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Conserved domains on  [gi|27894317|ref|NP_776213|]
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interleukin-1 receptor antagonist protein isoform 2 [Homo sapiens]

Protein Classification

beta-trefoil_IL1B domain-containing protein( domain architecture ID 10639008)

beta-trefoil_IL1B domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_IL1RA cd23297
beta-trefoil domain found in interleukin-1 receptor antagonist protein (IL-1RA) and similar ...
 36-179 2.41e-95

beta-trefoil domain found in interleukin-1 receptor antagonist protein (IL-1RA) and similar proteins; IL-1RA, also called IL-1RN, or IRAP, or ICIL-1RA, or IL1 inhibitor, inhibits the activity of interleukin-1 (IL-1) by binding to receptor IL1R1 and preventing its association with the co-receptor IL1RAP for signaling. It has no IL-1 like activity. IL-1RN binds functional interleukin-1 receptor IL1R1 with greater affinity than decoy receptor IL1R2; however, the physiological relevance of the latter association is unknown. IL-1RN 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.


:

Pssm-ID: 466779  Cd Length: 149  Bit Score: 273.16  E-value: 2.41e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317  36 SKMQAFRIWDVNQKTFYLRNNQLVAGYLQGPNVNLEEKIDVVPI-----EPHALFLGIHGGKMCLSCVKSGDETRLQLEA 110
Cdd:cd23297   1 SKVFAYRIWDVNQKSLYLRNNQLVAGYLQGPNAALEEKIFWVPNrafepEPLPVILGIHDGSRCLSCVKSGDEPRLQLED 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27894317 111 VNITDLSENRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVMVTKFYFQED 179
Cdd:cd23297  81 VDITDLPRNGKQSARFTFFRSYRDGLWRFESAAHPGWFLCTSMRADQPVSLTNMPDEGVMVTDFYFQLC 149
 
Name Accession Description Interval E-value
beta-trefoil_IL1RA cd23297
beta-trefoil domain found in interleukin-1 receptor antagonist protein (IL-1RA) and similar ...
 36-179 2.41e-95

beta-trefoil domain found in interleukin-1 receptor antagonist protein (IL-1RA) and similar proteins; IL-1RA, also called IL-1RN, or IRAP, or ICIL-1RA, or IL1 inhibitor, inhibits the activity of interleukin-1 (IL-1) by binding to receptor IL1R1 and preventing its association with the co-receptor IL1RAP for signaling. It has no IL-1 like activity. IL-1RN binds functional interleukin-1 receptor IL1R1 with greater affinity than decoy receptor IL1R2; however, the physiological relevance of the latter association is unknown. IL-1RN 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.


Pssm-ID: 466779  Cd Length: 149  Bit Score: 273.16  E-value: 2.41e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317  36 SKMQAFRIWDVNQKTFYLRNNQLVAGYLQGPNVNLEEKIDVVPI-----EPHALFLGIHGGKMCLSCVKSGDETRLQLEA 110
Cdd:cd23297   1 SKVFAYRIWDVNQKSLYLRNNQLVAGYLQGPNAALEEKIFWVPNrafepEPLPVILGIHDGSRCLSCVKSGDEPRLQLED 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27894317 111 VNITDLSENRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVMVTKFYFQED 179
Cdd:cd23297  81 VDITDLPRNGKQSARFTFFRSYRDGLWRFESAAHPGWFLCTSMRADQPVSLTNMPDEGVMVTDFYFQLC 149
IL1 smart00125
Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and ...
 37-177 2.00e-74

Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and beta are also known as hematopoietin and catabolin.


Pssm-ID: 128430  Cd Length: 147  Bit Score: 219.94  E-value: 2.00e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317     37 KMQAFRIWDVNQKTFYLRN-NQLVAGYLQGPNVNLEEKIDVVPIEPHA------LFLGIHGGKMCLSCVKSGDETRLQLE 109
Cdd:smart00125   2 ISQECRLNDANQKSLVLSNpQYLKALHLNGQNLNQEVKFDMSFVQGEEddskipVTLGISGTNLYLSCVKKGDEPTLQLE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27894317    110 AVNITDLSEnRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDeGVMVTKFYFQ 177
Cdd:smart00125  82 MVDPPKYPK-KEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQEEDKPVFLGNGPP-SQDITDFQME 147
IL1 pfam00340
Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.
 63-176 3.63e-52

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


Pssm-ID: 395269  Cd Length: 119  Bit Score: 162.62  E-value: 3.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317    63 LQGPNVNLEEKIDVVPIE--------PHALflGIHGGKMCLSCVKSgDETRLQLEAVNITDLSENRKQDKRFAFIRSDSG 134
Cdd:pfam00340   1 LQGQNLNLEVKFDMSFYKgdsddskiPVTL--GIKGKKLYLSCVNK-DEPVLQLEEVNIPKLIKNKESDKRFFFIRSESK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 27894317   135 PTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVMVTKFYF 176
Cdd:pfam00340  78 NYVEFESAAYPGWFIATKQEEDLPVFLVNTAGGQDSITDFQI 119
PHA02651 PHA02651
IL-1 receptor antagonist; Provisional
 34-179 5.40e-38

IL-1 receptor antagonist; Provisional


Pssm-ID: 165031  Cd Length: 165  Bit Score: 128.23  E-value: 5.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317   34 KSSKMQAFRIWDVNQKTFYLRNNQLVAGYLQgpNVNLEEKIDVVPIEPHALFLGIHGGKMCLSCVKSGDETRLQLEAVNI 113
Cdd:PHA02651  18 KAAGMFMYNIWDVNQKIFYLRNNQLVAGHIQ--DNSLAEKITAKLIDGNDIFLGVKNGEKSLECTEHGDKVTLSLSDKKT 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27894317  114 TDLSENrkQDKRFAFIRSDSGPTTSFESAACPGWFLCTAM-EADQPVSLT-----NMPDEGVMVTKFYFQED 179
Cdd:PHA02651  96 NSLDEN--QDKRFAFIRSDNGHTSTFESVAFPGWFLCTSSgDGIEPVGLTykgdkDDNDDDENNIYFYFEED 165
 
Name Accession Description Interval E-value
beta-trefoil_IL1RA cd23297
beta-trefoil domain found in interleukin-1 receptor antagonist protein (IL-1RA) and similar ...
 36-179 2.41e-95

beta-trefoil domain found in interleukin-1 receptor antagonist protein (IL-1RA) and similar proteins; IL-1RA, also called IL-1RN, or IRAP, or ICIL-1RA, or IL1 inhibitor, inhibits the activity of interleukin-1 (IL-1) by binding to receptor IL1R1 and preventing its association with the co-receptor IL1RAP for signaling. It has no IL-1 like activity. IL-1RN binds functional interleukin-1 receptor IL1R1 with greater affinity than decoy receptor IL1R2; however, the physiological relevance of the latter association is unknown. IL-1RN 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.


Pssm-ID: 466779  Cd Length: 149  Bit Score: 273.16  E-value: 2.41e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317  36 SKMQAFRIWDVNQKTFYLRNNQLVAGYLQGPNVNLEEKIDVVPI-----EPHALFLGIHGGKMCLSCVKSGDETRLQLEA 110
Cdd:cd23297   1 SKVFAYRIWDVNQKSLYLRNNQLVAGYLQGPNAALEEKIFWVPNrafepEPLPVILGIHDGSRCLSCVKSGDEPRLQLED 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27894317 111 VNITDLSENRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVMVTKFYFQED 179
Cdd:cd23297  81 VDITDLPRNGKQSARFTFFRSYRDGLWRFESAAHPGWFLCTSMRADQPVSLTNMPDEGVMVTDFYFQLC 149
IL1 smart00125
Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and ...
 37-177 2.00e-74

Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and beta are also known as hematopoietin and catabolin.


Pssm-ID: 128430  Cd Length: 147  Bit Score: 219.94  E-value: 2.00e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317     37 KMQAFRIWDVNQKTFYLRN-NQLVAGYLQGPNVNLEEKIDVVPIEPHA------LFLGIHGGKMCLSCVKSGDETRLQLE 109
Cdd:smart00125   2 ISQECRLNDANQKSLVLSNpQYLKALHLNGQNLNQEVKFDMSFVQGEEddskipVTLGISGTNLYLSCVKKGDEPTLQLE 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27894317    110 AVNITDLSEnRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDeGVMVTKFYFQ 177
Cdd:smart00125  82 MVDPPKYPK-KEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQEEDKPVFLGNGPP-SQDITDFQME 147
beta-trefoil_IL36RA cd23303
beta-trefoil domain found in interleukin-36 receptor antagonist protein (IL-36RA) and similar ...
 41-177 9.99e-54

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.


Pssm-ID: 466785  Cd Length: 146  Bit Score: 167.61  E-value: 9.99e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317  41 FRIWDVNQKTFYLRNNQLVAGYLQGPNVNLEEKIDVVP---IEPH--ALFLGIHGGKMCLSCvKSGDETRLQLEAVNITD 115
Cdd:cd23303   5 FRMRDTALKVLYLHNNQLVAGGLHAGKNIKGEEISVVPnrfLDRRlsPIILGVQGGSQCLSC-GTGQEPTLQLEPVNIMD 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27894317 116 LSENRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVmVTKFYFQ 177
Cdd:cd23303  84 LYLSAKEAKSFTFYRTDMGLTHRFESAAYPGWFLCTSPEADQPVRLTNRLGEAP-ITDFYFQ 144
IL1 pfam00340
Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.
 63-176 3.63e-52

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


Pssm-ID: 395269  Cd Length: 119  Bit Score: 162.62  E-value: 3.63e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317    63 LQGPNVNLEEKIDVVPIE--------PHALflGIHGGKMCLSCVKSgDETRLQLEAVNITDLSENRKQDKRFAFIRSDSG 134
Cdd:pfam00340   1 LQGQNLNLEVKFDMSFYKgdsddskiPVTL--GIKGKKLYLSCVNK-DEPVLQLEEVNIPKLIKNKESDKRFFFIRSESK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 27894317   135 PTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVMVTKFYF 176
Cdd:pfam00340  78 NYVEFESAAYPGWFIATKQEEDLPVFLVNTAGGQDSITDFQI 119
beta-trefoil_IL1 cd00100
beta-trefoil domain found in the interleukin-1 (IL-1) family of cytokines; The IL-1 family of ...
 37-176 9.95e-44

beta-trefoil domain found in the interleukin-1 (IL-1) family of cytokines; The IL-1 family of cytokines comprises 11 members, including 7 pro-inflammatory agonists (IL-1alpha, IL-1beta, IL-18, IL-33, IL-36alpha, IL-36beta, IL-36gamma) and 4 defined or putative antagonists (IL-1R antagonist (IL-1Ra), IL-36Ra, IL-37, and IL-38) exerting anti-inflammatory activities. These members can have complimentary or distinct biological functions. All family members share a common structure at the C-terminus, which is comprised by of a typical beta-trefoil fold consisting of 12-beta-strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466776  Cd Length: 145  Bit Score: 142.07  E-value: 9.95e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317  37 KMQAFRIWDVNQKTFYLR-NNQLVAGYLQgpNVNLEEKIDVVPIEP--------HALFLGIHGGKMCLSCVKSGDETRLQ 107
Cdd:cd00100   1 EKRNFVIRDSNDKSLYLRgNNELVAEDLS--DVEKSAKITIYYYKSdsdedfkgIPVVLNFTGTNCFLSCVKEGDKPSLQ 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317 108 LEAVNITDLSENRKQDKRFAFIRSDS-GPTTSFESAACPGWFLCTAMeaDQPVSLTNMPDeGVMVTKFYF 176
Cdd:cd00100  79 LEECNKEELKNGDEEEWPFVFYMKAShDNTCRFESAAHPGWFICTKK--DQPVGLTKELG-KTEDTDFYF 145
PHA02651 PHA02651
IL-1 receptor antagonist; Provisional
 34-179 5.40e-38

IL-1 receptor antagonist; Provisional


Pssm-ID: 165031  Cd Length: 165  Bit Score: 128.23  E-value: 5.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317   34 KSSKMQAFRIWDVNQKTFYLRNNQLVAGYLQgpNVNLEEKIDVVPIEPHALFLGIHGGKMCLSCVKSGDETRLQLEAVNI 113
Cdd:PHA02651  18 KAAGMFMYNIWDVNQKIFYLRNNQLVAGHIQ--DNSLAEKITAKLIDGNDIFLGVKNGEKSLECTEHGDKVTLSLSDKKT 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27894317  114 TDLSENrkQDKRFAFIRSDSGPTTSFESAACPGWFLCTAM-EADQPVSLT-----NMPDEGVMVTKFYFQED 179
Cdd:PHA02651  96 NSLDEN--QDKRFAFIRSDNGHTSTFESVAFPGWFLCTSSgDGIEPVGLTykgdkDDNDDDENNIYFYFEED 165
beta-trefoil_IL1B cd23296
beta-trefoil domain found in interleukin-1 beta (IL-1 beta) and similar proteins; IL-1 beta, ...
 36-167 2.55e-37

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.


Pssm-ID: 466778  Cd Length: 150  Bit Score: 125.81  E-value: 2.55e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317  36 SKMQAFRIWDVNQKTFYLRNN-QLVAGYLQGPNVNLEEKIDVV---------PIEPHALflGIHGGKMCLSCVKSGDETR 105
Cdd:cd23296   2 VRSLSCTIRDSEQKSLVLSGPyQLVALHLQGPNSSQEVKLNMSfyrspesngGKIPVAL--GIKGKNLYLSCVKKGDKPT 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27894317 106 LQLEAVNITDLSENrKQDKRFAFIRSDSGP-TTSFESAACPGWFLCTAMEADQPVSLTNMPDE 167
Cdd:cd23296  80 LQLEEVDPKNDSKS-KDLKRFLFYKIESIGsTTTFESAAFPGWYISTSQAENQPVFLGNQKGQ 141
beta-trefoil_IL38 cd23302
beta-trefoil domain found in interleukin-38 (IL-38) and similar proteins; IL-38, also called ...
 43-178 3.93e-32

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.


Pssm-ID: 466784  Cd Length: 149  Bit Score: 112.83  E-value: 3.93e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317  43 IWDVNQKTFYLRNNQLVAGYLQGPNVNlEEKIDVVPIE-----PHALFLGIHGGKMCLSCVKSGDETRLQLEAVNITDLS 117
Cdd:cd23302  10 IKYADQKALYTRDGQLLVGDPVADNCC-AEKICILPNRgldrtKVPIFLGIQGGSRCLACVETEEGPSLQLEDVNIEELY 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27894317 118 ENRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNmPDEGVMVTKFYFQE 178
Cdd:cd23302  89 KGGEEATRFTFFQSSSGSAFRLEAAAWPGWFLCGPAEPQQPVQLTK-ESEPSARTKFYFEQ 148
beta-trefoil_IL36 cd23300
beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The ...
 41-177 9.28e-31

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.


Pssm-ID: 466782  Cd Length: 148  Bit Score: 108.92  E-value: 9.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317  41 FRIWDVNQKTFYLRNNQLVAGYLqgpnvnleeKIDVVPIEPH----------------ALFLGIHGGKMCLSCVKSGDET 104
Cdd:cd23300   5 RHIRDLNQQVWVLQGNTLIAVPR---------SDNVTPVTLAlipcrdteflekdkgnPIYLGIKGPELCLFCEEIGGQP 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27894317 105 RLQLEAVNITDLSENRKQDKRFAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLTNMPDEGVmVTKFYFQ 177
Cdd:cd23300  76 TLQLKEKNIMDLYNEPEAVKPFLFYHNQTGSTSTFESAAYPGWFIASSSEGGQPIILTKERGKTY-NTNFYLD 147
beta-trefoil_IL37 cd23301
beta-trefoil domain found in interleukin-37 (IL-37) and similar proteins; IL-37, also called ...
 39-162 1.39e-17

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.


Pssm-ID: 466783  Cd Length: 151  Bit Score: 75.15  E-value: 1.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894317  39 QAFRIWDVNQKTFYLRNNQLVAgyLQGPNVNLEEKIDVVP--------IEPHALFLGIHGGKMCLSC--VKSGDETRLQL 108
Cdd:cd23301   4 KKFIIRDTNQQVLVLDSGNLVA--VPDKSYIKPETFYVLAshlrsaseEKGNPIFLAVSKGELCLCCekVKGQKHPSLQL 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27894317 109 EAVNITDLSENRKQDKR-FAFIRSDSGPTTSFESAACPGWFLCTAMEADQPVSLT 162
Cdd:cd23301  82 KKKKINELNSQKEKELLpFTFYKEKVGSYFTLESAANPGYFICTSNTPGQPVGVT 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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