CST, complex subunit STN1, C terminal; STN1 is a component of the CST complex, a complex that binds to single-stranded DNA and is required for protecting telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity on their own. In addition to telomere protection, the CST complex probably has a more general role in DNA metabolism at non-telomeric sites. This entry represents the C-terminal region of Stn1 which has two winged helix-turn-helix (wHTH) motifs, wHTH1 and wHTH2. wHTH1 is structurally similar to that in RPA32 with a large insertion between helices alpha2 and alpha3, unique to Stn1, that may allow interaction with a different set of proteins that function at telomeres such as Ctc1. wHTH2 is most similar to the DNA-binding wHTH motifs of the pur operon repressor and RepE replication initiator, but it does not bind double-stranded DNA.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046841796 212 AGLTALLSEKVKEFLQEKKVQSFYQKELEMVEPLQSLASQPVTHSTCSDQVELKNDAASD-IHSVFKNALHLLQEKGFVF 290
Cdd:pfam09170   1 PGLVSLLSEKIKEFLLENKVQTFYQQELETVESLVSLASRPVQHSSCSQQVDSKGPSTSKqIHSLFKEAIQLLQEKGLVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046841796 291 QRDGGSDKLYYVTSKDKDLHQKIYQIIKEDCQKPNHVEKGCHLMHVLNCVLLNLRWDLNKAVLQQVLELLEDQSDIVSTG 370
Cdd:pfam09170  81 QKDSSFDDLYYVTDQDKDLHKKILDIIREDCQKPKHAEKGCHFLHILSCVRQSYSPNLSEAVLQQVLDLLEDNSDIVSTM 160

                  ....*..
gi 1046841796 371 DHYYTAF 377
Cdd:pfam09170 161 EGYYTAF 167

CST, complex subunit STN1, C terminal; STN1 is a component of the CST complex, a complex that binds to single-stranded DNA and is required for protecting telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity on their own. In addition to telomere protection, the CST complex probably has a more general role in DNA metabolism at non-telomeric sites. This entry represents the C-terminal region of Stn1 which has two winged helix-turn-helix (wHTH) motifs, wHTH1 and wHTH2. wHTH1 is structurally similar to that in RPA32 with a large insertion between helices alpha2 and alpha3, unique to Stn1, that may allow interaction with a different set of proteins that function at telomeres such as Ctc1. wHTH2 is most similar to the DNA-binding wHTH motifs of the pur operon repressor and RepE replication initiator, but it does not bind double-stranded DNA.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046841796 212 AGLTALLSEKVKEFLQEKKVQSFYQKELEMVEPLQSLASQPVTHSTCSDQVELKNDAASD-IHSVFKNALHLLQEKGFVF 290
Cdd:pfam09170   1 PGLVSLLSEKIKEFLLENKVQTFYQQELETVESLVSLASRPVQHSSCSQQVDSKGPSTSKqIHSLFKEAIQLLQEKGLVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046841796 291 QRDGGSDKLYYVTSKDKDLHQKIYQIIKEDCQKPNHVEKGCHLMHVLNCVLLNLRWDLNKAVLQQVLELLEDQSDIVSTG 370
Cdd:pfam09170  81 QKDSSFDDLYYVTDQDKDLHKKILDIIREDCQKPKHAEKGCHFLHILSCVRQSYSPNLSEAVLQQVLDLLEDNSDIVSTM 160

                  ....*..
gi 1046841796 371 DHYYTAF 377
Cdd:pfam09170 161 EGYYTAF 167

CST, complex subunit STN1, C terminal; STN1 is a component of the CST complex, a complex that binds to single-stranded DNA and is required for protecting telomeres from DNA degradation. The CST complex binds single-stranded DNA with high affinity in a sequence-independent manner, while isolated subunits bind DNA with low affinity on their own. In addition to telomere protection, the CST complex probably has a more general role in DNA metabolism at non-telomeric sites. This entry represents the C-terminal region of Stn1 which has two winged helix-turn-helix (wHTH) motifs, wHTH1 and wHTH2. wHTH1 is structurally similar to that in RPA32 with a large insertion between helices alpha2 and alpha3, unique to Stn1, that may allow interaction with a different set of proteins that function at telomeres such as Ctc1. wHTH2 is most similar to the DNA-binding wHTH motifs of the pur operon repressor and RepE replication initiator, but it does not bind double-stranded DNA.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046841796 212 AGLTALLSEKVKEFLQEKKVQSFYQKELEMVEPLQSLASQPVTHSTCSDQVELKNDAASD-IHSVFKNALHLLQEKGFVF 290
Cdd:pfam09170   1 PGLVSLLSEKIKEFLLENKVQTFYQQELETVESLVSLASRPVQHSSCSQQVDSKGPSTSKqIHSLFKEAIQLLQEKGLVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046841796 291 QRDGGSDKLYYVTSKDKDLHQKIYQIIKEDCQKPNHVEKGCHLMHVLNCVLLNLRWDLNKAVLQQVLELLEDQSDIVSTG 370
Cdd:pfam09170  81 QKDSSFDDLYYVTDQDKDLHKKILDIIREDCQKPKHAEKGCHFLHILSCVRQSYSPNLSEAVLQQVLDLLEDNSDIVSTM 160

                  ....*..
gi 1046841796 371 DHYYTAF 377
Cdd:pfam09170 161 EGYYTAF 167

RPA2_DBD_D: A subfamily of OB folds corresponding to the OB fold of the central ssDNA-binding domain (DBD)-D of human RPA2 (also called RPA32). RPA2 is a subunit of Replication protein A (RPA). RPA is a nuclear ssDNA-binding protein (SSB) which appears to be involved in all aspects of DNA metabolism including replication, recombination, and repair. RPA also mediates specific interactions of various nuclear proteins. In animals, plants, and fungi, RPA is a heterotrimer with subunits of 70KDa (RPA1), 32kDa (RPA2), and 14 KDa (RPA3). The major DNA binding activity of RPA is associated with RPA1 DBD-A and DBD-B; RPA2 DBD-D is a weak ssDNA-binding domain. RPA2 DBD-D is also involved in trimerization. The ssDNA binding mechanism is believed to be multistep and to involve conformational change. N-terminal to human RPA2 DBD-D is a domain containing all the known phosphorylation sites of RPA. Human RPA2 is phosphorylated in a cell cycle dependent manner in response to DNA damage. RPA2 interacts physically with menin; the gene encoding menin is a tumor suppressor gene disrupted in multiple endocrine neoplasia type I. This subfamily also includes RPA2 from Cryptosporidium parvum (CpRPA2). CpRPA2 is an SSB, which can be phosphorylated by DNA-PK in vitro.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046841796  64 VDIMGAVISVKERETFYSYGVDDATGVINCVCWKrpsNAESSSDpailstsrelsmtsqlkklqetiEQKTKIGIGDIIR 143
Cdd:cd04478     2 VTLVGVVRNVEEQSTNITYTIDDGTGTIEVRQWL---DDDNDDS-----------------------SEVEPIEEGTYVR 55

                          90       100
                  ....*....|....*....|....*
gi 1046841796 144 VRGYVRMFREEREICATIYYKVDDP 168
Cdd:cd04478    56 VFGNLKSFQGKKSIMAFSIRPVTDF 80