NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|672064792|ref|XP_008765214|]
View 

interleukin-1 receptor-like 1 isoform X1 [Rattus norvegicus]

Protein Classification

Ig2_IL1R-like and TIR domain-containing protein( domain architecture ID 10309125)

protein containing domains Ig, Ig2_IL1R-like, 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 ...
 384-539 1.73e-47

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: 163.30  E-value: 1.73e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  384 YIIYPrvfrgSASGTGSVEYFVHYTLPDVleNKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFA 463
Cdd:pfam01582   1 YDVFL-----SFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  464 YEQEIALHSALiQNNSKVILIEMEPMGEASRLQLGDLQDSLQHLVK---MQGTIKWREDHVA-------DKQSLSSKFWK 533
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKvltEEKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 672064792  534 HVRYQM 539
Cdd:pfam01582 153 KIAYDI 158
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 123-210 2.04e-31

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: 117.04  E-value: 2.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792 123 MMYSTVDGSDKNSKITCPTIALYNW---TAPVQWFKNCKALQGP-RFRAHMSYLFIDKVSHVDEGDYTCRFTHTENGTNY 198
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNenvLPPIQWYKDCKPLQGDkRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                         90
                 ....*....|..
gi 672064792 199 IVTATRSFTVEE 210
Cdd:cd05757   81 NVTRTISLTVTE 92
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 33-110 4.37e-13

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: 65.14  E-value: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  33 LENEALIVRCPQRGGAINP-----VEWYYSNTNERIPTQKRNRIFVSRDRLKFLPAKVEDSGIYTCVIRSPESIKTGSLN 107
Cdd:cd05756   13 LEGEPDVIKCPLFPNFLAQsaglnLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRNSTYCSKVSIS 92


                 ...
gi 672064792 108 VTI 110
Cdd:cd05756   93 LEV 95
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 384-539 1.73e-47

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: 163.30  E-value: 1.73e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  384 YIIYPrvfrgSASGTGSVEYFVHYTLPDVleNKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFA 463
Cdd:pfam01582   1 YDVFL-----SFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  464 YEQEIALHSALiQNNSKVILIEMEPMGEASRLQLGDLQDSLQHLVK---MQGTIKWREDHVA-------DKQSLSSKFWK 533
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKvltEEKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 672064792  534 HVRYQM 539
Cdd:pfam01582 153 KIAYDI 158
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 123-210 2.04e-31

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: 117.04  E-value: 2.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792 123 MMYSTVDGSDKNSKITCPTIALYNW---TAPVQWFKNCKALQGP-RFRAHMSYLFIDKVSHVDEGDYTCRFTHTENGTNY 198
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNenvLPPIQWYKDCKPLQGDkRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                         90
                 ....*....|..
gi 672064792 199 IVTATRSFTVEE 210
Cdd:cd05757   81 NVTRTISLTVTE 92
TIR smart00255
Toll - interleukin 1 - resistance;
381-542 5.01e-31

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 117.42  E-value: 5.01e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792   381 YDAYIIYPRVfrgsasgtgsvEYFVHYTLPDVLENKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSK 460
Cdd:smart00255   2 YDVFISYSGK-----------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESE 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792   461 EFAYEQEIALHSALIQNNSKVILIEMEPMGEASRLQLGDLQDSLQHLvkmqgTIKWREDHvadkqslSSKFWKHVRYQMP 540
Cdd:smart00255  71 WCLDELVAALENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKN-----YLKWPEDE-------KEQFWKKALYAVP 138


                   ..
gi 672064792   541 VP 542
Cdd:smart00255 139 SK 140
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 33-110 4.37e-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; 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: 65.14  E-value: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  33 LENEALIVRCPQRGGAINP-----VEWYYSNTNERIPTQKRNRIFVSRDRLKFLPAKVEDSGIYTCVIRSPESIKTGSLN 107
Cdd:cd05756   13 LEGEPDVIKCPLFPNFLAQsaglnLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRNSTYCSKVSIS 92


                 ...
gi 672064792 108 VTI 110
Cdd:cd05756   93 LEV 95
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 33-315 2.40e-08

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 55.79  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  33 LENEALIVRCPQ-----RGGAINPVEWYYSNT-NERI-PTQKRNRIFVsrdrlkfLPAKVEDSGIYTCVIRSPESIKTGS 105
Cdd:PHA02785  39 LENEPVILPCPQintlsSGYNILDILWEKRGAdNDRIiPIDNGSNMLI-------LNPTQSDSGIYICITKNETYCDMMS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792 106 LNVTIYKRPPNcKIpDYMMYSTVDGSDKNSKITCPTIALY---NWTAPVQWfKNCKALQGPRFRAH-MSYLFIDKVSHVD 181
Cdd:PHA02785 112 LNLTIVSVSES-NI-DLISYPQIVNERSTGEMVCPNINAFiasNVNADIIW-SGHRRLRNKRLKQRtPGIITIEDVRKND 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792 182 EGDYTCRFTHTENGTNYIVTATRSFTVEEKgfsTFPVITNPPHNytVEVEIGKTANIACSACFGTASQFVAVLWQINktr 261
Cdd:PHA02785 189 AGYYTCVLKYIYGDKTYNVTRIVKLEVRDR---IIPPTMQLPEG--VVTSIGSNLTIACRVSLRPPTTDADVFWISN--- 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672064792 262 iGSFGKAriQEEKGPNKSSSNGMI-------CLTSLLRITGVTNKDfSLKYDCVAMNHHGV 315
Cdd:PHA02785 261 -GMYYEE--DDEDGDGRISVANKIyttdkrrVITSRLNINPVKEED-ATTFTCMAFTIPSI 317
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 31-110 4.67e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 4.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792    31 WGLENEALIVRCPQRGGAINPVEWYYsNTNERIPTQKRNRIFVSRDR--LKFLPAKVEDSGIYTCVIRSPESIKTGSLNV 108
Cdd:smart00410   5 TVKEGESVTLSCEASGSPPPEVTWYK-QGGKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83


                   ..
gi 672064792   109 TI 110
Cdd:smart00410  84 TV 85
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 57-208 1.40e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 43.36  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  57 SNTNERIPTQKRNRIFVSRDRLKFLPAKVEDSGIYTCVIRSPESIKTGSLNVTIykrppnckipDYMMYSTVDGSDKNSK 136
Cdd:PHA02826  79 SGARTKIKKITHNEIGDRSENLWIGNVINIDEGIYICTISSGNICEESTIRLTF----------DSGTINYQFNSGKDSK 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672064792 137 ITCPTIALYNWT---APVQWFKNCKALQGP---RFRAHMSYLFIDKVSHVDEGDYTCRFTHTENGTNYIVTATRSFTV 208
Cdd:PHA02826 149 LHCYGTDGISSTfkdYTLTWYKNGNIVLYTdriQLRNNNSTLVIKSATHDDSGIYTCNLRFNKNSNNYNITKEYKVTI 226
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 136-209 1.24e-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: 37.87  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792   136 KITCPtiALYNWTAPVQWFKNC--KALQGPRFRAHMS----YLFIDKVSHVDEGDYTCRFthtengTNYIVTATRSFTVE 209
Cdd:smart00410  13 TLSCE--ASGSPPPEVTWYKQGgkLLAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAA------TNSSGSASSGTTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
151-188 3.72e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.85  E-value: 3.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 672064792  151 VQWFKNCKAL-QGPRFRAHM----SYLFIDKVSHVDEGDYTCR 188
Cdd:pfam07679  32 VSWFKDGQPLrSSDRFKVTYeggtYTLTISNVQPDDSGKYTCV 74
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 28-109 4.16e-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: 37.05  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792   28 KTSWGLENEALIVRC---PQRGGAINPVEWY--------------YSNTNERIPTQKRNRIFVSRDR----LKFLPAKVE 86
Cdd:pfam07686   4 REVTVALGGSVTLPCtysSSMSEASTSVYWYrqppgkgptfliayYSNGSEEGVKKGRFSGRGDPSNgdgsLTIQNLTLS 83

                          90       100
                  ....*....|....*....|....*.
gi 672064792   87 DSGIYTCVIRSPESIKTGS---LNVT 109
Cdd:pfam07686  84 DSGTYTCAVIPSGEGVFGKgtrLTVL 109
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 384-539 1.73e-47

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: 163.30  E-value: 1.73e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  384 YIIYPrvfrgSASGTGSVEYFVHYTLPDVleNKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFA 463
Cdd:pfam01582   1 YDVFL-----SFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  464 YEQEIALHSALiQNNSKVILIEMEPMGEASRLQLGDLQDSLQHLVK---MQGTIKWREDHVA-------DKQSLSSKFWK 533
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKvltEEKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 672064792  534 HVRYQM 539
Cdd:pfam01582 153 KIAYDI 158
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 123-210 2.04e-31

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: 117.04  E-value: 2.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792 123 MMYSTVDGSDKNSKITCPTIALYNW---TAPVQWFKNCKALQGP-RFRAHMSYLFIDKVSHVDEGDYTCRFTHTENGTNY 198
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNenvLPPIQWYKDCKPLQGDkRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQY 80

                         90
                 ....*....|..
gi 672064792 199 IVTATRSFTVEE 210
Cdd:cd05757   81 NVTRTISLTVTE 92
TIR smart00255
Toll - interleukin 1 - resistance;
381-542 5.01e-31

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 117.42  E-value: 5.01e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792   381 YDAYIIYPRVfrgsasgtgsvEYFVHYTLPDVLENKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSK 460
Cdd:smart00255   2 YDVFISYSGK-----------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESE 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792   461 EFAYEQEIALHSALIQNNSKVILIEMEPMGEASRLQLGDLQDSLQHLvkmqgTIKWREDHvadkqslSSKFWKHVRYQMP 540
Cdd:smart00255  71 WCLDELVAALENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKN-----YLKWPEDE-------KEQFWKKALYAVP 138


                   ..
gi 672064792   541 VP 542
Cdd:smart00255 139 SK 140
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 33-110 4.37e-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; 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: 65.14  E-value: 4.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  33 LENEALIVRCPQRGGAINP-----VEWYYSNTNERIPTQKRNRIFVSRDRLKFLPAKVEDSGIYTCVIRSPESIKTGSLN 107
Cdd:cd05756   13 LEGEPDVIKCPLFPNFLAQsaglnLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRNSTYCSKVSIS 92


                 ...
gi 672064792 108 VTI 110
Cdd:cd05756   93 LEV 95
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 136-210 2.17e-12

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: 63.25  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792 136 KITCPTIALY----NWTAPVQWFKNCKALQG--PRFRAHMSYLFIDKVSHVDEGDYTCRFTHTENGTNYIVTATRSFTVE 209
Cdd:cd20994   14 RIVCPHLDFFkdenNNLPKVQWYKDCKPLLLddKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGKQYNISRTISLIVL 93


                 .
gi 672064792 210 E 210
Cdd:cd20994   94 E 94
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 34-97 7.26e-09

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: 53.06  E-value: 7.26e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672064792  34 ENEALIVRCPQRGGAIN-PVEWYYSNTNERIPTQKRNRIFVSRDRLKFLPAKVEDSGIYTCVIRS 97
Cdd:cd20991   13 ANEIDVRSCPLNPNESKgTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRN 77
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 33-315 2.40e-08

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 55.79  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  33 LENEALIVRCPQ-----RGGAINPVEWYYSNT-NERI-PTQKRNRIFVsrdrlkfLPAKVEDSGIYTCVIRSPESIKTGS 105
Cdd:PHA02785  39 LENEPVILPCPQintlsSGYNILDILWEKRGAdNDRIiPIDNGSNMLI-------LNPTQSDSGIYICITKNETYCDMMS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792 106 LNVTIYKRPPNcKIpDYMMYSTVDGSDKNSKITCPTIALY---NWTAPVQWfKNCKALQGPRFRAH-MSYLFIDKVSHVD 181
Cdd:PHA02785 112 LNLTIVSVSES-NI-DLISYPQIVNERSTGEMVCPNINAFiasNVNADIIW-SGHRRLRNKRLKQRtPGIITIEDVRKND 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792 182 EGDYTCRFTHTENGTNYIVTATRSFTVEEKgfsTFPVITNPPHNytVEVEIGKTANIACSACFGTASQFVAVLWQINktr 261
Cdd:PHA02785 189 AGYYTCVLKYIYGDKTYNVTRIVKLEVRDR---IIPPTMQLPEG--VVTSIGSNLTIACRVSLRPPTTDADVFWISN--- 260

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672064792 262 iGSFGKAriQEEKGPNKSSSNGMI-------CLTSLLRITGVTNKDfSLKYDCVAMNHHGV 315
Cdd:PHA02785 261 -GMYYEE--DDEDGDGRISVANKIyttdkrrVITSRLNINPVKEED-ATTFTCMAFTIPSI 317
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 28-110 4.14e-05

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 42.50  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  28 KTSWGLENEALIVRCPQRGGAINPVEWYYSNTNE---------RIPTQKRNrifvsrDRLKFLPAKVEDSGIYTCVIRSP 98
Cdd:cd05750    7 KSQTVQEGSKLVLKCEATSENPSPRYRWFKDGKElnrkrpkniKIRNKKKN------SELQINKAKLEDSGEYTCVVENI 80

                         90
                 ....*....|..
gi 672064792  99 ESIKTGSLNVTI 110
Cdd:cd05750   81 LGKDTVTGNVTV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 31-110 4.67e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 4.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792    31 WGLENEALIVRCPQRGGAINPVEWYYsNTNERIPTQKRNRIFVSRDR--LKFLPAKVEDSGIYTCVIRSPESIKTGSLNV 108
Cdd:smart00410   5 TVKEGESVTLSCEASGSPPPEVTWYK-QGGKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTTL 83


                   ..
gi 672064792   109 TI 110
Cdd:smart00410  84 TV 85
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 57-208 1.40e-04

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 43.36  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  57 SNTNERIPTQKRNRIFVSRDRLKFLPAKVEDSGIYTCVIRSPESIKTGSLNVTIykrppnckipDYMMYSTVDGSDKNSK 136
Cdd:PHA02826  79 SGARTKIKKITHNEIGDRSENLWIGNVINIDEGIYICTISSGNICEESTIRLTF----------DSGTINYQFNSGKDSK 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672064792 137 ITCPTIALYNWT---APVQWFKNCKALQGP---RFRAHMSYLFIDKVSHVDEGDYTCRFTHTENGTNYIVTATRSFTV 208
Cdd:PHA02826 149 LHCYGTDGISSTfkdYTLTWYKNGNIVLYTdriQLRNNNSTLVIKSATHDDSGIYTCNLRFNKNSNNYNITKEYKVTI 226
IgI_1_NCAM-1 cd05865
First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); member of the ...
 52-112 2.97e-04

First immunoglobulin (Ig)-like domain of neural cell adhesion molecule (NCAM-1); 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. 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: 409451  Cd Length: 97  Bit Score: 40.02  E-value: 2.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672064792  52 VEWYYSNTNERIPTQKRNRIFVSRD---RLKFLPAKVEDSGIYTCVIRSPESIKT-GSLNVTIYK 112
Cdd:cd05865   33 ISWFSPNGEKLTPNQQRISVVRNDDyssTLTIYNANIDDAGIYKCVVSNEDEGESeATVNVKIFQ 97
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 38-98 4.63e-04

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 38.85  E-value: 4.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672064792  38 LIVRCPQRGGAINPVEWYYSNTNERIPTQKRNRIFVSRDRLKFLPAKVEDSGIYTCVIRSP 98
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNS 61
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 134-208 4.64e-04

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


Pssm-ID: 409585  Cd Length: 93  Bit Score: 39.50  E-value: 4.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792 134 NSKITCPTIALY---NWTAPVQWFKNCKALQG--PRFRAHMSYLFIDKVSHvDEGDYTCRFTHTENGTNYIVTATRSFTV 208
Cdd:cd20993   13 GRTITCPDLDGIkppSVSPTVTWYHECNAFGNfnDRVPKGDKLVIHVMLEH-YQGNYTCVVTYETKGRTIKLTRTVNVKV 91
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 136-209 1.24e-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: 37.87  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792   136 KITCPtiALYNWTAPVQWFKNC--KALQGPRFRAHMS----YLFIDKVSHVDEGDYTCRFthtengTNYIVTATRSFTVE 209
Cdd:smart00410  13 TLSCE--ASGSPPPEVTWYKQGgkLLAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAA------TNSSGSASSGTTLT 84
I-set pfam07679
Immunoglobulin I-set domain;
151-188 3.72e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 36.85  E-value: 3.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 672064792  151 VQWFKNCKAL-QGPRFRAHM----SYLFIDKVSHVDEGDYTCR 188
Cdd:pfam07679  32 VSWFKDGQPLrSSDRFKVTYeggtYTLTISNVQPDDSGKYTCV 74
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 28-109 4.16e-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: 37.05  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792   28 KTSWGLENEALIVRC---PQRGGAINPVEWY--------------YSNTNERIPTQKRNRIFVSRDR----LKFLPAKVE 86
Cdd:pfam07686   4 REVTVALGGSVTLPCtysSSMSEASTSVYWYrqppgkgptfliayYSNGSEEGVKKGRFSGRGDPSNgdgsLTIQNLTLS 83

                          90       100
                  ....*....|....*....|....*.
gi 672064792   87 DSGIYTCVIRSPESIKTGS---LNVT 109
Cdd:pfam07686  84 DSGTYTCAVIPSGEGVFGKgtrLTVL 109
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 151-209 6.18e-03

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. 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, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 36.22  E-value: 6.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672064792 151 VQWFKNCKALQGPRFRAHM--SYLFIDKVSHVDEGDYTCRfthtenGTNYIVTATRSFTVE 209
Cdd:cd20978   33 ITWLHNGKPLQGPMERATVedGTLTIINVQPEDTGYYGCV------ATNEIGDIYTETLLH 87
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 411-501 9.54e-03

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 36.52  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672064792  411 DVLENKcGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFAYEQEIALhsALIQNNSKVILIEMEPmg 490
Cdd:pfam13676  18 DALEAA-GYRVWLDRWDIRPGDDWVEEIEEAIENSDRVLVVLSPNYLESPWCRAEWEAAL--ADPEGRKRLIPVRLEC-- 92

                          90
                  ....*....|.
gi 672064792  491 EASRLQLGDLQ 501
Cdd:pfam13676  93 DLELPGLAGLQ 103
 
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