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Conserved domains on  [gi|1708445|sp|P51745|]
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RecName: Full=Interleukin-1 beta; Short=IL-1 beta; Flags: Precursor

Protein Classification

IL1_propep and beta-trefoil_IL1B domain-containing protein( domain architecture ID 10493286)

IL1_propep and beta-trefoil_IL1B domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IL1 smart00125
Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and ...
 116-262 1.17e-86

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: 254.61  E-value: 1.17e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445     116 VQSVNCKLQDREQNSLVLASPCVLKALHLLSQEMSREVVFCMSFVQAEERDNKIPVALGIRDKNQYLSCVKKGDTPTLQL 195
Cdd:smart00125   1 VISQECRLNDANQKSLVLSNPQYLKALHLNGQNLNQEVKFDMSFVQGEEDDSKIPVTLGISGTNLYLSCVKKGDEPTLQL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708445     196 EEVDPKVYPKRNMEKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEEKPVFLGHFRGGQDITDFRME 262
Cdd:smart00125  81 EMVDPPKYPKKEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQEEDKPVFLGNGPPSQDITDFQME 147
IL1_propep pfam02394
Interleukin-1 propeptide; The Interleukin-1 cytokines are translated as precursor proteins. ...
 1-101 1.13e-43

Interleukin-1 propeptide; The Interleukin-1 cytokines are translated as precursor proteins. The N terminal approx. 115 amino acids form a propeptide that is cleaved off to release the active interleukin-1.


:

Pssm-ID: 426754  Cd Length: 106  Bit Score: 143.61  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445      1 MAPVPEPINEMMAYYSdENELLFEADGPKQMKSCIQHLDLGSVEV----GNIQLQISHQLYNKSFRQVVSVIVAMEKLRN 76
Cdd:pfam02394   1 MAKVPELFEDLMACYS-ENEEFFEADGPLSLKKSFQDLDLGPLHEdcmdKGIQLQISEQSKNSSFKESVVVVVAVEKLKK 79

                          90       100
                  ....*....|....*....|....*..
gi 1708445     77 S--AYAHVFHDDDLRNVLSFIFEEEPV 101
Cdd:pfam02394  80 RrlSCSQFFQDDDLEAIFSDIFEEEPI 106
 
Name Accession Description Interval E-value
IL1 smart00125
Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and ...
 116-262 1.17e-86

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: 254.61  E-value: 1.17e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445     116 VQSVNCKLQDREQNSLVLASPCVLKALHLLSQEMSREVVFCMSFVQAEERDNKIPVALGIRDKNQYLSCVKKGDTPTLQL 195
Cdd:smart00125   1 VISQECRLNDANQKSLVLSNPQYLKALHLNGQNLNQEVKFDMSFVQGEEDDSKIPVTLGISGTNLYLSCVKKGDEPTLQL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708445     196 EEVDPKVYPKRNMEKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEEKPVFLGHFRGGQDITDFRME 262
Cdd:smart00125  81 EMVDPPKYPKKEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQEEDKPVFLGNGPPSQDITDFQME 147
beta-trefoil_IL1B cd23296
beta-trefoil domain found in interleukin-1 beta (IL-1 beta) and similar proteins; IL-1 beta, ...
 116-262 3.60e-67

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: 205.16  E-value: 3.60e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  116 VQSVNCKLQDREQNSLVLASPCVLKALHLLSQEMSREVVFCMSFVQAEE-RDNKIPVALGIRDKNQYLSCVKKGDTPTLQ 194
Cdd:cd23296   2 VRSLSCTIRDSEQKSLVLSGPYQLVALHLQGPNSSQEVKLNMSFYRSPEsNGGKIPVALGIKGKNLYLSCVKKGDKPTLQ 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708445  195 LEEVDPKVYPKRNMEKRFVFYKTE-IKDTVEFESVLYPNWYISTSHPEEKPVFLGHFRGGQDITDFRME 262
Cdd:cd23296  82 LEEVDPKNDSKSKDLKRFLFYKIEsIGSTTTFESAAFPGWYISTSQAENQPVFLGNQKGQQRITDFTLQ 150
IL1 pfam00340
Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.
 144-261 8.62e-53

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


Pssm-ID: 395269  Cd Length: 119  Bit Score: 167.63  E-value: 8.62e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445    144 LLSQEMSREVVFCMSFVQAEERDNKIPVALGIRDKNQYLSCVKKgDTPTLQLEEVD-PKVYPKRNMEKRFVFYKTEIKDT 222
Cdd:pfam00340   1 LQGQNLNLEVKFDMSFYKGDSDDSKIPVTLGIKGKKLYLSCVNK-DEPVLQLEEVNiPKLIKNKESDKRFFFIRSESKNY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1708445    223 VEFESVLYPNWYISTSHPEEKPVFLGHFRGGQD-ITDFRM 261
Cdd:pfam00340  80 VEFESAAYPGWFIATKQEEDLPVFLVNTAGGQDsITDFQI 119
IL1_propep pfam02394
Interleukin-1 propeptide; The Interleukin-1 cytokines are translated as precursor proteins. ...
 1-101 1.13e-43

Interleukin-1 propeptide; The Interleukin-1 cytokines are translated as precursor proteins. The N terminal approx. 115 amino acids form a propeptide that is cleaved off to release the active interleukin-1.


Pssm-ID: 426754  Cd Length: 106  Bit Score: 143.61  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445      1 MAPVPEPINEMMAYYSdENELLFEADGPKQMKSCIQHLDLGSVEV----GNIQLQISHQLYNKSFRQVVSVIVAMEKLRN 76
Cdd:pfam02394   1 MAKVPELFEDLMACYS-ENEEFFEADGPLSLKKSFQDLDLGPLHEdcmdKGIQLQISEQSKNSSFKESVVVVVAVEKLKK 79

                          90       100
                  ....*....|....*....|....*..
gi 1708445     77 S--AYAHVFHDDDLRNVLSFIFEEEPV 101
Cdd:pfam02394  80 RrlSCSQFFQDDDLEAIFSDIFEEEPI 106
PHA02651 PHA02651
IL-1 receptor antagonist; Provisional
 173-258 5.37e-07

IL-1 receptor antagonist; Provisional


Pssm-ID: 165031  Cd Length: 165  Bit Score: 48.49  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445   173 LGIRDKNQYLSCVKKGDTPTLQLEEVDPKVYPKrNMEKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEE-KPVFLGhFR 251
Cdd:PHA02651  68 LGVKNGEKSLECTEHGDKVTLSLSDKKTNSLDE-NQDKRFAFIRSDNGHTSTFESVAFPGWFLCTSSGDGiEPVGLT-YK 145


                 ....*..
gi 1708445   252 GGQDITD 258
Cdd:PHA02651 146 GDKDDND 152
 
Name Accession Description Interval E-value
IL1 smart00125
Interleukin-1 homologues; Cytokines with various biological functions. Interluekin 1 alpha and ...
 116-262 1.17e-86

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: 254.61  E-value: 1.17e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445     116 VQSVNCKLQDREQNSLVLASPCVLKALHLLSQEMSREVVFCMSFVQAEERDNKIPVALGIRDKNQYLSCVKKGDTPTLQL 195
Cdd:smart00125   1 VISQECRLNDANQKSLVLSNPQYLKALHLNGQNLNQEVKFDMSFVQGEEDDSKIPVTLGISGTNLYLSCVKKGDEPTLQL 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708445     196 EEVDPKVYPKRNMEKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEEKPVFLGHFRGGQDITDFRME 262
Cdd:smart00125  81 EMVDPPKYPKKEMEKRFVFEKHEIGNKVEFESAAHPNWFISTSQEEDKPVFLGNGPPSQDITDFQME 147
beta-trefoil_IL1B cd23296
beta-trefoil domain found in interleukin-1 beta (IL-1 beta) and similar proteins; IL-1 beta, ...
 116-262 3.60e-67

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: 205.16  E-value: 3.60e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  116 VQSVNCKLQDREQNSLVLASPCVLKALHLLSQEMSREVVFCMSFVQAEE-RDNKIPVALGIRDKNQYLSCVKKGDTPTLQ 194
Cdd:cd23296   2 VRSLSCTIRDSEQKSLVLSGPYQLVALHLQGPNSSQEVKLNMSFYRSPEsNGGKIPVALGIKGKNLYLSCVKKGDKPTLQ 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708445  195 LEEVDPKVYPKRNMEKRFVFYKTE-IKDTVEFESVLYPNWYISTSHPEEKPVFLGHFRGGQDITDFRME 262
Cdd:cd23296  82 LEEVDPKNDSKSKDLKRFLFYKIEsIGSTTTFESAAFPGWYISTSQAENQPVFLGNQKGQQRITDFTLQ 150
IL1 pfam00340
Interleukin-1 / 18; This family includes interleukin-1 and interleukin-18.
 144-261 8.62e-53

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


Pssm-ID: 395269  Cd Length: 119  Bit Score: 167.63  E-value: 8.62e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445    144 LLSQEMSREVVFCMSFVQAEERDNKIPVALGIRDKNQYLSCVKKgDTPTLQLEEVD-PKVYPKRNMEKRFVFYKTEIKDT 222
Cdd:pfam00340   1 LQGQNLNLEVKFDMSFYKGDSDDSKIPVTLGIKGKKLYLSCVNK-DEPVLQLEEVNiPKLIKNKESDKRFFFIRSESKNY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1708445    223 VEFESVLYPNWYISTSHPEEKPVFLGHFRGGQD-ITDFRM 261
Cdd:pfam00340  80 VEFESAAYPGWFIATKQEEDLPVFLVNTAGGQDsITDFQI 119
IL1_propep pfam02394
Interleukin-1 propeptide; The Interleukin-1 cytokines are translated as precursor proteins. ...
 1-101 1.13e-43

Interleukin-1 propeptide; The Interleukin-1 cytokines are translated as precursor proteins. The N terminal approx. 115 amino acids form a propeptide that is cleaved off to release the active interleukin-1.


Pssm-ID: 426754  Cd Length: 106  Bit Score: 143.61  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445      1 MAPVPEPINEMMAYYSdENELLFEADGPKQMKSCIQHLDLGSVEV----GNIQLQISHQLYNKSFRQVVSVIVAMEKLRN 76
Cdd:pfam02394   1 MAKVPELFEDLMACYS-ENEEFFEADGPLSLKKSFQDLDLGPLHEdcmdKGIQLQISEQSKNSSFKESVVVVVAVEKLKK 79

                          90       100
                  ....*....|....*....|....*..
gi 1708445     77 S--AYAHVFHDDDLRNVLSFIFEEEPV 101
Cdd:pfam02394  80 RrlSCSQFFQDDDLEAIFSDIFEEEPI 106
beta-trefoil_IL1 cd00100
beta-trefoil domain found in the interleukin-1 (IL-1) family of cytokines; The IL-1 family of ...
 117-259 1.61e-30

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: 111.26  E-value: 1.61e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  117 QSVNCKLQDREQNSLVLASPCVLKALHLlsQEMSREVVFCMSFVQ-AEERDNK-IPVALGIRDKNQYLSCVKKGDTPTLQ 194
Cdd:cd00100   1 EKRNFVIRDSNDKSLYLRGNNELVAEDL--SDVEKSAKITIYYYKsDSDEDFKgIPVVLNFTGTNCFLSCVKEGDKPSLQ 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708445  195 LEEVD-PKVYPKRNMEKRFVFYKTEIKD-TVEFESVLYPNWYISTShpEEKPVFLGHFRGGQDITDF 259
Cdd:cd00100  79 LEECNkEELKNGDEEEWPFVFYMKASHDnTCRFESAAHPGWFICTK--KDQPVGLTKELGKTEDTDF 143
beta-trefoil_IL1RA cd23297
beta-trefoil domain found in interleukin-1 receptor antagonist protein (IL-1RA) and similar ...
 116-262 1.67e-30

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: 111.38  E-value: 1.67e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  116 VQSVNCKLQDREQNSLVLASPcVLKALHLLSQEMSREVVFCMSFVQAEERDnKIPVALGIRDKNQYLSCVKKGDTPTLQL 195
Cdd:cd23297   1 SKVFAYRIWDVNQKSLYLRNN-QLVAGYLQGPNAALEEKIFWVPNRAFEPE-PLPVILGIHDGSRCLSCVKSGDEPRLQL 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708445  196 EEVDPKVYPK-RNMEKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEEKPVFLGHFRG-GQDITDFRME 262
Cdd:cd23297  79 EDVDITDLPRnGKQSARFTFFRSYRDGLWRFESAAHPGWFLCTSMRADQPVSLTNMPDeGVMVTDFYFQ 147
beta-trefoil_IL36 cd23300
beta-trefoil domain found in the family of interleukin-36 (IL-36) and similar proteins; The ...
 164-263 2.39e-23

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: 92.35  E-value: 2.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  164 ERDNKIPVALGIRDKNQYLSCVKKGDTPTLQLEEVD-PKVYPKRNMEKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEE 242
Cdd:cd23300  48 EKDKGNPIYLGIKGPELCLFCEEIGGQPTLQLKEKNiMDLYNEPEAVKPFLFYHNQTGSTSTFESAAYPGWFIASSSEGG 127

                        90       100
                ....*....|....*....|.
gi 1708445  243 KPVFLGHFRGGQDITDFRMET 263
Cdd:cd23300 128 QPIILTKERGKTYNTNFYLDS 148
beta-trefoil_IL36RA cd23303
beta-trefoil domain found in interleukin-36 receptor antagonist protein (IL-36RA) and similar ...
 169-259 3.41e-17

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: 75.93  E-value: 3.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  169 IPVALGIRDKNQYLSCvKKGDTPTLQLEEVD-PKVYPKRNMEKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEEKPVFL 247
Cdd:cd23303  51 SPIILGVQGGSQCLSC-GTGQEPTLQLEPVNiMDLYLSAKEAKSFTFYRTDMGLTHRFESAAYPGWFLCTSPEADQPVRL 129

                        90
                ....*....|..
gi 1708445  248 GHFRGGQDITDF 259
Cdd:cd23303 130 TNRLGEAPITDF 141
beta-trefoil_IL38 cd23302
beta-trefoil domain found in interleukin-38 (IL-38) and similar proteins; IL-38, also called ...
 167-247 4.31e-09

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: 53.90  E-value: 4.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  167 NKIPVALGIRDKNQYLSCVKKGDTPTLQLEEVD-PKVYPKRNMEKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEEKPV 245
Cdd:cd23302  51 TKVPIFLGIQGGSRCLACVETEEGPSLQLEDVNiEELYKGGEEATRFTFFQSSSGSAFRLEAAAWPGWFLCGPAEPQQPV 130


                ..
gi 1708445  246 FL 247
Cdd:cd23302 131 QL 132
beta-trefoil_IL1A cd23295
beta-trefoil domain found in interleukin-1 alpha (IL-1 alpha) and similar proteins; IL-1 alpha, ...
 120-260 1.03e-08

beta-trefoil domain found in interleukin-1 alpha (IL-1 alpha) and similar proteins; IL-1 alpha, also called hematopoietin-1, is a potent inflammatory cytokine that activates the inflammatory process. It is produced by activated macrophages. IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. IL-1 alpha 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: 466777  Cd Length: 145  Bit Score: 52.72  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  120 NCKLQDREQNSLVLASPCVLKALHLlsQEMSREVVFCMSFVQAEERDNKIPVALGIRDKNQYLsCVKKGDTPTLQLEEVD 199
Cdd:cd23295  11 QFILNDALNQSIIRDPSQHLKAAAL--QNLDEEVKFDIGAYKSLDDDYKIPVTLRISNTQLFV-SAQGEDEPVLLKEMPE 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708445  200 -PKVYPKRnmEKRFVFYKTEIKDTVEFESVLYPNWYISTShpEEKPVFLGhfRGGQDITDFR 260
Cdd:cd23295  88 tPKTITGS--ETNLLFFWEEHGTKNFFSSAANPELFAATK--QDELVHLA--RGLPSITDFQ 143
beta-trefoil_IL18 cd23298
beta-trefoil domain found in interleukin-18 (IL-18) and similar proteins; IL-18, also called ...
 117-236 2.27e-08

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: 51.83  E-value: 2.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  117 QSVNCKLQDREQNSLVLASPCVLKALHLLSQEMSR-EVVFCMSFVQAEERDNKIPVALGIRDKNQ--YLSCVKKGdtpTL 193
Cdd:cd23298   1 KSKTSIIRNKDNKFLVLDPDGQFVFEDLTDQELNApDCKFTIQIYKDTSPPRGLPVALYVKKDGKtyVLCCEENK---EI 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 1708445  194 QLEEVDPkvyPKRNMEKR--FVFYKTEIK---DTVEFESVLYPNWYIS 236
Cdd:cd23298  78 RFKEMDL---PDDIEGTKsdAIFYQKKFPggtNKYKFESSLYPGYFLA 122
beta-trefoil_IL37 cd23301
beta-trefoil domain found in interleukin-37 (IL-37) and similar proteins; IL-37, also called ...
 121-262 9.19e-08

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: 50.11  E-value: 9.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445  121 CKLQDREQNSLVLASPcVLKALHLLSQeMSREV--VFCMSFVQAEErDNKIPVALGIRDKNQYLSC--VKKGDTPTLQL- 195
Cdd:cd23301   6 FIIRDTNQQVLVLDSG-NLVAVPDKSY-IKPETfyVLASHLRSASE-EKGNPIFLAVSKGELCLCCekVKGQKHPSLQLk 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708445  196 ----EEVDPKVYPKRnmeKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEEKPVFLGHFRGGQDITDFRME 262
Cdd:cd23301  83 kkkiNELNSQKEKEL---LPFTFYKEKVGSYFTLESAANPGYFICTSNTPGQPVGVTDKLGKEKNIEFSFV 150
PHA02651 PHA02651
IL-1 receptor antagonist; Provisional
 173-258 5.37e-07

IL-1 receptor antagonist; Provisional


Pssm-ID: 165031  Cd Length: 165  Bit Score: 48.49  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708445   173 LGIRDKNQYLSCVKKGDTPTLQLEEVDPKVYPKrNMEKRFVFYKTEIKDTVEFESVLYPNWYISTSHPEE-KPVFLGhFR 251
Cdd:PHA02651  68 LGVKNGEKSLECTEHGDKVTLSLSDKKTNSLDE-NQDKRFAFIRSDNGHTSTFESVAFPGWFLCTSSGDGiEPVGLT-YK 145


                 ....*..
gi 1708445   252 GGQDITD 258
Cdd:PHA02651 146 GDKDDND 152
 
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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