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Conserved domains on  [gi|297290801|ref|XP_001117305|]
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triggering receptor expressed on myeloid cells 2 isoform X1 [Macaca mulatta]

Protein Classification

immunoglobulin domain-containing family protein( domain architecture ID 34076)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 51-158 5.42e-18

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.


The actual alignment was detected with superfamily member cd05716:

Pssm-ID: 472250  Cd Length: 100  Bit Score: 76.67  E-value: 5.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297290801  51 TTVFQGVEGQSLQVSCPYDSmKHWGRRKAWCRQLGEKgpCQRVVSTHNLWllsflrrRNGSTAITDDTLGGTLTITLRNL 130
Cdd:cd05716    4 PEVVTGVEGGSVTIQCPYPP-KYASSRKYWCKWGSEG--CQTLVSSEGVV-------PGGRISLTDDPDNGVFTVTLNQL 73

                         90       100
                 ....*....|....*....|....*...
gi 297290801 131 QPHDAGFYQCQSlhGSEADTLRKVLVEV 158
Cdd:cd05716   74 RKEDAGWYWCGV--GDDGDRGLTVQVKL 99
 
Name Accession Description Interval E-value
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 51-158 5.42e-18

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 409381  Cd Length: 100  Bit Score: 76.67  E-value: 5.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297290801  51 TTVFQGVEGQSLQVSCPYDSmKHWGRRKAWCRQLGEKgpCQRVVSTHNLWllsflrrRNGSTAITDDTLGGTLTITLRNL 130
Cdd:cd05716    4 PEVVTGVEGGSVTIQCPYPP-KYASSRKYWCKWGSEG--CQTLVSSEGVV-------PGGRISLTDDPDNGVFTVTLNQL 73

                         90       100
                 ....*....|....*....|....*...
gi 297290801 131 QPHDAGFYQCQSlhGSEADTLRKVLVEV 158
Cdd:cd05716   74 RKEDAGWYWCGV--GDDGDRGLTVQVKL 99
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 52-159 1.27e-09

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 54.39  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297290801   52 TVFQGVEGQSLQVSCPY-DSMKHWGRRKAWCRQLGEKGPCQRVVSTHNLWLLSFLRRRngsTAITDDTLGGTLTITLRNL 130
Cdd:pfam07686   4 REVTVALGGSVTLPCTYsSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGR---FSGRGDPSNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
gi 297290801  131 QPHDAGFYQCQSLHGSEADTLRKVLVEVL 159
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKGTRLTVL 109
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 56-141 1.14e-03

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: 37.10  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297290801    56 GVEGQSLQVSCPYDSMKHWgrRKAWCRQLGEkgpcqrvvsthnlWLLSFLRrrngstaITDDTLGGTLTITLRNLQPHDA 135
Cdd:smart00410   6 VKEGESVTLSCEASGSPPP--EVTWYKQGGK-------------LLAESGR-------FSVSRSGSTSTLTISNVTPEDS 63


                   ....*.
gi 297290801   136 GFYQCQ 141
Cdd:smart00410  64 GTYTCA 69
 
Name Accession Description Interval E-value
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 51-158 5.42e-18

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.


Pssm-ID: 409381  Cd Length: 100  Bit Score: 76.67  E-value: 5.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297290801  51 TTVFQGVEGQSLQVSCPYDSmKHWGRRKAWCRQLGEKgpCQRVVSTHNLWllsflrrRNGSTAITDDTLGGTLTITLRNL 130
Cdd:cd05716    4 PEVVTGVEGGSVTIQCPYPP-KYASSRKYWCKWGSEG--CQTLVSSEGVV-------PGGRISLTDDPDNGVFTVTLNQL 73

                         90       100
                 ....*....|....*....|....*...
gi 297290801 131 QPHDAGFYQCQSlhGSEADTLRKVLVEV 158
Cdd:cd05716   74 RKEDAGWYWCGV--GDDGDRGLTVQVKL 99
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 52-159 1.27e-09

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 54.39  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297290801   52 TVFQGVEGQSLQVSCPY-DSMKHWGRRKAWCRQLGEKGPCQRVVSTHNLWLLSFLRRRngsTAITDDTLGGTLTITLRNL 130
Cdd:pfam07686   4 REVTVALGGSVTLPCTYsSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGR---FSGRGDPSNGDGSLTIQNL 80

                          90       100
                  ....*....|....*....|....*....
gi 297290801  131 QPHDAGFYQCQSLHGSEADTLRKVLVEVL 159
Cdd:pfam07686  81 TLSDSGTYTCAVIPSGEGVFGKGTRLTVL 109
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 56-141 1.14e-03

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: 37.10  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297290801    56 GVEGQSLQVSCPYDSMKHWgrRKAWCRQLGEkgpcqrvvsthnlWLLSFLRrrngstaITDDTLGGTLTITLRNLQPHDA 135
Cdd:smart00410   6 VKEGESVTLSCEASGSPPP--EVTWYKQGGK-------------LLAESGR-------FSVSRSGSTSTLTISNVTPEDS 63


                   ....*.
gi 297290801   136 GFYQCQ 141
Cdd:smart00410  64 GTYTCA 69
Ig_Semaphorin_C cd04979
Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are ...
 103-159 1.94e-03

Immunoglobulin (Ig)-like domain at the C-terminus of semaphorins; The members here are composed of the immunoglobulin (Ig)-like domain in semaphorins. Semaphorins are transmembrane protein that have important roles in a variety of tissues. Functionally, semaphorins were initially characterized for their importance in the development of the nervous system and in axonal guidance. Later they have been found to be important for the formation and functioning of the cardiovascular, endocrine, gastrointestinal, hepatic, immune, musculoskeletal, renal, reproductive, and respiratory systems. Semaphorins function through binding to their receptors and transmembrane semaphorins also serves as receptors themselves. Although molecular mechanism of semaphorins is poorly understood, the Ig-like domains may be involved in ligand binding or dimerization.


Pssm-ID: 409368  Cd Length: 88  Bit Score: 36.67  E-value: 1.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 297290801 103 SFLRRRNGSTAITDDTLGGTLTITLRNLQPHDAGFYQCQSLHGSEADTLRKVLVEVL 159
Cdd:cd04979   30 IHNGKKVPRYRSPRLVLKTERGLLIRSAQEADAGVYECHSGERVLGSTLRSVTLHVL 86
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 58-151 3.27e-03

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 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" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 36.54  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297290801  58 EGQSLQVSC------PYDSMkhwgrrkAWCRQLGEKGPcQRVVSthnlWLLSFLRRRNGS----TAITDDTLGGTLTITl 127
Cdd:cd00099   12 EGESVTLSCevsssfSSTYI-------YWYRQKPGQGP-EFLIY----LSSSKGKTKGGVpgrfSGSRDGTSSFSLTIS- 78

                         90       100
                 ....*....|....*....|....
gi 297290801 128 rNLQPHDAGFYQCQSLHGSEADTL 151
Cdd:cd00099   79 -NLQPEDSGTYYCAVSESGGTDKL 101
IGv smart00406
Immunoglobulin V-Type;
80-141 3.38e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 35.82  E-value: 3.38e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297290801    80 WCRQLGEKGP--CQRVVSTHNLWLLSFLRRRngsTAITDDTLGGTLTITLRNLQPHDAGFYQCQ 141
Cdd:smart00406  20 WVRQPPGKGLewLGYIGSNGSSYYQESYKGR---FTISKDTSKNDVSLTISNLRVEDTGTYYCA 80
 
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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