Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin and TSO1. This family is called a CXC domain in.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 169234723  375 SKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKN 410
Cdd:pfam03638   1 KKGCNCKKSKCLKLYCECFAAGVFCSSNCKCEGCKN 36

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234723  26 FAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTL-------NSTTQTPNKIAISPLKSPNKAV 98
Cdd:cd22540  157 PVQVLQQPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGGNVALTLpvnnlvgTQDGATQLQLAAAPSKPSKKIR 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234723  99 KSTVQTITVGGVSTSQFKTIIPLATAPNVQQ-------IQVPGSKFHYVRLVTATSASSSTQPVSQNPstntqplQQAKP 171
Cdd:cd22540  237 KKSAQAAQPAVTVAEQVETVLIETTADNIIQagnnlliVQSPGTGQPAVLQQVQVLQPKQEQQVVQIP-------QQALR 309

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169234723 172 VVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTG 245
Cdd:cd22540  310 VVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQVTANNGTG 383

Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin and TSO1. This family is called a CXC domain in.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 169234723  375 SKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKN 410
Cdd:pfam03638   1 KKGCNCKKSKCLKLYCECFAAGVFCSSNCKCEGCKN 36

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234723  26 FAKPINSKAVTGQTTQVSPPVIAGRVLSQSTPGTPSKTITISESGVIGSTL-------NSTTQTPNKIAISPLKSPNKAV 98
Cdd:cd22540  157 PVQVLQQPQQAHKPVPIKPAPLQTSNTNSASLQVPGNVIKLQSGGNVALTLpvnnlvgTQDGATQLQLAAAPSKPSKKIR 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169234723  99 KSTVQTITVGGVSTSQFKTIIPLATAPNVQQ-------IQVPGSKFHYVRLVTATSASSSTQPVSQNPstntqplQQAKP 171
Cdd:cd22540  237 KKSAQAAQPAVTVAEQVETVLIETTADNIIQagnnlliVQSPGTGQPAVLQQVQVLQPKQEQQVVQIP-------QQALR 309

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169234723 172 VVVNTTPVRMSVPIVSAQAVKQVVPKPINPTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTG 245
Cdd:cd22540  310 VVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQVTANNGTG 383

Tesmin/TSO1-like CXC domain, cysteine-rich domain; This family includes proteins that have two copies of a cysteine rich motif as follows: C-X-C-X4-C-X3-YC-X-C-X6-C-X3-C-X-C-X2-C. The family includes Tesmin and TSO1. This family is called a CXC domain in.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 169234723  375 SKGCNCKRSGCLKNYCECYEAKIMCSSICKCIGCKN 410
Cdd:pfam03638   1 KKGCNCKKSKCLKLYCECFAAGVFCSSNCKCEGCKN 36

CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain containing that binds three zinc ions. It lies on the E3 ubiquitin-protein ligase MSL2 in eukaryotes. The CXC domain critically contributes to the DNA-binding activity of MSL2. It carries 9 invariant cysteines within about a 50 residue region.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 169234723  371 DRRHSKGCNCKRSG-------CLKNYCECYEAKIMCSSiCKCIGCKN 410
Cdd:pfam16682   1 KPPEKKGCRCGTSTptppkltCRNQRCPCYSNGKSCTD-CKCRGCKN 46

DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC domain of Drosophila melanogaster MSL2 forms a Zn(3)Cys(9) cluster and is involved in recruiting members of the dosage compensation complex (DCC) to sites on the X chromosome.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 169234723 375 SKGCNCKRSG-------CLKNYCECYEAKIMCSSiCKCIGCKN 410
Cdd:cd13122    4 KKGCRCGTATqspgvltCRGQRCPCYSNGKSCLD-CKCRGCKN 45