm-ID: 469712 Cd Length: 76 Bit Score: 49.13 E-value: 1.73e-07
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
41-115
1.04e-45
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.
Pssm-ID: 239143 Cd Length: 75 Bit Score: 156.70 E-value: 1.04e-45
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
547-674
2.44e-35
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains.
Pssm-ID: 238132 Cd Length: 150 Bit Score: 130.50 E-value: 2.44e-35
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
43-108
2.19e-15
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.
Pssm-ID: 461228 Cd Length: 66 Bit Score: 71.03 E-value: 2.19e-15
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
555-661
4.35e-09
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.
Pssm-ID: 460050 Cd Length: 136 Bit Score: 55.24 E-value: 4.35e-09
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
1-32
1.73e-07
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.
Pssm-ID: 239144 Cd Length: 76 Bit Score: 49.13 E-value: 1.73e-07
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
41-115
1.04e-45
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.
Pssm-ID: 239143 Cd Length: 75 Bit Score: 156.70 E-value: 1.04e-45
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ...
547-674
2.44e-35
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains.
Pssm-ID: 238132 Cd Length: 150 Bit Score: 130.50 E-value: 2.44e-35
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
42-113
1.38e-19
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.
Pssm-ID: 239121 Cd Length: 75 Bit Score: 83.13 E-value: 1.38e-19
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
43-108
2.19e-15
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.
Pssm-ID: 461228 Cd Length: 66 Bit Score: 71.03 E-value: 2.19e-15
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ...
555-661
4.35e-09
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.
Pssm-ID: 460050 Cd Length: 136 Bit Score: 55.24 E-value: 4.35e-09
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
43-112
1.06e-07
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.
Pssm-ID: 239141 Cd Length: 75 Bit Score: 49.57 E-value: 1.06e-07
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
1-32
1.73e-07
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.
Pssm-ID: 239144 Cd Length: 76 Bit Score: 49.13 E-value: 1.73e-07
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
43-106
1.06e-03
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with an n-terminal serine/threonine kinase domain. The molecular function of the MIT domain is unclear.
Pssm-ID: 239147 Cd Length: 75 Bit Score: 38.26 E-value: 1.06e-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,
or click on the triangles, if present, that represent functional sites (conserved features)
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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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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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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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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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