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Conserved domains on  [gi|528996626|ref|XP_005221013|]
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CMRF35-like molecule 9 isoform X9 [Bos taurus]

Protein Classification

immunoglobulin domain-containing protein( domain architecture ID 10146027)

immunoglobulin (Ig) domain-containing protein with one or more Ig domains, which adopt a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and/or pattern recognition; similar to polymeric immunoglobulin receptor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 20-119 2.24e-22

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: 88.22  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626  20 VNPKEISGFEGDTVSLQCTYEEELKKHQKYWCREAGLfisRCTGTVFSGEYGQEGRVSVHDNPRENRFTVILRNLTLKDR 99
Cdd:cd05716    2 VGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGSE---GCQTLVSSEGVVPGGRISLTDDPDNGVFTVTLNQLRKEDA 78

                         90       100
                 ....*....|....*....|.
gi 528996626 100 GKYLCGVK-RLGFDKTMSVSL 119
Cdd:cd05716   79 GWYWCGVGdDGDRGLTVQVKL 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 ...
 20-119 2.24e-22

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: 88.22  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626  20 VNPKEISGFEGDTVSLQCTYEEELKKHQKYWCREAGLfisRCTGTVFSGEYGQEGRVSVHDNPRENRFTVILRNLTLKDR 99
Cdd:cd05716    2 VGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGSE---GCQTLVSSEGVVPGGRISLTDDPDNGVFTVTLNQLRKEDA 78

                         90       100
                 ....*....|....*....|.
gi 528996626 100 GKYLCGVK-RLGFDKTMSVSL 119
Cdd:cd05716   79 GWYWCGVGdDGDRGLTVQVKL 99
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 20-106 1.09e-10

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: 57.47  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626   20 VNPKEISGFEGDTVSLQCTY-EEELKKHQ-KYWCREAGLFISRCTGTVFSGEYGQE---GRVSVHDNPRENRFTVILRNL 94
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYsSSMSEASTsVYWYRQPPGKGPTFLIAYYSNGSEEGvkkGRFSGRGDPSNGDGSLTIQNL 80

                          90
                  ....*....|..
gi 528996626   95 TLKDRGKYLCGV 106
Cdd:pfam07686  81 TLSDSGTYTCAV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 22-121 3.32e-08

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: 49.81  E-value: 3.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626    22 PKEISGFEGDTVSLQCTYEEElKKHQKYWCREAGLFISrctgtvfsgeygQEGRVSVHDNPreNRFTVILRNLTLKDRGK 101
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGS-PPPEVTWYKQGGKLLA------------ESGRFSVSRSG--STSTLTISNVTPEDSGT 65

                           90       100
                   ....*....|....*....|
gi 528996626   102 YLCGVKRLGFDKTMSVSLLV 121
Cdd:smart00410  66 YTCAATNSSGSASSGTTLTV 85
 
Name Accession Description Interval E-value
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 20-119 2.24e-22

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: 88.22  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626  20 VNPKEISGFEGDTVSLQCTYEEELKKHQKYWCREAGLfisRCTGTVFSGEYGQEGRVSVHDNPRENRFTVILRNLTLKDR 99
Cdd:cd05716    2 VGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGSE---GCQTLVSSEGVVPGGRISLTDDPDNGVFTVTLNQLRKEDA 78

                         90       100
                 ....*....|....*....|.
gi 528996626 100 GKYLCGVK-RLGFDKTMSVSL 119
Cdd:cd05716   79 GWYWCGVGdDGDRGLTVQVKL 99
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 20-106 1.09e-10

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: 57.47  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626   20 VNPKEISGFEGDTVSLQCTY-EEELKKHQ-KYWCREAGLFISRCTGTVFSGEYGQE---GRVSVHDNPRENRFTVILRNL 94
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYsSSMSEASTsVYWYRQPPGKGPTFLIAYYSNGSEEGvkkGRFSGRGDPSNGDGSLTIQNL 80

                          90
                  ....*....|..
gi 528996626   95 TLKDRGKYLCGV 106
Cdd:pfam07686  81 TLSDSGTYTCAV 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 22-121 3.32e-08

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: 49.81  E-value: 3.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626    22 PKEISGFEGDTVSLQCTYEEElKKHQKYWCREAGLFISrctgtvfsgeygQEGRVSVHDNPreNRFTVILRNLTLKDRGK 101
Cdd:smart00410   1 PPSVTVKEGESVTLSCEASGS-PPPEVTWYKQGGKLLA------------ESGRFSVSRSG--STSTLTISNVTPEDSGT 65

                           90       100
                   ....*....|....*....|
gi 528996626   102 YLCGVKRLGFDKTMSVSLLV 121
Cdd:smart00410  66 YTCAATNSSGSASSGTTLTV 85
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 22-119 6.07e-06

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: 43.34  E-value: 6.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626   22 PKEISGFEGDTVSLQCTYEEELKKHQKYWcreaglfisrctgtVFSGEYGQEGRVSVHDNPRENRFTVILRNLTLKDRGK 101
Cdd:pfam00047   3 PPTVTVLEGDSATLTCSASTGSPGPDVTW--------------SKEGGTLIESLKVKHDNGRTTQSSLLISNVTKEDAGT 68

                          90
                  ....*....|....*...
gi 528996626  102 YLCGVKRLGFDKTMSVSL 119
Cdd:pfam00047  69 YTCVVNNPGGSATLSTSL 86
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 20-104 5.98e-05

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 41.28  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626  20 VNPkEISGFEGDTVSLQCTYE--EELKKHQKYWCREAGLfiSRCTGTVFSGEYGqegrVSVHdNPRENRF---------- 87
Cdd:cd05718    5 VPT-EVTGFLGGSVTLPCSLTspGTTKITQVTWMKIGAG--SSQNVAVFHPQYG----PSVP-NPYAERVeflaarlglr 76

                         90
                 ....*....|....*....
gi 528996626  88 --TVILRNLTLKDRGKYLC 104
Cdd:cd05718   77 naTLRIRNLRVEDEGNYIC 95
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
 22-106 2.68e-04

Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the immunoglobulin variable (IgV) region of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also known 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. Like all members of this family, the CRIg domain contains two beta-sheets: one composed of strands A', G, F, C, C' and C", and the other of strands B, E and D. The complement system is an important part of the innate immune system and is required for removal of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles. It is also a potent 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.


Pssm-ID: 409510  Cd Length: 117  Bit Score: 39.43  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626  22 PKEISGFEGDTVSLQCTY--EEELKKHQKYWCREAGlfisRCTGTVF----SGEYGQE----GRVSV-HDNPREnrFTVI 90
Cdd:cd16089    6 PESITGPWKGSVNLPCTYvpEEGYTQVLVKWLVQRD----SDPVTIFlrdsSGDHIQQakyrGRLEVsKDTPGD--VSLQ 79

                         90
                 ....*....|....*.
gi 528996626  91 LRNLTLKDRGKYLCGV 106
Cdd:cd16089   80 LDTLEMDDRGHYTCQV 95
IgV_CD80 cd16086
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here ...
 31-121 6.82e-04

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 80). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as cluster of differentiation 152/CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. CD80 contains two Ig-like domains, an amino-terminal immunoglobulin variable (IgV)-like domain characteristic of adhesion molecules and a membrane proximal immunoglobulin constant (IgC)-like domain similar to the constant domains of antigen receptors. Members of the Ig family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and Major Histocompatibility Complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions.


Pssm-ID: 319335  Cd Length: 105  Bit Score: 38.20  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626  31 DTVSLQCTYE---EELKKHQKYWCREAGLFISRCTGTV-FSGEYGQEgrvSVHDNPreNRFTVILRNLTLKDRGKYLCGV 106
Cdd:cd16086   10 EKALLSCDYNvsvDELAQVRIYWQKDDKMVLTIISGDVkVWPEYKNR---TLFDIT--NNLSIVILALRLSDRGTYTCVV 84

                         90       100
                 ....*....|....*....|
gi 528996626 107 KRL--GFDKT---MSVSLLV 121
Cdd:cd16086   85 QKKerGAYKRehlASVTLSV 104
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
 19-107 2.07e-03

Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an extracellular Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin. This group also contains the Ig domain of sodium channel subunit beta-2 (SCN2B), and of epithelial V-like antigen 1 (EVA). EVA, also known as myelin protein zero-like 2, is an adhesion molecule, which may play a role in structural organization of the thymus and early lymphocyte development. SCN2B subunits play a role in determining sodium channel density and function in neurons,and in control of electrical excitability in the brain.


Pssm-ID: 409380  Cd Length: 117  Bit Score: 37.02  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626  19 VVNPKEISGFEGDTVSLQCTYEEELKKHQKY---W--------CREAGLFISRctGTVFSGEYGQEG-RVSVHDNPRENR 86
Cdd:cd05715    3 VYTPRELNVLNGSDVRLTCTFTSCYTVGDAFsvtWtyqpeggnTTESMFHYSK--GKPYILKVGRFKdRVSWAGNPSKKD 80

                         90       100
                 ....*....|....*....|.
gi 528996626  87 FTVILRNLTLKDRGKYLCGVK 107
Cdd:cd05715   81 ASIVISNLQFSDNGTYTCDVK 101
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 23-106 3.66e-03

First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-4 (also known as poliovirus receptor related protein 4 or LNIR receptor). Nectin-4 belongs to the nectin family, which is comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example nectin-4 trans-interacts with nectin-1. Nectin-4 has also been shown to interact with the actin filament-binding protein, afadin. Unlike the other nectins, which are widely expressed in adult tissues, nectin-4 is mainly expressed during embryogenesis, and is not detected in normal adult tissue or in serum. Nectin-4 is re-expressed in breast carcinoma, and patients having metastatic breast cancer have a circulating form of nectin-4 formed from the ectodomain


Pssm-ID: 409471  Cd Length: 108  Bit Score: 36.03  E-value: 3.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528996626  23 KEISGFEGDTVSLQCTY--EEELKKHQKYWCREAGLFISRCTGTVFSgEYGQ------EGRVSVHDNPRENRFTVILRNL 94
Cdd:cd05888    1 DVVTVVLGQDAKLPCFYrgDSGEQVGQVAWARVDAGEGAQEIALLHS-KYGLhvfpayEGRVEQPPPPRPADGSVLLRNA 79

                         90
                 ....*....|..
gi 528996626  95 TLKDRGKYLCGV 106
Cdd:cd05888   80 VQADEGEYECRV 91
 
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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