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Conserved domains on  [gi|118601193|ref|NP_081439|]
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interleukin-36 beta [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
beta-trefoil_IL36 cd23300
beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The ...
34-181 4.48e-92

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: 264.92  E-value: 4.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  34 SPRNYRVHDSQQMVWVLTGNTLTAVPASNNVKPVILSLIACRDTEFQDVKKGNLVFLGIKNRNLCFCCVEMEGKPTLQLK 113
Cdd:cd23300    1 KPSSRHIRDLNQQVWVLQGNTLIAVPRSDNVTPVTLALIPCRDTEFLEKDKGNPIYLGIKGPELCLFCEEIGGQPTLQLK 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118601193 114 EVDIMNLYKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNFYIES 181
Cdd:cd23300   81 EKNIMDLYNEPEAVKPFLFYHNQTGSTSTFESAAYPGWFIASSSEGGQPIILTKERGKTYNTNFYLDS 148
 
Name Accession Description Interval E-value
beta-trefoil_IL36 cd23300
beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The ...
34-181 4.48e-92

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: 264.92  E-value: 4.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  34 SPRNYRVHDSQQMVWVLTGNTLTAVPASNNVKPVILSLIACRDTEFQDVKKGNLVFLGIKNRNLCFCCVEMEGKPTLQLK 113
Cdd:cd23300    1 KPSSRHIRDLNQQVWVLQGNTLIAVPRSDNVTPVTLALIPCRDTEFLEKDKGNPIYLGIKGPELCLFCEEIGGQPTLQLK 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118601193 114 EVDIMNLYKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNFYIES 181
Cdd:cd23300   81 EKNIMDLYNEPEAVKPFLFYHNQTGSTSTFESAAYPGWFIASSSEGGQPIILTKERGKTYNTNFYLDS 148
IL1 smart00125
Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and ...
37-180 1.40e-25

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: 95.91  E-value: 1.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193    37 NYRVHDSQQMVWVLTG-NTLTAVP-ASNNVK-PVILSLIACrDTEFQDVKKGnlVFLGIKNRNLCFCCVEMEGKPTLQLK 113
Cdd:smart00125   5 ECRLNDANQKSLVLSNpQYLKALHlNGQNLNqEVKFDMSFV-QGEEDDSKIP--VTLGISGTNLYLSCVKKGDEPTLQLE 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118601193   114 EVDIMNLYKeRKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNFYIE 180
Cdd:smart00125  82 MVDPPKYPK-KEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQEEDKPVFLGNGPPSQDITDFQME 147
IL1 pfam00340
Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.
88-179 8.04e-23

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


Pssm-ID: 395269  Cd Length: 119  Bit Score: 87.89  E-value: 8.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193   88 VFLGIKNRNLCFCCVeMEGKPTLQLKEVDIMNLYKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTH 167
Cdd:pfam00340  28 VTLGIKGKKLYLSCV-NKDEPVLQLEEVNIPKLIKNKESDKRFFFIRSESKNYVEFESAAYPGWFIATKQEEDLPVFLVN 106
                          90
                  ....*....|...
gi 118601193  168 QRGKL-VNTNFYI 179
Cdd:pfam00340 107 TAGGQdSITDFQI 119
PHA02651 PHA02651
IL-1 receptor antagonist; Provisional
38-182 2.42e-10

IL-1 receptor antagonist; Provisional


Pssm-ID: 165031  Cd Length: 165  Bit Score: 56.58  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  38 YRVHDSQQMVWVLTGNTLTAVPASNN--VKPVILSLIAcrdtefqdvkkGNLVFLGIKNRNLCFCCVEMEGKPTLQLKEV 115
Cdd:PHA02651  25 YNIWDVNQKIFYLRNNQLVAGHIQDNslAEKITAKLID-----------GNDIFLGVKNGEKSLECTEHGDKVTLSLSDK 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118601193 116 DIMNLykERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIER-QTIILTHQRGKLVNTN------FYIESE 182
Cdd:PHA02651  94 KTNSL--DENQDKRFAFIRSDNGHTSTFESVAFPGWFLCTSSGDGiEPVGLTYKGDKDDNDDdenniyFYFEED 165
 
Name Accession Description Interval E-value
beta-trefoil_IL36 cd23300
beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The ...
34-181 4.48e-92

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: 264.92  E-value: 4.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  34 SPRNYRVHDSQQMVWVLTGNTLTAVPASNNVKPVILSLIACRDTEFQDVKKGNLVFLGIKNRNLCFCCVEMEGKPTLQLK 113
Cdd:cd23300    1 KPSSRHIRDLNQQVWVLQGNTLIAVPRSDNVTPVTLALIPCRDTEFLEKDKGNPIYLGIKGPELCLFCEEIGGQPTLQLK 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118601193 114 EVDIMNLYKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNFYIES 181
Cdd:cd23300   81 EKNIMDLYNEPEAVKPFLFYHNQTGSTSTFESAAYPGWFIASSSEGGQPIILTKERGKTYNTNFYLDS 148
beta-trefoil_IL1 cd00100
beta-trefoil domain found in the interleukin-1 (IL-1) family of cytokines; The IL-1 family of ...
34-179 2.00e-33

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: 115.88  E-value: 2.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  34 SPRNYRVHDSQQMVWVLTG-NTLTAVPASNNVKPVILSLIACRDTEFQDvKKGNLVFLGIKNRNLCFCCVEMEGKPTLQL 112
Cdd:cd00100    1 EKRNFVIRDSNDKSLYLRGnNELVAEDLSDVEKSAKITIYYYKSDSDED-FKGIPVVLNFTGTNCFLSCVKEGDKPSLQL 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118601193 113 KEVDIMNLYKERKAQKAFLFY-HGIEGSTSVFQSVLYPGWFIATSSieRQTIILTHQRGKLVNTNFYI 179
Cdd:cd00100   80 EECNKEELKNGDEEEWPFVFYmKASHDNTCRFESAAHPGWFICTKK--DQPVGLTKELGKTEDTDFYF 145
beta-trefoil_IL37 cd23301
beta-trefoil domain found in interleukin-37 (IL-37) and similar proteins; IL-37, also called ...
33-177 7.90e-31

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: 109.43  E-value: 7.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  33 QSPRNYRVHDSQQMVWVLTGNTLTAVPASNNVKPVILSLIACRDTEFQDvKKGNLVFLGIKNRNLCFCC--VEMEGKPTL 110
Cdd:cd23301    1 QTPKKFIIRDTNQQVLVLDSGNLVAVPDKSYIKPETFYVLASHLRSASE-EKGNPIFLAVSKGELCLCCekVKGQKHPSL 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118601193 111 QLKEVDIMNL-YKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNF 177
Cdd:cd23301   80 QLKKKKINELnSQKEKELLPFTFYKEKVGSYFTLESAANPGYFICTSNTPGQPVGVTDKLGKEKNIEF 147
beta-trefoil_IL1B cd23296
beta-trefoil domain found in interleukin-1 beta (IL-1 beta) and similar proteins; IL-1 beta, ...
33-180 2.79e-30

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: 108.09  E-value: 2.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  33 QSPRNYRVHDSQQMVWVLTGNT-LTAVP--ASNNVKPVILSLIACRDTEFQDVKKGnlVFLGIKNRNLCFCCVEMEGKPT 109
Cdd:cd23296    2 VRSLSCTIRDSEQKSLVLSGPYqLVALHlqGPNSSQEVKLNMSFYRSPESNGGKIP--VALGIKGKNLYLSCVKKGDKPT 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118601193 110 LQLKEVDImNLYKERKAQKAFLFY-HGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNFYIE 180
Cdd:cd23296   80 LQLEEVDP-KNDSKSKDLKRFLFYkIESIGSTTTFESAAFPGWYISTSQAENQPVFLGNQKGQQRITDFTLQ 150
beta-trefoil_IL36RA cd23303
beta-trefoil domain found in interleukin-36 receptor antagonist protein (IL-36RA) and similar ...
34-180 1.76e-27

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: 100.58  E-value: 1.76e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  34 SPRNYRVHDSQQMVWVLTGNTLTAVP--ASNNVKPVILSLIACRDTEfqdvKKGNLVFLGIKNRNLCFCCvEMEGKPTLQ 111
Cdd:cd23303    1 GPLCFRMRDTALKVLYLHNNQLVAGGlhAGKNIKGEEISVVPNRFLD----RRLSPIILGVQGGSQCLSC-GTGQEPTLQ 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118601193 112 LKEVDIMNLYKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNFYIE 180
Cdd:cd23303   76 LEPVNIMDLYLSAKEAKSFTFYRTDMGLTHRFESAAYPGWFLCTSPEADQPVRLTNRLGEAPITDFYFQ 144
IL1 smart00125
Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and ...
37-180 1.40e-25

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: 95.91  E-value: 1.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193    37 NYRVHDSQQMVWVLTG-NTLTAVP-ASNNVK-PVILSLIACrDTEFQDVKKGnlVFLGIKNRNLCFCCVEMEGKPTLQLK 113
Cdd:smart00125   5 ECRLNDANQKSLVLSNpQYLKALHlNGQNLNqEVKFDMSFV-QGEEDDSKIP--VTLGISGTNLYLSCVKKGDEPTLQLE 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118601193   114 EVDIMNLYKeRKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNFYIE 180
Cdd:smart00125  82 MVDPPKYPK-KEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQEEDKPVFLGNGPPSQDITDFQME 147
IL1 pfam00340
Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.
88-179 8.04e-23

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


Pssm-ID: 395269  Cd Length: 119  Bit Score: 87.89  E-value: 8.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193   88 VFLGIKNRNLCFCCVeMEGKPTLQLKEVDIMNLYKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTH 167
Cdd:pfam00340  28 VTLGIKGKKLYLSCV-NKDEPVLQLEEVNIPKLIKNKESDKRFFFIRSESKNYVEFESAAYPGWFIATKQEEDLPVFLVN 106
                          90
                  ....*....|...
gi 118601193  168 QRGKL-VNTNFYI 179
Cdd:pfam00340 107 TAGGQdSITDFQI 119
beta-trefoil_IL1RA cd23297
beta-trefoil domain found in interleukin-1 receptor antagonist protein (IL-1RA) and similar ...
88-178 1.02e-20

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: 83.26  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  88 VFLGIKNRNLCFCCVEMEGKPTLQLKEVDIMNLYKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTH 167
Cdd:cd23297   54 VILGIHDGSRCLSCVKSGDEPRLQLEDVDITDLPRNGKQSARFTFFRSYRDGLWRFESAAHPGWFLCTSMRADQPVSLTN 133
                         90
                 ....*....|..
gi 118601193 168 QRGKLVN-TNFY 178
Cdd:cd23297  134 MPDEGVMvTDFY 145
beta-trefoil_IL38 cd23302
beta-trefoil domain found in interleukin-38 (IL-38) and similar proteins; IL-38, also called ...
36-180 2.96e-18

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: 77.01  E-value: 2.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  36 RNYRVHDS-QQMVWVLTGNTLTAVPASNNVKPVILSLIACRDTEFQDVKkgnlVFLGIKNRNLCFCCVEMEGKPTLQLKE 114
Cdd:cd23302    6 RYYIIKYAdQKALYTRDGQLLVGDPVADNCCAEKICILPNRGLDRTKVP----IFLGIQGGSRCLACVETEEGPSLQLED 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118601193 115 VDIMNLYKERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIERQTIILTHQRGKLVNTNFYIE 180
Cdd:cd23302   82 VNIEELYKGGEEATRFTFFQSSSGSAFRLEAAAWPGWFLCGPAEPQQPVQLTKESEPSARTKFYFE 147
PHA02651 PHA02651
IL-1 receptor antagonist; Provisional
38-182 2.42e-10

IL-1 receptor antagonist; Provisional


Pssm-ID: 165031  Cd Length: 165  Bit Score: 56.58  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118601193  38 YRVHDSQQMVWVLTGNTLTAVPASNN--VKPVILSLIAcrdtefqdvkkGNLVFLGIKNRNLCFCCVEMEGKPTLQLKEV 115
Cdd:PHA02651  25 YNIWDVNQKIFYLRNNQLVAGHIQDNslAEKITAKLID-----------GNDIFLGVKNGEKSLECTEHGDKVTLSLSDK 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118601193 116 DIMNLykERKAQKAFLFYHGIEGSTSVFQSVLYPGWFIATSSIER-QTIILTHQRGKLVNTN------FYIESE 182
Cdd:PHA02651  94 KTNSL--DENQDKRFAFIRSDNGHTSTFESVAFPGWFLCTSSGDGiEPVGLTYKGDKDDNDDdenniyFYFEED 165
 
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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