NCBI Conserved Domain Search

Conserved domains on [gi|2749266214|gb|XCA94950|]

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K14 [Human gammaherpesvirus 8]

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 ...

33-127

1.30e-31

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 cd05846:

Pssm-ID: 472250 Cd Length: 108 Bit Score: 112.82 E-value: 1.30e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  33 GSAALTCAITPRADIVSVTWQKRQLPGPVNVATYSHSYGVVVQTQYRHKANITCPGLWNSTLVIHNLAVDDEGCYLCIFN 112
Cdd:cd05846    14 GNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNVTLEDEGCYKCLFN 93

                          90
                  ....*....|....*
gi 2749266214 113 SFGGRQVSCTACLEV 127
Cdd:cd05846    94 TFPDGIKSGTACLTV 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; ...

33-127

1.30e-31

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: 112.82 E-value: 1.30e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  33 GSAALTCAITPRADIVSVTWQKRQLPGPVNVATYSHSYGVVVQTQYRHKANITCPGLWNSTLVIHNLAVDDEGCYLCIFN 112
Cdd:cd05846    14 GNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNVTLEDEGCYKCLFN 93

                          90
                  ....*....|....*
gi 2749266214 113 SFGGRQVSCTACLEV 127
Cdd:cd05846    94 TFPDGIKSGTACLTV 108

PHA02987

Ig domain OX-2-like protein; Provisional

37-130

6.10e-07

Ig domain OX-2-like protein; Provisional

Pssm-ID: 165290 [Multi-domain] Cd Length: 189 Bit Score: 48.71 E-value: 6.10e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  37 LTCAITPRADIVSVTWQKRQlpgpVNVATYSHSyGVVVQTQYRHKANITCPGLWNSTLVIHNLAVDDEGCYLCIFNSFGG 116
Cdd:PHA02987   35 ISCNKTSSFNSILITWKKNN----KTIAGYGPC-GPVIVDKFKNKIEYLSKSFNESTILIKNVSLKDNGCYTCIFNTLLS 109

                          90
                  ....*....|....*
gi 2749266214 117 RQV-SCTACLEVTSP 130
Cdd:PHA02987  110 KNNeKGVVCLNVTTD 124

IGv

smart00406

Immunoglobulin V-Type;

34-111

1.88e-06

Immunoglobulin V-Type;

Pssm-ID: 214650 Cd Length: 81 Bit Score: 45.07 E-value: 1.88e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214   34 SAALTCAITPRA-DIVSVTWQkRQLPG--PVNVATYSHSYGVVVQTQYRHKANITCPGLWNS-TLVIHNLAVDDEGCYLC 109
Cdd:smart00406   1 SVTLSCKFSGSTfSSYYVSWV-RQPPGkgLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDvSLTISNLRVEDTGTYYC 79


                   ..
gi 2749266214  110 IF 111
Cdd:smart00406  80 AV 81

I-set

pfam07679

Immunoglobulin I-set domain;

34-127

2.05e-04

Immunoglobulin I-set domain;

Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 39.55 E-value: 2.05e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  34 SAALTCAIT----PradivSVTWQKRqlpgpvnvatyshsyGVVVQTQYRHKanITCPGlWNSTLVIHNLAVDDEGCYLC 109
Cdd:pfam07679  17 SARFTCTVTgtpdP-----EVSWFKD---------------GQPLRSSDRFK--VTYEG-GTYTLTISNVQPDDSGKYTC 73

                          90
                  ....*....|....*....
gi 2749266214 110 IF-NSFGgrQVSCTACLEV 127
Cdd:pfam07679  74 VAtNSAG--EAEASAELTV 90

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; ...

33-127

1.30e-31

Pssm-ID: 409433 Cd Length: 108 Bit Score: 112.82 E-value: 1.30e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  33 GSAALTCAITPRADIVSVTWQKRQLPGPVNVATYSHSYGVVVQTQYRHKANITCPGLWNSTLVIHNLAVDDEGCYLCIFN 112
Cdd:cd05846    14 GNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNVTLEDEGCYKCLFN 93

                          90
                  ....*....|....*
gi 2749266214 113 SFGGRQVSCTACLEV 127
Cdd:cd05846    94 TFPDGIKSGTACLTV 108

IgV_1_PVR_like

cd05718

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...

27-122

5.68e-13

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: 64.01 E-value: 5.68e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  27 VQGPMRGSAALTCAITPRAD--IVSVTWQKRQLPGPVNVATYSHSYGVVVQTQYRHKANITCP--GLWNSTLVIHNLAVD 102
Cdd:cd05718     9 VTGFLGGSVTLPCSLTSPGTtkITQVTWMKIGAGSSQNVAVFHPQYGPSVPNPYAERVEFLAArlGLRNATLRIRNLRVE 88

                          90       100
                  ....*....|....*....|..
gi 2749266214 103 DEGCYLCIFNSF--GGRQVSCT 122
Cdd:cd05718    89 DEGNYICEFATFpqGNRQGTTW 110

IgV_1_Nectin-1_like

cd05886

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...

37-118

1.72e-09

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: 54.20 E-value: 1.72e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  37 LTCAIT---PRADIVSVTWQKRQLPGPVNVATYSHSYGVVVQTQYRHKANITCPGLWNSTLVIHNLAVDDEGCYLCIFNS 113
Cdd:cd05886    19 LHCSFAnplPSVKITQVTWQKSTNGSKQNVAIYNPSMGVSVLPPYRERVTFLNPSFTDGTIRLSRLELEDEGVYICEFAT 98


                  ....*..
gi 2749266214 114 F--GGRQ 118
Cdd:cd05886    99 FptGNRE 105

IgV_1_Nectin-3_like

cd05887

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...

36-122

2.73e-08

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: 50.70 E-value: 2.73e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  36 ALTCAITPRADIVSVTWQKRQLPGPVNVATYSHSYGVVVQTQYRHKANITCPGLWNSTLVIHNLAVDDEGCYLCIFNSF- 114
Cdd:cd05887    18 SLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHNVGFSDSGKYICKAVTFp 97


                  ....*....
gi 2749266214 115 -GGRQVSCT 122
Cdd:cd05887    98 lGNAQSSTT 106

IgV_1_Nectin-2_NecL-5_like_CD112_CD155

cd20989

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...

27-127

2.51e-07

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: 48.34 E-value: 2.51e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  27 VQGPMRGSAALTCAITPRADIVSV---TWQKRQLPGpvNVATYSHSYGVVVQTQYRHKANITCPG--LWNSTLVIHNLAV 101
Cdd:cd20989     9 VRGFLGGSVTLPCHLLPPNMVTHVsqvTWQRHDEHG--SVAVFHPKQGPSFPESERLSFVAARLGaeLRNASLAMFGLRV 86

                          90       100
                  ....*....|....*....|....*.
gi 2749266214 102 DDEGCYLCIFNSFGGRQVSCTACLEV 127
Cdd:cd20989    87 EDEGNYTCEFATFPQGSRSGDTWLRV 112

IgV_CRIg

cd16089

Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...

23-109

3.91e-07

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: 47.91 E-value: 3.91e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  23 GGARVQGPMRGSAALTCAITPRADI--VSVTWQKRQLPGPVNVATYSHSYGVVVQTQYRHKANIT--CPGlwNSTLVIHN 98
Cdd:cd16089     5 GPESITGPWKGSVNLPCTYVPEEGYtqVLVKWLVQRDSDPVTIFLRDSSGDHIQQAKYRGRLEVSkdTPG--DVSLQLDT 82

                          90
                  ....*....|.
gi 2749266214  99 LAVDDEGCYLC 109
Cdd:cd16089    83 LEMDDRGHYTC 93

PHA02987

Ig domain OX-2-like protein; Provisional

37-130

6.10e-07

Ig domain OX-2-like protein; Provisional

Pssm-ID: 165290 [Multi-domain] Cd Length: 189 Bit Score: 48.71 E-value: 6.10e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  37 LTCAITPRADIVSVTWQKRQlpgpVNVATYSHSyGVVVQTQYRHKANITCPGLWNSTLVIHNLAVDDEGCYLCIFNSFGG 116
Cdd:PHA02987   35 ISCNKTSSFNSILITWKKNN----KTIAGYGPC-GPVIVDKFKNKIEYLSKSFNESTILIKNVSLKDNGCYTCIFNTLLS 109

                          90
                  ....*....|....*
gi 2749266214 117 RQV-SCTACLEVTSP 130
Cdd:PHA02987  110 KNNeKGVVCLNVTTD 124

IGv

smart00406

Immunoglobulin V-Type;

34-111

1.88e-06

Immunoglobulin V-Type;

Pssm-ID: 214650 Cd Length: 81 Bit Score: 45.07 E-value: 1.88e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214   34 SAALTCAITPRA-DIVSVTWQkRQLPG--PVNVATYSHSYGVVVQTQYRHKANITCPGLWNS-TLVIHNLAVDDEGCYLC 109
Cdd:smart00406   1 SVTLSCKFSGSTfSSYYVSWV-RQPPGkgLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDvSLTISNLRVEDTGTYYC 79


                   ..
gi 2749266214  110 IF 111
Cdd:smart00406  80 AV 81

PHA02982

hypothetical protein; Provisional

25-149

4.62e-05

hypothetical protein; Provisional

Pssm-ID: 165285 [Multi-domain] Cd Length: 251 Bit Score: 43.55 E-value: 4.62e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  25 ARVQGPMRGSAALTCaITPRAD-IVSVTWQKRQ--LPGPVNVATYSHSYGVVVQTQYRHKANITCPGLwNSTLVIHNLAV 101
Cdd:PHA02982   32 ADVNATVDQEVKLQC-LFKDADeISRAMWKGDAgfMLAQEANGGTGINAFNYVPGPYKDKYALSVSGN-SSTFTMKKPDP 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2749266214 102 DDEGCYLCIFNSFGGRQVSCTACLEVTSPPTGHVqVNSTEDADTVTCL 149
Cdd:PHA02982  110 QNLGCFTCEAKDAEGKEETCEKCLEIQKEDILYV-VEEHNNETIITCF 156

I-set

pfam07679

Immunoglobulin I-set domain;

34-127

2.05e-04

Immunoglobulin I-set domain;

Pssm-ID: 400151 [Multi-domain] Cd Length: 90 Bit Score: 39.55 E-value: 2.05e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  34 SAALTCAIT----PradivSVTWQKRqlpgpvnvatyshsyGVVVQTQYRHKanITCPGlWNSTLVIHNLAVDDEGCYLC 109
Cdd:pfam07679  17 SARFTCTVTgtpdP-----EVSWFKD---------------GQPLRSSDRFK--VTYEG-GTYTLTISNVQPDDSGKYTC 73

                          90
                  ....*....|....*....
gi 2749266214 110 IF-NSFGgrQVSCTACLEV 127
Cdd:pfam07679  74 VAtNSAG--EAEASAELTV 90

V-set

pfam07686

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

33-109

6.08e-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: 38.59 E-value: 6.08e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  33 GSAALTCAITPRA--DIVSVTWQKRQLP-GPVNVATYSHSYGVVVQTQYRHKANiTCPGLWNSTLVIHNLAVDDEGCYLC 109
Cdd:pfam07686  12 GSVTLPCTYSSSMseASTSVYWYRQPPGkGPTFLIAYYSNGSEEGVKKGRFSGR-GDPSNGDGSLTIQNLTLSDSGTYTC 90

IgV_1_DNAM-1_like

cd05889

First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...

37-114

9.14e-04

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: 37.92 E-value: 9.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  37 LTCAITPRADIVSVTWQKrqLPG-PVNVATYSHSYGVVVQTQYRHKANI--TCPGLWNSTLVIHNLAVDDEGCYLCIFNS 113
Cdd:cd05889    19 LECVYPSTGILTQVEWTK--IGGqKDNIAVYHPTHGMHIRKPYAGRVYFlnSTMASNNMSLSFRNASEDDVGYYSCSLYT 96


                  .
gi 2749266214 114 F 114
Cdd:cd05889    97 Y 97

cd00096

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...

37-123

9.69e-03

Pssm-ID: 409353 [Multi-domain] Cd Length: 70 Bit Score: 34.23 E-value: 9.69e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2749266214  37 LTCAITPRADiVSVTWQKRQLPGPVNVATYSHSYGvvvqtqyrhkanitcpglWNSTLVIHNLAVDDEGCYLCIFNSFGG 116
Cdd:cd00096     3 LTCSASGNPP-PTITWYKNGKPLPPSSRDSRRSEL------------------GNGTLTISNVTLEDSGTYTCVASNSAG 63


                  ....*..
gi 2749266214 117 RQVSCTA 123
Cdd:cd00096    64 GSASASV 70

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