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Conserved domains on  [gi|6680417|ref|NP_032388|]
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interleukin-1 receptor type 1 isoform 1 precursor [Mus musculus]

Protein Classification

Ig and TIR domain-containing protein( domain architecture ID 10310486)

Ig and TIR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 229-332 4.29e-65

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.


The actual alignment was detected with superfamily member cd20932:

Pssm-ID: 472250  Cd Length: 104  Bit Score: 207.52  E-value: 4.29e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417  229 PVILSPRNETIEADPGSMIQLICNVTGQFSDLVYWKWNGSEIEWNDPFLAEDYQFVEHPSTKRKYTLITTLNISEVKSQF 308
Cdd:cd20932   1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                        90       100
                ....*....|....*....|....
gi 6680417  309 YRYPFICVVKNTNIFESAHVQLIY 332
Cdd:cd20932  81 YKHPFTCFAKNTHGLDAAYVQLIY 104
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 27-117 3.64e-42

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.


The actual alignment was detected with superfamily member cd20991:

Pssm-ID: 472250  Cd Length: 91  Bit Score: 146.28  E-value: 3.64e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   27 EYPNQIVLFLSVNEIDIRKCPLTPNKMHGdTIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTY 106
Cdd:cd20991   2 EREEQIILVSSANEIDVRSCPLNPNESKG-TITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTY 80

                        90
                ....*....|.
gi 6680417  107 CLKTKVTVTVL 117
Cdd:cd20991  81 CLKIKITAKFV 91
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 131-220 5.03e-37

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.


The actual alignment was detected with superfamily member cd20994:

Pssm-ID: 472250  Cd Length: 94  Bit Score: 132.59  E-value: 5.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417  131 FPQRLHIAGDGSLVCPYVSYFKDENNELPEVQWYKNCKPLLLDNVSFFGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQY 210
Cdd:cd20994   3 YKQKVPFTSGGRIVCPHLDFFKDENNNLPKVQWYKDCKPLLLDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGKQY 82

                        90
                ....*....|
gi 6680417  211 PVTRVIQFIT 220
Cdd:cd20994  83 NISRTISLIV 92
TIR smart00255
Toll - interleukin 1 - resistance;
387-542 3.17e-24

Toll - interleukin 1 - resistance;


:

Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 98.55  E-value: 3.17e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417     387 TYDAYILYPKTlgegsfsdlDTFVFKLLPEVLEGQFGYKLFIYGRDDYVGEDTIEVTNENVKKSRRLIIILVRDMGGFSW 466
Cdd:smart00255   1 EYDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEW 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6680417     467 LGQssEEQIAIYNALIQEGIKIVLLELEKI-QDYEKMPDSIQFIKQKHGVIcWSGDFQErpqsaktRFWKNLRYQMP 542
Cdd:smart00255  72 CLD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKNYLK-WPEDEKE-------QFWKKALYAVP 138
 
Name Accession Description Interval E-value
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 229-332 4.29e-65

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: 207.52  E-value: 4.29e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417  229 PVILSPRNETIEADPGSMIQLICNVTGQFSDLVYWKWNGSEIEWNDPFLAEDYQFVEHPSTKRKYTLITTLNISEVKSQF 308
Cdd:cd20932   1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                        90       100
                ....*....|....*....|....
gi 6680417  309 YRYPFICVVKNTNIFESAHVQLIY 332
Cdd:cd20932  81 YKHPFTCFAKNTHGLDAAYVQLIY 104
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 27-117 3.64e-42

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: 146.28  E-value: 3.64e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   27 EYPNQIVLFLSVNEIDIRKCPLTPNKMHGdTIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTY 106
Cdd:cd20991   2 EREEQIILVSSANEIDVRSCPLNPNESKG-TITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTY 80

                        90
                ....*....|.
gi 6680417  107 CLKTKVTVTVL 117
Cdd:cd20991  81 CLKIKITAKFV 91
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 131-220 5.03e-37

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: 132.59  E-value: 5.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417  131 FPQRLHIAGDGSLVCPYVSYFKDENNELPEVQWYKNCKPLLLDNVSFFGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQY 210
Cdd:cd20994   3 YKQKVPFTSGGRIVCPHLDFFKDENNNLPKVQWYKDCKPLLLDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGKQY 82

                        90
                ....*....|
gi 6680417  211 PVTRVIQFIT 220
Cdd:cd20994  83 NISRTISLIV 92
TIR smart00255
Toll - interleukin 1 - resistance;
387-542 3.17e-24

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 98.55  E-value: 3.17e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417     387 TYDAYILYPKTlgegsfsdlDTFVFKLLPEVLEGQFGYKLFIYGRDDYVGEDTIEVTNENVKKSRRLIIILVRDMGGFSW 466
Cdd:smart00255   1 EYDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEW 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6680417     467 LGQssEEQIAIYNALIQEGIKIVLLELEKI-QDYEKMPDSIQFIKQKHGVIcWSGDFQErpqsaktRFWKNLRYQMP 542
Cdd:smart00255  72 CLD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKNYLK-WPEDEKE-------QFWKKALYAVP 138
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 391-541 5.75e-22

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: 92.81  E-value: 5.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    391 YILYPKTLGEGSFsdlDTFVFKLLPEVleGQFGYKLFIYGRDDYVGEDTIEVTNENVKKSRRLIIILVRDMGGFSW-Lgq 469
Cdd:pfam01582   1 YDVFLSFRGSDTR---EWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWcL-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    470 sSEEQIAIYNALiQEGIKIVLLELEKIQDYE-----KMPDSIQFIKQKH---GVICWSGDFQERP-------QSAKTRFW 534
Cdd:pfam01582  74 -DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEVAniwhsksVSDESKFW 151


                  ....*..
gi 6680417    535 KNLRYQM 541
Cdd:pfam01582 152 KKIAYDI 158
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 39-307 2.26e-11

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 65.42  E-value: 2.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    39 NEIDIRKCPLTPNKMHGDT---IIWYKNDSKTpisaDRDSRIHQQNEHLWFVPAKvEDSGYYYCIVRNSTYC--LKTKVT 113
Cdd:PHA02785  41 NEPVILPCPQINTLSSGYNildILWEKRGADN----DRIIPIDNGSNMLILNPTQ-SDSGIYICITKNETYCdmMSLNLT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   114 -VTVLENDPGLCystqaTFPQRLHIAGDGSLVCPYVSYFKDENNELpEVQW-----YKNcKPLLLDNVSFFGVKDkllvr 187
Cdd:PHA02785 116 iVSVSESNIDLI-----SYPQIVNERSTGEMVCPNINAFIASNVNA-DIIWsghrrLRN-KRLKQRTPGIITIED----- 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   188 nVAEEHRGDYICRMSYTFRGKQYPVTRVIQFitideNKRDR---PVILSPrnETIEADPGSMIQLICNVTGQFSDL---V 261
Cdd:PHA02785 184 -VRKNDAGYYTCVLKYIYGDKTYNVTRIVKL-----EVRDRiipPTMQLP--EGVVTSIGSNLTIACRVSLRPPTTdadV 255

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 6680417   262 YWKWNGSEIEWNDPFLAEDYQFVEHPSTKRKYTLITT-LNISEVKSQ 307
Cdd:PHA02785 256 FWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEE 302
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 45-116 4.17e-08

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: 50.58  E-value: 4.17e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6680417      45 KCPLTPNKMHgdTIIWYKNDSKTPISADRDSRIHQQNEH-LWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTV 116
Cdd:smart00410  15 SCEASGSPPP--EVTWYKQGGKLLAESGRFSVSRSGSTStLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 58-214 2.02e-06

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 49.14  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    58 IIWYKNDS---------KTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTVLEndpglcystq 128
Cdd:PHA02826  65 VTWSKTDSlafvrdsgaRTKIKKITHNEIGDRSENLWIGNVINIDEGIYICTISSGNICEESTIRLTFDS---------- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   129 ATFPQRLHIAGDGSLVC----PYVSYFKDENnelpeVQWYKNCKPLL-LDNVSFFGVKDKLLVRNVAEEHRGDYICRMSY 203
Cdd:PHA02826 135 GTINYQFNSGKDSKLHCygtdGISSTFKDYT-----LTWYKNGNIVLyTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRF 209

                        170
                 ....*....|.
gi 6680417   204 TFRGKQYPVTR 214
Cdd:PHA02826 210 NKNSNNYNITK 220
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 132-216 1.04e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.92  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    132 PQRLHIAGDGSLVCPYVSyfkdenNELPEVQWYKNCKPLlldnvsffGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQYP 211
Cdd:pfam13895   8 PTVVTEGEPVTLTCSAPG------NPPPSYTWYKDGSAI--------SSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSN 73


                  ....*
gi 6680417    212 VTRVI 216
Cdd:pfam13895  74 PVELT 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 57-103 2.79e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 2.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6680417     57 TIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRN 103
Cdd:pfam13927  32 TITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 228-319 2.76e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.86  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    228 RPVILSPRNETIeADPGSMIQLICNVTGQFSDLVYWKWNGSEIEwndpflaedyqfVEHPSTKRKYTLITTLNISEVKSQ 307
Cdd:pfam13927   1 KPVITVSPSSVT-VREGETVTLTCEATGSPPPTITWYKNGEPIS------------SGSTRSRSLSGSNSTLTISNVTRS 67

                          90
                  ....*....|..
gi 6680417    308 FYRYpFICVVKN 319
Cdd:pfam13927  68 DAGT-YTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 237-331 5.09e-04

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: 39.03  E-value: 5.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417     237 ETIEADPGSMIQLICNVTGQFSDLVYWKWNGSEiewndpFLAEDYQFVEHPStkrkyTLITTLNISEVKSQFY-RYpfIC 315
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGK------LLAESGRFSVSRS-----GSTSTLTISNVTPEDSgTY--TC 68

                           90
                   ....*....|....*.
gi 6680417     316 VVKNTNIFESAHVQLI 331
Cdd:smart00410  69 AATNSSGSASSGTTLT 84
 
Name Accession Description Interval E-value
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 229-332 4.29e-65

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: 207.52  E-value: 4.29e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417  229 PVILSPRNETIEADPGSMIQLICNVTGQFSDLVYWKWNGSEIEWNDPFLAEDYQFVEHPSTKRKYTLITTLNISEVKSQF 308
Cdd:cd20932   1 PVIVSPANETMEVDLGSQIQLICNVTGQLSDLAYWKWNGSEIDEDDPVLGEDYYSVENPANKRKSTLITVLNISEIESRF 80

                        90       100
                ....*....|....*....|....
gi 6680417  309 YRYPFICVVKNTNIFESAHVQLIY 332
Cdd:cd20932  81 YKHPFTCFAKNTHGLDAAYVQLIY 104
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 27-117 3.64e-42

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: 146.28  E-value: 3.64e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   27 EYPNQIVLFLSVNEIDIRKCPLTPNKMHGdTIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTY 106
Cdd:cd20991   2 EREEQIILVSSANEIDVRSCPLNPNESKG-TITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTY 80

                        90
                ....*....|.
gi 6680417  107 CLKTKVTVTVL 117
Cdd:cd20991  81 CLKIKITAKFV 91
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 31-117 8.47e-39

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: 137.56  E-value: 8.47e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   31 QIVLFLSVNEIDIRKCPLTPN---KMHGDTIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTYC 107
Cdd:cd05756   7 IKILVVLEGEPDVIKCPLFPNflaQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRNSTYC 86

                        90
                ....*....|
gi 6680417  108 LKTKVTVTVL 117
Cdd:cd05756  87 SKVSISLEVV 96
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 131-220 5.03e-37

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: 132.59  E-value: 5.03e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417  131 FPQRLHIAGDGSLVCPYVSYFKDENNELPEVQWYKNCKPLLLDNVSFFGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQY 210
Cdd:cd20994   3 YKQKVPFTSGGRIVCPHLDFFKDENNNLPKVQWYKDCKPLLLDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGKQY 82

                        90
                ....*....|
gi 6680417  211 PVTRVIQFIT 220
Cdd:cd20994  83 NISRTISLIV 92
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 131-220 6.37e-29

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: 110.11  E-value: 6.37e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417  131 FPQRLHIAGDGSLVCPYVSYFKDENNeLPEVQWYKNCKPLLLDNVsFFGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQY 210
Cdd:cd05757   3 YKQKLPITKGGKITCPDLDDYKNENV-LPPIQWYKDCKPLQGDKR-FIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                        90
                ....*....|
gi 6680417  211 PVTRVIQFIT 220
Cdd:cd05757  81 NVTRTISLTV 90
TIR smart00255
Toll - interleukin 1 - resistance;
387-542 3.17e-24

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 98.55  E-value: 3.17e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417     387 TYDAYILYPKTlgegsfsdlDTFVFKLLPEVLEGQFGYKLFIYGRDDYVGEDTIEVTNENVKKSRRLIIILVRDMGGFSW 466
Cdd:smart00255   1 EYDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEW 71

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6680417     467 LGQssEEQIAIYNALIQEGIKIVLLELEKI-QDYEKMPDSIQFIKQKHGVIcWSGDFQErpqsaktRFWKNLRYQMP 542
Cdd:smart00255  72 CLD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKNYLK-WPEDEKE-------QFWKKALYAVP 138
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 391-541 5.75e-22

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: 92.81  E-value: 5.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    391 YILYPKTLGEGSFsdlDTFVFKLLPEVleGQFGYKLFIYGRDDYVGEDTIEVTNENVKKSRRLIIILVRDMGGFSW-Lgq 469
Cdd:pfam01582   1 YDVFLSFRGSDTR---EWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWcL-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    470 sSEEQIAIYNALiQEGIKIVLLELEKIQDYE-----KMPDSIQFIKQKH---GVICWSGDFQERP-------QSAKTRFW 534
Cdd:pfam01582  74 -DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEVAniwhsksVSDESKFW 151


                  ....*..
gi 6680417    535 KNLRYQM 541
Cdd:pfam01582 152 KKIAYDI 158
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
 55-116 1.11e-12

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: 64.59  E-value: 1.11e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6680417   55 GDTIIWYKN----DSKTPISADrDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTV 116
Cdd:cd05896  40 GLSLMWYKSsgpgDFEEPIIFD-GVRMSKEEDSIWFRPAELQDSGLYTCVLRNSTYCMKVSMSLTV 104
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 130-221 1.42e-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: 60.93  E-value: 1.42e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417  130 TFPQRLHIAGDGSLVCPYVSYFKDENNELpEVQWYKNCKPLLLDNVSFFGVKDK--LLVRNVAEEHRGDYICRMSYTFRG 207
Cdd:cd05897   2 SYPQILFTSTSGKLVCPDLSEFTINRTDV-EIQWYKDSLLLDKDNEKFLSVKGSthLLIHDVSLNDSGYYTCKLTFTHEG 80

                        90
                ....*....|....
gi 6680417  208 KQYPVTRVIQFITI 221
Cdd:cd05897  81 KKYNITRSIELRIV 94
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 39-307 2.26e-11

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 65.42  E-value: 2.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    39 NEIDIRKCPLTPNKMHGDT---IIWYKNDSKTpisaDRDSRIHQQNEHLWFVPAKvEDSGYYYCIVRNSTYC--LKTKVT 113
Cdd:PHA02785  41 NEPVILPCPQINTLSSGYNildILWEKRGADN----DRIIPIDNGSNMLILNPTQ-SDSGIYICITKNETYCdmMSLNLT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   114 -VTVLENDPGLCystqaTFPQRLHIAGDGSLVCPYVSYFKDENNELpEVQW-----YKNcKPLLLDNVSFFGVKDkllvr 187
Cdd:PHA02785 116 iVSVSESNIDLI-----SYPQIVNERSTGEMVCPNINAFIASNVNA-DIIWsghrrLRN-KRLKQRTPGIITIED----- 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   188 nVAEEHRGDYICRMSYTFRGKQYPVTRVIQFitideNKRDR---PVILSPrnETIEADPGSMIQLICNVTGQFSDL---V 261
Cdd:PHA02785 184 -VRKNDAGYYTCVLKYIYGDKTYNVTRIVKL-----EVRDRiipPTMQLP--EGVVTSIGSNLTIACRVSLRPPTTdadV 255

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 6680417   262 YWKWNGSEIEWNDPFLAEDYQFVEHPSTKRKYTLITT-LNISEVKSQ 307
Cdd:PHA02785 256 FWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEE 302
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 45-117 3.57e-10

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: 57.24  E-value: 3.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   45 KCPL--TPNKMH-------GDTIIWYK----NDSKTPISADR-DSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTYCLKT 110
Cdd:cd20992  22 KCPLfeHFLKYNystahsaGLTLIWYWtrqdRDLEEPINFRLpDNRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKV 101


                ....*..
gi 6680417  111 KVTVTVL 117
Cdd:cd20992 102 AFPLEVV 108
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 45-116 4.17e-08

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: 50.58  E-value: 4.17e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6680417      45 KCPLTPNKMHgdTIIWYKNDSKTPISADRDSRIHQQNEH-LWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTV 116
Cdd:smart00410  15 SCEASGSPPP--EVTWYKQGGKLLAESGRFSVSRSGSTStLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 57-104 1.47e-07

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: 48.86  E-value: 1.47e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6680417   57 TIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNS 104
Cdd:cd00096  14 TITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNS 61
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 58-214 2.02e-06

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 49.14  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    58 IIWYKNDS---------KTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTVLEndpglcystq 128
Cdd:PHA02826  65 VTWSKTDSlafvrdsgaRTKIKKITHNEIGDRSENLWIGNVINIDEGIYICTISSGNICEESTIRLTFDS---------- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417   129 ATFPQRLHIAGDGSLVC----PYVSYFKDENnelpeVQWYKNCKPLL-LDNVSFFGVKDKLLVRNVAEEHRGDYICRMSY 203
Cdd:PHA02826 135 GTINYQFNSGKDSKLHCygtdGISSTFKDYT-----LTWYKNGNIVLyTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRF 209

                        170
                 ....*....|.
gi 6680417   204 TFRGKQYPVTR 214
Cdd:PHA02826 210 NKNSNNYNITK 220
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 132-216 1.04e-05

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.92  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    132 PQRLHIAGDGSLVCPYVSyfkdenNELPEVQWYKNCKPLlldnvsffGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQYP 211
Cdd:pfam13895   8 PTVVTEGEPVTLTCSAPG------NPPPSYTWYKDGSAI--------SSSPNFFTLSVSAEDSGTYTCVARNGRGGKVSN 73


                  ....*
gi 6680417    212 VTRVI 216
Cdd:pfam13895  74 PVELT 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 142-209 2.36e-05

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: 42.70  E-value: 2.36e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6680417  142 SLVCPYvsyfkdENNELPEVQWYKNCKPLLLD---NVSFFGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQ 209
Cdd:cd00096   2 TLTCSA------SGNPPPTITWYKNGKPLPPSsrdSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 57-103 2.79e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 2.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6680417     57 TIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRN 103
Cdd:pfam13927  32 TITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
57-116 4.44e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 42.24  E-value: 4.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6680417     57 TIIWYKNDSktPISADRDSRIHQQNEH--LWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTV 116
Cdd:pfam07679  31 EVSWFKDGQ--PLRSSDRFKVTYEGGTytLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 28-103 6.17e-05

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: 41.75  E-value: 6.17e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6680417   28 YPNqiVLFLSVNEIDIRKCPLTPNKMHgdTIIWYKNDSKTPisadRDSRIHQQNEHLWFVPA-KVEDSGYYYCIVRN 103
Cdd:cd20957   7 DPP--VQTVDFGRTAVFNCSVTGNPIH--TVLWMKDGKPLG----HSSRVQILSEDVLVIPSvKREDKGMYQCFVRN 75
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
 58-117 1.84e-04

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup 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. 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. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin 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. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 40.68  E-value: 1.84e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6680417   58 IIWYKnDSKTPISADRDSRIHQQNEH--LWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTVL 117
Cdd:cd05763  31 IAWQK-DGGTDFPAARERRMHVMPEDdvFFIVDVKIEDTGVYSCTAQNSAGSISANATLTVL 91
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 228-319 2.76e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.86  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417    228 RPVILSPRNETIeADPGSMIQLICNVTGQFSDLVYWKWNGSEIEwndpflaedyqfVEHPSTKRKYTLITTLNISEVKSQ 307
Cdd:pfam13927   1 KPVITVSPSSVT-VREGETVTLTCEATGSPPPTITWYKNGEPIS------------SGSTRSRSLSGSNSTLTISNVTRS 67

                          90
                  ....*....|..
gi 6680417    308 FYRYpFICVVKN 319
Cdd:pfam13927  68 DAGT-YTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 237-331 5.09e-04

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: 39.03  E-value: 5.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417     237 ETIEADPGSMIQLICNVTGQFSDLVYWKWNGSEiewndpFLAEDYQFVEHPStkrkyTLITTLNISEVKSQFY-RYpfIC 315
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGK------LLAESGRFSVSRS-----GSTSTLTISNVTPEDSgTY--TC 68

                           90
                   ....*....|....*.
gi 6680417     316 VVKNTNIFESAHVQLI 331
Cdd:smart00410  69 AATNSSGSASSGTTLT 84
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 133-199 6.71e-04

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: 39.05  E-value: 6.71e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6680417  133 QRLHIAGDGSLVCPYVSyfkdenNELPEVQWYKNCKPLLLDNVSFFGVKDKLLVRNVAEEHRGDYIC 199
Cdd:cd20957  11 QTVDFGRTAVFNCSVTG------NPIHTVLWMKDGKPLGHSSRVQILSEDVLVIPSVKREDKGMYQC 71
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 132-216 7.94e-04

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: 38.73  E-value: 7.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680417  132 PQRLHIA-GDGSLVCPYVSYFKDENNElPEVQWYKNCKPLL-LDNVSFFGvkDKLLVRNVAEEHRGDYICRMSYTFRGKQ 209
Cdd:cd20993   4 PVIAYIEyGGRTITCPDLDGIKPPSVS-PTVTWYHECNAFGnFNDRVPKG--DKLVIHVMLEHYQGNYTCVVTYETKGRT 80


                ....*..
gi 6680417  210 YPVTRVI 216
Cdd:cd20993  81 IKLTRTV 87
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 57-116 4.82e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 36.22  E-value: 4.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6680417     57 TIIWYKNDskTPISADRDSrihqqnehlwFVPAK-VEDSGYYYCIVRNSTYCLKTK-VTVTV 116
Cdd:pfam13895  30 SYTWYKDG--SAISSSPNF----------FTLSVsAEDSGTYTCVARNGRGGKVSNpVELTV 79
 
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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