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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333 243 PQIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEVWWTIDGKKPDDVTVDITINESVSYSSTEDETRTQILSIKKVT 322
Cdd:cd20931    1 PQIYSPNDRVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDVTIDVTINESISYSSTEDETRTQILSIKKVT 80

                         90       100
                 ....*....|....*....|....*..
gi 226693333 323 PEDLRRNYVCHARNTKGEAEQAAKVKQ 349
Cdd:cd20931   81 PEDLKRNYVCHARNAKGEVEKAAKVKQ 107

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333 145 PVHKMYIEHGIHKITCPNVDGYFPSSVKPSVTWYKGCTEIVDFHNVLPEGMNLSFFIPLVSNNGNYTCVVTYPENGRLFH 224
Cdd:cd20993    3 TPVIAYIEYGGRTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDRVPKGDKLVIHVMLEHYQGNYTCVVTYETKGRTIK 82

                         90
                 ....*....|.
gi 226693333 225 LTRTVTVKVVG 235
Cdd:cd20993   83 LTRTVNVKVVG 93

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333 243 PQIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEVWWTIDGKKPDDVTVDITINESVSYSSTEDETRTQILSIKKVT 322
Cdd:cd20931    1 PQIYSPNDRVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDVTIDVTINESISYSSTEDETRTQILSIKKVT 80

                         90       100
                 ....*....|....*....|....*..
gi 226693333 323 PEDLRRNYVCHARNTKGEAEQAAKVKQ 349
Cdd:cd20931   81 PEDLKRNYVCHARNAKGEVEKAAKVKQ 107

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333 145 PVHKMYIEHGIHKITCPNVDGYFPSSVKPSVTWYKGCTEIVDFHNVLPEGMNLSFFIPLVSNNGNYTCVVTYPENGRLFH 224
Cdd:cd20993    3 TPVIAYIEYGGRTITCPDLDGIKPPSVSPTVTWYHECNAFGNFNDRVPKGDKLVIHVMLEHYQGNYTCVVTYETKGRTIK 82

                         90
                 ....*....|.
gi 226693333 225 LTRTVTVKVVG 235
Cdd:cd20993   83 LTRTVNVKVVG 93

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333  405 YDIYVSYARNVEEEEFVLLTLRGVleNEFGYKLCIFDRDSLPGGNTVEAVFDFIQRSRRMIVVLSPDYVTEKSiSMLEFK 484
Cdd:pfam01582   1 YDVFLSFRGSDTREWFVSHLLKEL--KQKGIKLFIDDRDLEPGEAIAPELLSAIEKSRRSVVVLSPNYASSGW-CLDELV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226693333  485 LGVMCQNSIATKLIVVEYRPLEQP-----------HPGIMQLKESVSFVSWKGE----------KSKHSGSKFWKALR 541
Cdd:pfam01582  78 KILECALDLGQKVIPIFYEVDPSDvrkqtgsfgkaFKKHKKVLTEEKVLKWRGAlnevaniwhsKSVSDESKFWKKIA 155

Immunoglobulin domain; This domain contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226693333  157 KITCPnvdgyFPSSVKPSVTWYKGCTEIvdfhnvlPEGMNLSFFIPLVSNNGNYTCVVTypeNGRLFHLTRTVTVKV 233
Cdd:pfam13895  18 TLTCS-----APGNPPPSYTWYKDGSAI-------SSSPNFFTLSVSAEDSGTYTCVAR---NGRGGKVSNPVELTV 79

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333  242 PPQIYSPNDRVVYEkePGEELVIPCKVYFSfimdSHNEVWWTIDGKKPDdvtvditineSVSYSSTEDETRTQILSIKKV 321
Cdd:pfam13927   1 KPVITVSPSSVTVR--EGETVTLTCEATGS----PPPTITWYKNGEPIS----------SGSTRSRSLSGSNSTLTISNV 64

                          90
                  ....*....|....*
gi 226693333  322 TPEDlRRNYVCHARN 336
Cdd:pfam13927  65 TRSD-AGTYTCVASN 78

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333 243 PQIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEVWWTIDGKKPDDVTVDITINESVSYSSTEDETRTQILSIKKVT 322
Cdd:cd20931    1 PQIYSPNDRVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDVTIDVTINESISYSSTEDETRTQILSIKKVT 80

                         90       100
                 ....*....|....*....|....*..
gi 226693333 323 PEDLRRNYVCHARNTKGEAEQAAKVKQ 349
Cdd:cd20931   81 PEDLKRNYVCHARNAKGEVEKAAKVKQ 107

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333  25 DDWGLDtMRQIQVFEDEPARIKCPLFEHFLkynystAHSSGLTLIWYWTrqdrDLEEPINFRlPENRISKEKDVLWFRPT 104
Cdd:cd05756    1 DEWGED-IKILVVLEGEPDVIKCPLFPNFL------AQSAGLNLTWYKN----DSETPISFE-PDSRIHQEKDKLWFVPA 68

                         90       100
                 ....*....|....*....|....*...
gi 226693333 105 LLNDTGNYTCMLRNTTYCSKVAFPLEVV 132
Cdd:cd05756   69 LLEDSGNYYCVVRNSTYCSKVSISLEVV 96

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333  26 DWGLDtMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFrlPENRISKEKDVLWFRPTL 105
Cdd:cd05896    2 DWSVD-LKKYMVLAGEPVRIKCALFYGYIRTNYSMAQSAGLSLMWYKSSGPGDFEEPIIF--DGVRMSKEEDSIWFRPAE 78

                         90       100
                 ....*....|....*....|....*.
gi 226693333 106 LNDTGNYTCMLRNTTYCSKVAFPLEV 131
Cdd:cd05896   79 LQDSGLYTCVLRNSTYCMKVSMSLTV 104

Toll - interleukin 1 - resistance;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333   404 EYDIYVSYARNveeEEFVLLTLRGVLENEFGYKLCIFDRDSLPGGNTVEAVFDFIQRSRRMIVVLSPDYVtEKSISMLEF 483
Cdd:smart00255   1 EYDVFISYSGK---EDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYA-ESEWCLDEL 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226693333   484 KLGVMCQNSI-ATKLIVVEYRPLEQPhpgIMQLKESVSFVS------WKGEKSKhsgsKFWKALRLALPLR 547
Cdd:smart00255  77 VAALENALEEgGLRVIPIFYEVIPSD---VRKQPGKFRKVFkknylkWPEDEKE----QFWKKALYAVPSK 140

IL-beta-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333   3 LLWYLMSLSFYG-ILQSHASERCDDWGLdTMRQIQVFEDEPARIKCPlfehflKYNYSTAHSSGLTLIWYWTRQDRDLEE 81
Cdd:PHA02785   4 LPVIFLPIFFYSsFVQTFNAPECIDKGQ-YFASFMELENEPVILPCP------QINTLSSGYNILDILWEKRGADNDRII 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333  82 PINfrlpenrisKEKDVLWFRPTLlNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSAMRFPvhKMYIEHGIHKITCP 161
Cdd:PHA02785  77 PID---------NGSNMLILNPTQ-SDSGIYICITKNETYCDMMSLNLTIVSVSESNIDLISYP--QIVNERSTGEMVCP 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333 162 NVDGYFPSSVKPSVTWyKGCTEIVDfhNVLPEGMNLSFFIPLVSNN--GNYTCVVTYPENGRLFHLTRTVTVKVvgspKD 239
Cdd:PHA02785 145 NINAFIASNVNADIIW-SGHRRLRN--KRLKQRTPGIITIEDVRKNdaGYYTCVLKYIYGDKTYNVTRIVKLEV----RD 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333 240 AL-PPQIYSPNDRVVyekEPGEELVIPCKVYFSfIMDSHNEVWWTIDGK--KPDDVTVD--ITINESVsYSSTEDETRTQ 314
Cdd:PHA02785 218 RIiPPTMQLPEGVVT---SIGSNLTIACRVSLR-PPTTDADVFWISNGMyyEEDDEDGDgrISVANKI-YTTDKRRVITS 292

                        330
                 ....*....|.
gi 226693333 315 ILSIKKVTPED 325
Cdd:PHA02785 293 RLNINPVKEED 303

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226693333  407 IYVSYARnvEEEEFVLlTLRGVLENEfGYKLCIFDRDSLPGGNTVEAVFDFIQRSRRMIVVLSPDYV 473
Cdd:pfam13676   1 VFISYAG--EDRAWAE-WLADALEAA-GYRVWLDRWDIRPGDDWVEEIEEAIENSDRVLVVLSPNYL 63

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333   253 VYEKEPGEELVIPCKVYFSfimdSHNEVWWTIDGKKPddvtvditINESVSYSSTEDETrTQILSIKKVTPEDlRRNYVC 332
Cdd:smart00410   3 SVTVKEGESVTLSCEASGS----PPPEVTWYKQGGKL--------LAESGRFSVSRSGS-TSTLTISNVTPED-SGTYTC 68

                           90
                   ....*....|....*.
gi 226693333   333 HARNTKGEAEQAAKVK 348
Cdd:smart00410  69 AATNSSGSASSGTTLT 84

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226693333   70 WYWTRQDRDLEEPINFRLPEnrISKEKDVLWFRPTLLNDTGNYTCMLRNTTY-----CSKVAfpLEVVQKD--SCFNSA 141
Cdd:pfam18452  48 WYWQPKNGDPLEAITESSPH--IIQEGNALWFLPVGVNDSGSYICRPRIRSPqdeacCLKII--LEVQPKTnaSCSGSV 122

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226693333 262 LVIPCKVYFsfimDSHNEVWWTIDGKKPDDVTVDITINESVSYSstedetrtqiLSIKKVTPEDlRRNYVCHARNTKGEA 341
Cdd:cd00096    1 VTLTCSASG----NPPPTITWYKNGKPLPPSSRDSRRSELGNGT----------LTISNVTLED-SGTYTCVASNSAGGS 65

                 ...
gi 226693333 342 EQA 344
Cdd:cd00096   66 ASA 68

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226693333 158 ITCPnvdgyFPSSVKPSVTWYKGCTEIV--DFHNVLPEGMNLSFFIPLV--SNNGNYTCVVTYPENGR 221
Cdd:cd00096    3 LTCS-----ASGNPPPTITWYKNGKPLPpsSRDSRRSELGNGTLTISNVtlEDSGTYTCVASNSAGGS 65