KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 55976740     3 SVAFEDVAVNFTQEEWALLSPSQKNLYRDVTLETFRNLASVG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55976740  149 ASISPSSGARrtVTPTRKRPYECKVCGKAFNSPNLFQIHQRT-H-----TGKRSYKCREIVRAFTVS 209
Cdd:cd11674   56 AVISPPQSKK--ATPINPSSYVCNVCMAEFSSMDQLAEHQRTtHsigasSLLTSPAINQAIESFLTS 120

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 55976740     3 SVAFEDVAVNFTQEEWALLSPSQKNLYRDVTLETFRNLASVG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 55976740   4 VAFEDVAVNFTQEEWALLSPSQKNLYRDVTLETFRNLAS 42
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 55976740   240 FQIHVRTHTGEKPYKCKQCGKAFIS 264
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

KRAB box; The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 55976740     3 SVAFEDVAVNFTQEEWALLSPSQKNLYRDVTLETFRNLASVG 44
Cdd:pfam01352   1 SVTFEDVAVDFTQEEWALLDPAQRNLYRDVMLENYRNLVSLG 42

KRAB (Kruppel-associated box) domain -A box; The KRAB domain is a transcription repression module, found in a subgroup of the zinc finger proteins (ZFPs) of the C2H2 family, KRAB-ZFPs. KRAB-ZFPs comprise the largest group of transcriptional regulators in mammals, and are only found in tetrapods. These proteins have been shown to play important roles in cell differentiation and organ development, and in regulating viral replication and transcription. A KRAB domain may consist of an A-box, or of an A-box plus either a B-box, a divergent B-box (b), or a C-box. Only the A-box is included in this model. The A-box is needed for repression, the B- and C- boxes are not. KRAB-ZFPs have one or two KRAB domains at their amino-terminal end, and multiple C2H2 zinc finger motifs at their C-termini. Some KRAB-ZFPs also contain a SCAN domain which mediates homo- and hetero-oligomerization. The KRAB domain is a protein-protein interaction module which represses transcription through recruiting corepressors. A key mechanism appears to be the following: KRAB-AFPs tethered to DNA recruit, via their KRAB domain, the repressor KAP1 (KRAB-associated protein-1, also known as transcription intermediary factor 1 beta , KRAB-A interacting protein , and tripartite motif protein 28). The KAP1/ KRAB-AFP complex in turn recruits the heterochromatin protein 1 (HP1) family, and other chromatin modulating proteins, leading to transcriptional repression through heterochromatin formation.

                        10        20        30
                ....*....|....*....|....*....|....*....
gi 55976740   4 VAFEDVAVNFTQEEWALLSPSQKNLYRDVTLETFRNLAS 42
Cdd:cd07765   1 VTFEDVAVYFSQEEWELLDPAQRDLYRDVMLENYENLVS 39

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*
gi 55976740   240 FQIHVRTHTGEKPYKCKQCGKAFIS 264
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPECGKSFKS 26

FOG: Zn-finger [General function prediction only];

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55976740 336 RPYECNKCGKTFNYPSCFRRHKKTHSGEKPYECTR--CGKAFGWCSSLRRHEMTHTGEKPFDCKQCGKVFTFSN 407
Cdd:COG5048  32 RPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYsgCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKA 105

inner capsid protein lambda-1 or VP3; The reovirus inner capsid protein lambda-1 displays nucleoside triphosphate phosphohydrolase (NTPase), RNA-5'-triphosphatase (RTPase), and RNA helicase activity and may play a role in the transcription of the virus genome, the unwinding or reannealing of double-stranded RNA during RNA synthesis. The RTPase activity constitutes the first step in the capping of RNA, resulting in a 5'-diphosphorylated RNA plus-strand. lambda1 is an Orthoreovirus core protein, VP3 is the homologous core protein in Aquareoviruses.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55976740  149 ASISPSSGARrtVTPTRKRPYECKVCGKAFNSPNLFQIHQRT-H-----TGKRSYKCREIVRAFTVS 209
Cdd:cd11674   56 AVISPPQSKK--ATPINPSSYVCNVCMAEFSSMDQLAEHQRTtHsigasSLLTSPAINQAIESFLTS 120