HIN-200/IF120x domain; This domain has no know function. It is found in one or two copies per protein, and is found associated with the PAAD/DAPIN domain pfam02758.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100061616 225 HSEPLTVMVLTATDPFEYESPEHEvKNMLHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVL 304
Cdd:pfam02760   1 QKGPKEVMVLKATEPFEYESQEGK-KKMFHATVATESEFFRVKVFNINLKEKFIPKKVIAISDYFGRNGFLEVNEASSVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100061616 305 EAAPDQMIEVPNSIIRNANASPKICDIQKGTSGAVFYGVFTLHKKTVNRKNTIYEIKDGSGSIEVVGSGKWHNINCKEGD 384
Cdd:pfam02760  80 EAGPDQKMEVPKSIIRKANETPKINKLKKQPSGTIVNGLFTVHKKTVNKKNTIYEIQDNTGKMEVVVYGKLTNIKCEEGD 159

                  ....*....
gi 1100061616 385 KLHLFCFHL 393
Cdd:pfam02760 160 KLRLFCFEL 168

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1100061616  10 LLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIAFCEEVPaLRKRAEILK 83
Cdd:cd08305     1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMP-LRSLANQLQ 73

HIN-200/IF120x domain; This domain has no know function. It is found in one or two copies per protein, and is found associated with the PAAD/DAPIN domain pfam02758.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100061616 225 HSEPLTVMVLTATDPFEYESPEHEvKNMLHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVL 304
Cdd:pfam02760   1 QKGPKEVMVLKATEPFEYESQEGK-KKMFHATVATESEFFRVKVFNINLKEKFIPKKVIAISDYFGRNGFLEVNEASSVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100061616 305 EAAPDQMIEVPNSIIRNANASPKICDIQKGTSGAVFYGVFTLHKKTVNRKNTIYEIKDGSGSIEVVGSGKWHNINCKEGD 384
Cdd:pfam02760  80 EAGPDQKMEVPKSIIRKANETPKINKLKKQPSGTIVNGLFTVHKKTVNKKNTIYEIQDNTGKMEVVVYGKLTNIKCEEGD 159

                  ....*....
gi 1100061616 385 KLHLFCFHL 393
Cdd:pfam02760 160 KLRLFCFEL 168

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1100061616  10 LLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIAFCEEVPaLRKRAEILK 83
Cdd:cd08305     1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMP-LRSLANQLQ 73

HIN-200/IF120x domain; This domain has no know function. It is found in one or two copies per protein, and is found associated with the PAAD/DAPIN domain pfam02758.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100061616 225 HSEPLTVMVLTATDPFEYESPEHEvKNMLHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVL 304
Cdd:pfam02760   1 QKGPKEVMVLKATEPFEYESQEGK-KKMFHATVATESEFFRVKVFNINLKEKFIPKKVIAISDYFGRNGFLEVNEASSVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100061616 305 EAAPDQMIEVPNSIIRNANASPKICDIQKGTSGAVFYGVFTLHKKTVNRKNTIYEIKDGSGSIEVVGSGKWHNINCKEGD 384
Cdd:pfam02760  80 EAGPDQKMEVPKSIIRKANETPKINKLKKQPSGTIVNGLFTVHKKTVNKKNTIYEIQDNTGKMEVVVYGKLTNIKCEEGD 159

                  ....*....
gi 1100061616 385 KLHLFCFHL 393
Cdd:pfam02760 160 KLRLFCFEL 168

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1100061616  10 LLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIAFCEEVPaLRKRAEILK 83
Cdd:cd08305     1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMP-LRSLANQLQ 73