NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622857890|ref|XP_014968513|]
View 

interleukin-1 receptor-like 2 [Macaca mulatta]

Protein Classification

immunoglobulin domain-containing protein( domain architecture ID 10309120)

immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and pattern recognition; similar to Drosophila melanogaster DIP/Dpr cell recognition proteins, which are members of the Wirin family of IgSF proteins with neuronal wiring functions, and human IgLON proteins, a family of cell adhesion molecules

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 ...
 386-536 3.60e-38

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: 138.27  E-value: 3.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 386 YVLYPKPRREsqrHAVDTLVLKILPEVleRQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGllKNL 465
Cdd:pfam01582   1 YDVFLSFRGS---DTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSG--WCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 466 SEEQIAVYNALiQDGMKVILIELEKIEDYTA-----MPESIQYIRQKH---GVIRWHGDFTE-------QSQCVKTKFWK 530
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVRkqtgsFGKAFKKHKKVLteeKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 1622857890 531 TVRYHM 536
Cdd:pfam01582 153 KIAYDI 158
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 130-218 1.88e-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: 111.65  E-value: 1.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 130 DEYKQILHLGKDDSLTCHLHFP--KSCILGPIKWYKDCNEITGE-RFTVLETRLLVSNVSAEDRGNYACQVILTHSGKQY 206
Cdd:cd05757     1 PRYKQKLPITKGGKITCPDLDDykNENVLPPIQWYKDCKPLQGDkRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                          90
                  ....*....|..
gi 1622857890 207 EVLNGITVSITE 218
Cdd:cd05757    81 NVTRTISLTVTE 92
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 24-113 6.18e-15

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: 70.53  E-value: 6.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890  24 DIFMKNEMLSASQPFAFNC---TFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGR 100
Cdd:cd05756     4 GEDIKILVVLEGEPDVIKCplfPNFLAQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRNS 83

                          90
                  ....*....|...
gi 1622857890 101 DSCHRIHVNLTLF 113
Cdd:cd05756    84 TYCSKVSISLEVV 96
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 227-327 1.22e-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: 55.75  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 227 PKIIYPKNNSIEVQLGTTLIVDCNITDTKdnTNLRCWRVNNTLVD--------DYYNeskriregVETHASFREHNLYTV 298
Cdd:cd20932     1 PVIVSPANETMEVDLGSQIQLICNVTGQL--SDLAYWKWNGSEIDeddpvlgeDYYS--------VENPANKRKSTLITV 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622857890 299 -NITflEVKMEDYGLPFMCHA----GVSAAYIML 327
Cdd:cd20932    71 lNIS--EIESRFYKHPFTCFAknthGLDAAYVQL 102
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 386-536 3.60e-38

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: 138.27  E-value: 3.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 386 YVLYPKPRREsqrHAVDTLVLKILPEVleRQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGllKNL 465
Cdd:pfam01582   1 YDVFLSFRGS---DTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSG--WCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 466 SEEQIAVYNALiQDGMKVILIELEKIEDYTA-----MPESIQYIRQKH---GVIRWHGDFTE-------QSQCVKTKFWK 530
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVRkqtgsFGKAFKKHKKVLteeKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 1622857890 531 TVRYHM 536
Cdd:pfam01582 153 KIAYDI 158
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 130-218 1.88e-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: 111.65  E-value: 1.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 130 DEYKQILHLGKDDSLTCHLHFP--KSCILGPIKWYKDCNEITGE-RFTVLETRLLVSNVSAEDRGNYACQVILTHSGKQY 206
Cdd:cd05757     1 PRYKQKLPITKGGKITCPDLDDykNENVLPPIQWYKDCKPLQGDkRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                          90
                  ....*....|..
gi 1622857890 207 EVLNGITVSITE 218
Cdd:cd05757    81 NVTRTISLTVTE 92
TIR smart00255
Toll - interleukin 1 - resistance;
383-536 3.83e-26

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 103.94  E-value: 3.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890  383 YDAYVLYPKPrresqrhavDTLVLKILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLL 462
Cdd:smart00255   2 YDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEWC 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622857890  463 KNlsEEQIAVYNALIQDGMKVILIELEKI-EDYTAMPESIQYIRQKHgVIRWHGDFTEQsqcvktkFWKTVRYHM 536
Cdd:smart00255  73 LD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKN-YLKWPEDEKEQ-------FWKKALYAV 137
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 24-113 6.18e-15

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: 70.53  E-value: 6.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890  24 DIFMKNEMLSASQPFAFNC---TFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGR 100
Cdd:cd05756     4 GEDIKILVVLEGEPDVIKCplfPNFLAQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRNS 83

                          90
                  ....*....|...
gi 1622857890 101 DSCHRIHVNLTLF 113
Cdd:cd05756    84 TYCSKVSISLEVV 96
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 227-327 1.22e-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: 55.75  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 227 PKIIYPKNNSIEVQLGTTLIVDCNITDTKdnTNLRCWRVNNTLVD--------DYYNeskriregVETHASFREHNLYTV 298
Cdd:cd20932     1 PVIVSPANETMEVDLGSQIQLICNVTGQL--SDLAYWKWNGSEIDeddpvlgeDYYS--------VENPANKRKSTLITV 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622857890 299 -NITflEVKMEDYGLPFMCHA----GVSAAYIML 327
Cdd:cd20932    71 lNIS--EIESRFYKHPFTCFAknthGLDAAYVQL 102
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 126-214 6.71e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 50.09  E-value: 6.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 126 PNLSDEYkQILHLGKDDSLTCHLHfpkSCILGPIKWYKDCNEITGERftvletRLLVSNVSAEDRGNYACQVILTHSGKQ 205
Cdd:pfam13895   2 PVLTPSP-TVVTEGEPVTLTCSAP---GNPPPSYTWYKDGSAISSSP------NFFTLSVSAEDSGTYTCVARNGRGGKV 71


                  ....*....
gi 1622857890 206 YEVLNgITV 214
Cdd:pfam13895  72 SNPVE-LTV 79
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 143-201 1.84e-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: 37.48  E-value: 1.84e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622857890  143 SLTCHLHFPKSCIlgpIKWYKDCNE--ITGERFTVLET----RLLVSNVSAEDRGNYACQVILTH 201
Cdd:smart00410  13 TLSCEASGSPPPE---VTWYKQGGKllAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSS 74
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 40-111 6.52e-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: 35.94  E-value: 6.52e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622857890   40 FNCTFPpiTSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLP-MEWGDSGVYQCVIKGRDSCHRIHVNLT 111
Cdd:smart00410  14 LSCEAS--GSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISnVTPEDSGTYTCAATNSSGSASSGTTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
40-104 6.52e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.08  E-value: 6.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890  40 FNCTfppiTSG--EVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIK---GRDSCH 104
Cdd:pfam07679  20 FTCT----VTGtpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATnsaGEAEAS 85
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 386-536 3.60e-38

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: 138.27  E-value: 3.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 386 YVLYPKPRREsqrHAVDTLVLKILPEVleRQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGllKNL 465
Cdd:pfam01582   1 YDVFLSFRGS---DTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSG--WCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 466 SEEQIAVYNALiQDGMKVILIELEKIEDYTA-----MPESIQYIRQKH---GVIRWHGDFTE-------QSQCVKTKFWK 530
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVRkqtgsFGKAFKKHKKVLteeKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 1622857890 531 TVRYHM 536
Cdd:pfam01582 153 KIAYDI 158
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 130-218 1.88e-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: 111.65  E-value: 1.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 130 DEYKQILHLGKDDSLTCHLHFP--KSCILGPIKWYKDCNEITGE-RFTVLETRLLVSNVSAEDRGNYACQVILTHSGKQY 206
Cdd:cd05757     1 PRYKQKLPITKGGKITCPDLDDykNENVLPPIQWYKDCKPLQGDkRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                          90
                  ....*....|..
gi 1622857890 207 EVLNGITVSITE 218
Cdd:cd05757    81 NVTRTISLTVTE 92
TIR smart00255
Toll - interleukin 1 - resistance;
383-536 3.83e-26

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 103.94  E-value: 3.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890  383 YDAYVLYPKPrresqrhavDTLVLKILPEVLERQCGYKLFIFGRDEFPGQAVANVIDENVKLCRRLIVIVVPESLGFGLL 462
Cdd:smart00255   2 YDVFISYSGK---------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESEWC 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622857890  463 KNlsEEQIAVYNALIQDGMKVILIELEKI-EDYTAMPESIQYIRQKHgVIRWHGDFTEQsqcvktkFWKTVRYHM 536
Cdd:smart00255  73 LD--ELVAALENALEEGGLRVIPIFYEVIpSDVRKQPGKFRKVFKKN-YLKWPEDEKEQ-------FWKKALYAV 137
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 130-218 5.94e-16

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: 73.27  E-value: 5.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 130 DEYKQILHLGKDDSLTC-HLHFPK--SCILGPIKWYKDCN--EITGERFTVLETRLLVSNVSAEDRGNYACQVILTHSGK 204
Cdd:cd20994     1 DFYKQKVPFTSGGRIVCpHLDFFKdeNNNLPKVQWYKDCKplLLDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGK 80

                          90
                  ....*....|....
gi 1622857890 205 QYEVLNGITVSITE 218
Cdd:cd20994    81 QYNISRTISLIVLE 94
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 24-113 6.18e-15

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: 70.53  E-value: 6.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890  24 DIFMKNEMLSASQPFAFNC---TFPPITSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGR 100
Cdd:cd05756     4 GEDIKILVVLEGEPDVIKCplfPNFLAQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRNS 83

                          90
                  ....*....|...
gi 1622857890 101 DSCHRIHVNLTLF 113
Cdd:cd05756    84 TYCSKVSISLEVV 96
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 53-108 2.78e-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. 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: 57.30  E-value: 2.78e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622857890  53 SVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIKGRDSCHRIHV 108
Cdd:cd20991    31 TITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKI 86
Ig3_IL1R_like cd20932
Third immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 227-327 1.22e-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: 55.75  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 227 PKIIYPKNNSIEVQLGTTLIVDCNITDTKdnTNLRCWRVNNTLVD--------DYYNeskriregVETHASFREHNLYTV 298
Cdd:cd20932     1 PVIVSPANETMEVDLGSQIQLICNVTGQL--SDLAYWKWNGSEIDeddpvlgeDYYS--------VENPANKRKSTLITV 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622857890 299 -NITflEVKMEDYGLPFMCHA----GVSAAYIML 327
Cdd:cd20932    71 lNIS--EIESRFYKHPFTCFAknthGLDAAYVQL 102
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 126-214 6.71e-08

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 50.09  E-value: 6.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890 126 PNLSDEYkQILHLGKDDSLTCHLHfpkSCILGPIKWYKDCNEITGERftvletRLLVSNVSAEDRGNYACQVILTHSGKQ 205
Cdd:pfam13895   2 PVLTPSP-TVVTEGEPVTLTCSAP---GNPPPSYTWYKDGSAISSSP------NFFTLSVSAEDSGTYTCVARNGRGGKV 71


                  ....*....
gi 1622857890 206 YEVLNgITV 214
Cdd:pfam13895  72 SNPVE-LTV 79
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 159-218 1.13e-06

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: 47.06  E-value: 1.13e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622857890 159 IKWYKDCN--EITGERFTVLE--TRLLVSNVSAEDRGNYACQVILTHSGKQYEVLNGITVSITE 218
Cdd:cd05897    32 IQWYKDSLllDKDNEKFLSVKgsTHLLIHDVSLNDSGYYTCKLTFTHEGKKYNITRSIELRIVK 95
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 40-98 1.75e-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: 43.09  E-value: 1.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622857890  40 FNCTFPPitSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIK 98
Cdd:cd00096     3 LTCSASG--NPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVAS 59
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
 49-112 3.27e-05

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: 43.01  E-value: 3.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622857890  49 SGEVSVTWYKNSSKIPVSKII---QSRIHQDETWILFLPMEWGDSGVYQCVIKGRDSCHRIHVNLTL 112
Cdd:cd05896    38 SAGLSLMWYKSSGPGDFEEPIifdGVRMSKEEDSIWFRPAELQDSGLYTCVLRNSTYCMKVSMSLTV 104
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
 134-197 2.17e-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: 40.21  E-value: 2.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622857890 134 QILHLGKDDSLTCHLH-FPKSCILgpikWYKDCNEIT--GERFTVLETRLLVSNVSAEDRGNYACQV 197
Cdd:cd20957    11 QTVDFGRTAVFNCSVTgNPIHTVL----WMKDGKPLGhsSRVQILSEDVLVIPSVKREDKGMYQCFV 73
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
 139-197 5.32e-04

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


Pssm-ID: 409559  Cd Length: 82  Bit Score: 39.15  E-value: 5.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622857890 139 GKDDSLTCHLHFPKscilGPIKWYKDCNEITGERFTVLET-----RLLVSNVSAEDRGNYACQV 197
Cdd:cd20967    12 GHKIRLTVELADPD----AEVKWYKDGQELQSSSKVIFESigakrTLTVQQASLADAGEYQCVA 71
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 143-201 1.84e-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: 37.48  E-value: 1.84e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622857890  143 SLTCHLHFPKSCIlgpIKWYKDCNE--ITGERFTVLET----RLLVSNVSAEDRGNYACQVILTH 201
Cdd:smart00410  13 TLSCEASGSPPPE---VTWYKQGGKllAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSS 74
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 136-208 5.42e-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: 36.40  E-value: 5.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622857890 136 LHLGKDDSLTCHLHFPKSciLGPIKWYKDCNEITGERFTVLETR------LLVSNVSAEDRGNYACQVILTHSGKQYEV 208
Cdd:pfam00047   8 VLEGDSATLTCSASTGSP--GPDVTWSKEGGTLIESLKVKHDNGrttqssLLISNVTKEDAGTYTCVVNNPGGSATLST 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 40-111 6.52e-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: 35.94  E-value: 6.52e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622857890   40 FNCTFPpiTSGEVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLP-MEWGDSGVYQCVIKGRDSCHRIHVNLT 111
Cdd:smart00410  14 LSCEAS--GSPPPEVTWYKQGGKLLAESGRFSVSRSGSTSTLTISnVTPEDSGTYTCAATNSSGSASSGTTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
40-104 6.52e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.08  E-value: 6.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622857890  40 FNCTfppiTSG--EVSVTWYKNSSKIPVSKIIQSRIHQDETWILFLPMEWGDSGVYQCVIK---GRDSCH 104
Cdd:pfam07679  20 FTCT----VTGtpDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATnsaGEAEAS 85
 
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