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Conserved domains on  [gi|2497762006|ref|NP_001407277|]
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interleukin-1 receptor-like 1 isoform a precursor [Mus musculus]

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

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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 ...
 385-540 5.65e-50

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: 169.85  E-value: 5.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 385 YIIYPrvfrgSAAGTHSVEYFVHHTLPDVleNKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFA 464
Cdd:pfam01582   1 YDVFL-----SFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 465 YEQEIALHSALiQNNSKVILIEMEPLGEASRLQVGDLQDSLQHLVKI---QGTIKWREDHVA-------DKQSLSSKFWK 534
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKVlteEKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 2497762006 535 HVRYQM 540
Cdd:pfam01582 153 KIAYDI 158
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 124-210 9.76e-35

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: 125.90  E-value: 9.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 124 MYSTVRGSDKNFKITCPTIDLYNW---TAPVQWFKNCKALQEP-RFRAHRSYLFIDNVTHDDEGDYTCQFTHAENGTNYI 199
Cdd:cd05757     2 RYKQKLPITKGGKITCPDLDDYKNenvLPPIQWYKDCKPLQGDkRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQYN 81

                          90
                  ....*....|.
gi 2497762006 200 VTATRSFTVEE 210
Cdd:cd05757    82 VTRTISLTVTE 92
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 33-97 1.34e-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: 66.68  E-value: 1.34e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  33 LENEALIVRCPQR-----GRSTYPVEWYYSDTNESIPTQKRNRIFVSRDRLKFLPARVEDSGIYACVIRS 97
Cdd:cd05756    13 LEGEPDVIKCPLFpnflaQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRN 82
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 291-324 8.66e-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.


The actual alignment was detected with superfamily member cd05731:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 83  Bit Score: 38.54  E-value: 8.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2497762006 291 VLRITGVTEKDlSLEYDCLALNLHGMIRHTIRLR 324
Cdd:cd05731    49 TLKIENVSEAD-SGEYQCTASNTMGSARHTISVT 81
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 385-540 5.65e-50

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: 169.85  E-value: 5.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 385 YIIYPrvfrgSAAGTHSVEYFVHHTLPDVleNKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFA 464
Cdd:pfam01582   1 YDVFL-----SFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 465 YEQEIALHSALiQNNSKVILIEMEPLGEASRLQVGDLQDSLQHLVKI---QGTIKWREDHVA-------DKQSLSSKFWK 534
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKVlteEKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 2497762006 535 HVRYQM 540
Cdd:pfam01582 153 KIAYDI 158
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 124-210 9.76e-35

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: 125.90  E-value: 9.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 124 MYSTVRGSDKNFKITCPTIDLYNW---TAPVQWFKNCKALQEP-RFRAHRSYLFIDNVTHDDEGDYTCQFTHAENGTNYI 199
Cdd:cd05757     2 RYKQKLPITKGGKITCPDLDDYKNenvLPPIQWYKDCKPLQGDkRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQYN 81

                          90
                  ....*....|.
gi 2497762006 200 VTATRSFTVEE 210
Cdd:cd05757    82 VTRTISLTVTE 92
TIR smart00255
Toll - interleukin 1 - resistance;
382-543 8.47e-31

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 117.04  E-value: 8.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  382 YDAYIIYPRVfrgsaagthsvEYFVHHTLPDVLENKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSK 461
Cdd:smart00255   2 YDVFISYSGK-----------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESE 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  462 EFAYEQEIALHSALIQNNSKVILIEMEPLGEASRLQVGDLQDSLQHLvkiqgTIKWREDHvadkqslSSKFWKHVRYQMP 541
Cdd:smart00255  71 WCLDELVAALENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKN-----YLKWPEDE-------KEQFWKKALYAVP 138


                   ..
gi 2497762006  542 VP 543
Cdd:smart00255 139 SK 140
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 33-97 1.34e-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: 66.68  E-value: 1.34e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  33 LENEALIVRCPQR-----GRSTYPVEWYYSDTNESIPTQKRNRIFVSRDRLKFLPARVEDSGIYACVIRS 97
Cdd:cd05756    13 LEGEPDVIKCPLFpnflaQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRN 82
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 33-316 8.14e-13

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 69.66  E-value: 8.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  33 LENEALIVRCPQ-----RGRSTYPVEWYY--SDTNESIPTQKRNRIFVsrdrlkfLPARVEDSGIYACVIRSPNLNKTGY 105
Cdd:PHA02785   39 LENEPVILPCPQintlsSGYNILDILWEKrgADNDRIIPIDNGSNMLI-------LNPTQSDSGIYICITKNETYCDMMS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 106 LNVTIHKKPPScNIpDYLMYSTVRGSDKNFKITCPTIDLY---NWTAPVQWfKNCKALQEPRFRAHR-SYLFIDNVTHDD 181
Cdd:PHA02785  112 LNLTIVSVSES-NI-DLISYPQIVNERSTGEMVCPNINAFiasNVNADIIW-SGHRRLRNKRLKQRTpGIITIEDVRKND 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 182 EGDYTCQFTHAENGTNYIVTATRSFTVEEKgfsMFPVITNPPynHTMEVEIGKPASIACSACFgKGSHFLADVLWQINkt 261
Cdd:PHA02785  189 AGYYTCVLKYIYGDKTYNVTRIVKLEVRDR---IIPPTMQLP--EGVVTSIGSNLTIACRVSL-RPPTTDADVFWISN-- 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 262 vvGNFGEARIQEEEGR----NESSSNDM-DCLTSVLRITGVTEKDLSlEYDCLALNLHGM 316
Cdd:PHA02785  261 --GMYYEEDDEDGDGRisvaNKIYTTDKrRVITSRLNINPVKEEDAT-TFTCMAFTIPSI 317
I-set pfam07679
Immunoglobulin I-set domain;
130-208 9.03e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 47.25  E-value: 9.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 130 GSDKNFKIT---CPTIDlynwtapVQWFKNCKALQE-PRFRAH----RSYLFIDNVTHDDEGDYTCQfthAEN--GTnyi 199
Cdd:pfam07679  15 GESARFTCTvtgTPDPE-------VSWFKDGQPLRSsDRFKVTyeggTYTLTISNVQPDDSGKYTCV---ATNsaGE--- 81


                  ....*....
gi 2497762006 200 VTATRSFTV 208
Cdd:pfam07679  82 AEASAELTV 90
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 48-208 1.33e-06

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 49.53  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  48 STYPVEWYYSDT---------NESIPTQKRNRIFVSRDRLKFLPARVEDSGIYACVIRSPNLNKTGYLNVTIhkkppscn 118
Cdd:PHA02826   61 TSYNVTWSKTDSlafvrdsgaRTKIKKITHNEIGDRSENLWIGNVINIDEGIYICTISSGNICEESTIRLTF-------- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 119 ipDYLMYSTVRGSDKNFKITCPTIDLYNWT---APVQWFKN-CKALQEPRF--RAHRSYLFIDNVTHDDEGDYTCQFTHA 192
Cdd:PHA02826  133 --DSGTINYQFNSGKDSKLHCYGTDGISSTfkdYTLTWYKNgNIVLYTDRIqlRNNNSTLVIKSATHDDSGIYTCNLRFN 210

                         170
                  ....*....|....*.
gi 2497762006 193 ENGTNYIVTATRSFTV 208
Cdd:PHA02826  211 KNSNNYNITKEYKVTI 226
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 27-110 2.49e-06

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: 45.57  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006   27 SKSSWGLENEALIVRCPQRGRSTYPVEWYYSDTNESIPtqkRNRIFVSRD----RLKFLPARVEDSGIYACVIRSPNLNK 102
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAE---SGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                   ....*...
gi 2497762006  103 TGYLNVTI 110
Cdd:smart00410  78 SSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 134-209 6.68e-06

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: 44.42  E-value: 6.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  134 NFKITCPTIDlyNWTAPVQWFKNC--KALQEPRFRAHRS----YLFIDNVTHDDEGDYTCQFthaengTNYIVTATRSFT 207
Cdd:smart00410  11 SVTLSCEASG--SPPPEVTWYKQGgkLLAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAA------TNSSGSASSGTT 82


                   ..
gi 2497762006  208 VE 209
Cdd:smart00410  83 LT 84
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 291-324 8.66e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 38.54  E-value: 8.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2497762006 291 VLRITGVTEKDlSLEYDCLALNLHGMIRHTIRLR 324
Cdd:cd05731    49 TLKIENVSEAD-SGEYQCTASNTMGSARHTISVT 81
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 25-109 6.03e-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: 36.67  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  25 EGSKSSWGLENEALIVRCPQRGRSTYP---VEWY--------------YSDTNESIPTQKRNRIFVSRDR----LKFLPA 83
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEAstsVYWYrqppgkgptfliayYSNGSEEGVKKGRFSGRGDPSNgdgsLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
gi 2497762006  84 RVEDSGIYACVIRSPNLNKTGY---LNVT 109
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKgtrLTVL 109
 
Name Accession Description Interval E-value
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 385-540 5.65e-50

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: 169.85  E-value: 5.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 385 YIIYPrvfrgSAAGTHSVEYFVHHTLPDVleNKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSKEFA 464
Cdd:pfam01582   1 YDVFL-----SFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGWCL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 465 YEQEIALHSALiQNNSKVILIEMEPLGEASRLQVGDLQDSLQHLVKI---QGTIKWREDHVA-------DKQSLSSKFWK 534
Cdd:pfam01582  74 DELVKILECAL-DLGQKVIPIFYEVDPSDVRKQTGSFGKAFKKHKKVlteEKVLKWRGALNEvaniwhsKSVSDESKFWK 152


                  ....*.
gi 2497762006 535 HVRYQM 540
Cdd:pfam01582 153 KIAYDI 158
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 124-210 9.76e-35

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: 125.90  E-value: 9.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 124 MYSTVRGSDKNFKITCPTIDLYNW---TAPVQWFKNCKALQEP-RFRAHRSYLFIDNVTHDDEGDYTCQFTHAENGTNYI 199
Cdd:cd05757     2 RYKQKLPITKGGKITCPDLDDYKNenvLPPIQWYKDCKPLQGDkRFIPKGSKLLIQNVTEEDAGNYTCKFTYTHNGKQYN 81

                          90
                  ....*....|.
gi 2497762006 200 VTATRSFTVEE 210
Cdd:cd05757    82 VTRTISLTVTE 92
TIR smart00255
Toll - interleukin 1 - resistance;
382-543 8.47e-31

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 117.04  E-value: 8.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  382 YDAYIIYPRVfrgsaagthsvEYFVHHTLPDVLENKCGYKLCIYGRDLLPGQDAATVVESSIQNSRRQVFVLAPHMMHSK 461
Cdd:smart00255   2 YDVFISYSGK-----------EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYAESE 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  462 EFAYEQEIALHSALIQNNSKVILIEMEPLGEASRLQVGDLQDSLQHLvkiqgTIKWREDHvadkqslSSKFWKHVRYQMP 541
Cdd:smart00255  71 WCLDELVAALENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKN-----YLKWPEDE-------KEQFWKKALYAVP 138


                   ..
gi 2497762006  542 VP 543
Cdd:smart00255 139 SK 140
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 136-210 5.87e-14

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: 67.49  E-value: 5.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 136 KITCPTIDLY----NWTAPVQWFKNCKAL--QEPRFRAHRSYLFIDNVTHDDEGDYTCQFTHAENGTNYIVTATRSFTVE 209
Cdd:cd20994    14 RIVCPHLDFFkdenNNLPKVQWYKDCKPLllDDKRFAGLESDLLIFNVTVQDQGNYTCHTSYTYMGKQYNISRTISLIVL 93


                  .
gi 2497762006 210 E 210
Cdd:cd20994    94 E 94
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 33-97 1.34e-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: 66.68  E-value: 1.34e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  33 LENEALIVRCPQR-----GRSTYPVEWYYSDTNESIPTQKRNRIFVSRDRLKFLPARVEDSGIYACVIRS 97
Cdd:cd05756    13 LEGEPDVIKCPLFpnflaQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYCVVRN 82
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 33-316 8.14e-13

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 69.66  E-value: 8.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  33 LENEALIVRCPQ-----RGRSTYPVEWYY--SDTNESIPTQKRNRIFVsrdrlkfLPARVEDSGIYACVIRSPNLNKTGY 105
Cdd:PHA02785   39 LENEPVILPCPQintlsSGYNILDILWEKrgADNDRIIPIDNGSNMLI-------LNPTQSDSGIYICITKNETYCDMMS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 106 LNVTIHKKPPScNIpDYLMYSTVRGSDKNFKITCPTIDLY---NWTAPVQWfKNCKALQEPRFRAHR-SYLFIDNVTHDD 181
Cdd:PHA02785  112 LNLTIVSVSES-NI-DLISYPQIVNERSTGEMVCPNINAFiasNVNADIIW-SGHRRLRNKRLKQRTpGIITIEDVRKND 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 182 EGDYTCQFTHAENGTNYIVTATRSFTVEEKgfsMFPVITNPPynHTMEVEIGKPASIACSACFgKGSHFLADVLWQINkt 261
Cdd:PHA02785  189 AGYYTCVLKYIYGDKTYNVTRIVKLEVRDR---IIPPTMQLP--EGVVTSIGSNLTIACRVSL-RPPTTDADVFWISN-- 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 262 vvGNFGEARIQEEEGR----NESSSNDM-DCLTSVLRITGVTEKDLSlEYDCLALNLHGM 316
Cdd:PHA02785  261 --GMYYEEDDEDGDGRisvaNKIYTTDKrRVITSRLNINPVKEEDAT-TFTCMAFTIPSI 317
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 34-97 4.51e-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: 56.53  E-value: 4.51e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2497762006  34 ENEALIVRCPQRGRSTY-PVEWYYSDTNESIPTQKRNRIFVSRDRLKFLPARVEDSGIYACVIRS 97
Cdd:cd20991    13 ANEIDVRSCPLNPNESKgTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRN 77
I-set pfam07679
Immunoglobulin I-set domain;
130-208 9.03e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 47.25  E-value: 9.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 130 GSDKNFKIT---CPTIDlynwtapVQWFKNCKALQE-PRFRAH----RSYLFIDNVTHDDEGDYTCQfthAEN--GTnyi 199
Cdd:pfam07679  15 GESARFTCTvtgTPDPE-------VSWFKDGQPLRSsDRFKVTyeggTYTLTISNVQPDDSGKYTCV---ATNsaGE--- 81


                  ....*....
gi 2497762006 200 VTATRSFTV 208
Cdd:pfam07679  82 AEASAELTV 90
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 48-208 1.33e-06

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 49.53  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  48 STYPVEWYYSDT---------NESIPTQKRNRIFVSRDRLKFLPARVEDSGIYACVIRSPNLNKTGYLNVTIhkkppscn 118
Cdd:PHA02826   61 TSYNVTWSKTDSlafvrdsgaRTKIKKITHNEIGDRSENLWIGNVINIDEGIYICTISSGNICEESTIRLTF-------- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006 119 ipDYLMYSTVRGSDKNFKITCPTIDLYNWT---APVQWFKN-CKALQEPRF--RAHRSYLFIDNVTHDDEGDYTCQFTHA 192
Cdd:PHA02826  133 --DSGTINYQFNSGKDSKLHCYGTDGISSTfkdYTLTWYKNgNIVLYTDRIqlRNNNSTLVIKSATHDDSGIYTCNLRFN 210

                         170
                  ....*....|....*.
gi 2497762006 193 ENGTNYIVTATRSFTV 208
Cdd:PHA02826  211 KNSNNYNITKEYKVTI 226
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 27-110 2.49e-06

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: 45.57  E-value: 2.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006   27 SKSSWGLENEALIVRCPQRGRSTYPVEWYYSDTNESIPtqkRNRIFVSRD----RLKFLPARVEDSGIYACVIRSPNLNK 102
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAE---SGRFSVSRSgstsTLTISNVTPEDSGTYTCAATNSSGSA 77


                   ....*...
gi 2497762006  103 TGYLNVTI 110
Cdd:smart00410  78 SSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 134-209 6.68e-06

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: 44.42  E-value: 6.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  134 NFKITCPTIDlyNWTAPVQWFKNC--KALQEPRFRAHRS----YLFIDNVTHDDEGDYTCQFthaengTNYIVTATRSFT 207
Cdd:smart00410  11 SVTLSCEASG--SPPPEVTWYKQGgkLLAESGRFSVSRSgstsTLTISNVTPEDSGTYTCAA------TNSSGSASSGTT 82


                   ..
gi 2497762006  208 VE 209
Cdd:smart00410  83 LT 84
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 151-203 2.17e-05

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 42.70  E-value: 2.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2497762006 151 VQWFKNCKALQ-----EPRFRAHRSYLFIDNVTHDDEGDYTCQfthAENGTNYIVTAT 203
Cdd:cd00096    15 ITWYKNGKPLPpssrdSRRSELGNGTLTISNVTLEDSGTYTCV---ASNSAGGSASAS 69
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 151-209 1.10e-04

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: 41.22  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2497762006 151 VQWFKNCKALQEPRFRA--HRSYLFIDNVTHDDEGDYTCqfthaeNGTNYIVTATRSFTVE 209
Cdd:cd20978    33 ITWLHNGKPLQGPMERAtvEDGTLTIINVQPEDTGYYGC------VATNEIGDIYTETLLH 87
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 136-208 1.23e-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: 41.04  E-value: 1.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2497762006 136 KITCPTIDLY---NWTAPVQWFKNCKALQEPRFRAHR-SYLFIDNVTHDDEGDYTCQFTHAENGTNYIVTATRSFTV 208
Cdd:cd20993    15 TITCPDLDGIkppSVSPTVTWYHECNAFGNFNDRVPKgDKLVIHVMLEHYQGNYTCVVTYETKGRTIKLTRTVNVKV 91
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
 28-110 1.39e-04

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: 40.96  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  28 KSSWGLENEALIVRCPQRGRSTYPVEWYYSDTNE---------SIPTQKRNrifvsrDRLKFLPARVEDSGIYACVIRSP 98
Cdd:cd05750     7 KSQTVQEGSKLVLKCEATSENPSPRYRWFKDGKElnrkrpkniKIRNKKKN------SELQINKAKLEDSGEYTCVVENI 80

                          90
                  ....*....|..
gi 2497762006  99 NLNKTGYLNVTI 110
Cdd:cd05750    81 LGKDTVTGNVTV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 38-98 2.40e-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: 39.62  E-value: 2.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2497762006  38 LIVRCPQRGRSTYPVEWYYSDTNESIPTQKRNRIFVSRDRLKFLPARVEDSGIYACVIRSP 98
Cdd:cd00096     1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNS 61
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 133-192 3.92e-04

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: 39.49  E-value: 3.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2497762006 133 KNFKITCPTIDLYnwTAP-VQWFKNCKALQEPRFRAHRSY------LFIDNVTHDDEGDYTCQFTHA 192
Cdd:pfam00047  12 DSATLTCSASTGS--PGPdVTWSKEGGTLIESLKVKHDNGrttqssLLISNVTKEDAGTYTCVVNNP 76
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 151-194 6.63e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.70  E-value: 6.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2497762006 151 VQWFKNCKALQEPRFRAHR-----SYLFIDNVTHDDEGDYTCQfthAEN 194
Cdd:pfam13927  33 ITWYKNGEPISSGSTRSRSlsgsnSTLTISNVTRSDAGTYTCV---ASN 78
IgC2_CEACAM5-like cd20948
Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell ...
 126-197 8.14e-04

Fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains; member of the C2-set IgSF domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain of the carcinoembryonic antigen (CEA) related cell adhesion molecule 5 (CEACAM5) and similar domains. 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. Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), also known as CD66e (Cluster of Differentiation 66e), is a cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression. Diseases associated with CEACAM5 include lung cancer and rectum cancer. 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' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409540  Cd Length: 76  Bit Score: 38.25  E-value: 8.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2497762006 126 STVRGSDKNFKITCPTIDlyNWTAPVQWFKNckalqePRFRAHRSYLFIDNVTHDDEGDYTCQFTHAENGTN 197
Cdd:cd20948     4 DTYYLSGENLNLSCHAAS--NPPAQYSWTIN------GTFQTSSQELFLPAITENNEGTYTCSAHNSLTGKN 67
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
 291-324 8.66e-04

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394 [Multi-domain]  Cd Length: 83  Bit Score: 38.54  E-value: 8.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2497762006 291 VLRITGVTEKDlSLEYDCLALNLHGMIRHTIRLR 324
Cdd:cd05731    49 TLKIENVSEAD-SGEYQCTASNTMGSARHTISVT 81
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 25-109 6.03e-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: 36.67  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2497762006  25 EGSKSSWGLENEALIVRCPQRGRSTYP---VEWY--------------YSDTNESIPTQKRNRIFVSRDR----LKFLPA 83
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEAstsVYWYrqppgkgptfliayYSNGSEEGVKKGRFSGRGDPSNgdgsLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
gi 2497762006  84 RVEDSGIYACVIRSPNLNKTGY---LNVT 109
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKgtrLTVL 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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