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Conserved domains on  [gi|1907067423|ref|XP_036018115|]
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interleukin-1 receptor type 2 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHA02785 super family cl31505
IL-beta-binding protein; Provisional
36-364 1.41e-43

IL-beta-binding protein; Provisional


The actual alignment was detected with superfamily member PHA02785:

Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 154.79  E-value: 1.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  36 TVHGDNCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFLtWSK--LDSSQLIPRDeprmwvKGNILWILPAVQQ 113
Cdd:PHA02785   20 TFNAPECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDIL-WEKrgADNDRIIPID------NGSNMLILNPTQS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 114 DSGTYICTFRNASHCEQMSVELKVFKNTEASLPHVSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGnk 193
Cdd:PHA02785   93 DSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGHRRLRNKR-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 194 efLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRVKGTTtepIPVIISPLETIPASLGSRLIVPCKVF 273
Cdd:PHA02785  171 --LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDRI---IPPTMQLPEGVVTSIGSNLTIACRVS 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 274 LGTGTsSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSENDENYVEVS-LIFDPVTREDLhTDFKCVAsnprssqslhTT 352
Cdd:PHA02785  246 LRPPT-TDADVFWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEEDA-TTFTCMA----------FT 313
                         330
                  ....*....|..
gi 1907067423 353 VKEVSSTFSWSI 364
Cdd:PHA02785  314 IPSISKTVTISI 325
 
Name Accession Description Interval E-value
PHA02785 PHA02785
IL-beta-binding protein; Provisional
36-364 1.41e-43

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 154.79  E-value: 1.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  36 TVHGDNCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFLtWSK--LDSSQLIPRDeprmwvKGNILWILPAVQQ 113
Cdd:PHA02785   20 TFNAPECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDIL-WEKrgADNDRIIPID------NGSNMLILNPTQS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 114 DSGTYICTFRNASHCEQMSVELKVFKNTEASLPHVSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGnk 193
Cdd:PHA02785   93 DSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGHRRLRNKR-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 194 efLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRVKGTTtepIPVIISPLETIPASLGSRLIVPCKVF 273
Cdd:PHA02785  171 --LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDRI---IPPTMQLPEGVVTSIGSNLTIACRVS 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 274 LGTGTsSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSENDENYVEVS-LIFDPVTREDLhTDFKCVAsnprssqslhTT 352
Cdd:PHA02785  246 LRPPT-TDADVFWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEEDA-TTFTCMA----------FT 313
                         330
                  ....*....|..
gi 1907067423 353 VKEVSSTFSWSI 364
Cdd:PHA02785  314 IPSISKTVTISI 325
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
148-242 2.89e-33

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: 119.86  E-value: 2.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 148 VSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNG 227
Cdd:cd05897     1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80
                          90
                  ....*....|....*
gi 1907067423 228 QEYNITRNIELRVKG 242
Cdd:cd05897    81 KKYNITRSIELRIVK 95
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
50-137 3.53e-07

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: 47.50  E-value: 3.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423   50 KSELRLEGEPVVLRCPLAPHSDISssshsfLTWSKLDSSQLIPRDEPRMWVKGNI--LWILPAVQQDSGTYICTFRNASH 127
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPE------VTWYKQGGKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSG 75
                           90
                   ....*....|
gi 1907067423  128 CEQMSVELKV 137
Cdd:smart00410  76 SASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
249-342 2.29e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.17  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 249 PVIISPLETIPASLGSRLIVPCKVflgTGTSSNTIVWwlanstfisaaYPRGRVTEGLHHQYSENDENYveVSLIFDPVT 328
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEA---TGSPPPTITW-----------YKNGEPISSGSTRSRSLSGSN--STLTISNVT 65
                          90
                  ....*....|....
gi 1907067423 329 REDlHTDFKCVASN 342
Cdd:pfam13927  66 RSD-AGTYTCVASN 78
 
Name Accession Description Interval E-value
PHA02785 PHA02785
IL-beta-binding protein; Provisional
36-364 1.41e-43

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 154.79  E-value: 1.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  36 TVHGDNCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFLtWSK--LDSSQLIPRDeprmwvKGNILWILPAVQQ 113
Cdd:PHA02785   20 TFNAPECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDIL-WEKrgADNDRIIPID------NGSNMLILNPTQS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 114 DSGTYICTFRNASHCEQMSVELKVFKNTEASLPHVSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGnk 193
Cdd:PHA02785   93 DSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGHRRLRNKR-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 194 efLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRVKGTTtepIPVIISPLETIPASLGSRLIVPCKVF 273
Cdd:PHA02785  171 --LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDRI---IPPTMQLPEGVVTSIGSNLTIACRVS 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 274 LGTGTsSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSENDENYVEVS-LIFDPVTREDLhTDFKCVAsnprssqslhTT 352
Cdd:PHA02785  246 LRPPT-TDADVFWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEEDA-TTFTCMA----------FT 313
                         330
                  ....*....|..
gi 1907067423 353 VKEVSSTFSWSI 364
Cdd:PHA02785  314 IPSISKTVTISI 325
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
148-242 2.89e-33

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: 119.86  E-value: 2.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 148 VSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNG 227
Cdd:cd05897     1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80
                          90
                  ....*....|....*
gi 1907067423 228 QEYNITRNIELRVKG 242
Cdd:cd05897    81 KKYNITRSIELRIVK 95
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
44-138 1.01e-26

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: 102.50  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  44 FRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSfLTWSKLDSSQLIPRD-EPRMWVKGNILWILPAVQQDSGTYICTF 122
Cdd:cd05756     2 EWGEDIKILVVLEGEPDVIKCPLFPNFLAQSAGLN-LTWYKNDSETPISFEpDSRIHQEKDKLWFVPALLEDSGNYYCVV 80
                          90
                  ....*....|....*.
gi 1907067423 123 RNASHCEQMSVELKVF 138
Cdd:cd05756    81 RNSTYCSKVSISLEVV 96
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
149-242 5.12e-26

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: 100.48  E-value: 5.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 149 SYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLdKGNKEFLSAGDptRLLISNTSMDDAGYYRCVMTFTYNGQ 228
Cdd:cd05757     2 RYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPL-QGDKRFIPKGS--KLLIQNVTEEDAGNYTCKFTYTHNGK 78
                          90
                  ....*....|....
gi 1907067423 229 EYNITRNIELRVKG 242
Cdd:cd05757    79 QYNVTRTISLTVTE 92
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
41-240 5.10e-21

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 90.74  E-value: 5.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  41 NCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFL-----TWSKLDSSQLIPRDEPRMWVK----------GNIL 105
Cdd:PHA02826   21 YCKYRGGDLTPVYAKFGDPMVLLCTGKHYKKSIFFDKTFItsynvTWSKTDSLAFVRDSGARTKIKkithneigdrSENL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 106 WILPAVQQDSGTYICTFRNASHCEQMSVELKVFKNTeaslphVSYLQISALSTTglLVCPDLKEFISSNADGKIQWYKGA 185
Cdd:PHA02826  101 WIGNVINIDEGIYICTISSGNICEESTIRLTFDSGT------INYQFNSGKDSK--LHCYGTDGISSTFKDYTLTWYKNG 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907067423 186 ILLdKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRV 240
Cdd:PHA02826  173 NIV-LYTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRFNKNSNNYNITKEYKVTI 226
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
150-242 6.29e-18

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R). 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: 78.28  E-value: 6.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 150 YLQISALSTTGLLVCPDLKEFISSNAD-GKIQWYKGAILLDKGNKEFlsAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQ 228
Cdd:cd20994     3 YKQKVPFTSGGRIVCPHLDFFKDENNNlPKVQWYKDCKPLLLDDKRF--AGLESDLLIFNVTVQDQGNYTCHTSYTYMGK 80
                          90
                  ....*....|....
gi 1907067423 229 EYNITRNIELRVKG 242
Cdd:cd20994    81 QYNISRTISLIVLE 94
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
56-137 7.05e-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. 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: 49.98  E-value: 7.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  56 EGEPVVLRCPLAPHSDISSsshsfLTWSKLDSSQLIPRDE-PRMWVKGNILWILPAVQQDSGTYICTFRNASHCEQMSVE 134
Cdd:cd20991    13 ANEIDVRSCPLNPNESKGT-----ITWYKNDSKTPISMEQdSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKIT 87

                  ...
gi 1907067423 135 LKV 137
Cdd:cd20991    88 AKF 90
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
146-242 2.06e-07

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: 48.74  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 146 PHVSYLQISALSTTgllvCPDLKEFISSNADGKIQWYKGAILLDKGNkEFLSAGDPTRLLISNTSMDdaGYYRCVMTFTY 225
Cdd:cd20993     4 PVIAYIEYGGRTIT----CPDLDGIKPPSVSPTVTWYHECNAFGNFN-DRVPKGDKLVIHVMLEHYQ--GNYTCVVTYET 76
                          90
                  ....*....|....*..
gi 1907067423 226 NGQEYNITRNIELRVKG 242
Cdd:cd20993    77 KGRTIKLTRTVNVKVVG 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
50-137 3.53e-07

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: 47.50  E-value: 3.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423   50 KSELRLEGEPVVLRCPLAPHSDISssshsfLTWSKLDSSQLIPRDEPRMWVKGNI--LWILPAVQQDSGTYICTFRNASH 127
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPE------VTWYKQGGKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSG 75
                           90
                   ....*....|
gi 1907067423  128 CEQMSVELKV 137
Cdd:smart00410  76 SASSGTTLTV 85
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
48-137 5.36e-07

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


Pssm-ID: 409477  Cd Length: 105  Bit Score: 47.64  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  48 EFKSELRLEGEPVVLRCPL-----APHSDISSSSHSFLTWSK----LDSSQLIPRDEPRMWVKGNILWILPAVQQDSGTY 118
Cdd:cd05896     6 DLKKYMVLAGEPVRIKCALfygyiRTNYSMAQSAGLSLMWYKssgpGDFEEPIIFDGVRMSKEEDSIWFRPAELQDSGLY 85
                          90
                  ....*....|....*....
gi 1907067423 119 ICTFRNASHCEQMSVELKV 137
Cdd:cd05896    86 TCVLRNSTYCMKVSMSLTV 104
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
55-137 6.55e-06

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


Pssm-ID: 409584  Cd Length: 108  Bit Score: 44.92  E-value: 6.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  55 LEGEPVVLRCPLAPHSDISSSSHSF-----LTWSKLDSSQLI--PRD----EPRMWVKGNILWILPAVQQDSGTYICTFR 123
Cdd:cd20992    14 FEGEPARIKCPLFEHFLKYNYSTAHsagltLIWYWTRQDRDLeePINfrlpDNRISKEKDVLWFRPTLLNDTGNYTCMLR 93
                          90
                  ....*....|....
gi 1907067423 124 NASHCEQMSVELKV 137
Cdd:cd20992    94 NTTYCSKVAFPLEV 107
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
249-342 2.29e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.17  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 249 PVIISPLETIPASLGSRLIVPCKVflgTGTSSNTIVWwlanstfisaaYPRGRVTEGLHHQYSENDENYveVSLIFDPVT 328
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEA---TGSPPPTITW-----------YKNGEPISSGSTRSRSLSGSN--STLTISNVT 65
                          90
                  ....*....|....
gi 1907067423 329 REDlHTDFKCVASN 342
Cdd:pfam13927  66 RSD-AGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
162-240 5.03e-05

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 41.72  E-value: 5.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  162 LVCPdlkefISSNADGKIQWYKGAI--LLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYngqeYNITRNIELR 239
Cdd:smart00410  14 LSCE-----ASGSPPPEVTWYKQGGklLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS----GSASSGTTLT 84

                   .
gi 1907067423  240 V 240
Cdd:smart00410  85 V 85
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
91-151 9.00e-05

Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 receptor alpha (IL-18Ra). IL-18Ra ectodomain folds into three immunoglobulin (Ig)-like domains, similar to IL-1 receptors. Each domain comprises a two-layer sandwich of six to nine beta-strands and contains at least one intra-domain disulfide bond.


Pssm-ID: 465773  Cd Length: 128  Bit Score: 42.02  E-value: 9.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067423  91 IPRDEPRMWVKGNILWILPAVQQDSGTYICTFRNASH-----CEQMSVELKVFKNT--EASLPHVSYL 151
Cdd:pfam18452  61 ITESSPHIIQEGNALWFLPVGVNDSGSYICRPRIRSPqdeacCLKIILEVQPKTNAscSGSVTNELYL 128
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
253-353 1.02e-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: 40.64  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 253 SPLETIPASLGSRLIVPCKVFlgTGTSSNTIVWWLANSTFISaayprgrVTEGLHHQYSENDEnyvevSLIFDPVTREDL 332
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIE-------SLKVKHDNGRTTQS-----SLLISNVTKEDA 66
                          90       100
                  ....*....|....*....|.
gi 1907067423 333 HTdFKCVASNPRSSQSLHTTV 353
Cdd:pfam00047  67 GT-YTCVVNNPGGSATLSTSL 86
Ig3_IL1RAP cd20931
Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members ...
249-355 1.18e-04

Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members here are composed of the third immunoglobulin Ig interleukin-1 receptor accessory protein (IL1RAP). The interleukin 1 receptor accessory protein (IL-1RAP), also known as IL-1R3, is a coreceptor of type 1 interleukin 1 receptor (IL-1R1) and is required for transmission of IL-1 signaling. The activated IL-1 receptor complex, which consists of IL-1R1 and IL-1RAP, induces multiple cellular responses including NF-kappa-B activation, IL-2 secretion, and IL-2 promoter activation. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective Toll/IL-1 receptor (TIR) domains of the receptor/coreceptor subunits. Moreover, IL1RAP is known to be the accessory co-receptor that activates signal transduction upon IL-36 binding to IL-36R. IL-36 cytokines, which are a subfamily of the IL-1 superfamily, bind to the IL-36 receptor (IL-36R) and use IL1RAP as a co-receptor.


Pssm-ID: 409525  Cd Length: 107  Bit Score: 41.17  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 249 PVIISPLETI--PASLGSRLIVPCKVFLGTGTSSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSEnDENYVEVsLIFDP 326
Cdd:cd20931     1 PQIYSPNDRVvyEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDVTIDVTINESISYSSTE-DETRTQI-LSIKK 78
                          90       100
                  ....*....|....*....|....*....
gi 1907067423 327 VTREDLHTDFKCVASNPRSSQSLHTTVKE 355
Cdd:cd20931    79 VTPEDLKRNYVCHARNAKGEVEKAAKVKQ 107
I-set pfam07679
Immunoglobulin I-set domain;
249-354 1.25e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 40.70  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423 249 PVIISPLETIPASLGSRLIVPCKVflgTGTSSNTIVWWLANSTfisaayprgrVTEGLHHQYSENDENYvevSLIFDPVT 328
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTV---TGTPDPEVSWFKDGQP----------LRSSDRFKVTYEGGTY---TLTISNVQ 64
                          90       100
                  ....*....|....*....|....*.
gi 1907067423 329 REDLHTdFKCVASNPRSSQSLHTTVK 354
Cdd:pfam07679  65 PDDSGK-YTCVATNSAGEAEASAELT 89
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
162-229 4.35e-04

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 38.46  E-value: 4.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067423 162 LVCPdlkefISSNADGKIQWYK-GAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQE 229
Cdd:cd00096     3 LTCS-----ASGNPPPTITWYKnGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
60-124 1.50e-03

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


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 36.92  E-value: 1.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907067423  60 VVLRCPLAPHSDISssshsfLTWSKLDSSQLIPRDEPRMWVKGN-ILWILPAVQQDSGTYICTFRN 124
Cdd:cd00096     1 VTLTCSASGNPPPT------ITWYKNGKPLPPSSRDSRRSELGNgTLTISNVTLEDSGTYTCVASN 60
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
173-220 3.83e-03

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


Pssm-ID: 409559  Cd Length: 82  Bit Score: 36.07  E-value: 3.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907067423 173 SNADGKIQWYK-GAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCV 220
Cdd:cd20967    22 ADPDAEVKWYKdGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV 70
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
50-135 4.04e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 36.40  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  50 KSELRLEGEPVVLRCPLAPHSDISSsshsfLTWSKLDSSQLIPRDEPRMWVKGNI--LWILPAVQQDSGTYICTFRNASH 127
Cdd:pfam00047   4 PTVTVLEGDSATLTCSASTGSPGPD-----VTWSKEGGTLIESLKVKHDNGRTTQssLLISNVTKEDAGTYTCVVNNPGG 78

                  ....*...
gi 1907067423 128 CEQMSVEL 135
Cdd:pfam00047  79 SATLSTSL 86
I-set pfam07679
Immunoglobulin I-set domain;
81-137 6.76e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 35.70  E-value: 6.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067423  81 TWSKlDSSQLIPRDEPRMWVKGNI--LWILPAVQQDSGTYICTFRNASHCEQMSVELKV 137
Cdd:pfam07679  33 SWFK-DGQPLRSSDRFKVTYEGGTytLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
CD19_double_Ig cd23997
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold domain; CD19, ...
56-137 9.26e-03

CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold domain; CD19, also known as B-Lymphocyte Surface Antigen B4, T-Cell Surface Antigen Leu-12, and CVID3, is a transmembrane receptor present on various types of B cells, including progenitor, naive, and memory B cells, as well as plasmablasts. Until recently, it was believed to comprise two extracellular immunoglobulin (Ig) structural domains arranged in tandem with C2 topology. However, recent crystal structures have shown that the CD19 extracellular domain contains a unique double Ig domain that is responsible for its binding to proteins such as CD21, CD81, and CD225, which regulate B cell activation and survival. A recent analysis of the CD19 extracellular domain sequence reveals two "Ig domains", but the structure demonstrates that these two domains are not folded independently and connected in tandem. Rather, they fold together as one intertwined domain that can be referred to as a "double Ig" domain. Each of the two regular Ig domain sequences has a noticeably short linker that forms a loop between strands C' and D, rather than allowing the formation of a C" strand. Additionally, the two Ig-domain sequences are separated by a long linker that is structured as a small insertion domain, enabling both Ig sequences to fold together as a unique double Ig-domain. The CD19 domain comprises four "protodomains": two formed by A'B-CC' strands and two by DE-FG strands that interdigitate to form a novel double Ig fold. When analyzing this double Ig domain in terms of the usual Ig-fold, A'B-CC' protodomain of the first Ig sequence combines with DE-FG protodomain of the second, and vice versa. Hence, the second combined Ig fold is inverted, with DE-FG protodomain of the first Ig sequence combining with A'B-CC' protodomain of the second Ig sequence and in that order, as if it were a circular permutation, obtained only through structural folding.


Pssm-ID: 467824  Cd Length: 89  Bit Score: 35.39  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  56 EGEPVVLRCPLAPHSDISSSshsfLTWSKldSSQLIP-----RDEPRMWVK---GNILWILP-AVQQDSGTYICTFRNAS 126
Cdd:cd23997     7 EGSTLWLPCLVPPSDGPRGP----LTWSR--GHPKTPllsleLGSPGLWVLvgpLGILLLLPnVSAQMGGFYLCELGNLS 80
                          90
                  ....*....|.
gi 1907067423 127 hcEQMSVELKV 137
Cdd:cd23997    81 --WTIGWTVSV 89
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
54-137 9.44e-03

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


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 35.06  E-value: 9.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067423  54 RLEGEPVVLRCPLAPHSDISssshsfLTWSKldSSQLIPRDEPRMWVKGNILWILPAVQQDSGTYICTFRNASHCEQMSV 133
Cdd:cd20978    13 VKGGQDVTLPCQVTGVPQPK------ITWLH--NGKPLQGPMERATVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTET 84

                  ....
gi 1907067423 134 ELKV 137
Cdd:cd20978    85 LLHV 88
PHA02633 PHA02633
hypothetical protein; Provisional
86-137 9.46e-03

hypothetical protein; Provisional


Pssm-ID: 165016  Cd Length: 63  Bit Score: 34.57  E-value: 9.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907067423  86 DSSQLIPRDeprmwvKGNILWILPAVQQDSGTYICTFRNASHCEQMSVELKV 137
Cdd:PHA02633    7 DNDRIILID------NCNNMLILNPTQSDSGIYMCITKNETYSDMMKFDLCI 52
 
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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