ERI1 exoribonuclease 2 isoform 2 [Mus musculus]
DNA topoisomerase( domain architecture ID 10536289)
type I DNA topoisomerase releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex
List of domain hits
Name | Accession | Description | Interval | E-value | ||
zf-GRF | pfam06839 | GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ... |
364-412 | 2.50e-18 | ||
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396. : Pssm-ID: 462017 Cd Length: 45 Bit Score: 78.21 E-value: 2.50e-18
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Name | Accession | Description | Interval | E-value | ||
zf-GRF | pfam06839 | GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ... |
364-412 | 2.50e-18 | ||
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396. Pssm-ID: 462017 Cd Length: 45 Bit Score: 78.21 E-value: 2.50e-18
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Name | Accession | Description | Interval | E-value | ||
zf-GRF | pfam06839 | GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding ... |
364-412 | 2.50e-18 | ||
GRF zinc finger; This presumed zinc binding domain is found in a variety of DNA-binding proteins. It seems likely that this domain is involved in nucleic acid binding. It is named GRF after three conserved residues in the centre of the alignment of the domain. This zinc finger may be related to pfam01396. Pssm-ID: 462017 Cd Length: 45 Bit Score: 78.21 E-value: 2.50e-18
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Blast search parameters | ||||
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