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Conserved domains on  [gi|530368626|ref|XP_005263991|]
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interleukin-1 receptor type 1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 226-329 6.91e-77

Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R) and similar proteins. Members of this family are characterized by extracellular immunoglobulin-like domains and intracellular Toll/Interleukin-1R (TIR) domain. Three naturally occurring ligands for the IL-1 receptor (IL1R) are known: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA. IL-1Rs are involved in immune host defense and hematopoiesis. After binding to interleukin-1, IL1R associates with the coreceptor IL1RAP (interleukin 1 receptor accessory protein, also known as IL-1R3) to form the high affinity interleukin-1 receptor complex, which 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 TIR domains of the receptor/coreceptor subunits. IL1R binds ligands with comparable affinity to its antagonist IL1RA, and binding of IL1RA to IL1R, prevents association of the latter with IL1RAP to form a signaling complex.


:

Pssm-ID: 409526  Cd Length: 104  Bit Score: 238.33  E-value: 6.91e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 226 PVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRF 305
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                         90       100
                 ....*....|....*....|....
gi 530368626 306 YKHPFTCFAKNTHGIDAAYIQLIY 329
Cdd:cd20932   81 YKHPFTCFAKNTHGLDAAYVQLIY 104
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 24-114 1.58e-58

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: 189.81  E-value: 1.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  24 KEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSY 103
Cdd:cd20991    1 EEREEQIILVSSANEIDVRSCPLNPNESKGTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTY 80

                         90
                 ....*....|.
gi 530368626 104 CLRIKISAKFV 114
Cdd:cd20991   81 CLKIKITAKFV 91
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 126-219 6.95e-52

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: 172.26  E-value: 6.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 126 AIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGK 205
Cdd:cd20994    1 DFYKQKVPFTSGGRIVCPHLDFFKDENNNLPKVQWYKDCKPLLLDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGK 80

                         90
                 ....*....|....
gi 530368626 206 QYPITRVIEFITLE 219
Cdd:cd20994   81 QYNISRTISLIVLE 94
TIR smart00255
Toll - interleukin 1 - resistance;
384-540 1.84e-28

Toll - interleukin 1 - resistance;


:

Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 110.49  E-value: 1.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626   384 TYDAYILYPKTvgegstsdcDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSW 463
Cdd:smart00255   1 EYDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEW 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530368626   464 LGGssEEQIAMYNALVQDGIKVVLLELEKI-QDYEKMPESIKFIKQKHgAIRWSGDFtqgpqsaKTRFWKNVRYHMPV 540
Cdd:smart00255  72 CLD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKN-YLKWPEDE-------KEQFWKKALYAVPS 139
 
Name Accession Description Interval E-value
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 226-329 6.91e-77

Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R) and similar proteins. Members of this family are characterized by extracellular immunoglobulin-like domains and intracellular Toll/Interleukin-1R (TIR) domain. Three naturally occurring ligands for the IL-1 receptor (IL1R) are known: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA. IL-1Rs are involved in immune host defense and hematopoiesis. After binding to interleukin-1, IL1R associates with the coreceptor IL1RAP (interleukin 1 receptor accessory protein, also known as IL-1R3) to form the high affinity interleukin-1 receptor complex, which 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 TIR domains of the receptor/coreceptor subunits. IL1R binds ligands with comparable affinity to its antagonist IL1RA, and binding of IL1RA to IL1R, prevents association of the latter with IL1RAP to form a signaling complex.


Pssm-ID: 409526  Cd Length: 104  Bit Score: 238.33  E-value: 6.91e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 226 PVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRF 305
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                         90       100
                 ....*....|....*....|....
gi 530368626 306 YKHPFTCFAKNTHGIDAAYIQLIY 329
Cdd:cd20932   81 YKHPFTCFAKNTHGLDAAYVQLIY 104
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 24-114 1.58e-58

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: 189.81  E-value: 1.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  24 KEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSY 103
Cdd:cd20991    1 EEREEQIILVSSANEIDVRSCPLNPNESKGTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTY 80

                         90
                 ....*....|.
gi 530368626 104 CLRIKISAKFV 114
Cdd:cd20991   81 CLKIKITAKFV 91
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 126-219 6.95e-52

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: 172.26  E-value: 6.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 126 AIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGK 205
Cdd:cd20994    1 DFYKQKVPFTSGGRIVCPHLDFFKDENNNLPKVQWYKDCKPLLLDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGK 80

                         90
                 ....*....|....
gi 530368626 206 QYPITRVIEFITLE 219
Cdd:cd20994   81 QYNISRTISLIVLE 94
TIR smart00255
Toll - interleukin 1 - resistance;
384-540 1.84e-28

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 110.49  E-value: 1.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626   384 TYDAYILYPKTvgegstsdcDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSW 463
Cdd:smart00255   1 EYDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEW 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530368626   464 LGGssEEQIAMYNALVQDGIKVVLLELEKI-QDYEKMPESIKFIKQKHgAIRWSGDFtqgpqsaKTRFWKNVRYHMPV 540
Cdd:smart00255  72 CLD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKN-YLKWPEDE-------KEQFWKKALYAVPS 139
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 388-538 7.59e-24

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 98.21  E-value: 7.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  388 YILYPKTVGEGSTsdcDIFVFKVLPEVleKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSW-Lgg 466
Cdd:pfam01582   1 YDVFLSFRGSDTR---EWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWcL-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  467 sSEEQIAMYNALvQDGIKVVLLELEKIQDYE-----KMPESIKFIKQKH---GAIRWSGDFTQGP-------QSAKTRFW 531
Cdd:pfam01582  74 -DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEVAniwhsksVSDESKFW 151


                  ....*..
gi 530368626  532 KNVRYHM 538
Cdd:pfam01582 152 KKIAYDI 158
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 3-320 2.70e-10

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 61.96  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626   3 VLLRLICFIALLISSLEADKCKEREEKII-LVSSANEIDVRPCP----LNPNEHKGTITWYK----DDSKTPvsteqasr 73
Cdd:PHA02785   6 VIFLPIFFYSSFVQTFNAPECIDKGQYFAsFMELENEPVILPCPqintLSSGYNILDILWEKrgadNDRIIP-------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  74 IHQHKEKLWFVPAKvEDSGHYYCVVRNSSYCLRIKISAKFVE-NEPNLCYNAqaiFKQKLPVAGDGGLVCPYMEFFKNEN 152
Cdd:PHA02785  78 IDNGSNMLILNPTQ-SDSGIYICITKNETYCDMMSLNLTIVSvSESNIDLIS---YPQIVNERSTGEMVCPNINAFIASN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 153 NELpKLQWYKDCKpllLDNIHFSGVKDRLIVM-NVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPtrPVIVSP 231
Cdd:PHA02785 154 VNA-DIIWSGHRR---LRNKRLKQRTPGIITIeDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDRIIP--PTMQLP 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 232 anETMEVDLGSQIQLICNVTGQLSDI---AYWKWNGSVIDEDDPVlGEDYYSVENP---ANKRRsTLITVLNISEIESRf 305
Cdd:PHA02785 228 --EGVVTSIGSNLTIACRVSLRPPTTdadVFWISNGMYYEEDDED-GDGRISVANKiytTDKRR-VITSRLNINPVKEE- 302

                        330
                 ....*....|....*
gi 530368626 306 YKHPFTCFAKNTHGI 320
Cdd:PHA02785 303 DATTFTCMAFTIPSI 317
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 55-211 2.50e-06

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 48.76  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  55 ITWYKDDS-------------KTPVSTEQASRihqhKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKIsaKFVENEPNLC 121
Cdd:PHA02826  65 VTWSKTDSlafvrdsgartkiKKITHNEIGDR----SENLWIGNVINIDEGIYICTISSGNICEESTI--RLTFDSGTIN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 122 YNAQAIFKQKLPVAGDGGLvcpyMEFFKNENnelpkLQWYKDCKPLL-LDNIHFSGVKDRLIVMNVAEKHRGNYTCHASY 200
Cdd:PHA02826 139 YQFNSGKDSKLHCYGTDGI----SSTFKDYT-----LTWYKNGNIVLyTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRF 209

                        170
                 ....*....|.
gi 530368626 201 TYLGKQYPITR 211
Cdd:PHA02826 210 NKNSNNYNITK 220
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 234-328 1.97e-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: 43.26  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626   234 ETMEVDLGSQIQLICNVTGQLSDIAYWKWNGsvideDDPVLGEDYYSVENpaNKRRSTLiTVLNISEIESRFYkhpfTCF 313
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQG-----GKLLAESGRFSVSR--SGSTSTL-TISNVTPEDSGTY----TCA 69

                           90
                   ....*....|....*
gi 530368626   314 AKNTHGIDAAYIQLI 328
Cdd:smart00410  70 ATNSSGSASSGTTLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 43-103 2.66e-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: 42.88  E-value: 2.66e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530368626    43 PCPLNPNEHkGTITWYKDDSKTPVSTEQASRIHQHKE-KLWFVPAKVEDSGHYYCVVRNSSY 103
Cdd:smart00410  15 SCEASGSPP-PEVTWYKQGGKLLAESGRFSVSRSGSTsTLTISNVTPEDSGTYTCAATNSSG 75
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 152-213 6.49e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 41.61  E-value: 6.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530368626  152 NNELPKLQWYKDCKPLlldnihfsGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVI 213
Cdd:pfam13895  25 GNPPPSYTWYKDGSAI--------SSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSNPVELT 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 54-100 6.71e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.40  E-value: 6.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530368626   54 TITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRN 100
Cdd:pfam13927  32 TITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 225-316 2.23e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.16  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  225 RPVIVSPaNETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDpvlgedyySVENPANKRRSTLiTVLNISEIESR 304
Cdd:pfam13927   1 KPVITVS-PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGS--------TRSRSLSGSNSTL-TISNVTRSDAG 70

                          90
                  ....*....|..
gi 530368626  305 FYkhpfTCFAKN 316
Cdd:pfam13927  71 TY----TCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 140-202 3.59e-03

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: 36.71  E-value: 3.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530368626   140 LVCPYmeffknENNELPKLQWYKDCKPLLLDNIHFSGVKD----RLIVMNVAEKHRGNYTCHASYTY 202
Cdd:smart00410  14 LSCEA------SGSPPPEVTWYKQGGKLLAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSS 74
 
Name Accession Description Interval E-value
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 226-329 6.91e-77

Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R) and similar proteins. Members of this family are characterized by extracellular immunoglobulin-like domains and intracellular Toll/Interleukin-1R (TIR) domain. Three naturally occurring ligands for the IL-1 receptor (IL1R) are known: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA. IL-1Rs are involved in immune host defense and hematopoiesis. After binding to interleukin-1, IL1R associates with the coreceptor IL1RAP (interleukin 1 receptor accessory protein, also known as IL-1R3) to form the high affinity interleukin-1 receptor complex, which 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 TIR domains of the receptor/coreceptor subunits. IL1R binds ligands with comparable affinity to its antagonist IL1RA, and binding of IL1RA to IL1R, prevents association of the latter with IL1RAP to form a signaling complex.


Pssm-ID: 409526  Cd Length: 104  Bit Score: 238.33  E-value: 6.91e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 226 PVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRF 305
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                         90       100
                 ....*....|....*....|....
gi 530368626 306 YKHPFTCFAKNTHGIDAAYIQLIY 329
Cdd:cd20932   81 YKHPFTCFAKNTHGLDAAYVQLIY 104
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 24-114 1.58e-58

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: 189.81  E-value: 1.58e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  24 KEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSY 103
Cdd:cd20991    1 EEREEQIILVSSANEIDVRSCPLNPNESKGTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTY 80

                         90
                 ....*....|.
gi 530368626 104 CLRIKISAKFV 114
Cdd:cd20991   81 CLKIKITAKFV 91
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 126-219 6.95e-52

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: 172.26  E-value: 6.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 126 AIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGK 205
Cdd:cd20994    1 DFYKQKVPFTSGGRIVCPHLDFFKDENNNLPKVQWYKDCKPLLLDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGK 80

                         90
                 ....*....|....
gi 530368626 206 QYPITRVIEFITLE 219
Cdd:cd20994   81 QYNISRTISLIVLE 94
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 27-114 3.95e-44

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: 151.81  E-value: 3.95e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  27 EEKIILVSSANEIDVRPCPLNPN----EHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSS 102
Cdd:cd05756    5 EDIKILVVLEGEPDVIKCPLFPNflaqSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRNST 84

                         90
                 ....*....|..
gi 530368626 103 YCLRIKISAKFV 114
Cdd:cd05756   85 YCSKVSISLEVV 96
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 128-219 9.95e-34

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: 123.20  E-value: 9.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 128 FKQKLPVAGDGGLVCPYMEFFKNENNeLPKLQWYKDCKPLLLDNiHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQY 207
Cdd:cd05757    3 YKQKLPITKGGKITCPDLDDYKNENV-LPPIQWYKDCKPLQGDK-RFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                         90
                 ....*....|..
gi 530368626 208 PITRVIEFITLE 219
Cdd:cd05757   81 NVTRTISLTVTE 92
TIR smart00255
Toll - interleukin 1 - resistance;
384-540 1.84e-28

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 110.49  E-value: 1.84e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626   384 TYDAYILYPKTvgegstsdcDIFVFKVLPEVLEKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSW 463
Cdd:smart00255   1 EYDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEW 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530368626   464 LGGssEEQIAMYNALVQDGIKVVLLELEKI-QDYEKMPESIKFIKQKHgAIRWSGDFtqgpqsaKTRFWKNVRYHMPV 540
Cdd:smart00255  72 CLD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKN-YLKWPEDE-------KEQFWKKALYAVPS 139
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 388-538 7.59e-24

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 98.21  E-value: 7.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  388 YILYPKTVGEGSTsdcDIFVFKVLPEVleKQCGYKLFIYGRDDYVGEDIVEVINENVKKSRRLIIILVRETSGFSW-Lgg 466
Cdd:pfam01582   1 YDVFLSFRGSDTR---EWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWcL-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  467 sSEEQIAMYNALvQDGIKVVLLELEKIQDYE-----KMPESIKFIKQKH---GAIRWSGDFTQGP-------QSAKTRFW 531
Cdd:pfam01582  74 -DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEVAniwhsksVSDESKFW 151


                  ....*..
gi 530368626  532 KNVRYHM 538
Cdd:pfam01582 152 KKIAYDI 158
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 128-219 5.22e-11

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: 59.39  E-value: 5.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 128 FKQKLPVAGDGGLVCPYM-EFFKNENNElpKLQWYKDCKPLLLDNIHFSGVKDR--LIVMNVAEKHRGNYTCHASYTYLG 204
Cdd:cd05897    3 YPQILFTSTSGKLVCPDLsEFTINRTDV--EIQWYKDSLLLDKDNEKFLSVKGSthLLIHDVSLNDSGYYTCKLTFTHEG 80

                         90
                 ....*....|....*
gi 530368626 205 KQYPITRVIEFITLE 219
Cdd:cd05897   81 KKYNITRSIELRIVK 95
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 3-320 2.70e-10

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 61.96  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626   3 VLLRLICFIALLISSLEADKCKEREEKII-LVSSANEIDVRPCP----LNPNEHKGTITWYK----DDSKTPvsteqasr 73
Cdd:PHA02785   6 VIFLPIFFYSSFVQTFNAPECIDKGQYFAsFMELENEPVILPCPqintLSSGYNILDILWEKrgadNDRIIP-------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  74 IHQHKEKLWFVPAKvEDSGHYYCVVRNSSYCLRIKISAKFVE-NEPNLCYNAqaiFKQKLPVAGDGGLVCPYMEFFKNEN 152
Cdd:PHA02785  78 IDNGSNMLILNPTQ-SDSGIYICITKNETYCDMMSLNLTIVSvSESNIDLIS---YPQIVNERSTGEMVCPNINAFIASN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 153 NELpKLQWYKDCKpllLDNIHFSGVKDRLIVM-NVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPtrPVIVSP 231
Cdd:PHA02785 154 VNA-DIIWSGHRR---LRNKRLKQRTPGIITIeDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDRIIP--PTMQLP 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 232 anETMEVDLGSQIQLICNVTGQLSDI---AYWKWNGSVIDEDDPVlGEDYYSVENP---ANKRRsTLITVLNISEIESRf 305
Cdd:PHA02785 228 --EGVVTSIGSNLTIACRVSLRPPTTdadVFWISNGMYYEEDDED-GDGRISVANKiytTDKRR-VITSRLNINPVKEE- 302

                        330
                 ....*....|....*
gi 530368626 306 YKHPFTCFAKNTHGI 320
Cdd:PHA02785 303 DATTFTCMAFTIPSI 317
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
 54-110 4.50e-09

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: 54.18  E-value: 4.50e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530368626  54 TITWYKD----DSKTPVSTEqASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKIS 110
Cdd:cd05896   42 SLMWYKSsgpgDFEEPIIFD-GVRMSKEEDSIWFRPAELQDSGLYTCVLRNSTYCMKVSMS 101
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 43-101 2.89e-08

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: 50.79  E-value: 2.89e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530368626  43 PCPLNPNEhKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNS 101
Cdd:cd00096    4 TCSASGNP-PPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNS 61
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 54-107 1.52e-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: 49.93  E-value: 1.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530368626  54 TITWYK----DDSKTPVSTEQA-SRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRI 107
Cdd:cd20992   43 TLIWYWtrqdRDLEEPINFRLPdNRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKV 101
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 55-211 2.50e-06

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 48.76  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  55 ITWYKDDS-------------KTPVSTEQASRihqhKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKIsaKFVENEPNLC 121
Cdd:PHA02826  65 VTWSKTDSlafvrdsgartkiKKITHNEIGDR----SENLWIGNVINIDEGIYICTISSGNICEESTI--RLTFDSGTIN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 122 YNAQAIFKQKLPVAGDGGLvcpyMEFFKNENnelpkLQWYKDCKPLL-LDNIHFSGVKDRLIVMNVAEKHRGNYTCHASY 200
Cdd:PHA02826 139 YQFNSGKDSKLHCYGTDGI----SSTFKDYT-----LTWYKNGNIVLyTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRF 209

                        170
                 ....*....|.
gi 530368626 201 TYLGKQYPITR 211
Cdd:PHA02826 210 NKNSNNYNITK 220
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 140-206 7.40e-06

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: 43.86  E-value: 7.40e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 140 LVCPYmeffknENNELPKLQWYKDCKPLLLD---NIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQ 206
Cdd:cd00096    3 LTCSA------SGNPPPTITWYKNGKPLPPSsrdSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 140-213 1.47e-05

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: 43.74  E-value: 1.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530368626 140 LVCPYMEFFKNENNElPKLQWYKDCKPLL-LDNIHFSGvkDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVI 213
Cdd:cd20993   16 ITCPDLDGIKPPSVS-PTVTWYHECNAFGnFNDRVPKG--DKLVIHVMLEHYQGNYTCVVTYETKGRTIKLTRTV 87
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 234-328 1.97e-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: 43.26  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626   234 ETMEVDLGSQIQLICNVTGQLSDIAYWKWNGsvideDDPVLGEDYYSVENpaNKRRSTLiTVLNISEIESRFYkhpfTCF 313
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQG-----GKLLAESGRFSVSR--SGSTSTL-TISNVTPEDSGTY----TCA 69

                           90
                   ....*....|....*
gi 530368626   314 AKNTHGIDAAYIQLI 328
Cdd:smart00410  70 ATNSSGSASSGTTLT 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 43-103 2.66e-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: 42.88  E-value: 2.66e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530368626    43 PCPLNPNEHkGTITWYKDDSKTPVSTEQASRIHQHKE-KLWFVPAKVEDSGHYYCVVRNSSY 103
Cdd:smart00410  15 SCEASGSPP-PEVTWYKQGGKLLAESGRFSVSRSGSTsTLTISNVTPEDSGTYTCAATNSSG 75
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 152-213 6.49e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 41.61  E-value: 6.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530368626  152 NNELPKLQWYKDCKPLlldnihfsGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVI 213
Cdd:pfam13895  25 GNPPPSYTWYKDGSAI--------SSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSNPVELT 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 54-100 6.71e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 41.40  E-value: 6.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530368626   54 TITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRN 100
Cdd:pfam13927  32 TITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
 25-100 8.53e-05

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 41.82  E-value: 8.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530368626  25 EREEKIILVSSANEIDVRpCPLNPNEhKGTITWYKDDskTPVSTEQASRIHQHKEKLWFV---PAKVEDSGHYYCVVRN 100
Cdd:cd05729    8 KMEEREHALPAANKVRLE-CGAGGNP-MPNITWLKDG--KEFKKEHRIGGTKVEEKGWSLiieRAIPRDKGKYTCIVEN 82
I-set pfam07679
Immunoglobulin I-set domain;
54-102 3.38e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.93  E-value: 3.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530368626   54 TITWYKDDSKTPVSteqaSRIHQHKE----KLWFVPAKVEDSGHYYCVVRNSS 102
Cdd:pfam07679  31 EVSWFKDGQPLRSS----DRFKVTYEggtyTLTISNVQPDDSGKYTCVATNSA 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 156-199 6.40e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.70  E-value: 6.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530368626  156 PKLQWYKD---CKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHAS 199
Cdd:pfam13927  31 PTITWYKNgepISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVAS 77
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
 43-107 2.00e-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: 2.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530368626   43 PCPLNPNEHKgtITWY---KDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSY-----CLRI 107
Cdd:pfam18452  36 PCSGSKDLSD--VQWYwqpKNGDPLEAITESSPHIIQEGNALWFLPVGVNDSGSYICRPRIRSPqdeacCLKI 106
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 225-316 2.23e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 37.16  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626  225 RPVIVSPaNETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDpvlgedyySVENPANKRRSTLiTVLNISEIESR 304
Cdd:pfam13927   1 KPVITVS-PSSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGS--------TRSRSLSGSNSTL-TISNVTRSDAG 70

                          90
                  ....*....|..
gi 530368626  305 FYkhpfTCFAKN 316
Cdd:pfam13927  71 TY----TCVASN 78
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 54-100 2.87e-03

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. 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. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549 [Multi-domain]  Cd Length: 88  Bit Score: 37.13  E-value: 2.87e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530368626  54 TITWYKDDSKTPVSteqaSRIHQHKEKLWFVPA-KVEDSGHYYCVVRN 100
Cdd:cd20957   32 TVLWMKDGKPLGHS----SRVQILSEDVLVIPSvKREDKGMYQCFVRN 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 140-202 3.59e-03

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: 36.71  E-value: 3.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530368626   140 LVCPYmeffknENNELPKLQWYKDCKPLLLDNIHFSGVKD----RLIVMNVAEKHRGNYTCHASYTY 202
Cdd:smart00410  14 LSCEA------SGSPPPEVTWYKQGGKLLAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSS 74
IgC1_hNephrin_like cd05773
Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig ...
 239-328 4.32e-03

Immunoglobulin-like domain of human nephrin and similar proteins; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin-like domain in human nephrin and similar proteins. Nephrin is an integral component of the slit diaphragm and is a central component of the glomerular ultrafilter. Nephrin plays a structural role and has a role in signaling. Nephrin is a transmembrane protein having a short intracellular portion, an extracellular portion comprised of eight Ig-like domains, and one fibronectin type III-like domain. The extracellular portions of nephrin from neighboring foot processes of separate podocyte cells may interact with each other, and in association with other components of the slit diaphragm form a porous molecular sieve within the slit pore. The intracellular portion of nephrin is associated with linker proteins, which connect nephrin to the actin cytoskeleton. The intracellular portion is tyrosine phosphorylated, and mediates signaling from the slit diaphragm into the podocytes.


Pssm-ID: 143250  Cd Length: 109  Bit Score: 37.22  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368626 239 DLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSvenpANKRRSTLITVLNISEIESRFYkhpFTCFAKNTH 318
Cdd:cd05773   21 DGSSDANLVCQAQGVPRVQFRWAKNGVPLDLGNPRYEETTEH----TGTVHTSILTIINVSAALDYAL---FTCTAHNSL 93

                         90
                 ....*....|
gi 530368626 319 GIDAAYIQLI 328
Cdd:cd05773   94 GEDSLDIQLV 103
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 43-102 6.22e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 36.02  E-value: 6.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530368626   43 PCPLNPNEHKGTITWYKDD-SKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSS 102
Cdd:pfam00047  17 TCSASTGSPGPDVTWSKEGgTLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPG 77
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 54-104 9.01e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 35.45  E-value: 9.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530368626   54 TITWYKDDskTPVSTEQASrihqhkeklwFVPAK-VEDSGHYYCVVRNSSYC 104
Cdd:pfam13895  30 SYTWYKDG--SAISSSPNF----------FTLSVsAEDSGTYTCVARNGRGG 69
 
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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