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 ...
71-268
1.01e-36
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.
The actual alignment was detected with superfamily member pfam02536:
Pssm-ID: 460581 [Multi-domain] Cd Length: 313 Bit Score: 132.73 E-value: 1.01e-36
mTERF; This family contains one sequence of known function Human mitochondrial transcription ...
71-268
1.01e-36
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: 132.73 E-value: 1.01e-36
Mitochondrial termination factor repeats; Human mitochondrial termination factor is a ...
224-253
5.45e-03
Mitochondrial termination factor repeats; Human mitochondrial termination factor is a DNA-binding protein that acts as a transcription termination factor. Six repeats occur in human mTERF, that also are present in numerous plant proteins.
Pssm-ID: 197848 Cd Length: 31 Bit Score: 33.95 E-value: 5.45e-03
mTERF; This family contains one sequence of known function Human mitochondrial transcription ...
71-268
1.01e-36
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: 132.73 E-value: 1.01e-36
mTERF; This family contains one sequence of known function Human mitochondrial transcription ...
175-253
1.38e-03
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: 39.51 E-value: 1.38e-03
Mitochondrial termination factor repeats; Human mitochondrial termination factor is a ...
224-253
5.45e-03
Mitochondrial termination factor repeats; Human mitochondrial termination factor is a DNA-binding protein that acts as a transcription termination factor. Six repeats occur in human mTERF, that also are present in numerous plant proteins.
Pssm-ID: 197848 Cd Length: 31 Bit Score: 33.95 E-value: 5.45e-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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