histone-fold domain found in protein Dr1 and similar proteins; Dr1, also called down-regulator of transcription 1 or negative cofactor 2-beta (NC2-beta), is a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription. It forms a heterodimer with DRAP1. The association of the Dr1/DRAP1 heterodimer with TBP results in functional repression of both activated and basal transcription of class II genes. Dr1 can bind to DNA on its own. Dr1 is a component of the ADA2A-containing complex (ATAC) that has histone acetyltransferase activity on histones H3 and H4.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357883823  65 EKEFSLPRTRLLEVIKSAMPEGfhpPAAKDYTMQLMNDACIEFMQLVASQAMVEHSKGNPKTekvsITPKHVLNALRNLD 144
Cdd:cd22905     1 DDDLSLPKATVNKLIKEVLPPD---MRVSKDTRELILECCTEFIHLISSEANEICEKEKKKT----ISPEHVLKALENLG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357883823 145 YKEYAETAKRELNLDEGRTTSRQPTKRLKKTKADMEregealraeqEALRVEQEKLFAQAREKMNQ 210
Cdd:cd22905    74 FGEYIEEVEEALEDHKEEAKKRPKKSNKLKKSGLTE----------EELLREQQELFAQARERQES 129

histone-fold domain found in protein Dr1 and similar proteins; Dr1, also called down-regulator of transcription 1 or negative cofactor 2-beta (NC2-beta), is a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription. It forms a heterodimer with DRAP1. The association of the Dr1/DRAP1 heterodimer with TBP results in functional repression of both activated and basal transcription of class II genes. Dr1 can bind to DNA on its own. Dr1 is a component of the ADA2A-containing complex (ATAC) that has histone acetyltransferase activity on histones H3 and H4.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357883823  65 EKEFSLPRTRLLEVIKSAMPEGfhpPAAKDYTMQLMNDACIEFMQLVASQAMVEHSKGNPKTekvsITPKHVLNALRNLD 144
Cdd:cd22905     1 DDDLSLPKATVNKLIKEVLPPD---MRVSKDTRELILECCTEFIHLISSEANEICEKEKKKT----ISPEHVLKALENLG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357883823 145 YKEYAETAKRELNLDEGRTTSRQPTKRLKKTKADMEregealraeqEALRVEQEKLFAQAREKMNQ 210
Cdd:cd22905    74 FGEYIEEVEEALEDHKEEAKKRPKKSNKLKKSGLTE----------EELLREQQELFAQARERQES 129

histone-fold domain found in protein Dr1 and similar proteins; Dr1, also called down-regulator of transcription 1 or negative cofactor 2-beta (NC2-beta), is a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription. It forms a heterodimer with DRAP1. The association of the Dr1/DRAP1 heterodimer with TBP results in functional repression of both activated and basal transcription of class II genes. Dr1 can bind to DNA on its own. Dr1 is a component of the ADA2A-containing complex (ATAC) that has histone acetyltransferase activity on histones H3 and H4.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357883823  65 EKEFSLPRTRLLEVIKSAMPEGfhpPAAKDYTMQLMNDACIEFMQLVASQAMVEHSKGNPKTekvsITPKHVLNALRNLD 144
Cdd:cd22905     1 DDDLSLPKATVNKLIKEVLPPD---MRVSKDTRELILECCTEFIHLISSEANEICEKEKKKT----ISPEHVLKALENLG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357883823 145 YKEYAETAKRELNLDEGRTTSRQPTKRLKKTKADMEregealraeqEALRVEQEKLFAQAREKMNQ 210
Cdd:cd22905    74 FGEYIEEVEEALEDHKEEAKKRPKKSNKLKKSGLTE----------EELLREQQELFAQARERQES 129

histone-fold domain found in DNA polymerase epsilon subunit 3 (POLE3) and similar proteins; POLE3, also called arsenic-transactivated protein (AsTP), chromatin accessibility complex 17 kDa protein (CHRAC-17), DNA polymerase II subunit 3, or DNA polymerase epsilon subunit p17, may participate in DNA repair and in chromosomal DNA replication. It is an accessory component of the DNA polymerase epsilon complex, which consists of four subunits: the catalytic subunit POLE and the accessory subunits POLE2, POLE3 and POLE4. It forms a complex with CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1. In fungi, POLE3 has been named as DNA polymerase epsilon subunit D (DPB4, also known as DNA polymerase II subunit D). DPB4 acts as an accessory component of the DNA polymerase epsilon (DNA polymerase II) that consists of POL2, DPB2, DPB3 and DPB4, and participates in chromosomal DNA replication. It also functions as a component of the ISW2 complex, which acts in remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357883823  67 EFSLPRTRLLEVIKSAMPEGFHppAAKDyTMQLMNDACIEFMQLVASQAMvEHSKGNpktEKVSITPKHVLNALRNLDYK 146
Cdd:cd22928     2 DLELPRAVITRIIKEALPEGVQ--VSKD-ARLALSRAATVFILYLTAAAN-EIAKSN---KRKTISADDVLKALEELEFD 74

                          90
                  ....*....|.
gi 1357883823 147 EYAETAKRELN 157
Cdd:cd22928    75 EFVPPLKEELE 85