Tim44/TimA family putative adaptor protein; Members of this family resemble both the ...
6-218
2.35e-105
Tim44/TimA family putative adaptor protein; Members of this family resemble both the eukaryotic protein Tim44, important to the assembly of a protein translocase in mitochondria, and the TimA protein of alpha-proteobacteria such as Caulobacter crescentus. TimA may assist in protein recruitment to the membrane, as Tim44, but appears not to be part of any complex associated with protein translocation.
:
Pssm-ID: 468184 Cd Length: 215 Bit Score: 302.57 E-value: 2.35e-105
Tim44/TimA family putative adaptor protein; Members of this family resemble both the ...
6-218
2.35e-105
Tim44/TimA family putative adaptor protein; Members of this family resemble both the eukaryotic protein Tim44, important to the assembly of a protein translocase in mitochondria, and the TimA protein of alpha-proteobacteria such as Caulobacter crescentus. TimA may assist in protein recruitment to the membrane, as Tim44, but appears not to be part of any complex associated with protein translocation.
Pssm-ID: 468184 Cd Length: 215 Bit Score: 302.57 E-value: 2.35e-105
Tim44-like domain; Tim44 is an essential component of the machinery that mediates the ...
73-218
6.57e-51
Tim44-like domain; Tim44 is an essential component of the machinery that mediates the translocation of nuclear-encoded proteins across the mitochondrial inner membrane. Tim44 is thought to bind phospholipids of the mitochondrial inner membrane both by electrostatic interactions and by penetrating the polar head group region. This family includes the C-terminal region of Tim44 that has been shown to form a stable proteolytic fragment in yeast. This region is also found in a set of smaller bacterial proteins. The molecular function of the bacterial members of this family is unknown but transport seems likely. The crystal structure of the C terminal of Tim44 has revealed a large hydrophobic pocket which might play an important role in interacting with the acyl chains of lipid molecules in the mitochondrial membrane.
Pssm-ID: 427835 Cd Length: 145 Bit Score: 162.02 E-value: 6.57e-51
Tim44 is an essential component of the machinery that mediates the translocation of ...
73-218
3.10e-45
Tim44 is an essential component of the machinery that mediates the translocation of nuclear-encoded proteins across the mitochondrial inner membrane; Tim44 is thought to bind phospholipids of the mitochondrial inner membrane both by electrostatic interactions and by penetrating the polar head group region.
Pssm-ID: 214950 Cd Length: 147 Bit Score: 147.47 E-value: 3.10e-45
TIM44-related membrane protein TimA; TimA was first described in Caulobacter crescentus, a ...
7-219
1.78e-41
TIM44-related membrane protein TimA; TimA was first described in Caulobacter crescentus, a member of the alpha-proteobacterial lineage that gave rise to the mitochondrion. It is notable because of homology to Tim44, a protein involved in protein translocation in both human and yeast mitochondria, although TimA itself is not considered involved in protein translocation. TimA is found localized to the plasma membrane, on the cytosolic face. The mitochondrial homolog, Tim44, is found as a peripheral protein of the inner face of the mitochondrial inner membrane, and serves as an adaptor to recruit other subunits into the translocation complex, rather than in transport channel itself.
Pssm-ID: 411362 Cd Length: 198 Bit Score: 139.42 E-value: 1.78e-41
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein ...
72-204
7.25e-08
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tim proteins. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130057 [Multi-domain] Cd Length: 378 Bit Score: 51.80 E-value: 7.25e-08
Tim44/TimA family putative adaptor protein; Members of this family resemble both the ...
6-218
2.35e-105
Tim44/TimA family putative adaptor protein; Members of this family resemble both the eukaryotic protein Tim44, important to the assembly of a protein translocase in mitochondria, and the TimA protein of alpha-proteobacteria such as Caulobacter crescentus. TimA may assist in protein recruitment to the membrane, as Tim44, but appears not to be part of any complex associated with protein translocation.
Pssm-ID: 468184 Cd Length: 215 Bit Score: 302.57 E-value: 2.35e-105
Tim44-like domain; Tim44 is an essential component of the machinery that mediates the ...
73-218
6.57e-51
Tim44-like domain; Tim44 is an essential component of the machinery that mediates the translocation of nuclear-encoded proteins across the mitochondrial inner membrane. Tim44 is thought to bind phospholipids of the mitochondrial inner membrane both by electrostatic interactions and by penetrating the polar head group region. This family includes the C-terminal region of Tim44 that has been shown to form a stable proteolytic fragment in yeast. This region is also found in a set of smaller bacterial proteins. The molecular function of the bacterial members of this family is unknown but transport seems likely. The crystal structure of the C terminal of Tim44 has revealed a large hydrophobic pocket which might play an important role in interacting with the acyl chains of lipid molecules in the mitochondrial membrane.
Pssm-ID: 427835 Cd Length: 145 Bit Score: 162.02 E-value: 6.57e-51
Tim44 is an essential component of the machinery that mediates the translocation of ...
73-218
3.10e-45
Tim44 is an essential component of the machinery that mediates the translocation of nuclear-encoded proteins across the mitochondrial inner membrane; Tim44 is thought to bind phospholipids of the mitochondrial inner membrane both by electrostatic interactions and by penetrating the polar head group region.
Pssm-ID: 214950 Cd Length: 147 Bit Score: 147.47 E-value: 3.10e-45
TIM44-related membrane protein TimA; TimA was first described in Caulobacter crescentus, a ...
7-219
1.78e-41
TIM44-related membrane protein TimA; TimA was first described in Caulobacter crescentus, a member of the alpha-proteobacterial lineage that gave rise to the mitochondrion. It is notable because of homology to Tim44, a protein involved in protein translocation in both human and yeast mitochondria, although TimA itself is not considered involved in protein translocation. TimA is found localized to the plasma membrane, on the cytosolic face. The mitochondrial homolog, Tim44, is found as a peripheral protein of the inner face of the mitochondrial inner membrane, and serves as an adaptor to recruit other subunits into the translocation complex, rather than in transport channel itself.
Pssm-ID: 411362 Cd Length: 198 Bit Score: 139.42 E-value: 1.78e-41
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein ...
72-204
7.25e-08
mitochondrial import inner membrane, translocase subunit; The mitochondrial protein translocase (MPT) family, which brings nuclearly encoded preproteins into mitochondria, is very complex with 19 currently identified protein constituents.These proteins include several chaperone proteins, four proteins of the outer membrane translocase (Tom) import receptor, five proteins of the Tom channel complex, five proteins of the inner membrane translocase (Tim) and three "motor" proteins. This family is specific for the Tim proteins. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130057 [Multi-domain] Cd Length: 378 Bit Score: 51.80 E-value: 7.25e-08
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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)
mapped to the query sequence.
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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
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
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
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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