NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568905608|ref|XP_006495672|]
View 

interleukin-1 receptor-like 2 isoform X1 [Mus musculus]

Protein Classification

Ig and TIR domain-containing protein( domain architecture ID 10309727)

protein containing domains Ig, and TIR

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 389-539 4.18e-36

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: 132.49  E-value: 4.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  389 YVLYPKYpRGSqgHDVDTLVLKILPEVleKQCGYKLFIFGRDEFPGQAVASVIDENIKLCRRLMVFVAPESSSFGflKNL 468
Cdd:pfam01582   1 YDVFLSF-RGS--DTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSG--WCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  469 SEEQIAVYNALiQHGMKVILIELEKVKDYS-----TMPESIQYIRQKH---GAIQWDGDFTE-------QSQCAKTKFWK 533
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 568905608  534 KVRYHM 539
Cdd:pfam01582 153 KIAYDI 158
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 25-115 1.55e-19

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 cd05756:

Pssm-ID: 472250  Cd Length: 96  Bit Score: 83.63  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  25 EDIFMHNVIISEGQPFPFNC---TYPPETNGAVNLTWYKTPSKSPVSNNRHLRVHQDQTWILFLPLTLEDSGIYQCVIRN 101
Cdd:cd05756    3 WGEDIKILVVLEGEPDVIKCplfPNFLAQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRN 82

                         90
                 ....*....|....
gi 568905608 102 AHNCYQIAVNLTVL 115
Cdd:cd05756   83 STYCSKVSISLEVV 96
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 135-222 1.80e-18

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 cd05757:

Pssm-ID: 472250  Cd Length: 92  Bit Score: 80.45  E-value: 1.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 135 YQQILPIGKSGSLNCHLYFPESCA--LDSIKWYKGCEEIKAGKKYSPSGAKLLVNNVAVEDGGSYACSARLTHLGRHFTI 212
Cdd:cd05757    3 YKQKLPITKGGKITCPDLDDYKNEnvLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQYNV 82

                         90
                 ....*....|
gi 568905608 213 RNYIAVNTKE 222
Cdd:cd05757   83 TRTISLTVTE 92
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 230-332 6.70e-09

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: 53.44  E-value: 6.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 230 PNITYPKNNSIEVPLGSTLIVNCNITDtkENTNLRCWRVNNTLVD--------DYYKdskriqegIETNVSLRdqiRYTV 301
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTG--QLSDLAYWKWNGSEIDeddpvlgeDYYS--------VENPANKR---KSTL 67

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568905608 302 nITFL---KVKMEDYGRPFTCHA----GVSAAYIILIY 332
Cdd:cd20932   68 -ITVLnisEIESRFYKHPFTCFAknthGLDAAYVQLIY 104
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 389-539 4.18e-36

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: 132.49  E-value: 4.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  389 YVLYPKYpRGSqgHDVDTLVLKILPEVleKQCGYKLFIFGRDEFPGQAVASVIDENIKLCRRLMVFVAPESSSFGflKNL 468
Cdd:pfam01582   1 YDVFLSF-RGS--DTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSG--WCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  469 SEEQIAVYNALiQHGMKVILIELEKVKDYS-----TMPESIQYIRQKH---GAIQWDGDFTE-------QSQCAKTKFWK 533
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 568905608  534 KVRYHM 539
Cdd:pfam01582 153 KIAYDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
386-540 9.15e-28

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 108.56  E-value: 9.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608   386 YDAYVLYPKyprgsqghdVDTLVLKILPEVLEKQCGYKLFIFGRDEFPGQAVASVIDENIKLCRRLMVFVAPESSSFGFL 465
Cdd:smart00255   2 YDVFISYSG---------KEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEWC 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568905608   466 KNlsEEQIAVYNALIQHGMKVILIELEKVKDYST-MPESIQYIRQKHgAIQWDGDFTEQsqcaktkFWKKVRYHMP 540
Cdd:smart00255  73 LD--ELVAALENALEEGGLRVIPIFYEVIPSDVRkQPGKFRKVFKKN-YLKWPEDEKEQ-------FWKKALYAVP 138
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 25-115 1.55e-19

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: 83.63  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  25 EDIFMHNVIISEGQPFPFNC---TYPPETNGAVNLTWYKTPSKSPVSNNRHLRVHQDQTWILFLPLTLEDSGIYQCVIRN 101
Cdd:cd05756    3 WGEDIKILVVLEGEPDVIKCplfPNFLAQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRN 82

                         90
                 ....*....|....
gi 568905608 102 AHNCYQIAVNLTVL 115
Cdd:cd05756   83 STYCSKVSISLEVV 96
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 135-222 1.80e-18

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; 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: 80.45  E-value: 1.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 135 YQQILPIGKSGSLNCHLYFPESCA--LDSIKWYKGCEEIKAGKKYSPSGAKLLVNNVAVEDGGSYACSARLTHLGRHFTI 212
Cdd:cd05757    3 YKQKLPITKGGKITCPDLDDYKNEnvLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQYNV 82

                         90
                 ....*....|
gi 568905608 213 RNYIAVNTKE 222
Cdd:cd05757   83 TRTISLTVTE 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 31-114 1.16e-11

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: 60.98  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608    31 NVIISEGQPFPFNCTYPPETNgaVNLTWYKTPSKSPVSNNRHLRVHQDQTWILFLP-LTLEDSGIYQCVIRNAHNCYQIA 109
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPP--PEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISnVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 568905608   110 VNLTV 114
Cdd:smart00410  81 TTLTV 85
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 133-207 3.86e-10

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 56.25  E-value: 3.86e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568905608  133 DVYQQILPIGKSGSLNCHLYfpeSCALDSIKWYKGCEEIkagkkysPSGAKLLVNNVAVEDGGSYACSARLTHLG 207
Cdd:pfam13895   5 TPSPTVVTEGEPVTLTCSAP---GNPPPSYTWYKDGSAI-------SSSPNFFTLSVSAEDSGTYTCVARNGRGG 69
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 230-332 6.70e-09

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: 53.44  E-value: 6.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 230 PNITYPKNNSIEVPLGSTLIVNCNITDtkENTNLRCWRVNNTLVD--------DYYKdskriqegIETNVSLRdqiRYTV 301
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTG--QLSDLAYWKWNGSEIDeddpvlgeDYYS--------VENPANKR---KSTL 67

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568905608 302 nITFL---KVKMEDYGRPFTCHA----GVSAAYIILIY 332
Cdd:cd20932   68 -ITVLnisEIESRFYKHPFTCFAknthGLDAAYVQLIY 104
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 1-321 5.01e-07

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 51.94  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608   1 MGVTSLLFCGVFFLLLLFVAADTCEDI----FMHNVIISEGQPFPFNCtypPETN------GAVNLTWyktpSKSPVSNN 70
Cdd:PHA02785   1 MSILPVIFLPIFFYSSFVQTFNAPECIdkgqYFASFMELENEPVILPC---PQINtlssgyNILDILW----EKRGADND 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  71 RHLRVHQDQTWILFLPlTLEDSGIYQCVIRNAHNCYQIAVNLTVLKNHWCDSSMEGSP--VNSPDVYQQILPigksgslN 148
Cdd:PHA02785  74 RIIPIDNGSNMLILNP-TQSDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPqiVNERSTGEMVCP-------N 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 149 CHLYFPESCALDSIkwYKGCEEIKAGKKYSPSGAKLLVNNVAVEDGGSYACSARLTHLGRHFTIRNYIAVNTKEveygRR 228
Cdd:PHA02785 146 INAFIASNVNADII--WSGHRRLRNKRLKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRD----RI 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 229 IPNiTYPKNNSIEVPLGSTLIVNCNITDTKENTNLRCWRVNNTLvddYYKDSKRIQEG---IETNVSLRDQIRY-TVNIT 304
Cdd:PHA02785 220 IPP-TMQLPEGVVTSIGSNLTIACRVSLRPPTTDADVFWISNGM---YYEEDDEDGDGrisVANKIYTTDKRRViTSRLN 295

                        330
                 ....*....|....*..
gi 568905608 305 FLKVKMEDyGRPFTCHA 321
Cdd:PHA02785 296 INPVKEED-ATTFTCMA 311
I-set pfam07679
Immunoglobulin I-set domain;
26-114 5.74e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.94  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608   26 DIFMHNVIISEGQPFPFNCT---YPPETngavnLTWYKtpSKSPVSNNRHLRVHQDQ--TWILFLPLTLEDSGIYQCVIR 100
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTvtgTPDPE-----VSWFK--DGQPLRSSDRFKVTYEGgtYTLTISNVQPDDSGKYTCVAT 76

                          90
                  ....*....|....
gi 568905608  101 NAHNCYQIAVNLTV 114
Cdd:pfam07679  77 NSAGEAEASAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 142-205 1.15e-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: 38.26  E-value: 1.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568905608   142 GKSGSLNCHLYFPEScalDSIKWYK-GCEEIKAGKKYS----PSGAKLLVNNVAVEDGGSYACSARLTH 205
Cdd:smart00410   9 GESVTLSCEASGSPP---PEVTWYKqGGKLLAESGRFSvsrsGSTSTLTISNVTPEDSGTYTCAATNSS 74
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 389-539 4.18e-36

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: 132.49  E-value: 4.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  389 YVLYPKYpRGSqgHDVDTLVLKILPEVleKQCGYKLFIFGRDEFPGQAVASVIDENIKLCRRLMVFVAPESSSFGflKNL 468
Cdd:pfam01582   1 YDVFLSF-RGS--DTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSG--WCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  469 SEEQIAVYNALiQHGMKVILIELEKVKDYS-----TMPESIQYIRQKH---GAIQWDGDFTE-------QSQCAKTKFWK 533
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVrkqtgSFGKAFKKHKKVLteeKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 568905608  534 KVRYHM 539
Cdd:pfam01582 153 KIAYDI 158
TIR smart00255
Toll - interleukin 1 - resistance;
386-540 9.15e-28

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 108.56  E-value: 9.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608   386 YDAYVLYPKyprgsqghdVDTLVLKILPEVLEKQCGYKLFIFGRDEFPGQAVASVIDENIKLCRRLMVFVAPESSSFGFL 465
Cdd:smart00255   2 YDVFISYSG---------KEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEWC 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568905608   466 KNlsEEQIAVYNALIQHGMKVILIELEKVKDYST-MPESIQYIRQKHgAIQWDGDFTEQsqcaktkFWKKVRYHMP 540
Cdd:smart00255  73 LD--ELVAALENALEEGGLRVIPIFYEVIPSDVRkQPGKFRKVFKKN-YLKWPEDEKEQ-------FWKKALYAVP 138
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 25-115 1.55e-19

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: 83.63  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  25 EDIFMHNVIISEGQPFPFNC---TYPPETNGAVNLTWYKTPSKSPVSNNRHLRVHQDQTWILFLPLTLEDSGIYQCVIRN 101
Cdd:cd05756    3 WGEDIKILVVLEGEPDVIKCplfPNFLAQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRN 82

                         90
                 ....*....|....
gi 568905608 102 AHNCYQIAVNLTVL 115
Cdd:cd05756   83 STYCSKVSISLEVV 96
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 135-222 1.80e-18

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; 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: 80.45  E-value: 1.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 135 YQQILPIGKSGSLNCHLYFPESCA--LDSIKWYKGCEEIKAGKKYSPSGAKLLVNNVAVEDGGSYACSARLTHLGRHFTI 212
Cdd:cd05757    3 YKQKLPITKGGKITCPDLDDYKNEnvLPPIQWYKDCKPLQGDKRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQYNV 82

                         90
                 ....*....|
gi 568905608 213 RNYIAVNTKE 222
Cdd:cd05757   83 TRTISLTVTE 92
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 47-115 1.84e-13

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: 66.16  E-value: 1.84e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568905608  47 PPETNGavNLTWYKTPSKSPVSNNRHLRVHQDQTWILFLPLTLEDSGIYQCVIRNAHNCYQIAVNLTVL 115
Cdd:cd20991   25 PNESKG--TITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKITAKFV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 31-114 1.16e-11

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: 60.98  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608    31 NVIISEGQPFPFNCTYPPETNgaVNLTWYKTPSKSPVSNNRHLRVHQDQTWILFLP-LTLEDSGIYQCVIRNAHNCYQIA 109
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPP--PEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISnVTPEDSGTYTCAATNSSGSASSG 80


                   ....*
gi 568905608   110 VNLTV 114
Cdd:smart00410  81 TTLTV 85
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 133-222 3.21e-10

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: 57.09  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 133 DVYQQILPIGKSGSLNC-HLYF--PESCALDSIKWYKGCEEIK-AGKKYSPSGAKLLVNNVAVEDGGSYACSARLTHLGR 208
Cdd:cd20994    1 DFYKQKVPFTSGGRIVCpHLDFfkDENNNLPKVQWYKDCKPLLlDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGK 80

                         90
                 ....*....|....
gi 568905608 209 HFTIRNYIAVNTKE 222
Cdd:cd20994   81 QYNISRTISLIVLE 94
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 133-207 3.86e-10

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 56.25  E-value: 3.86e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568905608  133 DVYQQILPIGKSGSLNCHLYfpeSCALDSIKWYKGCEEIkagkkysPSGAKLLVNNVAVEDGGSYACSARLTHLG 207
Cdd:pfam13895   5 TPSPTVVTEGEPVTLTCSAP---GNPPPSYTWYKDGSAI-------SSSPNFFTLSVSAEDSGTYTCVARNGRGG 69
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 230-332 6.70e-09

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: 53.44  E-value: 6.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 230 PNITYPKNNSIEVPLGSTLIVNCNITDtkENTNLRCWRVNNTLVD--------DYYKdskriqegIETNVSLRdqiRYTV 301
Cdd:cd20932    1 PVIVSPANETMEVDLGSQIQLICNVTG--QLSDLAYWKWNGSEIDeddpvlgeDYYS--------VENPANKR---KSTL 67

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568905608 302 nITFL---KVKMEDYGRPFTCHA----GVSAAYIILIY 332
Cdd:cd20932   68 -ITVLnisEIESRFYKHPFTCFAknthGLDAAYVQLIY 104
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 1-321 5.01e-07

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 51.94  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608   1 MGVTSLLFCGVFFLLLLFVAADTCEDI----FMHNVIISEGQPFPFNCtypPETN------GAVNLTWyktpSKSPVSNN 70
Cdd:PHA02785   1 MSILPVIFLPIFFYSSFVQTFNAPECIdkgqYFASFMELENEPVILPC---PQINtlssgyNILDILW----EKRGADND 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  71 RHLRVHQDQTWILFLPlTLEDSGIYQCVIRNAHNCYQIAVNLTVLKNHWCDSSMEGSP--VNSPDVYQQILPigksgslN 148
Cdd:PHA02785  74 RIIPIDNGSNMLILNP-TQSDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPqiVNERSTGEMVCP-------N 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 149 CHLYFPESCALDSIkwYKGCEEIKAGKKYSPSGAKLLVNNVAVEDGGSYACSARLTHLGRHFTIRNYIAVNTKEveygRR 228
Cdd:PHA02785 146 INAFIASNVNADII--WSGHRRLRNKRLKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRD----RI 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608 229 IPNiTYPKNNSIEVPLGSTLIVNCNITDTKENTNLRCWRVNNTLvddYYKDSKRIQEG---IETNVSLRDQIRY-TVNIT 304
Cdd:PHA02785 220 IPP-TMQLPEGVVTSIGSNLTIACRVSLRPPTTDADVFWISNGM---YYEEDDEDGDGrisVANKIYTTDKRRViTSRLN 295

                        330
                 ....*....|....*..
gi 568905608 305 FLKVKMEDyGRPFTCHA 321
Cdd:PHA02785 296 INPVKEED-ATTFTCMA 311
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
 37-114 6.88e-07

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: 48.02  E-value: 6.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  37 GQPFPFNCT---------YPPETNGAVNLTWYKTPS----KSPVSNNrHLRVHQDQTWILFLPLTLEDSGIYQCVIRNAH 103
Cdd:cd05896   15 GEPVRIKCAlfygyirtnYSMAQSAGLSLMWYKSSGpgdfEEPIIFD-GVRMSKEEDSIWFRPAELQDSGLYTCVLRNST 93

                         90
                 ....*....|.
gi 568905608 104 NCYQIAVNLTV 114
Cdd:cd05896   94 YCMKVSMSLTV 104
I-set pfam07679
Immunoglobulin I-set domain;
26-114 5.74e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.94  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608   26 DIFMHNVIISEGQPFPFNCT---YPPETngavnLTWYKtpSKSPVSNNRHLRVHQDQ--TWILFLPLTLEDSGIYQCVIR 100
Cdd:pfam07679   4 TQKPKDVEVQEGESARFTCTvtgTPDPE-----VSWFK--DGQPLRSSDRFKVTYEGgtYTLTISNVQPDDSGKYTCVAT 76

                          90
                  ....*....|....
gi 568905608  101 NAHNCYQIAVNLTV 114
Cdd:pfam07679  77 NSAGEAEASAELTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 42-103 8.08e-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: 8.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568905608  42 FNCTYPPetNGAVNLTWYKTPSKSPVSNNRHLRVHQDQTWILFLPLTLEDSGIYQCVIRNAH 103
Cdd:cd00096    3 LTCSASG--NPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSA 62
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 27-114 8.21e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 43.92  E-value: 8.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608   27 IFMHNVIISEGQPFPFNCTYPpeTNGAVNLTWYKtpskspvsNNRHLRVHQDqtwILFLPLTLEDSGIYQCVIRNAH-NC 105
Cdd:pfam13895   4 LTPSPTVVTEGEPVTLTCSAP--GNPPPSYTWYK--------DGSAISSSPN---FFTLSVSAEDSGTYTCVARNGRgGK 70


                  ....*....
gi 568905608  106 YQIAVNLTV 114
Cdd:pfam13895  71 VSNPVELTV 79
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 29-115 1.36e-05

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: 44.15  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  29 MHNVIISEGQPFPFNC---------TYPPETNGAVNLTWYKTPS----KSPVsNNRH--LRVHQDQTWILFLPLTLEDSG 93
Cdd:cd20992    8 MRQIQVFEGEPARIKCplfehflkyNYSTAHSAGLTLIWYWTRQdrdlEEPI-NFRLpdNRISKEKDVLWFRPTLLNDTG 86

                         90       100
                 ....*....|....*....|..
gi 568905608  94 IYQCVIRNAHNCYQIAVNLTVL 115
Cdd:cd20992   87 NYTCMLRNTTYCSKVAFPLEVV 108
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 31-101 2.80e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 2.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568905608   31 NVIISEGQPFPFNCT---YPPETngavnLTWYKTPSKSPVSNNRHLRVHQDQTWILFLPLTLEDSGIYQCVIRN 101
Cdd:pfam13927  10 SVTVREGETVTLTCEatgSPPPT-----ITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 37-101 8.57e-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: 41.36  E-value: 8.57e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  37 GQPFPFNCTYppETNGAVNLTWYKtpskspvsNNRHL----RVHQDQTWILFLP-LTLEDSGIYQCVIRN 101
Cdd:cd20957   16 GRTAVFNCSV--TGNPIHTVLWMK--------DGKPLghssRVQILSEDVLVIPsVKREDKGMYQCFVRN 75
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
 142-202 9.34e-05

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 41.48  E-value: 9.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568905608 142 GKSGSLNCHLyfpESCALDSIKWYKGCEEI--KAGKKYS--PSGAKLLVNNVAVEDGGSYACSAR 202
Cdd:cd05736   15 GVEASLRCHA---EGIPLPRVQWLKNGMDInpKLSKQLTliANGSELHISNVRYEDTGAYTCIAK 76
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 32-108 3.76e-04

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409372 [Multi-domain]  Cd Length: 109  Bit Score: 40.33  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  32 VIISEGQPFPFNCTYppETNGAVNLTWYKT-PSKSPVS-----------NNRHLRVHQDQTWILFL----PLTLEDSGIY 95
Cdd:cd04983    8 LSVQEGENVTLNCNY--STSTFYYLFWYRQyPGQGPQFliyissdsgnkKKGRFSATLDKSRKSSSlhisAAQLSDSAVY 85

                         90
                 ....*....|...
gi 568905608  96 QCVIRNAHNCYQI 108
Cdd:cd04983   86 FCALSESGGTGKL 98
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
 26-114 9.43e-04

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and similar proteins; member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and related proteins. The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGF-A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF; VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group also contains alpha-type platelet-derived growth factor receptor precursor (PDGFR)-alpha (CD140a), and PDGFR-beta (CD140b). PDGFRs alpha and beta have an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion that has protein tyrosine kinase activity.


Pssm-ID: 409404  Cd Length: 102  Bit Score: 39.06  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  26 DIFM--HNVIISEGQPFPFNCTYPPETNGAVNLTWyKTPSK---SPVSNNRHLRVHQDQTWILFLPLT-----LEDSGIY 95
Cdd:cd05742    4 ELSPnaEPTVLPQGETLVLNCTANVNLNEVVDFQW-TYPSEkegKLALLKPDIKVDWSEPGEFVSTLTipeatLKDSGTY 82

                         90
                 ....*....|....*....
gi 568905608  96 QCVIRNAHNCYQIAVNLTV 114
Cdd:cd05742   83 TCAARSGVMKKEKQTSVSV 101
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 142-205 1.15e-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: 38.26  E-value: 1.15e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568905608   142 GKSGSLNCHLYFPEScalDSIKWYK-GCEEIKAGKKYS----PSGAKLLVNNVAVEDGGSYACSARLTH 205
Cdd:smart00410   9 GESVTLSCEASGSPP---PEVTWYKqGGKLLAESGRFSvsrsGSTSTLTISNVTPEDSGTYTCAATNSS 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 30-112 1.42e-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: 37.94  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608   30 HNVIISEGQPFPFNCTYPPETnGAVNLTWYK------TPSKSPVSNNRHlRVHQdqtwILFLPLTLEDSGIYQCVIRNAH 103
Cdd:pfam00047   4 PTVTVLEGDSATLTCSASTGS-PGPDVTWSKeggtliESLKVKHDNGRT-TQSS----LLISNVTKEDAGTYTCVVNNPG 77


                  ....*....
gi 568905608  104 NCYQIAVNL 112
Cdd:pfam00047  78 GSATLSTSL 86
I-set pfam07679
Immunoglobulin I-set domain;
141-201 1.55e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 38.01  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568905608  141 IGKSGSLNCHLY-FPEScaldSIKWYKGCEEIKAGKKYS----PSGAKLLVNNVAVEDGGSYACSA 201
Cdd:pfam07679  14 EGESARFTCTVTgTPDP----EVSWFKDGQPLRSSDRFKvtyeGGTYTLTISNVQPDDSGKYTCVA 75
IgI_1_NCAM-1_like cd04977
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar ...
 26-115 1.80e-03

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of neural cell adhesion molecule NCAM-1. NCAM-1 plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-nonNCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves the Ig1, Ig2, and Ig3 domains. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM). NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409366  Cd Length: 95  Bit Score: 38.00  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  26 DIFMHNVIISEGQPFPFNCTYPPEtngAVNLTWYKTPSKSPVSNNRHLRVHQ---DQTWILFLPLTLEDSGIYQCVIRNA 102
Cdd:cd04977    4 KIIPSYAEISVGESKFFLCKVSGD---AKNINWVSPNGEKVLTKHGNLKVVNhgsVLSSLTIYNANINDAGIYKCVATNG 80

                         90
                 ....*....|....
gi 568905608 103 HNCYQIA-VNLTVL 115
Cdd:cd04977   81 KGTESEAtVKLDII 94
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 35-115 3.16e-03

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 37.44  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608   35 SEGQPFPFNCTYPP-ETNGAVNLTWYKTPSKSP-------VSNNRHLRVHQDQ-TW----------ILFLPLTLEDSGIY 95
Cdd:pfam07686   9 ALGGSVTLPCTYSSsMSEASTSVYWYRQPPGKGptfliayYSNGSEEGVKKGRfSGrgdpsngdgsLTIQNLTLSDSGTY 88

                          90       100
                  ....*....|....*....|.
gi 568905608   96 QCVIR-NAHNCYQIAVNLTVL 115
Cdd:pfam07686  89 TCAVIpSGEGVFGKGTRLTVL 109
IgI_hCEACAM_2_4_6_like cd05740
Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion ...
 36-115 5.32e-03

Immunoglobulin (Ig)-like domain of human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) domains 2, 4, and 6, and similar domains; The members here are composed of the second, fourth, and sixth immunoglobulin (Ig)-like domains in human carcinoembryonic antigen (CEA) related cell adhesion molecule (CEACAM) protein subfamily. The CEA family is a group of anchored or secreted glycoproteins expressed by epithelial cells, leukocytes, endothelial cells, and placenta. The CEA family is divided into the CEACAM and pregnancy-specific glycoprotein (PSG) subfamilies. This group represents the CEACAM subfamily. CEACAM1 has many important cellular functions; it is a cell adhesion molecule and a signaling molecule that regulates the growth of tumor cells, an angiogenic factor, and a receptor for bacterial and viral pathogens, including mouse hepatitis virus (MHV). In mice, four isoforms of CEACAM1 generated by alternative splicing have either two [D1, D4] or four [D1-D4] Ig-like domains on the cell surface.


Pssm-ID: 409402 [Multi-domain]  Cd Length: 89  Bit Score: 36.22  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905608  36 EGQPFPFNCTypPETNGAVNLTWYktpskspvsNNRHLRVH------QDQTWILFLPLTLEDSGIYQCVIRN-AHNCYQI 108
Cdd:cd05740   14 DKDAVTLTCE--PETQNTSYLWWF---------NGQSLPVTprltlsNGNRTLTLLNVTREDAGAYQCEISNpVSANRSD 82


                 ....*..
gi 568905608 109 AVNLTVL 115
Cdd:cd05740   83 PVTLDVI 89
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 161-208 5.39e-03

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: 35.77  E-value: 5.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568905608 161 SIKWYKGCEEIKAGKKYS----PSGAKLLVNNVAVEDGGSYACSARLTHLGR 208
Cdd:cd00096   14 TITWYKNGKPLPPSSRDSrrseLGNGTLTISNVTLEDSGTYTCVASNSAGGS 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH