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Conserved domains on  [gi|1622900910|ref|XP_028699106|]
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OX-2 membrane glycoprotein isoform X5 [Macaca mulatta]

Protein Classification

Ig1_MRC-OX-2_like and ig domain-containing protein( domain architecture ID 10861887)

Ig1_MRC-OX-2_like and ig 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; ...
25-132 9.63e-58

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: 179.46  E-value: 9.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  25 VQVVTQDEREQLYTPASLRCSLQNAQEVLIVTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNTTITFWNI 104
Cdd:cd05846     1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80
                          90       100
                  ....*....|....*....|....*...
gi 1622900910 105 TLEDEGCYMCLFNTFGSGKISGTACLTV 132
Cdd:cd05846    81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
136-213 8.16e-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: 8.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900910 136 PIVSLHYKYSEDHLNITCSA-TARPAPMIFWKVPRSGFENSTVTlSHPNGTTSVTSILHVKDPKNQVGkEVICQVLHLG 213
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKV-KHDNGRTTQSSLLISNVTKEDAG-TYTCVVNNPG 77
 
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; ...
25-132 9.63e-58

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: 179.46  E-value: 9.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  25 VQVVTQDEREQLYTPASLRCSLQNAQEVLIVTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNTTITFWNI 104
Cdd:cd05846     1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80
                          90       100
                  ....*....|....*....|....*...
gi 1622900910 105 TLEDEGCYMCLFNTFGSGKISGTACLTV 132
Cdd:cd05846    81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
IGv smart00406
Immunoglobulin V-Type;
40-116 1.75e-09

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 53.15  E-value: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910   40 ASLRCSL-QNAQEVLIVTWQKKK-AVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNT-TITFWNITLEDEGCYMCLF 116
Cdd:smart00406   2 VTLSCKFsGSTFSSYYVSWVRQPpGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDvSLTISNLRVEDTGTYYCAV 81
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
40-129 2.44e-07

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: 47.57  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  40 ASLRCSLQNAQEVLIVTWQKKKAVSPENMvtfsenhgvviqpaykdKINITQLGLQNTTITFWNITLEDEGCYMCLFNTF 119
Cdd:pfam00047  14 ATLTCSASTGSPGPDVTWSKEGGTLIESL-----------------KVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNP 76
                          90
                  ....*....|
gi 1622900910 120 GSGKISGTAC 129
Cdd:pfam00047  77 GGSATLSTSL 86
PHA02987 PHA02987
Ig domain OX-2-like protein; Provisional
36-132 3.60e-07

Ig domain OX-2-like protein; Provisional


Pssm-ID: 165290 [Multi-domain]  Cd Length: 189  Bit Score: 49.09  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  36 LYTPASLRCSLQNAQEVLIVTWQKKKavspENMVTFSEnHGVVIQPAYKDKINITQLGLQNTTITFWNITLEDEGCYMCL 115
Cdd:PHA02987   29 EHVNVKISCNKTSSFNSILITWKKNN----KTIAGYGP-CGPVIVDKFKNKIEYLSKSFNESTILIKNVSLKDNGCYTCI 103
                          90
                  ....*....|....*...
gi 1622900910 116 FNTFGS-GKISGTACLTV 132
Cdd:PHA02987  104 FNTLLSkNNEKGVVCLNV 121
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
136-213 8.16e-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: 8.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900910 136 PIVSLHYKYSEDHLNITCSA-TARPAPMIFWKVPRSGFENSTVTlSHPNGTTSVTSILHVKDPKNQVGkEVICQVLHLG 213
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKV-KHDNGRTTQSSLLISNVTKEDAG-TYTCVVNNPG 77
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
152-222 2.51e-05

Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. 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), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while 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" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111.


Pssm-ID: 409384  Cd Length: 96  Bit Score: 42.09  E-value: 2.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900910 152 TC-SATARPAPMIFWKVpRSGFENSTVTLSHPNGTTSVTSILHVKDPKNQVGKEVICQVLHLGTVTDFKQTF 222
Cdd:cd05719    22 TCiSANGKPPASVTWET-DLKGEASTTQVRGSNGTVTVTSRYRLVPSREADGQPLTCVVEHPSLEKDQRISV 92
PHA03376 PHA03376
BARF1; Provisional
106-197 7.82e-03

BARF1; Provisional


Pssm-ID: 177613  Cd Length: 221  Bit Score: 36.61  E-value: 7.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910 106 LEDEGCYMCLFNtFGSGKISGTACLTVyVQPI-VSLHYKYSE----DHLNITCSATARPAPMIFWKVPRSGFENSTVT-- 178
Cdd:PHA03376   96 ISHDGNYLCRMK-LGETEVTKQEHLSV-VKPLtLSVHSERSQfpdfSVLTVTCTVNAFPHPHVQWLMPEGVEPAPTAAng 173
                          90       100
                  ....*....|....*....|.
gi 1622900910 179 --LSHPNGTTSVTSILHVKDP 197
Cdd:PHA03376  174 gvMKEKDGSLSVAVDLSLPKP 194
 
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; ...
25-132 9.63e-58

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: 179.46  E-value: 9.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  25 VQVVTQDEREQLYTPASLRCSLQNAQEVLIVTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNTTITFWNI 104
Cdd:cd05846     1 VVVHTGDTRAVLGGNATLSCNLTLPEEVLQVTWQKIKASSPENIVTYSKKYGVKIQPSYVRRISFTSSGLNSTSITIWNV 80
                          90       100
                  ....*....|....*....|....*...
gi 1622900910 105 TLEDEGCYMCLFNTFGSGKISGTACLTV 132
Cdd:cd05846    81 TLEDEGCYKCLFNTFPDGIKSGTACLTV 108
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
24-132 6.99e-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: 79.41  E-value: 6.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  24 QVQVVTQdEREQLYTPASLRCSLQNAQEVLI--VTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINIT--QLGLQNTTI 99
Cdd:cd05718     2 RVQVPTE-VTGFLGGSVTLPCSLTSPGTTKItqVTWMKIGAGSSQNVAVFHPQYGPSVPNPYAERVEFLaaRLGLRNATL 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622900910 100 TFWNITLEDEGCYMCLFNTFGSGKISGTACLTV 132
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 ...
26-133 3.26e-15

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: 69.99  E-value: 3.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  26 QVVTQDEREQLY--TPASLRCSLQNAQ---EVLIVTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNTTIT 100
Cdd:cd05886     1 QTVQVNDSMSGFigTDVVLHCSFANPLpsvKITQVTWQKSTNGSKQNVAIYNPSMGVSVLPPYRERVTFLNPSFTDGTIR 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622900910 101 FWNITLEDEGCYMCLFNTFGSGKISGTACLTVY 133
Cdd:cd05886    81 LSRLELEDEGVYICEFATFPTGNRESQLNLTVM 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 ...
25-132 6.42e-11

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: 57.97  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  25 VQVVTQdEREQLYTPASLRCSLQ---NAQEVLIVTWQKKKavSPENMVTFSENHGVVIQPAYKDKINITQLG--LQNTTI 99
Cdd:cd20989     3 VQVPPE-VRGFLGGSVTLPCHLLppnMVTHVSQVTWQRHD--EHGSVAVFHPKQGPSFPESERLSFVAARLGaeLRNASL 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622900910 100 TFWNITLEDEGCYMCLFNTFGSGKISGTACLTV 132
Cdd:cd20989    80 AMFGLRVEDEGNYTCEFATFPQGSRSGDTWLRV 112
IGv smart00406
Immunoglobulin V-Type;
40-116 1.75e-09

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 53.15  E-value: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910   40 ASLRCSL-QNAQEVLIVTWQKKK-AVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNT-TITFWNITLEDEGCYMCLF 116
Cdd:smart00406   2 VTLSCKFsGSTFSSYYVSWVRQPpGKGLEWLGYIGSNGSSYYQESYKGRFTISKDTSKNDvSLTISNLRVEDTGTYYCAV 81
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
40-129 2.44e-07

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: 47.57  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  40 ASLRCSLQNAQEVLIVTWQKKKAVSPENMvtfsenhgvviqpaykdKINITQLGLQNTTITFWNITLEDEGCYMCLFNTF 119
Cdd:pfam00047  14 ATLTCSASTGSPGPDVTWSKEGGTLIESL-----------------KVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNP 76
                          90
                  ....*....|
gi 1622900910 120 GSGKISGTAC 129
Cdd:pfam00047  77 GGSATLSTSL 86
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
41-132 2.62e-07

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: 48.01  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  41 SLRCSLQNAQEVLIVTWQKKKAVSPENMVTFSENHGVVIQPAYKDKINITQLGLQNTTITFWNITLEDEGCYMCLFNTFG 120
Cdd:cd05887    18 SLKCLIEVNETITQISWEKIHGKSSQTVAVHHPQYGISIQGEYQGRVSFKNYSLNDATITLHNVGFSDSGKYICKAVTFP 97
                          90
                  ....*....|..
gi 1622900910 121 SGKISGTACLTV 132
Cdd:cd05887    98 LGNAQSSTTVTV 109
PHA02987 PHA02987
Ig domain OX-2-like protein; Provisional
36-132 3.60e-07

Ig domain OX-2-like protein; Provisional


Pssm-ID: 165290 [Multi-domain]  Cd Length: 189  Bit Score: 49.09  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  36 LYTPASLRCSLQNAQEVLIVTWQKKKavspENMVTFSEnHGVVIQPAYKDKINITQLGLQNTTITFWNITLEDEGCYMCL 115
Cdd:PHA02987   29 EHVNVKISCNKTSSFNSILITWKKNN----KTIAGYGP-CGPVIVDKFKNKIEYLSKSFNESTILIKNVSLKDNGCYTCI 103
                          90
                  ....*....|....*...
gi 1622900910 116 FNTFGS-GKISGTACLTV 132
Cdd:PHA02987  104 FNTLLSkNNEKGVVCLNV 121
IgV_1_DNAM-1_like cd05889
First immunoglobulin variable (IgV) domain of DNAX accessory molecule 1, and similar domains; ...
41-122 4.21e-06

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: 44.47  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  41 SLRCSLQNAQEVLIVTWQKKKAVSpENMVTFSENHGVVIQPAYKDKINI--TQLGLQNTTITFWNITLEDEGCYMCLFNT 118
Cdd:cd05889    18 SLECVYPSTGILTQVEWTKIGGQK-DNIAVYHPTHGMHIRKPYAGRVYFlnSTMASNNMSLSFRNASEDDVGYYSCSLYT 96

                  ....
gi 1622900910 119 FGSG 122
Cdd:cd05889    97 YPQG 100
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
136-213 8.16e-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: 8.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900910 136 PIVSLHYKYSEDHLNITCSA-TARPAPMIFWKVPRSGFENSTVTlSHPNGTTSVTSILHVKDPKNQVGkEVICQVLHLG 213
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGTLIESLKV-KHDNGRTTQSSLLISNVTKEDAG-TYTCVVNNPG 77
IgC1_2_PVR_like cd05719
Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), ...
152-222 2.51e-05

Second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and Necl-5), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (Necl-5)) and similar proteins. 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), these result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted, while 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" and has a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the second Ig-like domain of nectin-1, also known as poliovirus receptor related protein(PVRL)1 or CD111.


Pssm-ID: 409384  Cd Length: 96  Bit Score: 42.09  E-value: 2.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900910 152 TC-SATARPAPMIFWKVpRSGFENSTVTLSHPNGTTSVTSILHVKDPKNQVGKEVICQVLHLGTVTDFKQTF 222
Cdd:cd05719    22 TCiSANGKPPASVTWET-DLKGEASTTQVRGSNGTVTVTSRYRLVPSREADGQPLTCVVEHPSLEKDQRISV 92
IgC1_2_Nectin-2_Necl-5_like cd07703
Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; ...
152-211 1.59e-04

Second immunoglobulin (Ig) domain of Nectin-2 and Nectin-like protein 5, and similar domains; member of the C1-set of the Ig superfamily (IgSF) 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: 409500  Cd Length: 97  Bit Score: 39.69  E-value: 1.59e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900910 152 TC-SATARPAPMIFWKVPRSGFENSTVTLSHPNGTTSVTSILHVKdPKNQV-GKEVICQVLH 211
Cdd:cd07703    21 RCvSANGRPPARISWSSTLNGNANTTQVPGPDSGTVTVTSEYSLV-PTPEAnGKEVTCKVEH 81
IgC1_2_Nectin-3-4_like cd07704
Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related ...
152-222 2.68e-04

Second immunoglobulin (Ig) domain of nectin-3 and nectin-4 (poliovirus receptor related protein 4), and similar domains; member of the C1-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 or cluster of differentiation (CD) 113) and nectin-4 (poliovirus receptor related protein 4). Nectin-3 and nectin-4 belong to the nectin family comprised of four transmembrane glycoproteins (nectin-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. 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. Nectin-3 has also been shown to form a heterophilic trans-interaction with nectin-1 in ciliary epithelia, establishing the apex-apex adhesion between the pigment and non-pigment cell layers. Nectin-4 has recently been identified in several types of breast carcinoma and can be used as a histological and serological marker for breast cancer.


Pssm-ID: 409501  Cd Length: 96  Bit Score: 39.03  E-value: 2.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622900910 152 TCSA-TARPAPMIFWKVPRSGFEnSTVTLSHPNgTTSVTSILHVKDPKNQVGKEVICQVLHLGTVTDFKQTF 222
Cdd:cd07704    23 SCTAeTGKPAASVTWETDLGGME-SSRTFEHNR-TATVTSEYHLVPTRFANGRPLTCVVSHPALQQDIRITH 92
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
64-132 3.39e-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: 38.64  E-value: 3.39e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900910   64 SPENMVTFSENHGVVIqpAYKDKINITQLGlQNTTITFWNITLEDEGCYMCLFnTFGSGKISGTACLTV 132
Cdd:smart00410  21 SPPPEVTWYKQGGKLL--AESGRFSVSRSG-STSTLTISNVTPEDSGTYTCAA-TNSSGSASSGTTLTV 85
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
28-135 6.11e-04

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. 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. The first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.


Pssm-ID: 409538  Cd Length: 102  Bit Score: 38.29  E-value: 6.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  28 VTQDERE---QLYTPASLRCSLQNAQEVLIVTWQK-KKAVSpenMVTFSENHgvvIQPAYKDKINITqlglqNTTITFWN 103
Cdd:cd20946     2 VPSSQQVvtvVENQEVILSCKTPKKTSSPRVEWKKlQRDVT---FVVFQNNK---IQGDYKGRAEIL-----GTNITIKN 70
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622900910 104 ITLEDEGCYMCLFNTFGSGKISGTACLTVYVQ 135
Cdd:cd20946    71 VTRSDSGKYRCEVSARSDGQNLGEVTVTLEVL 102
PHA02982 PHA02982
hypothetical protein; Provisional
24-167 2.66e-03

hypothetical protein; Provisional


Pssm-ID: 165285 [Multi-domain]  Cd Length: 251  Bit Score: 38.15  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  24 QVQVVTQDEREQLYTPASLRCSLQNAQEVLIVTWQKKK--AVSPENMVTFSENHGVVIQPAYKDKINITQLGlQNTTITF 101
Cdd:PHA02982   26 DLKEDTADVNATVDQEVKLQCLFKDADEISRAMWKGDAgfMLAQEANGGTGINAFNYVPGPYKDKYALSVSG-NSSTFTM 104
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622900910 102 WNITLEDEGCYMCLFNTFGSGKISGTACLTVYVQPIVSLhykySEDHLN---ITCSATARPAPMIFWKV 167
Cdd:PHA02982  105 KKPDPQNLGCFTCEAKDAEGKEETCEKCLEIQKEDILYV----VEEHNNetiITCFVGSKHGDVPRFIV 169
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
38-133 3.99e-03

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: 36.28  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910  38 TPASLRCSLQN--AQEVLIVTWQKKKA-VSPENMVTFSENHGVviQPAYKDKINITQLGLQ-NTTITFWNITLEDEGCYM 113
Cdd:pfam07686  12 GSVTLPCTYSSsmSEASTSVYWYRQPPgKGPTFLIAYYSNGSE--EGVKKGRFSGRGDPSNgDGSLTIQNLTLSDSGTYT 89
                          90       100
                  ....*....|....*....|
gi 1622900910 114 CLFNTFGSGKISGTACLTVY 133
Cdd:pfam07686  90 CAVIPSGEGVFGKGTRLTVL 109
PHA03376 PHA03376
BARF1; Provisional
106-197 7.82e-03

BARF1; Provisional


Pssm-ID: 177613  Cd Length: 221  Bit Score: 36.61  E-value: 7.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622900910 106 LEDEGCYMCLFNtFGSGKISGTACLTVyVQPI-VSLHYKYSE----DHLNITCSATARPAPMIFWKVPRSGFENSTVT-- 178
Cdd:PHA03376   96 ISHDGNYLCRMK-LGETEVTKQEHLSV-VKPLtLSVHSERSQfpdfSVLTVTCTVNAFPHPHVQWLMPEGVEPAPTAAng 173
                          90       100
                  ....*....|....*....|.
gi 1622900910 179 --LSHPNGTTSVTSILHVKDP 197
Cdd:PHA03376  174 gvMKEKDGSLSVAVDLSLPKP 194
 
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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