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 1085987369 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 1085987369  40 TQASPPVVTGRVLSQSTPGTPSKTITISESgvigsTLNSTTQTPNKIAISPLKSPNKTVKSAVQTITVGGMSTSQFKTII 119
Cdd:cd22540   183 TNSASLQVPGNVIKLQSGGNVALTLPVNNL-----VGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVL 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085987369 120 PLATAPNVQQ-------IQVPGSKFHYVRLVTATTASSSAQPVSQSPsvntqplQQAKPVVVNTTPVRMSVPFVQAQAVK 192
Cdd:cd22540   258 IETTADNIIQagnnlliVQSPGTGQPAVLQQVQVLQPKQEQQVVQIP-------QQALRVVQAASATLPTVPQKPLQNIQ 330

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1085987369 193 QVVPKPINSTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTG 245
Cdd:cd22540   331 IQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQVTANNGTG 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 1085987369 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 1085987369  40 TQASPPVVTGRVLSQSTPGTPSKTITISESgvigsTLNSTTQTPNKIAISPLKSPNKTVKSAVQTITVGGMSTSQFKTII 119
Cdd:cd22540   183 TNSASLQVPGNVIKLQSGGNVALTLPVNNL-----VGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVL 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085987369 120 PLATAPNVQQ-------IQVPGSKFHYVRLVTATTASSSAQPVSQSPsvntqplQQAKPVVVNTTPVRMSVPFVQAQAVK 192
Cdd:cd22540   258 IETTADNIIQagnnlliVQSPGTGQPAVLQQVQVLQPKQEQQVVQIP-------QQALRVVQAASATLPTVPQKPLQNIQ 330

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1085987369 193 QVVPKPINSTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTG 245
Cdd:cd22540   331 IQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQVTANNGTG 383

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 1085987369 375 SKGCNCKRSG-------CLKNYCECYEAKIMCSSiCKCIGCKN 410
Cdd:cd13122     4 KKGCRCGTATqspgvltCRGQRCPCYSNGKSCLD-CKCRGCKN 45

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 1085987369 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 1085987369  40 TQASPPVVTGRVLSQSTPGTPSKTITISESgvigsTLNSTTQTPNKIAISPLKSPNKTVKSAVQTITVGGMSTSQFKTII 119
Cdd:cd22540   183 TNSASLQVPGNVIKLQSGGNVALTLPVNNL-----VGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVL 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085987369 120 PLATAPNVQQ-------IQVPGSKFHYVRLVTATTASSSAQPVSQSPsvntqplQQAKPVVVNTTPVRMSVPFVQAQAVK 192
Cdd:cd22540   258 IETTADNIIQagnnlliVQSPGTGQPAVLQQVQVLQPKQEQQVVQIP-------QQALRVVQAASATLPTVPQKPLQNIQ 330

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1085987369 193 QVVPKPINSTSQIVTTSQPQQRLIMPATPLPQIQPNLTNLPPGTVLAPAPGTG 245
Cdd:cd22540   331 IQNSEPTPTQVYIKTPSGEVQTVLLQEAPAATATPSSSTSTVQQQVTANNGTG 383

large tegument protein UL36; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085987369    5 PAEIAKKPRTPTSGPVItklifakPINSKAVTGQTTQASPPVVTGrvlSQSTPGTPSKTITISESGVIGSTLNSTTQTPN 84
Cdd:PHA03247  2734 ALPAAPAPPAVPAGPAT-------PGGPARPARPPTTAGPPAPAP---PAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085987369   85 KIAI-SPLKSPNKTVKSAVQTITVGGMSTSQFKTIIPLATAPNVQQIQ-----VPGSKFHY---VRLVTATTASSSAQPV 155
Cdd:PHA03247  2804 PADPpAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPlggsvAPGGDVRRrppSRSPAAKPAAPARPPV 2883

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085987369  156 SQ--SPSVNTQPLQQAKPvvvNTTPVRMSVPFVQAQAVKQVVPKPinstsQIVTTSQPQQRLIMPATPLPQIQPNLTNLP 233
Cdd:PHA03247  2884 RRlaRPAVSRSTESFALP---PDQPERPPQPQAPPPPQPQPQPPP-----PPQPQPPPPPPPRPQPPLAPTTDPAGAGEP 2955

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1085987369  234 PGTVLAPAPGTGNVGYAVLPAQYVTQLQQSSYVSIASNSNFTGTS 278
Cdd:PHA03247  2956 SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHS 3000