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Conserved domains on  [gi|294997286|ref|NP_001005854|]
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uncharacterized protein LOC208166 [Mus musculus]

Protein Classification

Ig1_MRC-OX-2_like domain-containing protein( domain architecture ID 10146993)

Ig1_MRC-OX-2_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 14-121 1.36e-54

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


:

Pssm-ID: 409433  Cd Length: 108  Bit Score: 172.91  E-value: 1.36e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  14 RIKHNTYERAVLGGNISIFCNFTSLENVEQITWQKIQGSLPQNIGTYSHKYGEKILPPYVNRLQCKILEPSTYFMTIQGV 93
Cdd:cd05846    1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80

                         90       100
                 ....*....|....*....|....*...
gi 294997286  94 TFEDEACYKCLFNTFPHGSHGGQTCLTI 121
Cdd:cd05846   81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
 
Name Accession Description Interval E-value
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 14-121 1.36e-54

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 172.91  E-value: 1.36e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  14 RIKHNTYERAVLGGNISIFCNFTSLENVEQITWQKIQGSLPQNIGTYSHKYGEKILPPYVNRLQCKILEPSTYFMTIQGV 93
Cdd:cd05846    1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80

                         90       100
                 ....*....|....*....|....*...
gi 294997286  94 TFEDEACYKCLFNTFPHGSHGGQTCLTI 121
Cdd:cd05846   81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
IGv smart00406
Immunoglobulin V-Type;
28-105 8.14e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 48.92  E-value: 8.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286    28 NISIFCNFTSLENVE-QITWQK-IQGSLPQNIGTYSHKYGEKILPPYVNRLQC-KILEPSTYFMTIQGVTFEDEACYKCL 104
Cdd:smart00406   1 SVTLSCKFSGSTFSSyYVSWVRqPPGKGLEWLGYIGSNGSSYYQESYKGRFTIsKDTSKNDVSLTISNLRVEDTGTYYCA 80


                   .
gi 294997286   105 F 105
Cdd:smart00406  81 V 81
PHA02987 PHA02987
Ig domain OX-2-like protein; Provisional
 28-123 7.30e-05

Ig domain OX-2-like protein; Provisional


Pssm-ID: 165290 [Multi-domain]  Cd Length: 189  Bit Score: 42.93  E-value: 7.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  28 NISIFCNFTSLENVEQITWQKIQgslpQNIGTYShkygekILPPYV-NRLQCKILEPSTYFMT----IQGVTFEDEACYK 102
Cdd:PHA02987  32 NVKISCNKTSSFNSILITWKKNN----KTIAGYG------PCGPVIvDKFKNKIEYLSKSFNEstilIKNVSLKDNGCYT 101

                         90       100
                 ....*....|....*....|..
gi 294997286 103 CLFNTF-PHGSHGGQTCLTIIT 123
Cdd:PHA02987 102 CIFNTLlSKNNEKGVVCLNVTT 123
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 23-121 2.52e-04

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: 39.75  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286   23 AVLGGNISIFCNFTSLENVE--QITWQK-IQGSLPQNIGTYSHKYGEKILPP--YVNRlqcKILEPSTYFMTIQGVTFED 97
Cdd:pfam07686   8 VALGGSVTLPCTYSSSMSEAstSVYWYRqPPGKGPTFLIAYYSNGSEEGVKKgrFSGR---GDPSNGDGSLTIQNLTLSD 84

                          90       100
                  ....*....|....*....|....
gi 294997286   98 EACYKCLFNTFPHGSHGGQTCLTI 121
Cdd:pfam07686  85 SGTYTCAVIPSGEGVFGKGTRLTV 108
 
Name Accession Description Interval E-value
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 14-121 1.36e-54

First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of rat MRC OX-2 antigen (also known as CD200) and similar proteins. MRC OX-2 is a membrane glycoprotein expressed in a variety of lymphoid and non-lymphoid cells in rats. It has a similar broad distribution pattern in humans. MRC OX-2 may regulate myeloid cell activity. The protein has an extracellular portion containing two Ig-like domains, a transmembrane portion, and a cytoplasmic portion.


Pssm-ID: 409433  Cd Length: 108  Bit Score: 172.91  E-value: 1.36e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  14 RIKHNTYERAVLGGNISIFCNFTSLENVEQITWQKIQGSLPQNIGTYSHKYGEKILPPYVNRLQCKILEPSTYFMTIQGV 93
Cdd:cd05846    1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80

                         90       100
                 ....*....|....*....|....*...
gi 294997286  94 TFEDEACYKCLFNTFPHGSHGGQTCLTI 121
Cdd:cd05846   81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 13-121 6.95e-19

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: 80.18  E-value: 6.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  13 QRIKHNTYERAVLGGNISIFCNFTSLEN--VEQITWQKIQGSLPQNIGTYSHKYGEKILPPYVNRLQCKILEPSTYFMTI 90
Cdd:cd05718    1 QRVQVPTEVTGFLGGSVTLPCSLTSPGTtkITQVTWMKIGAGSSQNVAVFHPQYGPSVPNPYAERVEFLAARLGLRNATL 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 294997286  91 --QGVTFEDEACYKCLFNTFPHGSHGGQTCLTI 121
Cdd:cd05718   81 riRNLRVEDEGNYICEFATFPQGNRQGTTWLRV 113
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 13-122 7.84e-13

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.


Pssm-ID: 409469  Cd Length: 113  Bit Score: 63.83  E-value: 7.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  13 QRIKHNTYERAVLGGNISIFCNFT-SLENVE--QITWQKIQGSLPQNIGTYSHKYGEKILPPYVNRLQckILEPSTYFMT 89
Cdd:cd05886    1 QTVQVNDSMSGFIGTDVVLHCSFAnPLPSVKitQVTWQKSTNGSKQNVAIYNPSMGVSVLPPYRERVT--FLNPSFTDGT 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 294997286  90 IQ--GVTFEDEACYKCLFNTFPHGSHGGQTCLTII 122
Cdd:cd05886   79 IRlsRLELEDEGVYICEFATFPTGNRESQLNLTVM 113
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 22-121 3.27e-10

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409581  Cd Length: 112  Bit Score: 56.43  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  22 RAVLGGNISIFCNFTSLENVE---QITWQKIQGSlpQNIGTYSHKYGEKILPP----YVNRLQCKILEPSTyfMTIQGVT 94
Cdd:cd20989   10 RGFLGGSVTLPCHLLPPNMVThvsQVTWQRHDEH--GSVAVFHPKQGPSFPESerlsFVAARLGAELRNAS--LAMFGLR 85

                         90       100
                 ....*....|....*....|....*..
gi 294997286  95 FEDEACYKCLFNTFPHGSHGGQTCLTI 121
Cdd:cd20989   86 VEDEGNYTCEFATFPQGSRSGDTWLRV 112
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 23-122 8.95e-10

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family 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, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 55.33  E-value: 8.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  23 AVLGGNISIFCNFTSLENVEQITWQKIQGSLPQNIGTYSHKYGEKILPPYVNRLQCKILEPSTYFMTIQGVTFEDEACYK 102
Cdd:cd05887   11 AVWGKNVSLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHNVGFSDSGKYI 90

                         90       100
                 ....*....|....*....|
gi 294997286 103 CLFNTFPHGSHGGQTCLTII 122
Cdd:cd05887   91 CKAVTFPLGNAQSSTTVTVL 110
IGv smart00406
Immunoglobulin V-Type;
28-105 8.14e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 48.92  E-value: 8.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286    28 NISIFCNFTSLENVE-QITWQK-IQGSLPQNIGTYSHKYGEKILPPYVNRLQC-KILEPSTYFMTIQGVTFEDEACYKCL 104
Cdd:smart00406   1 SVTLSCKFSGSTFSSyYVSWVRqPPGKGLEWLGYIGSNGSSYYQESYKGRFTIsKDTSKNDVSLTISNLRVEDTGTYYCA 80


                   .
gi 294997286   105 F 105
Cdd:smart00406  81 V 81
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 23-122 8.95e-08

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: 49.51  E-value: 8.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  23 AVLGGNISIFCNF--TSLENVEQITWQKI-QGSLPQNIGTYSHKYGEKILPPYVNRLQCKI-LEPSTYFMTIQGVTFEDE 98
Cdd:cd05888    5 VVLGQDAKLPCFYrgDSGEQVGQVAWARVdAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPpPRPADGSVLLRNAVQADE 84

                         90       100
                 ....*....|....*....|....
gi 294997286  99 ACYKCLFNTFPHGSHGGQTCLTII 122
Cdd:cd05888   85 GEYECRVSTFPAGNFQAELRLRVL 108
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
 24-112 2.72e-05

First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of DNAX accessory molecule 1 (DNAM-1, also known as CD226). DNAM-1 is a transmembrane protein having two Ig-like domains. It is an adhesion molecule which plays a part in tumor-directed cytotoxicity and adhesion in natural killer (NK) cells and T lymphocytes. It has been shown to regulate the NK cell killing of several tumor types, including myeloma cells and ovarian carcinoma cells. DNAM-1 interacts specifically with poliovirus receptor (PVR; CD155) and nectin -2 (CD211), other members of the Ig superfamily. DNAM-1 is expressed in most peripheral T cells, NK cells, monocytes and a subset of B lymphocytes.


Pssm-ID: 409472  Cd Length: 111  Bit Score: 42.54  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  24 VLGGNISIFCNFTSLENVEQITWQKIQGSlPQNIGTYSHKYGEKILPPYVNRLQckILEPSTYFM----TIQGVTFEDEA 99
Cdd:cd05889   12 PLSENMSLECVYPSTGILTQVEWTKIGGQ-KDNIAVYHPTHGMHIRKPYAGRVY--FLNSTMASNnmslSFRNASEDDVG 88

                         90
                 ....*....|...
gi 294997286 100 CYKCLFNTFPHGS 112
Cdd:cd05889   89 YYSCSLYTYPQGS 101
PHA02987 PHA02987
Ig domain OX-2-like protein; Provisional
 28-123 7.30e-05

Ig domain OX-2-like protein; Provisional


Pssm-ID: 165290 [Multi-domain]  Cd Length: 189  Bit Score: 42.93  E-value: 7.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286  28 NISIFCNFTSLENVEQITWQKIQgslpQNIGTYShkygekILPPYV-NRLQCKILEPSTYFMT----IQGVTFEDEACYK 102
Cdd:PHA02987  32 NVKISCNKTSSFNSILITWKKNN----KTIAGYG------PCGPVIvDKFKNKIEYLSKSFNEstilIKNVSLKDNGCYT 101

                         90       100
                 ....*....|....*....|..
gi 294997286 103 CLFNTF-PHGSHGGQTCLTIIT 123
Cdd:PHA02987 102 CIFNTLlSKNNEKGVVCLNVTT 123
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 23-121 2.52e-04

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: 39.75  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286   23 AVLGGNISIFCNFTSLENVE--QITWQK-IQGSLPQNIGTYSHKYGEKILPP--YVNRlqcKILEPSTYFMTIQGVTFED 97
Cdd:pfam07686   8 VALGGSVTLPCTYSSSMSEAstSVYWYRqPPGKGPTFLIAYYSNGSEEGVKKgrFSGR---GDPSNGDGSLTIQNLTLSD 84

                          90       100
                  ....*....|....*....|....
gi 294997286   98 EACYKCLFNTFPHGSHGGQTCLTI 121
Cdd:pfam07686  85 SGTYTCAVIPSGEGVFGKGTRLTV 108
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 23-121 7.17e-04

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: 37.87  E-value: 7.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294997286    23 AVLGGNISIFCNFTSLENVeQITWQKIQGSLPQNIGTYSHKYgekilppyvnrlqckilEPSTYFMTIQGVTFEDEACYK 102
Cdd:smart00410   6 VKEGESVTLSCEASGSPPP-EVTWYKQGGKLLAESGRFSVSR-----------------SGSTSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*....
gi 294997286   103 CLFnTFPHGSHGGQTCLTI 121
Cdd:smart00410  68 CAA-TNSSGSASSGTTLTV 85
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 26-103 8.98e-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: 35.39  E-value: 8.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 294997286  26 GGNISIFCNFTSLENVEQITW-QKIQGSLPQNIGTYSHKyGEKILPPYVNRLQCKILEPSTYFMTIQGVTFEDEACYKC 103
Cdd:cd00099   13 GESVTLSCEVSSSFSSTYIYWyRQKPGQGPEFLIYLSSS-KGKTKGGVPGRFSGSRDGTSSFSLTISNLQPEDSGTYYC 90
 
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.
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