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Conserved domains on  [gi|578804865|ref|XP_006712799|]
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interleukin-1 receptor type 2 isoform X2 [Homo sapiens]

Protein Classification

immunoglobulin domain-containing protein; immunoglobulin domain-containing family protein( domain architecture ID 10861562)

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| immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
161-255 2.06e-54

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


:

Pssm-ID: 409478  Cd Length: 95  Bit Score: 175.72  E-value: 2.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 161 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEG 240
Cdd:cd05897    1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80
                         90
                 ....*....|....*
gi 578804865 241 QQYNITRSIELRIKK 255
Cdd:cd05897   81 KKYNITRSIELRIVK 95
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
54-151 7.85e-46

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: 153.35  E-value: 7.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  54 RFRGRHYKREFRLEGEPVALRCPQVPYWLwaSVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVC 133
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL--AQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYC 78
                         90
                 ....*....|....*...
gi 578804865 134 TTRNASYCDKMSIELRVF 151
Cdd:cd05756   79 VVRNSTYCSKVSISLEVV 96
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
266-366 6.10e-10

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: 55.66  E-value: 6.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  266 SPLKTISASLGSRLTIPCKVFlgTGTPLTTMLWWTANDTHIESAypggRVTEGPRQEYSENnenyievpLIFDPVTREDL 345
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIESL----KVKHDNGRTTQSS--------LLISNVTKEDA 66
                          90       100
                  ....*....|....*....|.
gi 578804865  346 HmDFKCVVHNTLSFQTLRTTV 366
Cdd:pfam00047  67 G-TYTCVVNNPGGSATLSTSL 86
 
Name Accession Description Interval E-value
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
161-255 2.06e-54

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409478  Cd Length: 95  Bit Score: 175.72  E-value: 2.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 161 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEG 240
Cdd:cd05897    1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80
                         90
                 ....*....|....*
gi 578804865 241 QQYNITRSIELRIKK 255
Cdd:cd05897   81 KKYNITRSIELRIVK 95
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
54-151 7.85e-46

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: 153.35  E-value: 7.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  54 RFRGRHYKREFRLEGEPVALRCPQVPYWLwaSVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVC 133
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL--AQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYC 78
                         90
                 ....*....|....*...
gi 578804865 134 TTRNASYCDKMSIELRVF 151
Cdd:cd05756   79 VVRNSTYCSKVSISLEVV 96
PHA02785 PHA02785
IL-beta-binding protein; Provisional
31-352 1.34e-43

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 155.17  E-value: 1.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  31 VLVMGVSAFTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPywLWASVSPRINLTWHKN--DSARTVPGEEE 108
Cdd:PHA02785   4 LPVIFLPIFFYSSFVQTFNAPECIDKGQYFASFMELENEPVILPCPQIN--TLSSGYNILDILWEKRgaDNDRIIPIDNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 109 TRMwaqdgaLWLLPAlQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKT 188
Cdd:PHA02785  82 SNM------LILNPT-QSDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 189 DVKIQWYKDSLLLDKDnekfLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKkeeTIPVIISPL 268
Cdd:PHA02785 155 NADIIWSGHRRLRNKR----LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDR---IIPPTMQLP 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 269 KTISASLGSRLTIPCKVFLGTGTPLTTMLWWTANDTHIESAYPG-GRVTEGPRQeYSENNENYIEVPLIFDPVTREDLhM 347
Cdd:PHA02785 228 EGVVTSIGSNLTIACRVSLRPPTTDADVFWISNGMYYEEDDEDGdGRISVANKI-YTTDKRRVITSRLNINPVKEEDA-T 305

                 ....*
gi 578804865 348 DFKCV 352
Cdd:PHA02785 306 TFTCM 310
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
266-366 6.10e-10

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: 55.66  E-value: 6.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  266 SPLKTISASLGSRLTIPCKVFlgTGTPLTTMLWWTANDTHIESAypggRVTEGPRQEYSENnenyievpLIFDPVTREDL 345
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIESL----KVKHDNGRTTQSS--------LLISNVTKEDA 66
                          90       100
                  ....*....|....*....|.
gi 578804865  346 HmDFKCVVHNTLSFQTLRTTV 366
Cdd:pfam00047  67 G-TYTCVVNNPGGSATLSTSL 86
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
67-150 7.43e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 7.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865    67 EGEPVALRCPqvpywlwASVSPRINLTWHKNDSAR-TVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMS 145
Cdd:smart00410   8 EGESVTLSCE-------ASGSPPPEVTWYKQGGKLlAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 578804865   146 IELRV 150
Cdd:smart00410  81 TTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
66-137 8.23e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 40.63  E-value: 8.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804865   66 LEGEPVALRCpqvpywlWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 137
Cdd:pfam13927  14 REGETVTLTC-------EATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
174-253 3.47e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.41  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865   174 VLVCPdlsefTRDKTDVKIQWYKD--SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHegqqYNITRSIEL 251
Cdd:smart00410  13 TLSCE-----ASGSPPPEVTWYKQggKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS----GSASSGTTL 83

                   ..
gi 578804865   252 RI 253
Cdd:smart00410  84 TV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
191-233 2.50e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.77  E-value: 2.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578804865  191 KIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCV 233
Cdd:pfam13927  32 TITWYKNgEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
PHA02633 PHA02633
hypothetical protein; Provisional
120-150 8.26e-03

hypothetical protein; Provisional


Pssm-ID: 165016  Cd Length: 63  Bit Score: 34.57  E-value: 8.26e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 578804865 120 LLPALQEDSGTYVCTTRNASYCDKMSIELRV 150
Cdd:PHA02633  22 ILNPTQSDSGIYMCITKNETYSDMMKFDLCI 52
 
Name Accession Description Interval E-value
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
161-255 2.06e-54

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds the IL-1 receptor, type II (IL1R2) represented in this group. Mature IL1R2 consists of three IG-like domains, a transmembrane domain, and a short cytoplasmic domain. It lacks the large cytoplasmic domain of mature IL1R1 and does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta.


Pssm-ID: 409478  Cd Length: 95  Bit Score: 175.72  E-value: 2.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 161 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEG 240
Cdd:cd05897    1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80
                         90
                 ....*....|....*
gi 578804865 241 QQYNITRSIELRIKK 255
Cdd:cd05897   81 KKYNITRSIELRIVK 95
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
54-151 7.85e-46

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: 153.35  E-value: 7.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  54 RFRGRHYKREFRLEGEPVALRCPQVPYWLwaSVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVC 133
Cdd:cd05756    1 DEWGEDIKILVVLEGEPDVIKCPLFPNFL--AQSAGLNLTWYKNDSETPISFEPDSRIHQEKDKLWFVPALLEDSGNYYC 78
                         90
                 ....*....|....*...
gi 578804865 134 TTRNASYCDKMSIELRVF 151
Cdd:cd05756   79 VVRNSTYCSKVSISLEVV 96
PHA02785 PHA02785
IL-beta-binding protein; Provisional
31-352 1.34e-43

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 155.17  E-value: 1.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  31 VLVMGVSAFTLQPAAHTGAARSCRFRGRHYKREFRLEGEPVALRCPQVPywLWASVSPRINLTWHKN--DSARTVPGEEE 108
Cdd:PHA02785   4 LPVIFLPIFFYSSFVQTFNAPECIDKGQYFASFMELENEPVILPCPQIN--TLSSGYNILDILWEKRgaDNDRIIPIDNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 109 TRMwaqdgaLWLLPAlQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFLPFISYPQILTLSTSGVLVCPDLSEFTRDKT 188
Cdd:PHA02785  82 SNM------LILNPT-QSDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 189 DVKIQWYKDSLLLDKDnekfLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRIKKKkeeTIPVIISPL 268
Cdd:PHA02785 155 NADIIWSGHRRLRNKR----LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDR---IIPPTMQLP 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 269 KTISASLGSRLTIPCKVFLGTGTPLTTMLWWTANDTHIESAYPG-GRVTEGPRQeYSENNENYIEVPLIFDPVTREDLhM 347
Cdd:PHA02785 228 EGVVTSIGSNLTIACRVSLRPPTTDADVFWISNGMYYEEDDEDGdGRISVANKI-YTTDKRRVITSRLNINPVKEEDA-T 305

                 ....*
gi 578804865 348 DFKCV 352
Cdd:PHA02785 306 TFTCM 310
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
161-254 1.79e-32

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: 118.20  E-value: 1.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 161 ISYPQILTLSTSGVLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNeKFLSVRgtTHLLVHDVALEDAGYYRCVLTFAHEG 240
Cdd:cd05757    1 PRYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPLQGDK-RFIPKG--SKLLIQNVTEEDAGNYTCKFTYTHNG 77
                         90
                 ....*....|....
gi 578804865 241 QQYNITRSIELRIK 254
Cdd:cd05757   78 KQYNVTRTISLTVT 91
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
163-254 3.15e-21

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: 87.52  E-value: 3.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 163 YPQILTLSTSGVLVCPDLsEFTRDKTDV--KIQWYKDSLLLDKDNEKFLSVRGTthLLVHDVALEDAGYYRCVLTFAHEG 240
Cdd:cd20994    3 YKQKVPFTSGGRIVCPHL-DFFKDENNNlpKVQWYKDCKPLLLDDKRFAGLESD--LLIFNVTVQDQGNYTCHTSYTYMG 79
                         90
                 ....*....|....
gi 578804865 241 QQYNITRSIELRIK 254
Cdd:cd20994   80 KQYNISRTISLIVL 93
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
52-253 8.17e-13

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 67.63  E-value: 8.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  52 SCRFRGRHYKREFRLEGEPVALRCPQVPY----WLWASVSPRINLTWHKNDS--------ART-----VPGEEETRmwaq 114
Cdd:PHA02826  21 YCKYRGGDLTPVYAKFGDPMVLLCTGKHYkksiFFDKTFITSYNVTWSKTDSlafvrdsgARTkikkiTHNEIGDR---- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 115 DGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRVFENTDAFlPFISypqiltlSTSGVLVCPDLSEFTRDKTDVKIQW 194
Cdd:PHA02826  97 SENLWIGNVINIDEGIYICTISSGNICEESTIRLTFDSGTINY-QFNS-------GKDSKLHCYGTDGISSTFKDYTLTW 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578804865 195 YKDSLLLDKDnEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQYNITRSIELRI 253
Cdd:PHA02826 169 YKNGNIVLYT-DRIQLRNNNSTLVIKSATHDDSGIYTCNLRFNKNSNNYNITKEYKVTI 226
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
75-150 5.17e-12

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: 61.54  E-value: 5.17e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804865  75 CPQVPYwlwasvSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMSIELRV 150
Cdd:cd20991   21 CPLNPN------ESKGTITWYKNDSKTPISMEQDSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKITAKF 90
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
60-150 3.90e-10

First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1), and similar domains; The members here are composed of the first immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory protein-like 1 (IL1RAPL-1). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three Ig-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. IL1RAPL is encoded by a gene on the X-chromosome, this gene is wholly or partially deleted in multiple cases of non-syndromic intellectual disability. This group also contains IL1RAPL-2 which is also encoded by a gene on the X-chromosome and is a candidate for another non-syndromic intellectual disability loci.


Pssm-ID: 409477  Cd Length: 105  Bit Score: 56.88  E-value: 3.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  60 YKREFRLEGEPVALRCPQVPYWLWASV----SPRINLTWHKNDSARTVpgEE-----ETRMWAQDGALWLLPALQEDSGT 130
Cdd:cd05896    7 LKKYMVLAGEPVRIKCALFYGYIRTNYsmaqSAGLSLMWYKSSGPGDF--EEpiifdGVRMSKEEDSIWFRPAELQDSGL 84
                         90       100
                 ....*....|....*....|
gi 578804865 131 YVCTTRNASYCDKMSIELRV 150
Cdd:cd05896   85 YTCVLRNSTYCMKVSMSLTV 104
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
266-366 6.10e-10

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: 55.66  E-value: 6.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  266 SPLKTISASLGSRLTIPCKVFlgTGTPLTTMLWWTANDTHIESAypggRVTEGPRQEYSENnenyievpLIFDPVTREDL 345
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIESL----KVKHDNGRTTQSS--------LLISNVTKEDA 66
                          90       100
                  ....*....|....*....|.
gi 578804865  346 HmDFKCVVHNTLSFQTLRTTV 366
Cdd:pfam00047  67 G-TYTCVVNNPGGSATLSTSL 86
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
66-150 1.04e-08

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


Pssm-ID: 409584  Cd Length: 108  Bit Score: 52.62  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  66 LEGEPVALRCPQVPYWL---WASV-SPRINLTWHKNDSARTVpgEE-------ETRMWAQDGALWLLPALQEDSGTYVCT 134
Cdd:cd20992   14 FEGEPARIKCPLFEHFLkynYSTAhSAGLTLIWYWTRQDRDL--EEpinfrlpDNRISKEKDVLWFRPTLLNDTGNYTCM 91
                         90
                 ....*....|....*.
gi 578804865 135 TRNASYCDKMSIELRV 150
Cdd:cd20992   92 LRNTTYCSKVAFPLEV 107
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
67-150 7.43e-08

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 49.81  E-value: 7.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865    67 EGEPVALRCPqvpywlwASVSPRINLTWHKNDSAR-TVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMS 145
Cdd:smart00410   8 EGESVTLSCE-------ASGSPPPEVTWYKQGGKLlAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSG 80

                   ....*
gi 578804865   146 IELRV 150
Cdd:smart00410  81 TTLTV 85
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
164-253 4.74e-06

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: 44.89  E-value: 4.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 164 PQILTLSTSG-VLVCPDLSEFTRDKTDVKIQWYKDSLLLDKDNEKflsVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQ 242
Cdd:cd20993    4 PVIAYIEYGGrTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDR---VPKGDKLVIHVMLEHYQGNYTCVVTYETKGRT 80
                         90
                 ....*....|.
gi 578804865 243 YNITRSIELRI 253
Cdd:cd20993   81 IKLTRTVNVKV 91
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
54-150 5.01e-06

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. 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 hemolymph protein hemolin, 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: 409561  Cd Length: 92  Bit Score: 44.69  E-value: 5.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  54 RFRGRHYKREFRLEGEPVALRC------PQVPYWLWASVSPrinLTWHKNDSARTVPgeeetrmwaqDGALWLLPALQED 127
Cdd:cd20969    3 AIRDRKAQQVFVDEGHTVQFVCradgdpPPAILWLSPRKHL---VSAKSNGRLTVFP----------DGTLEVRYAQVQD 69
                         90       100
                 ....*....|....*....|...
gi 578804865 128 SGTYVCTTRNASYCDKMSIELRV 150
Cdd:cd20969   70 NGTYLCIAANAGGNDSMPAHLHV 92
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
174-242 7.49e-06

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.47  E-value: 7.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865 174 VLVCPdlsefTRDKTDVKIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHEGQQ 242
Cdd:cd00096    2 TLTCS-----ASGNPPPTITWYKNgKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
262-355 1.86e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  262 PVIISPLKTISASLGSRLTIPCKVflgTGTPLTTMLWWtandthiesaYPGGRVTEGPRQEYSENNENYIevpLIFDPVT 341
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEA---TGSPPPTITWY----------KNGEPISSGSTRSRSLSGSNST---LTISNVT 65
                          90
                  ....*....|....
gi 578804865  342 REDlHMDFKCVVHN 355
Cdd:pfam13927  66 RSD-AGTYTCVASN 78
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
71-137 2.00e-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: 42.32  E-value: 2.00e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578804865  71 VALRCPqvpywlwASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 137
Cdd:cd00096    1 VTLTCS-------ASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASN 60
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
66-137 8.23e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 40.63  E-value: 8.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578804865   66 LEGEPVALRCpqvpywlWASVSPRINLTWHKNDSARTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 137
Cdd:pfam13927  14 REGETVTLTC-------EATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
65-137 3.03e-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: 39.30  E-value: 3.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804865  65 RLEGEPVALRCPqvpywlwASVSPRINLTWHKNdsARTVPGEEETRMWaQDGALWLLPALQEDSGTYVCTTRN 137
Cdd:cd20978   13 VKGGQDVTLPCQ-------VTGVPQPKITWLHN--GKPLQGPMERATV-EDGTLTIINVQPEDTGYYGCVATN 75
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
174-253 3.47e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.41  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865   174 VLVCPdlsefTRDKTDVKIQWYKD--SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCVLTFAHegqqYNITRSIEL 251
Cdd:smart00410  13 TLSCE-----ASGSPPPEVTWYKQggKLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS----GSASSGTTL 83

                   ..
gi 578804865   252 RI 253
Cdd:smart00410  84 TV 85
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
66-150 5.91e-04

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. 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 hemolymph protein hemolin, 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: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 38.77  E-value: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  66 LEGEPVALRCPqvpywlwASVSPRINLTWHKNDSARTVPGEEETrMWAQDGALWLLPALQEDSGTYVCTTRNASYCDKMS 145
Cdd:cd20976   14 VEGQDFVAQCS-------ARGKPVPRITWIRNAQPLQYAADRST-CEAGVGELHIQDVLPEDHGTYTCLAKNAAGQVSCS 85

                 ....*
gi 578804865 146 IELRV 150
Cdd:cd20976   86 AWVTV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
66-139 8.55e-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: 38.33  E-value: 8.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578804865   66 LEGEPVALRCPQVPywlwasVSPRINLTWHKNDSaRTVPGEEETRMWAQDGA--LWLLPALQEDSGTYVCTTRNAS 139
Cdd:pfam00047   9 LEGDSATLTCSAST------GSPGPDVTWSKEGG-TLIESLKVKHDNGRTTQssLLISNVTKEDAGTYTCVVNNPG 77
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
67-141 9.13e-04

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 37.76  E-value: 9.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578804865   67 EGEPVALRCPqvpywlwASVSPRINLTWHKNDSArtvpgeeetrmWAQDGALWLLPALQEDSGTYVCTTRNASYC 141
Cdd:pfam13895  13 EGEPVTLTCS-------APGNPPPSYTWYKDGSA-----------ISSSPNFFTLSVSAEDSGTYTCVARNGRGG 69
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
66-137 1.36e-03

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. 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 hemolymph protein hemolin, 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: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 37.87  E-value: 1.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804865  66 LEGEPVALRCPqvpywlwASVSPRINLTWHKNDSARTVPGE-EETRMWAQDgaLWLLPALQEDSGTYVCTTRN 137
Cdd:cd20970   15 REGENATFMCR-------AEGSPEPEISWTRNGNLIIEFNTrYIVRENGTT--LTIRNIRRSDMGIYLCIASN 78
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
191-233 2.50e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.77  E-value: 2.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578804865  191 KIQWYKD-SLLLDKDNEKFLSVRGTTHLLVHDVALEDAGYYRCV 233
Cdd:pfam13927  32 TITWYKNgEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCV 75
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
66-137 3.40e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. 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: 409389 [Multi-domain]  Cd Length: 87  Bit Score: 36.61  E-value: 3.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578804865  66 LEGEPVALRC-PQVPYwlwasvsPRINLTWHKNDSarTVPGEEETRMWAQDGALWLLPALQEDSGTYVCTTRN 137
Cdd:cd05724   10 AVGEMAVLECsPPRGH-------PEPTVSWRKDGQ--PLNLDNERVRIVDDGNLLIAEARKSDEGTYKCVATN 73
PHA02633 PHA02633
hypothetical protein; Provisional
120-150 8.26e-03

hypothetical protein; Provisional


Pssm-ID: 165016  Cd Length: 63  Bit Score: 34.57  E-value: 8.26e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 578804865 120 LLPALQEDSGTYVCTTRNASYCDKMSIELRV 150
Cdd:PHA02633  22 ILNPTQSDSGIYMCITKNETYSDMMKFDLCI 52
I-set pfam07679
Immunoglobulin I-set domain;
262-355 8.76e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 35.31  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578804865  262 PVIISPLKTISASLGSRLTIPCKVFlGTGTPLTTmlwWTANDTHIesaypggrvTEGPRQEYSENNENYIevpLIFDPVT 341
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTVT-GTPDPEVS---WFKDGQPL---------RSSDRFKVTYEGGTYT---LTISNVQ 64
                          90
                  ....*....|....
gi 578804865  342 REDLHmDFKCVVHN 355
Cdd:pfam07679  65 PDDSG-KYTCVATN 77
 
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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