third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the third BRCT domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159163289  35 QAPEDLLDGCRIYLCGFSGRKLDKLRRLINSGGGVRFNQLNEDVTHVIVGDYDDELKQFWNKSAHRPHVVGAKWLLECFS 114
Cdd:cd17718    1 EKAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNESVTHVVVGESSEELLKELAKLAGRPHVVTPSWLLECFK 80

                 ..
gi 159163289 115 KG 116
Cdd:cd17718   81 QG 82

third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the third BRCT domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159163289  35 QAPEDLLDGCRIYLCGFSGRKLDKLRRLINSGGGVRFNQLNEDVTHVIVGDYDDELKQFWNKSAHRPHVVGAKWLLECFS 114
Cdd:cd17718    1 EKAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNESVTHVVVGESSEELLKELAKLAGRPHVVTPSWLLECFK 80

                 ..
gi 159163289 115 KG 116
Cdd:cd17718   81 QG 82

breast cancer carboxy-terminal domain;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 159163289    38 EDLLDGCRIYLCG-FSGRKLDKLRRLINSGGGVRFNQLNE-DVTHVIVGDYDDELKQFWNKSAHRPHVVGAKWLLECF 113
Cdd:smart00292   1 PKLFKGKTFYITGsFDKEERDELKELIEALGGKVTSSLSSkTTTHVIVGSPEGGKLELLKAIALGIPIVKEEWLLDCL 78

third BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the third BRCT domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159163289  35 QAPEDLLDGCRIYLCGFSGRKLDKLRRLINSGGGVRFNQLNEDVTHVIVGDYDDELKQFWNKSAHRPHVVGAKWLLECFS 114
Cdd:cd17718    1 EKAGDFLDGCKIYLSGFSGAELDKLRRIINAGGGTRFNQLNESVTHVVVGESSEELLKELAKLAGRPHVVTPSWLLECFK 80

                 ..
gi 159163289 115 KG 116
Cdd:cd17718   81 QG 82

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159163289  44 CRIYLCGFSGRKLDKLRRLINSGGGVRFNQLNEDVTHVIVGDYDDELKqFWNKSAHRPHVVGAKWLLEC 112
Cdd:cd00027    1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKY-YLAALAWGIPIVSPEWLLDC 68

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159163289   37 PEDLLDGCRIYLCGFSGRKLDKLRRLINSGGGVRFNQLNEDVTHVIVgdydDELKQFWNKSAHRPHVVGAKWLLECFSKG 116
Cdd:pfam16589   1 LPNLFEPLRFYINAIPSPSRSKLKRLIEANGGTVVDNINPAVYIVIA----PYNKTDKLAENTKLGVVSPQWIFDCVKKG 76

                  ....*...
gi 159163289  117 YMLSEEPY 124
Cdd:pfam16589  77 KLLPLENY 84

Second (C-terminal) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins; XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This model corresponds to the second BRCT domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159163289  39 DLLDGCRIYLCG-FSGRKLDKLRRLINSGGGVRFNQLNEDVTHVIV-GDYDDELKQFWNKSAH----RPhvvgaKWLLEC 112
Cdd:cd17707    4 DFFSGKHFFLYGdFPADERRLLKRYITAFNGEVEDYMSDKVTFVVTnQEWDDNFDEALAENPSlafvRP-----RWIYAC 78

                         90
                 ....*....|...
gi 159163289 113 FSKGYMLSEEPYI 125
Cdd:cd17707   79 HEKQKLLPCQPYL 91

first (N-terminal) BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the first BRCT domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159163289  42 DGCRIYLCGfsgrKLD-KLRRLINSGGGVRFNQLNEDVTHVIVGDYDD----ELKQFWNKSahrphVVGAKWLLECFSKG 116
Cdd:cd17714    2 KDVKYFVVG----NLDeKVEQLLKNGGAKEVSYLSDMATHVIVDDNDNpevgEARDLFELP-----VVTSSWVILSIKAG 72

                 ....
gi 159163289 117 YMLS 120
Cdd:cd17714   73 KLLP 76

second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159163289  40 LLDGCRIYLCG-F-SGRKLDKLRRLINSGGGV---RFNQLNEDV-------------------THVIVgdYdDELKQFWN 95
Cdd:cd17720    1 LFDGCHFYFHGtFkPPTTKDDLEQLVKAGGGTvlsREPKPDSDVtqtintvayarpdsdlancTHYII--Y-DKLNDKKP 77

                         90       100
                 ....*....|....*....|...
gi 159163289  96 KSAHRPHV--VGAKWLLECFSKG 116
Cdd:cd17720   78 AKVRQGKVrvVPVSWLLDCISQF 100

BRCT domain of DNA ligase 3 (LIG3) and similar proteins; LIG3 (EC 6.5.1.1), also termed DNA ligase III, or polydeoxyribonucleotide synthase [ATP] 3, functions as heterodimer with DNA-repair protein XRCC1 in the nucleus and can correct defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159163289  39 DLLDGCRIYLCGFSGRKLDKLRRLINSGGGVRFNQLN-EDVTHVIVgDYDDELKqfwNKSAhrpHVVGAKWLLECFSKG 116
Cdd:cd18431    3 DIFTGVKVYLPGSVEDDYKKLKRYFIAYDGDVVEEYDeEDATHVVV-DRDDKLG---NPSA---KVVSPEWLWDCIKKQ 74

second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159163289  41 LDGCRIYLCGFSGRKLDKLRRLINSGGGVRFNQLNEDVTHVIVGD-----YDDELKqfWNKSahrpHVVGAKWLLECFSK 115
Cdd:cd17731    3 FKGLVICVTGFDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSpsgqkYEFARK--WNSI----HIVTPEWLYDSIEA 76

                 .
gi 159163289 116 G 116
Cdd:cd17731   77 G 77

BRCT domain of DNA polymerase lambda and similar proteins; DNA polymerase lambda, also termed Pol Lambda, or DNA polymerase beta-2 (Pol beta2), or DNA polymerase kappa, is involved in base excision repair (BER) and is responsible for repair of lesions that give rise to abasic (AP) sites in DNA. It also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. DNA polymerase lambda has both template-dependent and template-independent (terminal transferase) DNA polymerase activities, as well as a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity. DNA polymerase lambda contains one BRCT domain.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 159163289  57 DKLRRLINSGGGVRFNQLNEDVTHVIVGDYDDELKQFwNKSAHRPHVVGAKWLLECFSKGYML 119
Cdd:cd17715   19 ELFQRYIVQYGGQIVEDFGEGVTHVVVDDGMDAERKV-DRDPPGAQLVKSGWLSACIQEKRLV 80

BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159163289  41 LDGCRIYLCGF--SGRKLDK--LRRLINSGGGVRFNQLNEDVTHVIVGDYDDElKQFWNKSAHRPHVVGAKWLLECFSKG 116
Cdd:cd17729   14 LKGCVIVFSGVipTGIDPERsrLWKLAESLGAKVVTDLSPRTTHLVAAKLGTE-KVKQALKMPGIHVVHPDWLWACAERW 92

                 ....*
gi 159163289 117 YMLSE 121
Cdd:cd17729   93 ERVDE 97