"Interacting selectively with DNA (deoxyribonucleic acid) [goid 3677] [evidence IEA]; The function of binding to a specific DNA sequence in order to modulate transcription. The transcription factor may or may not also interact selectively with a protein or macromolecular complex [goid 3700] [evidence IEA]; Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine) [goid 4252] [evidence IEA]; Interacting selectively with DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding [goid 43565] [evidence IEA]; The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits [goid 46983] [evidence IEA]; Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine) [goid 4252] [evidence IEA]; Interacting selectively with DNA (deoxyribonucleic acid) [goid 3677] [evidence IEA]; Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine) [goid 4252] [evidence IEA]; The function of binding to a specific DNA sequence in order to modulate transcription. The transcription factor may or may not also interact selectively with a protein or macromolecular complex [goid 3700] [evidence IEA]; Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine) [goid 4252] [evidence IEA]; Interacting selectively with DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding [goid 43565] [evidence IEA]; The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits [goid 46983] [evidence IEA]; Interacting selectively with DNA (deoxyribonucleic acid) [goid 3677] [evidence IEA]; Interacting selectively with DNA (deoxyribonucleic acid) [goid 3677] [evidence IEA]; The function of binding to a specific DNA sequence in order to modulate transcription. The transcription factor may or may not also interact selectively with a protein or macromolecular complex [goid 3700] [evidence IEA]; Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine) [goid 4252] [evidence IEA]; Interacting selectively with a transcription factor, any protein required to initiate or regulate transcription [goid 8134] [pmid 1900040] [evidence TAS]; Interacting selectively with DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding [goid 43565] [evidence IEA]; The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits [goid 46983] [evidence IEA]"