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Conserved domains on  [gi|27894310|ref|NP_775262|]
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interleukin-36 receptor antagonist protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
beta-trefoil_IL36RA cd23303
beta-trefoil domain found in interleukin-36 receptor antagonist protein (IL-36RA) and similar ...
5-154 4.93e-106

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: 298.96  E-value: 4.93e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310   5 GALCFRMKDSALKVLYLHNNQLLAGGLHAGKVIKGEEISVVPNRWLDASLSPVILGVQGGSQCLSCGVGQEPTLTLEPVN 84
Cdd:cd23303   1 GPLCFRMRDTALKVLYLHNNQLVAGGLHAGKNIKGEEISVVPNRFLDRRLSPIILGVQGGSQCLSCGTGQEPTLQLEPVN 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310  85 IMELYLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTQLPEnggwNAPITDFYFQQC 154
Cdd:cd23303  81 IMDLYLSAKEAKSFTFYRTDMGLTHRFESAAYPGWFLCTSPEADQPVRLTNRLG----EAPITDFYFQQC 146
 
Name Accession Description Interval E-value
beta-trefoil_IL36RA cd23303
beta-trefoil domain found in interleukin-36 receptor antagonist protein (IL-36RA) and similar ...
5-154 4.93e-106

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: 298.96  E-value: 4.93e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310   5 GALCFRMKDSALKVLYLHNNQLLAGGLHAGKVIKGEEISVVPNRWLDASLSPVILGVQGGSQCLSCGVGQEPTLTLEPVN 84
Cdd:cd23303   1 GPLCFRMRDTALKVLYLHNNQLVAGGLHAGKNIKGEEISVVPNRFLDRRLSPIILGVQGGSQCLSCGTGQEPTLQLEPVN 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310  85 IMELYLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTQLPEnggwNAPITDFYFQQC 154
Cdd:cd23303  81 IMDLYLSAKEAKSFTFYRTDMGLTHRFESAAYPGWFLCTSPEADQPVRLTNRLG----EAPITDFYFQQC 146
IL1 smart00125
Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and ...
9-152 7.18e-34

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: 115.94  E-value: 7.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310      9 FRMKDSALKVLYLHN-NQLLAGGLHAGKVIKGEEISVVP-NRWLDASLSPVILGVQGGSQCLSC-GVGQEPTLTLEPVNI 85
Cdd:smart00125   6 CRLNDANQKSLVLSNpQYLKALHLNGQNLNQEVKFDMSFvQGEEDDSKIPVTLGISGTNLYLSCvKKGDEPTLQLEMVDP 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27894310     86 MElYLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTqlpeNGGWNAPITDFYFQ 152
Cdd:smart00125  86 PK-YPKKEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQEEDKPVFLG----NGPPSQDITDFQME 147
IL1 pfam00340
Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.
56-151 1.17e-28

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


Pssm-ID: 395269  Cd Length: 119  Bit Score: 101.76  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310    56 PVILGVQGGSQCLSCGVGQEPTLTLEPVNIMELYLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTQ 135
Cdd:pfam00340  27 PVTLGIKGKKLYLSCVNKDEPVLQLEEVNIPKLIKNKESDKRFFFIRSESKNYVEFESAAYPGWFIATKQEEDLPVFLVN 106
                          90
                  ....*....|....*.
gi 27894310   136 LPENGgwnAPITDFYF 151
Cdd:pfam00340 107 TAGGQ---DSITDFQI 119
PHA02651 PHA02651
IL-1 receptor antagonist; Provisional
4-134 2.02e-17

IL-1 receptor antagonist; Provisional


Pssm-ID: 165031  Cd Length: 165  Bit Score: 74.30  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310    4 SGALCFRMKDSALKVLYLHNNQLLAGGLHAGKVikGEEISVVPNRWLDaslspVILGVQGGSQCLSCGV-GQEPTLTLEP 82
Cdd:PHA02651  20 AGMFMYNIWDVNQKIFYLRNNQLVAGHIQDNSL--AEKITAKLIDGND-----IFLGVKNGEKSLECTEhGDKVTLSLSD 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 27894310   83 VNIMELylGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVP-EADQPVRLT 134
Cdd:PHA02651  93 KKTNSL--DENQDKRFAFIRSDNGHTSTFESVAFPGWFLCTSSgDGIEPVGLT 143
 
Name Accession Description Interval E-value
beta-trefoil_IL36RA cd23303
beta-trefoil domain found in interleukin-36 receptor antagonist protein (IL-36RA) and similar ...
5-154 4.93e-106

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: 298.96  E-value: 4.93e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310   5 GALCFRMKDSALKVLYLHNNQLLAGGLHAGKVIKGEEISVVPNRWLDASLSPVILGVQGGSQCLSCGVGQEPTLTLEPVN 84
Cdd:cd23303   1 GPLCFRMRDTALKVLYLHNNQLVAGGLHAGKNIKGEEISVVPNRFLDRRLSPIILGVQGGSQCLSCGTGQEPTLQLEPVN 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310  85 IMELYLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTQLPEnggwNAPITDFYFQQC 154
Cdd:cd23303  81 IMDLYLSAKEAKSFTFYRTDMGLTHRFESAAYPGWFLCTSPEADQPVRLTNRLG----EAPITDFYFQQC 146
beta-trefoil_IL1RA cd23297
beta-trefoil domain found in interleukin-1 receptor antagonist protein (IL-1RA) and similar ...
9-154 2.99e-52

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: 163.00  E-value: 2.99e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310   9 FRMKDSALKVLYLHNNQLLAGGLHAGKVIKGEEISVVPNRWLDASLSPVILGVQGGSQCLSC-GVGQEPTLTLEPVNIME 87
Cdd:cd23297   6 YRIWDVNQKSLYLRNNQLVAGYLQGPNAALEEKIFWVPNRAFEPEPLPVILGIHDGSRCLSCvKSGDEPRLQLEDVDITD 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27894310  88 LYLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTQLPENGgwnAPITDFYFQQC 154
Cdd:cd23297  86 LPRNGKQSARFTFFRSYRDGLWRFESAAHPGWFLCTSMRADQPVSLTNMPDEG---VMVTDFYFQLC 149
beta-trefoil_IL1 cd00100
beta-trefoil domain found in the interleukin-1 (IL-1) family of cytokines; The IL-1 family of ...
8-151 1.55e-43

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: 140.53  E-value: 1.55e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310   8 CFRMKDSALKVLYLH-NNQLLAGGLHagKVIKGEEISVVPNRWLDASL---SPVILGVQGGSQCLSC-GVGQEPTLTLEP 82
Cdd:cd00100   4 NFVIRDSNDKSLYLRgNNELVAEDLS--DVEKSAKITIYYYKSDSDEDfkgIPVVLNFTGTNCFLSCvKEGDKPSLQLEE 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310  83 VNIMELYLGAKESKSFTFYRRD-MGLTSSFESAAYPGWFLCTVPeaDQPVRLTQLPEnggwNAPITDFYF 151
Cdd:cd00100  82 CNKEELKNGDEEEWPFVFYMKAsHDNTCRFESAAHPGWFICTKK--DQPVGLTKELG----KTEDTDFYF 145
beta-trefoil_IL38 cd23302
beta-trefoil domain found in interleukin-38 (IL-38) and similar proteins; IL-38, also called ...
11-153 3.14e-38

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: 127.47  E-value: 3.14e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310  11 MKDSALKVLYLHNNQLLAGGLHAGKViKGEEISVVPNRWLDASLSPVILGVQGGSQCLSCGVGQE-PTLTLEPVNIMELY 89
Cdd:cd23302  10 IKYADQKALYTRDGQLLVGDPVADNC-CAEKICILPNRGLDRTKVPIFLGIQGGSRCLACVETEEgPSLQLEDVNIEELY 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27894310  90 LGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTQLPEnggwNAPITDFYFQQ 153
Cdd:cd23302  89 KGGEEATRFTFFQSSSGSAFRLEAAAWPGWFLCGPAEPQQPVQLTKESE----PSARTKFYFEQ 148
IL1 smart00125
Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and ...
9-152 7.18e-34

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: 115.94  E-value: 7.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310      9 FRMKDSALKVLYLHN-NQLLAGGLHAGKVIKGEEISVVP-NRWLDASLSPVILGVQGGSQCLSC-GVGQEPTLTLEPVNI 85
Cdd:smart00125   6 CRLNDANQKSLVLSNpQYLKALHLNGQNLNQEVKFDMSFvQGEEDDSKIPVTLGISGTNLYLSCvKKGDEPTLQLEMVDP 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27894310     86 MElYLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTqlpeNGGWNAPITDFYFQ 152
Cdd:smart00125  86 PK-YPKKEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQEEDKPVFLG----NGPPSQDITDFQME 147
beta-trefoil_IL36 cd23300
beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The ...
8-153 1.02e-30

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: 108.15  E-value: 1.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310   8 CFRMKDSALKVLYLHNNQLLAGGLHAGkvIKGEEISVVPNRWLDASL----SPVILGVQGGSQCLSCG-VGQEPTLTLEP 82
Cdd:cd23300   4 SRHIRDLNQQVWVLQGNTLIAVPRSDN--VTPVTLALIPCRDTEFLEkdkgNPIYLGIKGPELCLFCEeIGGQPTLQLKE 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27894310  83 VNIMELYLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTQlpENGGWNapITDFYFQQ 153
Cdd:cd23300  82 KNIMDLYNEPEAVKPFLFYHNQTGSTSTFESAAYPGWFIASSSEGGQPIILTK--ERGKTY--NTNFYLDS 148
IL1 pfam00340
Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.
56-151 1.17e-28

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


Pssm-ID: 395269  Cd Length: 119  Bit Score: 101.76  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310    56 PVILGVQGGSQCLSCGVGQEPTLTLEPVNIMELYLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLTQ 135
Cdd:pfam00340  27 PVTLGIKGKKLYLSCVNKDEPVLQLEEVNIPKLIKNKESDKRFFFIRSESKNYVEFESAAYPGWFIATKQEEDLPVFLVN 106
                          90
                  ....*....|....*.
gi 27894310   136 LPENGgwnAPITDFYF 151
Cdd:pfam00340 107 TAGGQ---DSITDFQI 119
beta-trefoil_IL1B cd23296
beta-trefoil domain found in interleukin-1 beta (IL-1 beta) and similar proteins; IL-1 beta, ...
55-150 1.40e-23

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: 89.98  E-value: 1.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310  55 SPVILGVQGGSQCLSC-GVGQEPTLTLEPVNImELYLGAKESKSFTFYRRD-MGLTSSFESAAYPGWFLCTVPEADQPVR 132
Cdd:cd23296  56 IPVALGIKGKNLYLSCvKKGDKPTLQLEEVDP-KNDSKSKDLKRFLFYKIEsIGSTTTFESAAFPGWYISTSQAENQPVF 134
                        90
                ....*....|....*...
gi 27894310 133 LTQLPengGWNApITDFY 150
Cdd:cd23296 135 LGNQK---GQQR-ITDFT 148
beta-trefoil_IL37 cd23301
beta-trefoil domain found in interleukin-37 (IL-37) and similar proteins; IL-37, also called ...
9-134 4.02e-23

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: 88.63  E-value: 4.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310   9 FRMKDSALKVLYLHNNQLLAggLHAGKVIKGEEISVVPNRWLDASL---SPVILGVQGGSQCLSCGVGQE---PTLTLEP 82
Cdd:cd23301   6 FIIRDTNQQVLVLDSGNLVA--VPDKSYIKPETFYVLASHLRSASEekgNPIFLAVSKGELCLCCEKVKGqkhPSLQLKK 83
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 27894310  83 VNIMEL-YLGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVPEADQPVRLT 134
Cdd:cd23301  84 KKINELnSQKEKELLPFTFYKEKVGSYFTLESAANPGYFICTSNTPGQPVGVT 136
PHA02651 PHA02651
IL-1 receptor antagonist; Provisional
4-134 2.02e-17

IL-1 receptor antagonist; Provisional


Pssm-ID: 165031  Cd Length: 165  Bit Score: 74.30  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310    4 SGALCFRMKDSALKVLYLHNNQLLAGGLHAGKVikGEEISVVPNRWLDaslspVILGVQGGSQCLSCGV-GQEPTLTLEP 82
Cdd:PHA02651  20 AGMFMYNIWDVNQKIFYLRNNQLVAGHIQDNSL--AEKITAKLIDGND-----IFLGVKNGEKSLECTEhGDKVTLSLSD 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 27894310   83 VNIMELylGAKESKSFTFYRRDMGLTSSFESAAYPGWFLCTVP-EADQPVRLT 134
Cdd:PHA02651  93 KKTNSL--DENQDKRFAFIRSDNGHTSTFESVAFPGWFLCTSSgDGIEPVGLT 143
beta-trefoil_IL18 cd23298
beta-trefoil domain found in interleukin-18 (IL-18) and similar proteins; IL-18, also called ...
56-129 2.09e-04

beta-trefoil domain found in interleukin-18 (IL-18) and similar proteins; IL-18, also called Iboctadekin, or interferon gamma-inducing factor, or IFN-gamma-inducing factor, or interleukin-1 gamma, or IL-1 gamma, is a proinflammatory cytokine primarily involved in polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses. Upon binding to IL18R1 and IL18RAP, it forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators. IL-18 works synergistically with IL12/interleukin-12 to induce IFN-gamma synthesis from Th1 cells and natural killer (NK) cells. IL-18 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: 466780  Cd Length: 149  Bit Score: 39.12  E-value: 2.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27894310  56 PVILGVQGGSQ--CLSCGvgQEPTLTLEPvniMELYLGAKESKS-FTFYRRDMGLTS---SFESAAYPGWFLCTVPEADQ 129
Cdd:cd23298  55 PVALYVKKDGKtyVLCCE--ENKEIRFKE---MDLPDDIEGTKSdAIFYQKKFPGGTnkyKFESSLYPGYFLAFEPENDL 129
 
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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