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Conserved domains on  [gi|1170532|sp|P43303|]
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RecName: Full=Interleukin-1 receptor type 2; Short=IL-1R-2; Short=IL-1RT-2; Short=IL-1RT2; AltName: Full=CD121 antigen-like family member B; AltName: Full=IL-1 type II receptor; AltName: Full=Interleukin-1 receptor beta; Short=IL-1R-beta; AltName: Full=Interleukin-1 receptor type II; AltName: CD_antigen=CD121b; Contains: RecName: Full=Interleukin-1 receptor type 2, membrane form; Short=mIL-1R2; Short=mIL-1RII; Contains: RecName: Full=Interleukin-1 receptor type 2, soluble form; Short=sIL-1R2; Short=sIL-1RII; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHA02785 super family cl31505
IL-beta-binding protein; Provisional
41-340 3.17e-41

IL-beta-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02785:

Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 148.63  E-value: 3.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532    41 DCWFRGRDFKSELRLEGEPVVLRCPLVPHSDTSSSSRSLLTWSK-SDSSQLIPGDeprmwvKDDTLWVLPAVQQDSGTYI 119
Cdd:PHA02785  25 ECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDILWEKRgADNDRIIPID------NGSNMLILNPTQSDSGIYI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   120 CTFRNASHCEQMSLELKVFKNTEASFPLVSYLQISALSSTGLLVCPDLKEFISSRTDGKIQWYKGSILLDKGnkkfLSAG 199
Cdd:PHA02785  99 CITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGHRRLRNKR----LKQR 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   200 DPTRLLISNTSMGDAGYYRCVMTFTYEGKEYNITRNIELRVKgitTEPIPVIISPLETIPASLGSRLIVPCKVFLGTGTs 279
Cdd:PHA02785 175 TPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVR---DRIIPPTMQLPEGVVTSIGSNLTIACRVSLRPPT- 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1170532   280 SNTIVWWMANSTFISVAYPRGRVTEGLHHQYSENDENYVEVS-LIFDPVTKEDLNTdFKCVA 340
Cdd:PHA02785 251 TDADVFWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEEDATT-FTCMA 311
 
Name Accession Description Interval E-value
PHA02785 PHA02785
IL-beta-binding protein; Provisional
41-340 3.17e-41

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 148.63  E-value: 3.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532    41 DCWFRGRDFKSELRLEGEPVVLRCPLVPHSDTSSSSRSLLTWSK-SDSSQLIPGDeprmwvKDDTLWVLPAVQQDSGTYI 119
Cdd:PHA02785  25 ECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDILWEKRgADNDRIIPID------NGSNMLILNPTQSDSGIYI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   120 CTFRNASHCEQMSLELKVFKNTEASFPLVSYLQISALSSTGLLVCPDLKEFISSRTDGKIQWYKGSILLDKGnkkfLSAG 199
Cdd:PHA02785  99 CITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGHRRLRNKR----LKQR 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   200 DPTRLLISNTSMGDAGYYRCVMTFTYEGKEYNITRNIELRVKgitTEPIPVIISPLETIPASLGSRLIVPCKVFLGTGTs 279
Cdd:PHA02785 175 TPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVR---DRIIPPTMQLPEGVVTSIGSNLTIACRVSLRPPT- 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1170532   280 SNTIVWWMANSTFISVAYPRGRVTEGLHHQYSENDENYVEVS-LIFDPVTKEDLNTdFKCVA 340
Cdd:PHA02785 251 TDADVFWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEEDATT-FTCMA 311
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
148-242 2.84e-37

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409478  Cd Length: 95  Bit Score: 130.65  E-value: 2.84e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532  148 VSYLQISALSSTGLLVCPDLKEFISSRTDGKIQWYKGSILLDKGNKKFLSAGDPTRLLISNTSMGDAGYYRCVMTFTYEG 227
Cdd:cd05897   1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80
                        90
                ....*....|....*
gi 1170532  228 KEYNITRNIELRVKG 242
Cdd:cd05897  81 KKYNITRSIELRIVK 95
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
249-342 1.84e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532    249 PVIISPLETIPASLGSRLIVPCKVflgTGTSSNTIVWwmanstfisvaYPRGRVTEGLHHQYSENDENYveVSLIFDPVT 328
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEA---TGSPPPTITW-----------YKNGEPISSGSTRSRSLSGSN--STLTISNVT 65
                          90
                  ....*....|....
gi 1170532    329 KEDlNTDFKCVATN 342
Cdd:pfam13927  66 RSD-AGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
162-240 7.93e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.95  E-value: 7.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532     162 LVCPdlkefISSRTDGKIQWYK--GSILLDKGNKKFLSAGDPTRLLISNTSMGDAGYYRCVMTFTYegkeYNITRNIELR 239
Cdd:smart00410  14 LSCE-----ASGSPPPEVTWYKqgGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS----GSASSGTTLT 84

                   .
gi 1170532     240 V 240
Cdd:smart00410  85 V 85
 
Name Accession Description Interval E-value
PHA02785 PHA02785
IL-beta-binding protein; Provisional
41-340 3.17e-41

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 148.63  E-value: 3.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532    41 DCWFRGRDFKSELRLEGEPVVLRCPLVPHSDTSSSSRSLLTWSK-SDSSQLIPGDeprmwvKDDTLWVLPAVQQDSGTYI 119
Cdd:PHA02785  25 ECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDILWEKRgADNDRIIPID------NGSNMLILNPTQSDSGIYI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   120 CTFRNASHCEQMSLELKVFKNTEASFPLVSYLQISALSSTGLLVCPDLKEFISSRTDGKIQWYKGSILLDKGnkkfLSAG 199
Cdd:PHA02785  99 CITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGHRRLRNKR----LKQR 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   200 DPTRLLISNTSMGDAGYYRCVMTFTYEGKEYNITRNIELRVKgitTEPIPVIISPLETIPASLGSRLIVPCKVFLGTGTs 279
Cdd:PHA02785 175 TPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVR---DRIIPPTMQLPEGVVTSIGSNLTIACRVSLRPPT- 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1170532   280 SNTIVWWMANSTFISVAYPRGRVTEGLHHQYSENDENYVEVS-LIFDPVTKEDLNTdFKCVA 340
Cdd:PHA02785 251 TDADVFWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEEDATT-FTCMA 311
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
148-242 2.84e-37

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409478  Cd Length: 95  Bit Score: 130.65  E-value: 2.84e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532  148 VSYLQISALSSTGLLVCPDLKEFISSRTDGKIQWYKGSILLDKGNKKFLSAGDPTRLLISNTSMGDAGYYRCVMTFTYEG 227
Cdd:cd05897   1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80
                        90
                ....*....|....*
gi 1170532  228 KEYNITRNIELRVKG 242
Cdd:cd05897  81 KKYNITRSIELRIVK 95
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
44-138 2.77e-26

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409414  Cd Length: 96  Bit Score: 101.35  E-value: 2.77e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   44 FRGRDFKSELRLEGEPVVLRCPLVPHSDTSSSSRSLLTWsKSDSSQLIPGD-EPRMWVKDDTLWVLPAVQQDSGTYICTF 122
Cdd:cd05756   2 EWGEDIKILVVLEGEPDVIKCPLFPNFLAQSAGLNLTWY-KNDSETPISFEpDSRIHQEKDKLWFVPALLEDSGNYYCVV 80
                        90
                ....*....|....*.
gi 1170532  123 RNASHCEQMSLELKVF 138
Cdd:cd05756  81 RNSTYCSKVSISLEVV 96
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
149-242 2.48e-25

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409415  Cd Length: 92  Bit Score: 98.55  E-value: 2.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532  149 SYLQISALSSTGLLVCPDLKEFISSRTDGKIQWYKGSILLdKGNKKFLSAGDptRLLISNTSMGDAGYYRCVMTFTYEGK 228
Cdd:cd05757   2 RYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPL-QGDKRFIPKGS--KLLIQNVTEEDAGNYTCKFTYTHNGK 78
                        90
                ....*....|....
gi 1170532  229 EYNITRNIELRVKG 242
Cdd:cd05757  79 QYNVTRTISLTVTE 92
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
150-242 9.29e-18

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409586  Cd Length: 94  Bit Score: 77.89  E-value: 9.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532  150 YLQISALSSTGLLVCPDLKEFISSRTD-GKIQWYKGSILLDKGNKKFlsAGDPTRLLISNTSMGDAGYYRCVMTFTYEGK 228
Cdd:cd20994   3 YKQKVPFTSGGRIVCPHLDFFKDENNNlPKVQWYKDCKPLLLDDKRF--AGLESDLLIFNVTVQDQGNYTCHTSYTYMGK 80
                        90
                ....*....|....
gi 1170532  229 EYNITRNIELRVKG 242
Cdd:cd20994  81 QYNISRTISLIVLE 94
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
38-240 2.39e-14

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 71.87  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532    38 LGDDCWFRGRDFKSELRLEGEPVVLRCPLVPHSDTSSSSRSLLTW-----SKSDSSQLIPGDEPRMWVK----------D 102
Cdd:PHA02826  18 LCLYCKYRGGDLTPVYAKFGDPMVLLCTGKHYKKSIFFDKTFITSynvtwSKTDSLAFVRDSGARTKIKkithneigdrS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   103 DTLWVLPAVQQDSGTYICTFRNASHCEQMSLELKVFKNTeasfplVSYLQISALSSTglLVCPDLKEFISSRTDGKIQWY 182
Cdd:PHA02826  98 ENLWIGNVINIDEGIYICTISSGNICEESTIRLTFDSGT------INYQFNSGKDSK--LHCYGTDGISSTFKDYTLTWY 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1170532   183 KGSILLdKGNKKFLSAGDPTRLLISNTSMGDAGYYRCVMTFTYEGKEYNITRNIELRV 240
Cdd:PHA02826 170 KNGNIV-LYTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRFNKNSNNYNITKEYKVTI 226
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
48-137 4.51e-08

First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. IL1RAPL is encoded by a gene on the X-chromosome, this gene is wholly or partially deleted in multiple cases of non-syndromic intellectual disability. This group also contains IL1RAPL-2 which is also encoded by a gene on the X-chromosome and is a candidate for another non-syndromic intellectual disability loci.


Pssm-ID: 409477  Cd Length: 105  Bit Score: 50.72  E-value: 4.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   48 DFKSELRLEGEPVVLRCPLV-----PHSDTSSSSRSLLTWSKS----DSSQLIPGDEPRMWVKDDTLWVLPAVQQDSGTY 118
Cdd:cd05896   6 DLKKYMVLAGEPVRIKCALFygyirTNYSMAQSAGLSLMWYKSsgpgDFEEPIIFDGVRMSKEEDSIWFRPAELQDSGLY 85
                        90
                ....*....|....*....
gi 1170532  119 ICTFRNASHCEQMSLELKV 137
Cdd:cd05896  86 TCVLRNSTYCMKVSMSLTV 104
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
55-137 6.22e-07

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409584  Cd Length: 108  Bit Score: 47.61  E-value: 6.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532   55 LEGEPVVLRCPLVPHSDTSSSSRSLL---------TWSKSDSSQLIPGDEP--RMWVKDDTLWVLPAVQQDSGTYICTFR 123
Cdd:cd20992  14 FEGEPARIKCPLFEHFLKYNYSTAHSagltliwywTRQDRDLEEPINFRLPdnRISKEKDVLWFRPTLLNDTGNYTCMLR 93
                        90
                ....*....|....
gi 1170532  124 NASHCEQMSLELKV 137
Cdd:cd20992  94 NTTYCSKVAFPLEV 107
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
84-137 5.11e-06

First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. IL-1 receptor antagonist (IL-1RA), a naturally occurring cytokine, is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409583  Cd Length: 91  Bit Score: 44.59  E-value: 5.11e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 1170532   84 KSDSSQLIPGDE-PRMWVKDDTLWVLPAVQQDSGTYICTFRNASHCEQMSLELKV 137
Cdd:cd20991  36 KNDSKTPISMEQdSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKITAKF 90
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
162-242 6.30e-06

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409585  Cd Length: 93  Bit Score: 44.51  E-value: 6.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532  162 LVCPDLKEFISSRTDGKIQWYKGSILLDKGNKKfLSAGDptRLLISNTSMGDAGYYRCVMTFTYEGKEYNITRNIELRVK 241
Cdd:cd20993  16 ITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDR-VPKGD--KLVIHVMLEHYQGNYTCVVTYETKGRTIKLTRTVNVKVV 92

                .
gi 1170532  242 G 242
Cdd:cd20993  93 G 93
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
249-342 1.84e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532    249 PVIISPLETIPASLGSRLIVPCKVflgTGTSSNTIVWwmanstfisvaYPRGRVTEGLHHQYSENDENYveVSLIFDPVT 328
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEA---TGSPPPTITW-----------YKNGEPISSGSTRSRSLSGSN--STLTISNVT 65
                          90
                  ....*....|....
gi 1170532    329 KEDlNTDFKCVATN 342
Cdd:pfam13927  66 RSD-AGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
162-240 7.93e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 40.95  E-value: 7.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532     162 LVCPdlkefISSRTDGKIQWYK--GSILLDKGNKKFLSAGDPTRLLISNTSMGDAGYYRCVMTFTYegkeYNITRNIELR 239
Cdd:smart00410  14 LSCE-----ASGSPPPEVTWYKqgGKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS----GSASSGTTLT 84

                   .
gi 1170532     240 V 240
Cdd:smart00410  85 V 85
Ig3_IL1RAP cd20931
Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members ...
249-344 1.23e-04

Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members here are composed of the third immunoglobulin Ig interleukin-1 receptor accessory protein (IL1RAP). The interleukin 1 receptor accessory protein (IL-1RAP), also known as IL-1R3, is a coreceptor of type 1 interleukin 1 receptor (IL-1R1) and is required for transmission of IL-1 signaling. The activated IL-1 receptor complex, which consists of IL-1R1 and IL-1RAP, induces multiple cellular responses including NF-kappa-B activation, IL-2 secretion, and IL-2 promoter activation. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective Toll/IL-1 receptor (TIR) domains of the receptor/coreceptor subunits. Moreover, IL1RAP is known to be the accessory co-receptor that activates signal transduction upon IL-36 binding to IL-36R. IL-36 cytokines, which are a subfamily of the IL-1 superfamily, bind to the IL-36 receptor (IL-36R) and use IL1RAP as a co-receptor.


Pssm-ID: 409525  Cd Length: 107  Bit Score: 41.17  E-value: 1.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532  249 PVIISPLETI--PASLGSRLIVPCKVFLGTGTSSNTIVWWM-----ANSTFISVAyprgrVTEGLHHQYSEnDENYVEVs 321
Cdd:cd20931   1 PQIYSPNDRVvyEKEPGEELLIPCTVYFSFLMDSRNEVWWTidgkkPDDVTIDVT-----INESISYSSTE-DETRTQI- 73
                        90       100
                ....*....|....*....|...
gi 1170532  322 LIFDPVTKEDLNTDFKCVATNPR 344
Cdd:cd20931  74 LSIKKVTPEDLKRNYVCHARNAK 96
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
178-229 5.22e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 38.46  E-value: 5.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 1170532  178 KIQWYK-GSILLDKGNKKFLSAGDPTRLLISNTSMGDAGYYRCVMTFTYEGKE 229
Cdd:cd00096  14 TITWYKnGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
Ig_Sema4D_like cd05873
Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members ...
178-233 1.03e-03

Immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain of semaphorin 4D (Sema4D) and similar proteins. Sema4D is a Class IV semaphorin. Semaphorins are classified based on structural features additional to the Sema domain. Sema4D has extracellular Sema and Ig domains, a transmembrane domain, and a short cytoplasmic domain. Sema4D plays a part in the development of GABAergic synapses. Sema4D in addition is an immune semaphorin. It is abundant on resting T cells; its expression is weak on resting B cells and antigen presenting cells (APCs), but is upregulated by various stimuli. The receptor used by Sema4D in the immune system is CD72. Sem4D enhances the activation of B cells and DCs through binding CD72, perhaps by reducing CD72s inhibitory signals. The receptor used by Sema4D in the non-lymphatic tissues is plexin-B1. Sem4D is anchored to the cell surface but its extracellular domain can be released from the cell surface by a metalloprotease-dependent process. Sem4D may mediate its effects in its membrane-bound form and/or its cleaved form.


Pssm-ID: 409457  Cd Length: 87  Bit Score: 37.87  E-value: 1.03e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 1170532  178 KIQW-YKGSILLDKgNKKFLSAGDPtrLLISNTSMGDAGYYRCVMTFTYEGKEYNIT 233
Cdd:cd05873  26 RVVWkFQGKVLKAE-SPKYGLYGDG--LLIFNASEADAGRYQCLSVEKSKAKTFFQT 79
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
91-141 1.31e-03

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


Pssm-ID: 465773  Cd Length: 128  Bit Score: 38.55  E-value: 1.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1170532     91 IPGDEPRMWVKDDTLWVLPAVQQDSGTYICTFRNASH-----CEQMSLELKVFKNT 141
Cdd:pfam18452  61 ITESSPHIIQEGNALWFLPVGVNDSGSYICRPRIRSPqdeacCLKIILEVQPKTNA 116
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
173-220 1.74e-03

Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) Domain C2 of human cardiac Myosin Binding Protein C (MyBP-C) and similar domains. MyBP-C is a thick filament protein involved in the regulation of muscle contraction. Mutations in cardiac MyBP-C gene are the second most frequent cause of hypertrophic cardiomyopathy. MyBP-C binds to myosin with two binding sites, one at its C-terminus and another at its N-terminus. The N-terminal binding site, consisting of immunoglobulin (lg) domains C1 and C2 connected by a flexible linker, interacts with the S2 segment of myosin in a phosphorylation-regulated manner. The C1 and C2 Ig domains can bind to and activate or inhibit the thin filament. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structures of the Ig domains of MyBP-C lack this strand and thus belong to the I-set of Ig superfamily domains. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409559  Cd Length: 82  Bit Score: 37.22  E-value: 1.74e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 1170532  173 SRTDGKIQWYK-GSILLDKGNKKFLSAGDPTRLLISNTSMGDAGYYRCV 220
Cdd:cd20967  22 ADPDAEVKWYKdGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV 70
I-set pfam07679
Immunoglobulin I-set domain;
249-343 1.93e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 37.24  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170532    249 PVIISPLETIPASLGSRLIVPCKVflgTGTSSNTIVWWMANSTfisvayprgrVTEGLHHQYSENDENYvevSLIFDPVT 328
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTV---TGTPDPEVSWFKDGQP----------LRSSDRFKVTYEGGTY---TLTISNVQ 64
                          90
                  ....*....|....*
gi 1170532    329 KEDLNTdFKCVATNP 343
Cdd:pfam07679  65 PDDSGK-YTCVATNS 78
 
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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