beta-trefoil domain found in interleukin-36 receptor antagonist protein (IL-36RA) and similar proteins; IL-36RA, also called FIL1 delta, or IL-1-related protein 3, or IL-1RP3, or interleukin-1 HY1, or IL-1HY1, or interleukin-1 delta, or IL-1 delta, or interleukin-1 family member 5, or IL-1F5, or interleukin-1 receptor antagonist homolog 1, or IL-1ra homolog 1, or interleukin-1-like protein 1, or IL-1L1, inhibits the activity of interleukin-36 (IL36 alpha,IL36 beta and IL36 gamma) by binding to receptor IL1RL2 and preventing its association with the coreceptor IL1RAP for signaling. It is part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; like the IL-1 system with which it shares the coreceptor. It may play a role in skin inflammation, as well as in the innate immune response to fungal pathogens, such as Aspergillus fumigatus. It may activate an anti-inflammatory signaling pathway by recruiting SIGIRR. IL-36RA contains a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729132355  58 QPFHYQIRDTSHKAFYLRDNSLVAANLQGENASQEEMVSVVPNRTLERKRCPLILGIKGGSQGLSCGTAEQPQLQLEDMH 137
Cdd:cd23303     1 GPLCFRMRDTALKVLYLHNNQLVAGGLHAGKNIKGEEISVVPNRFLDRRLSPIILGVQGGSQCLSCGTGQEPTLQLEPVN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729132355 138 LIDLFYQDEEAKRFTFFKTYNGSTHRFEAAAYPGWFLCTSTQANEPISLTTRLGETAITDFYFQPK 203
Cdd:cd23303    81 IMDLYLSAKEAKSFTFYRTDMGLTHRFESAAYPGWFLCTSPEADQPVRLTNRLGEAPITDFYFQQC 146

beta-trefoil domain found in interleukin-36 receptor antagonist protein (IL-36RA) and similar proteins; IL-36RA, also called FIL1 delta, or IL-1-related protein 3, or IL-1RP3, or interleukin-1 HY1, or IL-1HY1, or interleukin-1 delta, or IL-1 delta, or interleukin-1 family member 5, or IL-1F5, or interleukin-1 receptor antagonist homolog 1, or IL-1ra homolog 1, or interleukin-1-like protein 1, or IL-1L1, inhibits the activity of interleukin-36 (IL36 alpha,IL36 beta and IL36 gamma) by binding to receptor IL1RL2 and preventing its association with the coreceptor IL1RAP for signaling. It is part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; like the IL-1 system with which it shares the coreceptor. It may play a role in skin inflammation, as well as in the innate immune response to fungal pathogens, such as Aspergillus fumigatus. It may activate an anti-inflammatory signaling pathway by recruiting SIGIRR. IL-36RA contains a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729132355  58 QPFHYQIRDTSHKAFYLRDNSLVAANLQGENASQEEMVSVVPNRTLERKRCPLILGIKGGSQGLSCGTAEQPQLQLEDMH 137
Cdd:cd23303     1 GPLCFRMRDTALKVLYLHNNQLVAGGLHAGKNIKGEEISVVPNRFLDRRLSPIILGVQGGSQCLSCGTGQEPTLQLEPVN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729132355 138 LIDLFYQDEEAKRFTFFKTYNGSTHRFEAAAYPGWFLCTSTQANEPISLTTRLGETAITDFYFQPK 203
Cdd:cd23303    81 IMDLYLSAKEAKSFTFYRTDMGLTHRFESAAYPGWFLCTSPEADQPVRLTNRLGEAPITDFYFQQC 146

Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729132355  84 LQGENASQEEMVSVVPNRTLERKR-CPLILGIKGGSQGLSCGTAEQPQLQLEDMHLIDLFYQDEEAKRFTFFKTYNGSTH 162
Cdd:pfam00340   1 LQGQNLNLEVKFDMSFYKGDSDDSkIPVTLGIKGKKLYLSCVNKDEPVLQLEEVNIPKLIKNKESDKRFFFIRSESKNYV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1729132355 163 RFEAAAYPGWFLCTSTQANEPISLT-TRLGETAITDFYF 200
Cdd:pfam00340  81 EFESAAYPGWFIATKQEEDLPVFLVnTAGGQDSITDFQI 119

beta-trefoil domain found in interleukin-36 receptor antagonist protein (IL-36RA) and similar proteins; IL-36RA, also called FIL1 delta, or IL-1-related protein 3, or IL-1RP3, or interleukin-1 HY1, or IL-1HY1, or interleukin-1 delta, or IL-1 delta, or interleukin-1 family member 5, or IL-1F5, or interleukin-1 receptor antagonist homolog 1, or IL-1ra homolog 1, or interleukin-1-like protein 1, or IL-1L1, inhibits the activity of interleukin-36 (IL36 alpha,IL36 beta and IL36 gamma) by binding to receptor IL1RL2 and preventing its association with the coreceptor IL1RAP for signaling. It is part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; like the IL-1 system with which it shares the coreceptor. It may play a role in skin inflammation, as well as in the innate immune response to fungal pathogens, such as Aspergillus fumigatus. It may activate an anti-inflammatory signaling pathway by recruiting SIGIRR. IL-36RA contains a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729132355  58 QPFHYQIRDTSHKAFYLRDNSLVAANLQGENASQEEMVSVVPNRTLERKRCPLILGIKGGSQGLSCGTAEQPQLQLEDMH 137
Cdd:cd23303     1 GPLCFRMRDTALKVLYLHNNQLVAGGLHAGKNIKGEEISVVPNRFLDRRLSPIILGVQGGSQCLSCGTGQEPTLQLEPVN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729132355 138 LIDLFYQDEEAKRFTFFKTYNGSTHRFEAAAYPGWFLCTSTQANEPISLTTRLGETAITDFYFQPK 203
Cdd:cd23303    81 IMDLYLSAKEAKSFTFYRTDMGLTHRFESAAYPGWFLCTSPEADQPVRLTNRLGEAPITDFYFQQC 146

beta-trefoil domain found in interleukin-38 (IL-38) and similar proteins; IL-38, also called interleukin-1 family member 10, or IL-1F10, or family of interleukin 1-theta, or FIL1 theta, or interleukin-1 HY2, or IL-1HY2, or interleukin-1 theta, or IL-1 theta, acts as cytokine with immunomodulatory activity. Alone, it does not induce cytokine production, but reduces IL22 and IL17A production by T-cells in response to heat-killed Candida albicans. It also reduces IL36G-induced production of IL8 by peripheral blood mononuclear cells. It increases IL6 production by dendritic cells stimulated by bacterial lipopolysaccharides (LPS). IL-38 contains a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729132355  61 HYQIRDTSHKAFYLRDNSLVAANLQGENASQEEmVSVVPNRTLERKRCPLILGIKGGSQGLSC-GTAEQPQLQLEDMHLI 139
Cdd:cd23302     7 YYIIKYADQKALYTRDGQLLVGDPVADNCCAEK-ICILPNRGLDRTKVPIFLGIQGGSRCLACvETEEGPSLQLEDVNIE 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729132355 140 DLFYQDEEAKRFTFFKTYNGSTHRFEAAAYPGWFLCTSTQANEPISLTTRLGETAITDFYFQ 201
Cdd:cd23302    86 ELYKGGEEATRFTFFQSSSGSAFRLEAAAWPGWFLCGPAEPQQPVQLTKESEPSARTKFYFE 147

beta-trefoil domain found in interleukin-1 beta (IL-1 beta) and similar proteins; IL-1 beta, also called catabolin, is a potent inflammatory cytokine that activates the inflammatory process. It was initially discovered as the major endogenous pyrogen. It induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. IL-1 beta promotes Th17 differentiation of T-cells and synergizes with IL12/interleukin-12 to induce IFN-gamma synthesis from T-helper 1 (Th1) cells. It plays a role in angiogenesis by inducing vascular endothelial growth factor (VEGF) production synergistically with tumor necrosis factor (TNF) and IL-6. IL-1 beta contains a C-terminal beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729132355  61 HYQIRDTSHKAFYLRDNS-LVAANLQGENASQE---EMVSVVPNRTLERKRcPLILGIKGGSQGLSC-GTAEQPQLQLE- 134
Cdd:cd23296     6 SCTIRDSEQKSLVLSGPYqLVALHLQGPNSSQEvklNMSFYRSPESNGGKI-PVALGIKGKNLYLSCvKKGDKPTLQLEe 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729132355 135 --DMHLIDlfyqDEEAKRFTFFKTYN-GSTHRFEAAAYPGWFLCTSTQANEPISLTTRLGETAITDFY 199
Cdd:cd23296    85 vdPKNDSK----SKDLKRFLFYKIESiGSTTTFESAAFPGWYISTSQAENQPVFLGNQKGQQRITDFT 148

beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The IL-36 family includes three members, IL-36 alpha (also called FIL1 epsilon, or interleukin-1 epsilon, or IL-1 epsilon, or interleukin-1 family member 6, or IL-1F6), IL-36 beta (also called FIL1 eta, or interleukin-1 eta, or IL-1 eta, or interleukin-1 family member 8, or IL-1F8, or interleukin-1 homolog 2, or IL-1H2), and IL-36 gamma (also called IL-1-related protein 2, or IL-1RP2, or interleukin-1 epsilon, or IL-1 epsilon, or interleukin-1 family member 9, or IL-1F9, or interleukin-1 homolog 1, or IL-1H1). They act as cytokines that bind to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. They are parts of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; like the IL-1 system with which they share the co-receptor IL1RAP. They may be involved in skin inflammatory response by acting on keratinocytes, dendritic cells, and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. Members in this family contain a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729132355  58 QPFHYQIRDTSHKAFYLRDNSLVAANLqgENASQEEMVSVVPNR---TLERKR-CPLILGIKGGSQGLSCGTAE-QPQLQ 132
Cdd:cd23300     1 KPSSRHIRDLNQQVWVLQGNTLIAVPR--SDNVTPVTLALIPCRdteFLEKDKgNPIYLGIKGPELCLFCEEIGgQPTLQ 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729132355 133 LEDMHLIDLFYQDEEAKRFTFFKTYNGSTHRFEAAAYPGWFLCTSTQANEPISLTTRLGETAITDFYFQP 202
Cdd:cd23300    79 LKEKNIMDLYNEPEAVKPFLFYHNQTGSTSTFESAAYPGWFIASSSEGGQPIILTKERGKTYNTNFYLDS 148

beta-trefoil domain found in interleukin-37 (IL-37) and similar proteins; IL-37, also called FIL1 zeta, or IL-1X, or interleukin-1 family member 7, or IL-1F7, or interleukin-1 homolog 4, or IL-1H, or IL-1H4, or interleukin-1 zeta, or IL-1 zeta, or interleukin-1-related protein, or IL-1RP1, or interleukin-23, or IL-23, acts as a suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. This function requires SMAD3. It suppresses, or reduces, proinflammatory cytokine production, including IL1A and IL6, as well as CCL12, CSF1, CSF2, CXCL13, IL1B, IL23A, and IL1RN, but spares anti-inflammatory cytokines and inhibits dendritic cell activation. IL-37 contains a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729132355  57 KQPFHYQIRDTSHKAFYLRDNSLVAANlqGENASQEEMVSVVPN---RTLERKRCPLILGIKGGSQGLSCGTAE---QPQ 130
Cdd:cd23301     1 QTPKKFIIRDTNQQVLVLDSGNLVAVP--DKSYIKPETFYVLAShlrSASEEKGNPIFLAVSKGELCLCCEKVKgqkHPS 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729132355 131 LQLEDMHLIDLFYQDE-EAKRFTFFKTYNGSTHRFEAAAYPGWFLCTSTQANEPISLTTRLGETAITDFYFQP 202
Cdd:cd23301    79 LQLKKKKINELNSQKEkELLPFTFYKEKVGSYFTLESAANPGYFICTSNTPGQPVGVTDKLGKEKNIEFSFVP 151