mTERF (mitochondrial transcription termination factor) domain-containing protein may function as a transcription termination factor that binds promoter DNA and regulates mitochondrial replication and transcription
mTERF; This family contains one sequence of known function Human mitochondrial transcription ...
76-389
7.77e-92
mTERF; This family contains one sequence of known function Human mitochondrial transcription termination factor (mTERF) the rest of the family consists of hypothetical proteins none of which have any functional information. mTERF is a multizipper protein possessing three putative leucine zippers one of which is bipartite. The protein binds DNA as a monomer. The leucine zippers are not implicated in a dimerization role as in other leucine zippers.
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Pssm-ID: 460581 [Multi-domain] Cd Length: 313 Bit Score: 278.72 E-value: 7.77e-92
mTERF; This family contains one sequence of known function Human mitochondrial transcription ...
76-389
7.77e-92
mTERF; This family contains one sequence of known function Human mitochondrial transcription termination factor (mTERF) the rest of the family consists of hypothetical proteins none of which have any functional information. mTERF is a multizipper protein possessing three putative leucine zippers one of which is bipartite. The protein binds DNA as a monomer. The leucine zippers are not implicated in a dimerization role as in other leucine zippers.
Pssm-ID: 460581 [Multi-domain] Cd Length: 313 Bit Score: 278.72 E-value: 7.77e-92
mTERF; This family contains one sequence of known function Human mitochondrial transcription ...
76-389
7.77e-92
mTERF; This family contains one sequence of known function Human mitochondrial transcription termination factor (mTERF) the rest of the family consists of hypothetical proteins none of which have any functional information. mTERF is a multizipper protein possessing three putative leucine zippers one of which is bipartite. The protein binds DNA as a monomer. The leucine zippers are not implicated in a dimerization role as in other leucine zippers.
Pssm-ID: 460581 [Multi-domain] Cd Length: 313 Bit Score: 278.72 E-value: 7.77e-92
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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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.
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(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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specific hits meet or exceed a domain-specific e-value threshold
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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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