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Conserved domains on  [gi|47207698|emb|CAF89861|]
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unnamed protein product [Tetraodon nigroviridis]

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 ...
 155-255 1.74e-20

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: 84.76  E-value: 1.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47207698 155 RCQTQAQTVKTAAGETVPCDPPRWGAMSELFFCKENSNTCAEMLSTRSSERT-IGSFTLKETDGNFSIFISQASSRDNGV 233
Cdd:cd05716   1 SVGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGSEGCQTLVSSEGVVPGgRISLTDDPDNGVFTVTLNQLRKEDAGW 80

                        90       100
                ....*....|....*....|..
gi 47207698 234 YWCASKTELYRagLQKITIKVK 255
Cdd:cd05716  81 YWCGVGDDGDR--GLTVQVKLV 100
 
Name Accession Description Interval E-value
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 155-255 1.74e-20

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: 84.76  E-value: 1.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47207698 155 RCQTQAQTVKTAAGETVPCDPPRWGAMSELFFCKENSNTCAEMLSTRSSERT-IGSFTLKETDGNFSIFISQASSRDNGV 233
Cdd:cd05716   1 SVGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGSEGCQTLVSSEGVVPGgRISLTDDPDNGVFTVTLNQLRKEDAGW 80

                        90       100
                ....*....|....*....|..
gi 47207698 234 YWCASKTELYRagLQKITIKVK 255
Cdd:cd05716  81 YWCGVGDDGDR--GLTVQVKLV 100
 
Name Accession Description Interval E-value
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 155-255 1.74e-20

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: 84.76  E-value: 1.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47207698 155 RCQTQAQTVKTAAGETVPCDPPRWGAMSELFFCKENSNTCAEMLSTRSSERT-IGSFTLKETDGNFSIFISQASSRDNGV 233
Cdd:cd05716   1 SVGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGSEGCQTLVSSEGVVPGgRISLTDDPDNGVFTVTLNQLRKEDAGW 80

                        90       100
                ....*....|....*....|..
gi 47207698 234 YWCASKTELYRagLQKITIKVK 255
Cdd:cd05716  81 YWCGVGDDGDR--GLTVQVKLV 100
 
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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