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Conserved domains on  [gi|1343294306|ref|NP_001347729|]
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interleukin-1 receptor type 2 isoform 1 precursor [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
 54-382 1.22e-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: 155.17  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  54 TVHGDNCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFLtWSK--LDSSQLIPRDeprmwvKGNILWILPAVQQ 131
Cdd:PHA02785   20 TFNAPECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDIL-WEKrgADNDRIIPID------NGSNMLILNPTQS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 132 DSGTYICTFRNASHCEQMSVELKVFKNTEASLPHVSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGnk 211
Cdd:PHA02785   93 DSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGHRRLRNKR-- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 212 efLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRVKGTTtepIPVIISPLETIPASLGSRLIVPCKVF 291
Cdd:PHA02785  171 --LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDRI---IPPTMQLPEGVVTSIGSNLTIACRVS 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 292 LGTGTsSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSENDENYVEVS-LIFDPVTREDLhTDFKCVAsnprssqslhTT 370
Cdd:PHA02785  246 LRPPT-TDADVFWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEEDA-TTFTCMA----------FT 313

                         330
                  ....*....|..
gi 1343294306 371 VKEVSSTFSWSI 382
Cdd:PHA02785  314 IPSISKTVTISI 325
 
Name Accession Description Interval E-value
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 54-382 1.22e-43

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 155.17  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  54 TVHGDNCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFLtWSK--LDSSQLIPRDeprmwvKGNILWILPAVQQ 131
Cdd:PHA02785   20 TFNAPECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDIL-WEKrgADNDRIIPID------NGSNMLILNPTQS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 132 DSGTYICTFRNASHCEQMSVELKVFKNTEASLPHVSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGnk 211
Cdd:PHA02785   93 DSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGHRRLRNKR-- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 212 efLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRVKGTTtepIPVIISPLETIPASLGSRLIVPCKVF 291
Cdd:PHA02785  171 --LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDRI---IPPTMQLPEGVVTSIGSNLTIACRVS 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 292 LGTGTsSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSENDENYVEVS-LIFDPVTREDLhTDFKCVAsnprssqslhTT 370
Cdd:PHA02785  246 LRPPT-TDADVFWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEEDA-TTFTCMA----------FT 313

                         330
                  ....*....|..
gi 1343294306 371 VKEVSSTFSWSI 382
Cdd:PHA02785  314 IPSISKTVTISI 325
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 166-260 3.33e-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: 120.25  E-value: 3.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 166 VSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNG 245
Cdd:cd05897     1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80

                          90
                  ....*....|....*
gi 1343294306 246 QEYNITRNIELRVKG 260
Cdd:cd05897    81 KKYNITRSIELRIVK 95
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 68-155 3.67e-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: 3.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306   68 KSELRLEGEPVVLRCPLAPHSDISssshsfLTWSKLDSSQLIPRDEPRMWVKGNI--LWILPAVQQDSGTYICTFRNASH 145
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPE------VTWYKQGGKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSG 75

                           90
                   ....*....|
gi 1343294306  146 CEQMSVELKV 155
Cdd:smart00410  76 SASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 267-360 1.92e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 267 PVIISPLETIPASLGSRLIVPCKVflgTGTSSNTIVWwlanstfisaaYPRGRVTEGLHHQYSENDENYveVSLIFDPVT 346
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEA---TGSPPPTITW-----------YKNGEPISSGSTRSRSLSGSN--STLTISNVT 65

                          90
                  ....*....|....
gi 1343294306 347 REDlHTDFKCVASN 360
Cdd:pfam13927  66 RSD-AGTYTCVASN 78
 
Name Accession Description Interval E-value
PHA02785 PHA02785
IL-beta-binding protein; Provisional
 54-382 1.22e-43

IL-beta-binding protein; Provisional


Pssm-ID: 165149 [Multi-domain]  Cd Length: 326  Bit Score: 155.17  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  54 TVHGDNCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFLtWSK--LDSSQLIPRDeprmwvKGNILWILPAVQQ 131
Cdd:PHA02785   20 TFNAPECIDKGQYFASFMELENEPVILPCPQINTLSSGYNILDIL-WEKrgADNDRIIPID------NGSNMLILNPTQS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 132 DSGTYICTFRNASHCEQMSVELKVFKNTEASLPHVSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGnk 211
Cdd:PHA02785   93 DSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYPQIVNERSTGEMVCPNINAFIASNVNADIIWSGHRRLRNKR-- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 212 efLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRVKGTTtepIPVIISPLETIPASLGSRLIVPCKVF 291
Cdd:PHA02785  171 --LKQRTPGIITIEDVRKNDAGYYTCVLKYIYGDKTYNVTRIVKLEVRDRI---IPPTMQLPEGVVTSIGSNLTIACRVS 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 292 LGTGTsSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSENDENYVEVS-LIFDPVTREDLhTDFKCVAsnprssqslhTT 370
Cdd:PHA02785  246 LRPPT-TDADVFWISNGMYYEEDDEDGDGRISVANKIYTTDKRRVITSrLNINPVKEEDA-TTFTCMA----------FT 313

                         330
                  ....*....|..
gi 1343294306 371 VKEVSSTFSWSI 382
Cdd:PHA02785  314 IPSISKTVTISI 325
Ig2_IL1R2_like cd05897
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor-2 (IL1R2), and similar ...
 166-260 3.33e-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: 120.25  E-value: 3.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 166 VSYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNG 245
Cdd:cd05897     1 ISYPQILFTSTSGKLVCPDLSEFTINRTDVEIQWYKDSLLLDKDNEKFLSVKGSTHLLIHDVSLNDSGYYTCKLTFTHEG 80

                          90
                  ....*....|....*
gi 1343294306 246 QEYNITRNIELRVKG 260
Cdd:cd05897    81 KKYNITRSIELRIVK 95
Ig1_IL1R_like cd05756
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 62-156 1.10e-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: 1.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  62 FRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSfLTWSKLDSSQLIPRD-EPRMWVKGNILWILPAVQQDSGTYICTF 140
Cdd:cd05756     2 EWGEDIKILVVLEGEPDVIKCPLFPNFLAQSAGLN-LTWYKNDSETPISFEpDSRIHQEKDKLWFVPALLEDSGNYYCVV 80

                          90
                  ....*....|....*.
gi 1343294306 141 RNASHCEQMSVELKVF 156
Cdd:cd05756    81 RNSTYCSKVSISLEVV 96
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 167-260 5.45e-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: 5.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 167 SYLQISALSTTGLLVCPDLKEFISSNADGKIQWYKGAILLdKGNKEFLSAGDptRLLISNTSMDDAGYYRCVMTFTYNGQ 246
Cdd:cd05757     2 RYKQKLPITKGGKITCPDLDDYKNENVLPPIQWYKDCKPL-QGDKRFIPKGS--KLLIQNVTEEDAGNYTCKFTYTHNGK 78

                          90
                  ....*....|....
gi 1343294306 247 EYNITRNIELRVKG 260
Cdd:cd05757    79 QYNVTRTISLTVTE 92
PHA02826 PHA02826
IL-1 receptor-like protein; Provisional
 59-258 4.65e-21

IL-1 receptor-like protein; Provisional


Pssm-ID: 165173 [Multi-domain]  Cd Length: 227  Bit Score: 91.13  E-value: 4.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  59 NCQFRGREFKSELRLEGEPVVLRCPLAPHSDISSSSHSFL-----TWSKLDSSQLIPRDEPRMWVK----------GNIL 123
Cdd:PHA02826   21 YCKYRGGDLTPVYAKFGDPMVLLCTGKHYKKSIFFDKTFItsynvTWSKTDSLAFVRDSGARTKIKkithneigdrSENL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 124 WILPAVQQDSGTYICTFRNASHCEQMSVELKVFKNTeaslphVSYLQISALSTTglLVCPDLKEFISSNADGKIQWYKGA 203
Cdd:PHA02826  101 WIGNVINIDEGIYICTISSGNICEESTIRLTFDSGT------INYQFNSGKDSK--LHCYGTDGISSTFKDYTLTWYKNG 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1343294306 204 ILLdKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQEYNITRNIELRV 258
Cdd:PHA02826  173 NIV-LYTDRIQLRNNNSTLVIKSATHDDSGIYTCNLRFNKNSNNYNITKEYKVTI 226
Ig2_IL1R_like cd20994
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 168-260 6.91e-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: 6.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 168 YLQISALSTTGLLVCPDLKEFISSNAD-GKIQWYKGAILLDKGNKEFlsAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQ 246
Cdd:cd20994     3 YKQKVPFTSGGRIVCPHLDFFKDENNNlPKVQWYKDCKPLLLDDKRF--AGLESDLLIFNVTVQDQGNYTCHTSYTYMGK 80

                          90
                  ....*....|....
gi 1343294306 247 EYNITRNIELRVKG 260
Cdd:cd20994    81 QYNISRTISLIVLE 94
Ig1_IL1R_like cd20991
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 74-155 6.70e-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: 6.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  74 EGEPVVLRCPLAPHSDISSsshsfLTWSKLDSSQLIPRDE-PRMWVKGNILWILPAVQQDSGTYICTFRNASHCEQMSVE 152
Cdd:cd20991    13 ANEIDVRSCPLNPNESKGT-----ITWYKNDSKTPISMEQdSRIHQYKEKLWFVPAKVEDSGHYYCVVRNSTYCLKIKIT 87


                  ...
gi 1343294306 153 LKV 155
Cdd:cd20991    88 AKF 90
Ig2_IL-1RAP_like cd20993
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 164-260 1.92e-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: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 164 PHVSYLQISALSTTgllvCPDLKEFISSNADGKIQWYKGAILLDKGNkEFLSAGDPTRLLISNTSMDdaGYYRCVMTFTY 243
Cdd:cd20993     4 PVIAYIEYGGRTIT----CPDLDGIKPPSVSPTVTWYHECNAFGNFN-DRVPKGDKLVIHVMLEHYQ--GNYTCVVTYET 76

                          90
                  ....*....|....*..
gi 1343294306 244 NGQEYNITRNIELRVKG 260
Cdd:cd20993    77 KGRTIKLTRTVNVKVVG 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 68-155 3.67e-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: 3.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306   68 KSELRLEGEPVVLRCPLAPHSDISssshsfLTWSKLDSSQLIPRDEPRMWVKGNI--LWILPAVQQDSGTYICTFRNASH 145
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPE------VTWYKQGGKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSG 75

                           90
                   ....*....|
gi 1343294306  146 CEQMSVELKV 155
Cdd:smart00410  76 SASSGTTLTV 85
Ig1_IL1RAPL-1_like cd05896
First immunoglobulin (Ig)-like domain of X-linked interleukin-1 receptor accessory ...
 66-155 6.08e-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: 6.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  66 EFKSELRLEGEPVVLRCPL-----APHSDISSSSHSFLTWSK----LDSSQLIPRDEPRMWVKGNILWILPAVQQDSGTY 136
Cdd:cd05896     6 DLKKYMVLAGEPVRIKCALfygyiRTNYSMAQSAGLSLMWYKssgpGDFEEPIIFDGVRMSKEEDSIWFRPAELQDSGLY 85

                          90
                  ....*....|....*....
gi 1343294306 137 ICTFRNASHCEQMSVELKV 155
Cdd:cd05896    86 TCVLRNSTYCMKVSMSLTV 104
Ig1_IL1R_like cd20992
First immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 73-155 6.12e-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: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  73 LEGEPVVLRCPLAPHSDISSSSHSF-----LTWSKLDSSQLI--PRD----EPRMWVKGNILWILPAVQQDSGTYICTFR 141
Cdd:cd20992    14 FEGEPARIKCPLFEHFLKYNYSTAHsagltLIWYWTRQDRDLeePINfrlpDNRISKEKDVLWFRPTLLNDTGNYTCMLR 93

                          90
                  ....*....|....
gi 1343294306 142 NASHCEQMSVELKV 155
Cdd:cd20992    94 NTTYCSKVAFPLEV 107
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 267-360 1.92e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 267 PVIISPLETIPASLGSRLIVPCKVflgTGTSSNTIVWwlanstfisaaYPRGRVTEGLHHQYSENDENYveVSLIFDPVT 346
Cdd:pfam13927   2 PVITVSPSSVTVREGETVTLTCEA---TGSPPPTITW-----------YKNGEPISSGSTRSRSLSGSN--STLTISNVT 65

                          90
                  ....*....|....
gi 1343294306 347 REDlHTDFKCVASN 360
Cdd:pfam13927  66 RSD-AGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 180-258 4.92e-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: 4.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  180 LVCPdlkefISSNADGKIQWYKGAI--LLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYngqeYNITRNIELR 257
Cdd:smart00410  14 LSCE-----ASGSPPPEVTWYKQGGklLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSS----GSASSGTTLT 84


                   .
gi 1343294306  258 V 258
Cdd:smart00410  85 V 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 271-371 8.52e-05

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: 41.03  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 271 SPLETIPASLGSRLIVPCKVFlgTGTSSNTIVWWLANSTFISaayprgrVTEGLHHQYSENDEnyvevSLIFDPVTREDL 350
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAS--TGSPGPDVTWSKEGGTLIE-------SLKVKHDNGRTTQS-----SLLISNVTKEDA 66

                          90       100
                  ....*....|....*....|.
gi 1343294306 351 HTdFKCVASNPRSSQSLHTTV 371
Cdd:pfam00047  67 GT-YTCVVNNPGGSATLSTSL 86
Ig_6 pfam18452
Immunoglobulin domain; This is an immunoglobulin domain which can be found in Interleukin-18 ...
 109-169 9.29e-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: 9.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343294306 109 IPRDEPRMWVKGNILWILPAVQQDSGTYICTFRNASH-----CEQMSVELKVFKNT--EASLPHVSYL 169
Cdd:pfam18452  61 ITESSPHIIQEGNALWFLPVGVNDSGSYICRPRIRSPqdeacCLKIILEVQPKTNAscSGSVTNELYL 128
I-set pfam07679
Immunoglobulin I-set domain;
267-372 1.08e-04

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 40.70  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 267 PVIISPLETIPASLGSRLIVPCKVflgTGTSSNTIVWWLANSTfisaayprgrVTEGLHHQYSENDENYvevSLIFDPVT 346
Cdd:pfam07679   1 PKFTQKPKDVEVQEGESARFTCTV---TGTPDPEVSWFKDGQP----------LRSSDRFKVTYEGGTY---TLTISNVQ 64

                          90       100
                  ....*....|....*....|....*.
gi 1343294306 347 REDLHTdFKCVASNPRSSQSLHTTVK 372
Cdd:pfam07679  65 PDDSGK-YTCVATNSAGEAEASAELT 89
Ig3_IL1RAP cd20931
Third immunoglobulin domain of interleukin-1 receptor accessory protein (IL1RAP); The members ...
 267-373 1.24e-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: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306 267 PVIISPLETI--PASLGSRLIVPCKVFLGTGTSSNTIVWWLANSTFISAAYPRGRVTEGLHHQYSEnDENYVEVsLIFDP 344
Cdd:cd20931     1 PQIYSPNDRVvyEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDVTIDVTINESISYSSTE-DETRTQI-LSIKK 78

                          90       100
                  ....*....|....*....|....*....
gi 1343294306 345 VTREDLHTDFKCVASNPRSSQSLHTTVKE 373
Cdd:cd20931    79 VTPEDLKRNYVCHARNAKGEVEKAAKVKQ 107
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 180-247 4.17e-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: 4.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1343294306 180 LVCPdlkefISSNADGKIQWYK-GAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCVMTFTYNGQE 247
Cdd:cd00096     3 LTCS-----ASGNPPPTITWYKnGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSA 66
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 78-142 1.48e-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: 1.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343294306  78 VVLRCPLAPHSDISssshsfLTWSKLDSSQLIPRDEPRMWVKGN-ILWILPAVQQDSGTYICTFRN 142
Cdd:cd00096     1 VTLTCSASGNPPPT------ITWYKNGKPLPPSSRDSRRSELGNgTLTISNVTLEDSGTYTCVASN 60
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 68-153 3.65e-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: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  68 KSELRLEGEPVVLRCPLAPHSDISSsshsfLTWSKLDSSQLIPRDEPRMWVKGNI--LWILPAVQQDSGTYICTFRNASH 145
Cdd:pfam00047   4 PTVTVLEGDSATLTCSASTGSPGPD-----VTWSKEGGTLIESLKVKHDNGRTTQssLLISNVTKEDAGTYTCVVNNPGG 78


                  ....*...
gi 1343294306 146 CEQMSVEL 153
Cdd:pfam00047  79 SATLSTSL 86
IgI_C2_MyBP-C-like cd20967
Domain C2 of human cardiac Myosin Binding Protein C and similar domains; a member of the I-set ...
 191-238 4.01e-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: 4.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1343294306 191 SNADGKIQWYK-GAILLDKGNKEFLSAGDPTRLLISNTSMDDAGYYRCV 238
Cdd:cd20967    22 ADPDAEVKWYKdGQELQSSSKVIFESIGAKRTLTVQQASLADAGEYQCV 70
I-set pfam07679
Immunoglobulin I-set domain;
99-155 6.36e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 35.70  E-value: 6.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1343294306  99 TWSKlDSSQLIPRDEPRMWVKGNI--LWILPAVQQDSGTYICTFRNASHCEQMSVELKV 155
Cdd:pfam07679  33 SWFK-DGQPLRSSDRFKVTYEGGTytLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
 72-155 9.51e-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: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  72 RLEGEPVVLRCPLAPHSDISssshsfLTWSKldSSQLIPRDEPRMWVKGNILWILPAVQQDSGTYICTFRNASHCEQMSV 151
Cdd:cd20978    13 VKGGQDVTLPCQVTGVPQPK------ITWLH--NGKPLQGPMERATVEDGTLTIINVQPEDTGYYGCVATNEIGDIYTET 84


                  ....
gi 1343294306 152 ELKV 155
Cdd:cd20978    85 LLHV 88
CD19_double_Ig cd23997
CD19 (Cluster of Differentiation 19), a unique double immunoglobulin (Ig)-fold domain; CD19, ...
 74-155 9.71e-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: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343294306  74 EGEPVVLRCPLAPHSDISSSshsfLTWSKldSSQLIP-----RDEPRMWVK---GNILWILP-AVQQDSGTYICTFRNAS 144
Cdd:cd23997     7 EGSTLWLPCLVPPSDGPRGP----LTWSR--GHPKTPllsleLGSPGLWVLvgpLGILLLLPnVSAQMGGFYLCELGNLS 80

                          90
                  ....*....|.
gi 1343294306 145 hcEQMSVELKV 155
Cdd:cd23997    81 --WTIGWTVSV 89
PHA02633 PHA02633
hypothetical protein; Provisional
 104-155 9.89e-03

hypothetical protein; Provisional


Pssm-ID: 165016  Cd Length: 63  Bit Score: 34.57  E-value: 9.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1343294306 104 DSSQLIPRDeprmwvKGNILWILPAVQQDSGTYICTFRNASHCEQMSVELKV 155
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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