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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530431009    43 PDWTVQNGKNLTLQCFADVSTTSHV---KPQHQMLFYKDDvlfYNISSMKSTESYFIPEVRIYDSGTYKCTViVNNKEKT 119
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVtwyKQGGKLLAESGR---FSVSRSGSTSTLTISNVTPEDSGTYTCAA-TNSSGSA 77

                   ....*...
gi 530431009   120 TAEYQVLV 127
Cdd:smart00410  78 SSGTTLTV 85

C17orf99 Ig domain; This Ig domain is found in tandem in the uncharacterized human protein C17orf99, which is found across mammalian species.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530431009  423 KGQTIEVRCESISGTLPISYQLLKTS-KVLENSTKNSNDPAVFKDNPTE-----DVEYQCVADN 480
Cdd:pfam17736  15 SGRRVLISCHASQGSPPITYSLVGSDgIVVAKKIPLHGEPANFSLNITLksspdLLTYQCQAAN 78

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530431009    43 PDWTVQNGKNLTLQCFADVSTTSHV---KPQHQMLFYKDDvlfYNISSMKSTESYFIPEVRIYDSGTYKCTViVNNKEKT 119
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVtwyKQGGKLLAESGR---FSVSRSGSTSTLTISNVTPEDSGTYTCAA-TNSSGSA 77

                   ....*...
gi 530431009   120 TAEYQVLV 127
Cdd:smart00410  78 SSGTTLTV 85

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530431009  43 PDWTVQNGKNLTLQCfadvsTTSHVKPQHQMLFYKDDVLFYNissMKSTESYFIPEVRIYDSGTYKCTVIVNNKEKTTAE 122
Cdd:cd05753    7 PSAVVFEGEPLTLRC-----HGWKDKKVHKVTYYKDGKALKF---SYENSNFSIPQATLSDSGSYHCSGTVRIKRRSSES 78

                 ....*
gi 530431009 123 YQVLV 127
Cdd:cd05753   79 VNITV 83

Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also referred to as Z39Ig and V-set and Ig domain-containing 4 (VSIG4)) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. CRIg plays a role in the complement system, an inhibitor of the alternative pathway convertases, and a negative regulator of T cell activation. 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 such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins such as 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530431009 339 QGERLNLSCSIPGAPPANFTIQKEDTivsQTQDFTKIASKS----------DSGTYICTA-GIDKVVKKSNTVQIVV 404
Cdd:cd16082   12 QGMRISLQCQAWGSPPISYVWYKEQT---NNQEPIKVAALStllfkpavvaDSGSYFCTAkGRVGSEQRSDIVKFVV 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530431009  509 SSKVVESGEDIVLQCAVnEGSGPITYKFYREKEGK---PFYQMTSNATQAFWTKQKASKEQEGEYYCTAFN 576
Cdd:pfam13927   9 SSVTVREGETVTLTCEA-TGSPPPTITWYKNGEPIssgSTRSRSLSGSNSTLTISNVTRSDAGTYTCVASN 78

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530431009    43 PDWTVQNGKNLTLQCFADVSTTSHV---KPQHQMLFYKDDvlfYNISSMKSTESYFIPEVRIYDSGTYKCTViVNNKEKT 119
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVtwyKQGGKLLAESGR---FSVSRSGSTSTLTISNVTPEDSGTYTCAA-TNSSGSA 77

                   ....*...
gi 530431009   120 TAEYQVLV 127
Cdd:smart00410  78 SSGTTLTV 85

Second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of Fcgamma-receptors (FcgammaRs). Interactions between IgG and FcgammaR are important to the initiation of cellular and humoral response. IgG binding to FcgammaR leads to a cascade of signals and ultimately to functions such as antibody-dependent-cellular-cytotoxicity (ADCC), endocytosis, phagocytosis, release of inflammatory mediators, etc. FcgammaR has two Ig-like domains. This group also contains FcepsilonRI which binds IgE with high affinity.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530431009  43 PDWTVQNGKNLTLQCfadvsTTSHVKPQHQMLFYKDDVLFYNissMKSTESYFIPEVRIYDSGTYKCTVIVNNKEKTTAE 122
Cdd:cd05753    7 PSAVVFEGEPLTLRC-----HGWKDKKVHKVTYYKDGKALKF---SYENSNFSIPQATLSDSGSYHCSGTVRIKRRSSES 78

                 ....*
gi 530431009 123 YQVLV 127
Cdd:cd05753   79 VNITV 83

Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the Immunoglobulin (Ig) constant domain of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also referred to as Z39Ig and V-set and Ig domain-containing 4 (VSIG4)) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. CRIg plays a role in the complement system, an inhibitor of the alternative pathway convertases, and a negative regulator of T cell activation. 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 such as T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins such as 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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530431009 339 QGERLNLSCSIPGAPPANFTIQKEDTivsQTQDFTKIASKS----------DSGTYICTA-GIDKVVKKSNTVQIVV 404
Cdd:cd16082   12 QGMRISLQCQAWGSPPISYVWYKEQT---NNQEPIKVAALStllfkpavvaDSGSYFCTAkGRVGSEQRSDIVKFVV 85

Immunoglobulin domain; This family contains immunoglobulin-like domains.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530431009  327 KPELESSF--THLDQGERLNLSCSIPGAPPANFTIQKEDTIVSQTQDFTKI------------ASKSDSGTYICTA 388
Cdd:pfam13927   1 KPVITVSPssVTVREGETVTLTCEATGSPPPTITWYKNGEPISSGSTRSRSlsgsnstltisnVTRSDAGTYTCVA 76

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530431009  506 SILSSKVVESGEDIVLQCAVNEGSGPITYKFYREKEGKPF-------YQMTSNATQAFWtkqKASKEQEGEYYCTAFnra 578
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPDVTWSKEGGTLIEslkvkhdNGRTTQSSLLIS---NVTKEDAGTYTCVVN--- 74

                          90
                  ....*....|..
gi 530431009  579 NHASSVPRSKIL 590
Cdd:pfam00047  75 NPGGSATLSTSL 86

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
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530431009 343 LNLSCSIPGAPPANFTIQKEDTIVSQTQDFTKI------------ASKSDSGTYICTA 388
Cdd:cd00096    1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRselgngtltisnVTLEDSGTYTCVA 58