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Conserved domains on  [gi|2842765|sp|Q99795|]
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RecName: Full=Cell surface A33 antigen; AltName: Full=Glycoprotein A33; Flags: Precursor

Protein Classification

V-set and Ig domain-containing protein (domain architecture ID 11169091)

V-set and Ig domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
26-138 7.96e-21

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


:

Pssm-ID: 400157  Cd Length: 109  Bit Score: 85.59  E-value: 7.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765     26 TPQDVLRASQGKSVTLPCTYHTSTSSREGLIQWDKLLLTHTERVVIWPFSNKNyiHGELYKNRVSISNNAEQSDASITID 105
Cdd:pfam07686   1 QTPRSVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGS--EEGKKKGRFSLRGDPSNSDGSLTIQ 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2842765    106 QLTMADNGTYECSVslMSDLEGNTKSRVRLLVL 138
Cdd:pfam07686  79 NLTLSDSGTYTCAV--IPSGEGVFGKGTRLTVL 109
IGc2 smart00408
Immunoglobulin C-2 Type;
154-218 4.61e-09

Immunoglobulin C-2 Type;


:

Pssm-ID: 197706  Cd Length: 63  Bit Score: 52.02  E-value: 4.61e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2842765     154 IGNNIQLTCQsKEGSPTPQYSWKRYNILNQEqPLAQPASGQPVSLKNISTDTSGYYICTSSNEEG 218
Cdd:smart00408   1 EGQSVTLTCP-AEGNPVPNITWLKDGKPLPE-SNRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
 
Name Accession Description Interval E-value
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
26-138 7.96e-21

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 400157  Cd Length: 109  Bit Score: 85.59  E-value: 7.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765     26 TPQDVLRASQGKSVTLPCTYHTSTSSREGLIQWDKLLLTHTERVVIWPFSNKNyiHGELYKNRVSISNNAEQSDASITID 105
Cdd:pfam07686   1 QTPRSVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGS--EEGKKKGRFSLRGDPSNSDGSLTIQ 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2842765    106 QLTMADNGTYECSVslMSDLEGNTKSRVRLLVL 138
Cdd:pfam07686  79 NLTLSDSGTYTCAV--IPSGEGVFGKGTRLTVL 109
IGv smart00406
Immunoglobulin V-Type;
38-119 1.83e-14

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 67.41  E-value: 1.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765      38 SVTLPCTYHTSTSSREGlIQW-DKLLLTHTERVVIWPFSNKNYIHGElYKNRVSISNNAEQSDASITIDQLTMADNGTYE 116
Cdd:smart00406   1 SVTLSCKFSGSTFSSYY-VSWvRQPPGKGLEWLGYIGSNGSSYYQES-YKGRFTISKDTSKNDVSLTISNLRVEDTGTYY 78

                   ...
gi 2842765     117 CSV 119
Cdd:smart00406  79 CAV 81
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
22-119 1.45e-10

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 57.46  E-value: 1.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   22 ISVETPQDVLRASQGKSVTLPCTYHTSTSSREGL-IQWDKLLLTHTERVVIWPFSNKNYIH-GELYKNRVSISNNAEQSD 99
Cdd:cd20960   1 LLITSAQTEIKKVAGENVTLPCHHQLGLEDQGTLdIEWLLLPSDKVEKVVITYSGDRVYNHyYPALKGRVAFTSNDLSGD 80
                        90       100
                ....*....|....*....|
gi 2842765  100 ASITIDQLTMADNGTYECSV 119
Cdd:cd20960  81 ASLNISNLKLSDTGTYQCKV 100
IGc2 smart00408
Immunoglobulin C-2 Type;
154-218 4.61e-09

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 52.02  E-value: 4.61e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2842765     154 IGNNIQLTCQsKEGSPTPQYSWKRYNILNQEqPLAQPASGQPVSLKNISTDTSGYYICTSSNEEG 218
Cdd:smart00408   1 EGQSVTLTCP-AEGNPVPNITWLKDGKPLPE-SNRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
153-216 2.24e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. 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. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562  Cd Length: 92  Bit Score: 45.19  E-value: 2.24e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2842765  153 IIGNNIQLTCQSkEGSPTPQYSWKRYNILNQE--QPLAQPASGQPVSLKNISTDTSGYYICTSSNE 216
Cdd:cd20970  15 REGENATFMCRA-EGSPEPEISWTRNGNLIIEfnTRYIVRENGTTLTIRNIRRSDMGIYLCIASNG 79
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
143-215 2.83e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 404760  Cd Length: 79  Bit Score: 44.44  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765    143 KPECGIEGETII---GNNIQLTCQSkEGSPTPQYSWKRYNILNQEQPLAQPASGQPVS----LKNISTDTSGYYICTSSN 215
Cdd:pfam13927   1 KPVITVSPSSVVvveGESVTLTCEA-TGGPPPTITWYKNGEEILSGSTSDRISLSGSNstltISNVTRSDSGTYTCVASN 79
 
Name Accession Description Interval E-value
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
26-138 7.96e-21

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 400157  Cd Length: 109  Bit Score: 85.59  E-value: 7.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765     26 TPQDVLRASQGKSVTLPCTYHTSTSSREGLIQWDKLLLTHTERVVIWPFSNKNyiHGELYKNRVSISNNAEQSDASITID 105
Cdd:pfam07686   1 QTPRSVTVALGGSVTLPCTYSSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGS--EEGKKKGRFSLRGDPSNSDGSLTIQ 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2842765    106 QLTMADNGTYECSVslMSDLEGNTKSRVRLLVL 138
Cdd:pfam07686  79 NLTLSDSGTYTCAV--IPSGEGVFGKGTRLTVL 109
IGv smart00406
Immunoglobulin V-Type;
38-119 1.83e-14

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 67.41  E-value: 1.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765      38 SVTLPCTYHTSTSSREGlIQW-DKLLLTHTERVVIWPFSNKNYIHGElYKNRVSISNNAEQSDASITIDQLTMADNGTYE 116
Cdd:smart00406   1 SVTLSCKFSGSTFSSYY-VSWvRQPPGKGLEWLGYIGSNGSSYYQES-YKGRFTISKDTSKNDVSLTISNLRVEDTGTYY 78

                   ...
gi 2842765     117 CSV 119
Cdd:smart00406  79 CAV 81
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
22-119 1.45e-10

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 57.46  E-value: 1.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   22 ISVETPQDVLRASQGKSVTLPCTYHTSTSSREGL-IQWDKLLLTHTERVVIWPFSNKNYIH-GELYKNRVSISNNAEQSD 99
Cdd:cd20960   1 LLITSAQTEIKKVAGENVTLPCHHQLGLEDQGTLdIEWLLLPSDKVEKVVITYSGDRVYNHyYPALKGRVAFTSNDLSGD 80
                        90       100
                ....*....|....*....|
gi 2842765  100 ASITIDQLTMADNGTYECSV 119
Cdd:cd20960  81 ASLNISNLKLSDTGTYQCKV 100
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
25-120 2.40e-10

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 56.95  E-value: 2.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   25 ETPQDVLRASQGKSVTLPCTYH---TSTSSREGLIQWDKLLLTHT--ERVVIW-PFSNKNYIHgelYKNRVSIsNNAEQS 98
Cdd:cd05877   1 ETVQAKVFSHRGGNVTLPCRYHyepELSAPRKIRVKWTKLEVDYAkeEDVLVAiGTRHKSYGS---YQGRVFL-RRADDL 76
                        90       100
                ....*....|....*....|..
gi 2842765   99 DASITIDQLTMADNGTYECSVS 120
Cdd:cd05877  77 DASLVITDLRLEDYGRYRCEVI 98
IGc2 smart00408
Immunoglobulin C-2 Type;
154-218 4.61e-09

Immunoglobulin C-2 Type;


Pssm-ID: 197706  Cd Length: 63  Bit Score: 52.02  E-value: 4.61e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2842765     154 IGNNIQLTCQsKEGSPTPQYSWKRYNILNQEqPLAQPASGQPVSLKNISTDTSGYYICTSSNEEG 218
Cdd:smart00408   1 EGQSVTLTCP-AEGNPVPNITWLKDGKPLPE-SNRFVASGSTLTIKSVSLEDSGLYTCVAENSAG 63
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
31-119 7.29e-08

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409379  Cd Length: 123  Bit Score: 50.29  E-value: 7.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   31 LRASQGKSVTLPCTYHTS----TSSREGL-IQWDKLLLTHTER--VVIWPFSNKNYIHGELYKNRVSISNNAEQ-SDASI 102
Cdd:cd05714   7 VFSHLGGNVTLPCKFYRDptafGSGIHKIrIKWTKLTSDSGYLkeVDVLVAMGNVVYHKKTYGGRVSVPLKPGSdSDASL 86
                        90
                ....*....|....*..
gi 2842765  103 TIDQLTMADNGTYECSV 119
Cdd:cd05714  87 VITDLTASDYGLYRCEV 103
IgV_P0-like cd05715
Immunoglobulin (Ig)-like domain of protein zero (P0) and similar proteins; The members here ...
22-137 1.23e-07

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


Pssm-ID: 409380  Cd Length: 117  Bit Score: 49.35  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   22 ISVETPQdVLRASQGKSVTLPCTY-HTSTSSREGLIQWDKLLLTHTERVVIWPFSNKNYIHGEL--YKNRVSISNNAEQS 98
Cdd:cd05715   1 MEVYTPR-ELNVLNGSDVRLTCTFtSCYTVGDAFSVTWTYQPEGGNTTESMFHYSKGKPYILKVgrFKDRVSWAGNPSKK 79
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2842765   99 DASITIDQLTMADNGTYECSVSLMSDLEGNTkSRVRLLV 137
Cdd:cd05715  80 DASIVISNLQFSDNGTYTCDVKNPPDIVGGH-GEIRLYV 117
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
29-138 2.71e-07

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: 48.36  E-value: 2.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   29 DVLRASQGKSVTLPCTYHTSTSSREGLIQWDK---------LLLTHTERvviwpfsNKNYIHGelYKNRVSISNNAEQSD 99
Cdd:cd05888   1 DVVTVVLGQDAKLPCFYRGDSGEQVGQVAWARvdagegaqeIALLHSKY-------GLHVFPA--YEGRVEQPPPPRPAD 71
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2842765  100 ASITIDQLTMADNGTYECSVSLMSdlEGNTKSRVRLLVL 138
Cdd:cd05888  72 GSVLLRNAVQADEGEYECRVSTFP--AGNFQAELRLRVL 108
IgV_EVA1 cd05880
Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are ...
22-137 4.83e-07

Immunoglobulin (Ig)-like domain of epithelial V-like antigen (EVA) 1; The members here are composed of the immunoglobulin (Ig) domain of epithelial V-like antigen 1 (EVA 1). EVA is also known as myelin protein zero-like 2. EVA is an adhesion molecule and may play a role in the structural organization of the thymus and early lymphocyte development.


Pssm-ID: 409464  Cd Length: 116  Bit Score: 47.90  E-value: 4.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   22 ISVETPQDVlRASQGKSVTLPCTYHTSTSSREGL-IQWDKLLLTHTERVVIWPFSNKNYIHGE-LYKNRVSISNNAEQSD 99
Cdd:cd05880   1 IEVYTSKEV-EAVNGTDVRLKCTFSSSAPIGDTLvITWNFRPLDGGREESVFYYHKRPYPPPDgRFKGRVVWDGNIMRRD 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 2842765  100 ASITIDQLTMADNGTYECSVSLMSDLEGnTKSRVRLLV 137
Cdd:cd05880  80 ASILIWQLQPTDNGTYTCQVKNPPDVHG-PIGEIRLRV 116
IG smart00409
Immunoglobulin;
155-228 4.99e-07

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 46.73  E-value: 4.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765     155 GNNIQLTCQSKeGSPTPQYSWKRynilNQEQPLAQPA------SGQPVSL--KNISTDTSGYYICTSSNEEGTQFCNITV 226
Cdd:smart00409   9 GESVTLSCEAS-GSPPPEVTWYK----QGGKLLAESGrfsvsrSGSTSTLtiSNVTPEDSGTYTCAATNSSGSASSGTTL 83

                   ..
gi 2842765     227 AV 228
Cdd:smart00409  84 TV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
155-228 4.99e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 46.73  E-value: 4.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765     155 GNNIQLTCQSKeGSPTPQYSWKRynilNQEQPLAQPA------SGQPVSL--KNISTDTSGYYICTSSNEEGTQFCNITV 226
Cdd:smart00410   9 GESVTLSCEAS-GSPPPEVTWYK----QGGKLLAESGrfsvsrSGSTSTLtiSNVTPEDSGTYTCAATNSSGSASSGTTL 83

                   ..
gi 2842765     227 AV 228
Cdd:smart00410  84 TV 85
IG smart00409
Immunoglobulin;
27-137 6.44e-07

Immunoglobulin;


Pssm-ID: 214652  Cd Length: 85  Bit Score: 46.34  E-value: 6.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765      27 PQDVLrASQGKSVTLPCTYHTSTSSReglIQWdklllthtervviwpfsNKNYIHGELYKNRVSISNNaeQSDASITIDQ 106
Cdd:smart00409   1 PPSVT-VKEGESVTLSCEASGSPPPE---VTW-----------------YKQGGKLLAESGRFSVSRS--GSTSTLTISN 57
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2842765     107 LTMADNGTYECSVSLMSdleGNTKSRVRLLV 137
Cdd:smart00409  58 VTPEDSGTYTCAATNSS---GSASSGTTLTV 85
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
27-137 6.44e-07

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653  Cd Length: 85  Bit Score: 46.34  E-value: 6.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765      27 PQDVLrASQGKSVTLPCTYHTSTSSReglIQWdklllthtervviwpfsNKNYIHGELYKNRVSISNNaeQSDASITIDQ 106
Cdd:smart00410   1 PPSVT-VKEGESVTLSCEASGSPPPE---VTW-----------------YKQGGKLLAESGRFSVSRS--GSTSTLTISN 57
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2842765     107 LTMADNGTYECSVSLMSdleGNTKSRVRLLV 137
Cdd:smart00410  58 VTPEDSGTYTCAATNSS---GSASSGTTLTV 85
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
31-119 7.91e-07

Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG); The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409462  Cd Length: 125  Bit Score: 47.23  E-value: 7.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   31 LRASQGKSVTLPCTY------HTSTSSREGL-IQWDKLLLTHTER--VVIWPFSNKNYIHGELYKNRVSISNNAEQ-SDA 100
Cdd:cd05878   7 VRVLLGTSVTLPCYFidpphpVTPSTAPLAPrIKWSKVSVDGKKEkeVVLLVATEGRVRVNSAYQGRVSLPNYPAIpSDA 86
                        90
                ....*....|....*....
gi 2842765  101 SITIDQLTMADNGTYECSV 119
Cdd:cd05878  87 TLEVQSLRASDSGLYRCEV 105
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
32-119 1.03e-06

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: 46.67  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   32 RASQGKSVTLPCTYHTSTSSREGLIQWDKLllTHTERVVIWPFSNKNYIH-GELYKNRVSISNNAEQS-DASITIDQLTM 109
Cdd:cd05718  10 TGFLGGSVTLPCSLTSPGTTKITQVTWMKI--GAGSSQNVAVFHPQYGPSvPNPYAERVEFLAARLGLrNATLRIRNLRV 87
                        90
                ....*....|
gi 2842765  110 ADNGTYECSV 119
Cdd:cd05718  88 EDEGNYICEF 97
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
24-120 1.25e-06

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar proteins; The members here are composed of the immunoglobulin (Ig) variable domain of the alpha chain of alpha/beta T-cell antigen receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are composed of alpha and beta, or gamma and delta polypeptide chains with variable (V) and constant (C) regions. This group represents the variable domain of the alpha chain of TCRs and also includes the variable domain of delta chains of TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. The variable domain of TCRs is responsible for antigen recognition, and is located at the N-terminus of the receptor. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409372  Cd Length: 109  Bit Score: 46.49  E-value: 1.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   24 VETPQDVLRASQGKSVTLPCTYHTSTSSReglIQWDKLLLTHTERVVIwpfsnKNYIHGELYKN-RVSISNNAEQSDASI 102
Cdd:cd04983   1 VTQSPQSLSVQEGENVTLNCNYSTSTFYY---LFWYRQYPGQGPQFLI-----YISSDSGNKKKgRFSATLDKSRKSSSL 72
                        90
                ....*....|....*...
gi 2842765  103 TIDQLTMADNGTYECSVS 120
Cdd:cd04983  73 HISAAQLSDSAVYFCALS 90
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
31-119 1.74e-06

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409482  Cd Length: 128  Bit Score: 46.49  E-value: 1.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   31 LRASQGKSVTLPCTYHT-------STSSREGL-IQWDKLLLT-----HTERVVIWPfSNKNYIHGELYKNRVSISNNAE- 96
Cdd:cd05901   7 VHGSLSGSVVLPCRFSTlptlppsYNITSEFLrIKWTKIQVDkngkdHKETTVLVA-QNGIIKIGQEYMGRVSVPSHPEd 85
                        90       100
                ....*....|....*....|...
gi 2842765   97 QSDASITIDQLTMADNGTYECSV 119
Cdd:cd05901  86 QGDASLTIVKLRASDAGVYRCEV 108
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
153-216 2.24e-06

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. 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. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562  Cd Length: 92  Bit Score: 45.19  E-value: 2.24e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2842765  153 IIGNNIQLTCQSkEGSPTPQYSWKRYNILNQE--QPLAQPASGQPVSLKNISTDTSGYYICTSSNE 216
Cdd:cd20970  15 REGENATFMCRA-EGSPEPEISWTRNGNLIIEfnTRYIVRENGTTLTIRNIRRSDMGIYLCIASNG 79
IgV_TIM-3_like cd20982
Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3) ...
32-119 2.60e-06

Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3), and similar domains; The members here are composed of the immunoglobulin variable (IgV) domain of T cell immunoglobulin domain and mucin domain 3 (Tim-3; also known as Hepatitis A virus cellular receptor 2 (HAVcr-2) and Cluster of Differentiation 366 (CD366)) and similar proteins. TIM-3 is a checkpoint inhibitor in immune responses to tumors, as well as involved in chronic viral infections. Thus, Tim-3 has emerged as one of most promising immune checkpoint targets for cancer immunotherapy. Tim-3 is highly expressed on Th1 lymphocytes and CD11b(+) macrophages and is upregulated on activated T and myeloid cells. TIM-3 regulates macrophage, activation and inhibits Th1 mediated immune responses to promote immunological tolerance. There are three TIM family members in humans (TIM-1, TIM-3, and TIM-4) and eight members in mice (TIM-1 to TIM-8). The IgV domain of human TIM-3 has been shown to bind ligands such as carcinoembryonic antigen cell adhesion molecule 1 (CEACAM1), high mobility group protein B1 (HMGB1)and galectin-9 (GAL9). The binding of GAL9 to TIM-3 can negatively regulate Th1 immune response, enhance immune tolerance and inhibit anti#tumor immunity. Dysregulation of the TIM-3/GAL9 pathway is implicated in numerous chronic autoimmune diseases, such as multiple sclerosis and systemic lupus erythematosus.


Pssm-ID: 409574  Cd Length: 107  Bit Score: 45.53  E-value: 2.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   32 RASQGKSVTLPCTYHTSTSSREGLIQWDKLLLTHTE--RVVIWPfSNKNYIHGElyKNRVSISNNAEQSDASITIDQLTM 109
Cdd:cd20982   4 RAEVGHNAYLPCSYTTAAPGNLVPVCWGKGACPVSYcgNVLLRT-DERDVTYQK--SSRYQLKGDFSKGDVSLTIENVTL 80
                        90
                ....*....|
gi 2842765  110 ADNGTYECSV 119
Cdd:cd20982  81 ADSGIYCCRI 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
143-215 2.83e-06

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 404760  Cd Length: 79  Bit Score: 44.44  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765    143 KPECGIEGETII---GNNIQLTCQSkEGSPTPQYSWKRYNILNQEQPLAQPASGQPVS----LKNISTDTSGYYICTSSN 215
Cdd:pfam13927   1 KPVITVSPSSVVvveGESVTLTCEA-TGGPPPTITWYKNGEEILSGSTSDRISLSGSNstltISNVTRSDSGTYTCVASN 79
IgV_P0 cd05879
Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the ...
22-137 3.40e-06

Immunoglobulin (Ig)-like domain of protein zero (P0); The members here are composed of the immunoglobulin (Ig) domain of protein zero (P0), a myelin membrane adhesion molecule. P0 accounts for over 50% of the total protein in peripheral nervous system (PNS) myelin. P0 is a single-pass transmembrane glycoprotein with a highly basic intracellular domain and an Ig domain. The extracellular domain of P0 (P0-ED) is similar to the Ig variable domain, carrying one acceptor sequence for N-linked glycosylation. P0 plays a role in membrane adhesion in the spiral wraps of the myelin sheath. The intracellular domain is thought to mediate membrane apposition of the cytoplasmic faces and may, through electrostatic interactions, interact directly with lipid headgroups. It is thought that homophilic interactions of the P0 extracellular domain mediate membrane juxtaposition in the extracellular space of PNS myelin.


Pssm-ID: 409463  Cd Length: 117  Bit Score: 45.25  E-value: 3.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   22 ISVETPQDVlRASQGKSVTLPCTYHTST-SSREGLIQWDKLLLTHTERVVIWPFSN-KNYI-HGELYKNRVSISNNAEQS 98
Cdd:cd05879   1 IVVYTDREV-YGTVGSDVTLSCSFWSSEwISDDISFTWHYQPDGSRDAISIFHYGKgQPYIdNVGPFKERIEWVGNPSRK 79
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2842765   99 DASITIDQLTMADNGTYECSVSLMSDLEGNTkSRVRLLV 137
Cdd:cd05879  80 DGSIVIHNLDYTDNGTFTCDVKNPPDIVGKS-SQVTLYV 117
IgI_2_JAM1 cd20950
Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF ...
144-229 3.90e-06

Second Ig-like domain of Junctional adhesion molecule-1 (JAM1); a member of the I-set of IgSF domains; The members here are composed of the second Ig-like domain of Junctional adhesion molecule-1 (JAM1). 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 second Ig-like domain of JAM1 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, the A strand of the I-set is discontinuous but lacks a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors.


Pssm-ID: 409542  Cd Length: 97  Bit Score: 44.62  E-value: 3.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765  144 PECGIEGETIIGNNIQLTCQSKEGSPTPQYSWKRYNILNQEQPLA-----------QPASGQPVSLKNISTDTsGYYICT 212
Cdd:cd20950   1 PTVNIPSSATIGNRAVLTCSEPDGSPPSEYTWFKDGVVMPTNPKStrafsnssyslDPTTGELVFDPLSASDT-GEYSCE 79
                        90
                ....*....|....*...
gi 2842765  213 SSNEEGT-QFCNitvAVR 229
Cdd:cd20950  80 ARNGYGTpMRSN---AVR 94
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
24-120 8.90e-06

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  Cd Length: 111  Bit Score: 43.86  E-value: 8.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   24 VETPQDVLRaSQGKSVTLPCTYHTSTSSreGLIQWDKLLLTHT-ERVVIWPFSNKNYihGELYKNRVSISNNaEQSDASI 102
Cdd:cd00099   2 TQSPRSLSV-QEGESVTLSCEVSSSFSS--TYIYWYRQKPGQGpEFLIYLSSSKGKT--KGGVPGRFSGSRD-GTSSFSL 75
                        90
                ....*....|....*...
gi 2842765  103 TIDQLTMADNGTYECSVS 120
Cdd:cd00099  76 TISNLQPEDSGTYYCAVS 93
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
23-138 9.84e-06

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: 43.68  E-value: 9.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   23 SVETPQDVLRASQGKSVTLPCTYHTSTSSREglIQWDKLllthtERVVIWPFSNKNYIHGElYKNRVSISnnaeqsDASI 102
Cdd:cd20946   1 TVPSSQQVVTVVENQEVILSCKTPKKTSSPR--VEWKKL-----QRDVTFVVFQNNKIQGD-YKGRAEIL------GTNI 66
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 2842765  103 TIDQLTMADNGTYECSVSLMSDLEGNTKSRVRLLVL 138
Cdd:cd20946  67 TIKNVTRSDSGKYRCEVSARSDGQNLGEVTVTLEVL 102
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
155-219 1.49e-05

Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the seventh immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409546  Cd Length: 96  Bit Score: 43.07  E-value: 1.49e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2842765  155 GNNIQLTCQSkEGSPTPQYSWKR--------YNILNQEQPLAQPASGQpVSLKNISTDTSGYYICTSSNEEGT 219
Cdd:cd20954  16 GQDVMLHCQA-DGFPTPTVTWKKatgstpgeYKDLLYDPNVRILPNGT-LVFGHVQKENEGHYLCEAKNGIGS 86
I-set pfam07679
Immunoglobulin I-set domain;
148-228 2.30e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151  Cd Length: 90  Bit Score: 42.24  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765    148 IEGETIIgnniqLTCQSkEGSPTPQYSWKRynilnQEQPLAQP------ASGQPVSL--KNISTDTSGYYICTSSNEEGT 219
Cdd:pfam07679  13 QEGESAR-----FTCTV-TGTPDPEVSWFK-----DGQPLRSSdrfkvtYEGGTYTLtiSNVQPDDSGKYTCVATNSAGE 81

                  ....*....
gi 2842765    220 QFCNITVAV 228
Cdd:pfam07679  82 AEASAELTV 90
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
149-215 3.47e-05

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: 41.80  E-value: 3.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2842765    149 EGETIIGNNIQLTCQSKEGSPTPQYSWKR---YNILNQEQPLAQPASGQ-PVSLKNISTDTSGYYICTSSN 215
Cdd:pfam00047   5 TVTVLEGDSATLTCSASTGSPGPDVTWSKeggTLIESLKVKHDNGRTTQsSLLISNVTKEDAGTYTCVVNN 75
Ig3_L1-CAM_like cd05731
Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar ...
155-229 4.22e-05

Third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM), and similar domains; The members here are composed of the third immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, and spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains the chicken neuron-glia cell adhesion molecule, Ng-CAM and human neurofascin.


Pssm-ID: 409394  Cd Length: 83  Bit Score: 41.24  E-value: 4.22e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2842765  155 GNNIQLTCQSkEGSPTPQYSWKRyniLNQEQPLAQPAS---GQPVSLKNISTDTSGYYICTSSNEEGTQFCNITVAVR 229
Cdd:cd05731  10 GGVLLLECIA-EGLPTPDIRWIK---LGGELPKGRTKFenfNKTLKIENVSEADSGEYQCTASNTMGSARHTISVTVE 83
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
31-120 4.43e-05

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: 41.41  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765     31 LRASQGKSVTLPCTYHTSTSSREgliqwdklllthtervVIWPFSNKNYIHGELYKNrvsisNNAEQSDASITIDQLTMA 110
Cdd:pfam00047   6 VTVLEGDSATLTCSASTGSPGPD----------------VTWSKEGGTLIESLKVKH-----DNGRTTQSSLLISNVTKE 64
                          90
                  ....*....|
gi 2842765    111 DNGTYECSVS 120
Cdd:pfam00047  65 DAGTYTCVVN 74
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
151-228 5.51e-05

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405  Cd Length: 91  Bit Score: 41.33  E-value: 5.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765  151 ETIIGNNIQLTCQSKeGSPTPQYSWKRYNIL---NQEQPLAQPASGQpVSL--KNISTDTSGYYICTSSNEEGTQFCNIT 225
Cdd:cd05744  11 EVQEGRLCRFDCKVS-GLPTPDLFWQLNGKPvrpDSAHKMLVRENGR-HSLiiEPVTKRDAGIYTCIARNRAGENSFNAE 88

                ...
gi 2842765  226 VAV 228
Cdd:cd05744  89 LVV 91
IgV_CD80 cd16086
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here ...
37-119 6.36e-05

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


Pssm-ID: 319335  Cd Length: 105  Bit Score: 41.28  E-value: 6.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   37 KSV----TLPCTYHTSTSS-REGLIQW---DKLLLTHTERVV-IWPfsnknyihgeLYKNR--VSISNNAeqsdaSITID 105
Cdd:cd16086   6 KSVkekaLLSCDYNVSVDElAQVRIYWqkdDKMVLTIISGDVkVWP----------EYKNRtlFDITNNL-----SIVIL 70
                        90
                ....*....|....
gi 2842765  106 QLTMADNGTYECSV 119
Cdd:cd16086  71 ALRLSDRGTYTCVV 84
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
38-120 8.49e-05

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: 41.36  E-value: 8.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   38 SVTLPCTYHTSTSSREGLIQWdkLLLTHTERVVIWPF-SNKNYIHGELYKNRVSISNNAEqSDASITIDQLTMADNGTYE 116
Cdd:cd16089  16 SVNLPCTYVPEEGYTQVLVKW--LVQRDSDPVTIFLRdSSGDHIQQAKYRGRLEVSKDTP-GDVSLQLDTLEMDDRGHYT 92

                ....
gi 2842765  117 CSVS 120
Cdd:cd16089  93 CQVT 96
IgI_L1-CAM_like cd05733
Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; ...
157-223 1.25e-04

Immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM) and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of the L1 cell adhesion molecule (CAM). L1 belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. L1 is primarily expressed in the nervous system and is involved in its development and function. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth. This group also contains NrCAM [Ng(neuronglia)CAM-related cell adhesion molecule], which is primarily expressed in the nervous system, and human neurofascin. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lacks a C" strand.


Pssm-ID: 409396  Cd Length: 94  Bit Score: 40.08  E-value: 1.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2842765  157 NIQLTCQSKeGSPTPQYSWKR----YNILNQEQPLAQPASGQPV-SLKNIS-TDTSGYYICTSSNEEGTQFCN 223
Cdd:cd05733  18 NITIKCEAK-GNPQPTFRWTKdgkfFDPAKDPRVSMRRRSGTLViDNHNGGpEDYQGEYQCYASNELGTAISN 89
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
154-228 1.97e-04

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205  Cd Length: 85  Bit Score: 39.51  E-value: 1.97e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2842765  154 IGNNIQLTCQSKeGSPTPQYSWkryniLNQEQPLAQP----ASGQPVSLKNISTDTSGYYICTSSNEEGTQFCNITVAV 228
Cdd:cd05728  13 IGSSLRWECKAS-GNPRPAYRW-----LKNGQPLASEnrieVEAGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
IgV_VCBP cd20963
Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set ...
33-120 2.27e-04

Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set domain; The members here are composed of the immunoglobulin variable (IgV) region-containing chitin-binding proteins (VCBPs). VCBPs are secreted, immune-type molecules that have been identified in both amphioxus and sea squirt (Ciona intestinalis). VCBPs, which consist of a leader peptide, two tandem N-terminal immunoglobulin V-type domains and a single C-terminal chitin-binding domain, belong to a multigene family encoding secreted proteins. The VCBPs were identified first in the cephalochordate Branchiostoma floridae and show structural similarities with V-type domains of immunoglobulins and T cell receptors, suggesting that VCBPs represent a unique gut-associated form of innate immune proteins. 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. 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. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other.


Pssm-ID: 409555  Cd Length: 123  Bit Score: 40.29  E-value: 2.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   33 ASQGKSVTLPCTYHTSTSSREGLIQWDKLLLTHTERVVIWPF--------SNKNYIHGelYKNRVSISNNAEqsdASITI 104
Cdd:cd20963  14 PTWGNRVELPCSYTISPAAQPPTITWLKGISVDRAEVVFKGFkywnetssSGEVYFGD--YAGRASVASLTQ---PTLVL 88
                        90
                ....*....|....*.
gi 2842765  105 DQLTMADNGTYECSVS 120
Cdd:cd20963  89 TDLKFDDWGRYWCRVA 104
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
27-123 4.14e-04

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 39.51  E-value: 4.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   27 PQDVLRASQGKSVTLPCTYHTST--SSREGLIQWDkllLTHTERVV--IWPFSNKNYIHGELYKNRVSI-SNNAEQSDAS 101
Cdd:cd20934   3 PEDPVVALVGTDATLRCSFSPEPgfSLAQLSVFWQ---LTDTKQLVhsFTESQDQGRDQGSAYANRTALfPDLLAQGNAS 79
                        90       100
                ....*....|....*....|..
gi 2842765  102 ITIDQLTMADNGTYECSVSLMS 123
Cdd:cd20934  80 LRLQRVRVADEGSYTCFVSVQD 101
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
158-218 4.48e-04

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277  Cd Length: 97  Bit Score: 38.81  E-value: 4.48e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2842765  158 IQLTCQSKeGSPTPQYSWK--RYNILNQEQPL------AQPASGQPVSLKNISTDTSGYYICTSSNEEG 218
Cdd:cd05869  20 ITLTCEAS-GDPIPSITWRtsTRNISSEEKTLdghivvRSHARVSSLTLKYIQYTDAGEYLCTASNTIG 87
Ig_SLAM-like_N cd16842
N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule ...
36-116 4.68e-04

N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain of the signaling lymphocyte activation molecule (SLAM) family and similar proteins. The SLAM family is a group of immune-cell specific receptors that can regulate both adaptive and innate immune responses. Members of this group include proteins such as CD84, SLAM (CD150), Ly-9 (CD229), NTB-A (ly-108, SLAM6), 19A (CRACC), and SLAMF9. The genes coding for the SLAM family are nested on chromosome 1, in humans at 1q23, and in mice at 1H2. The SLAM family is a subset of the CD2 family, which also includes CD2 and CD58 located on chromosome 1 at 1p13 in humans. In mice, CD2 is located on chromosome 3, and there is no CD58 homolog. The SLAM family proteins are organized as an extracellular domain with either two or four Ig-like domains, a single transmembrane segment, and a cytoplasmic region having Tyr-based motifs. The extracellular domain is organized as a membrane-distal Ig variable (IgV) domain that is responsible for ligand recognition and a membrane-proximal truncated Ig constant-2 (IgC2) domain.


Pssm-ID: 409517  Cd Length: 102  Bit Score: 38.84  E-value: 4.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   36 GKSVTLPCTYhtSTSSREGLIQWdkllLTHTERVVI-WPFSNKNYIHGE--LYKNRVSISNNaeqsDASITIDQLTMADN 112
Cdd:cd16842   8 GGSVTFPLNI--SDGQEIENITW----SFKTSLAVIaPGEGGAPEIIITdkSYKERLNISQN----DYSLQISNLTMEDA 77

                ....
gi 2842765  113 GTYE 116
Cdd:cd16842  78 GSYR 81
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
33-138 8.54e-04

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: 38.38  E-value: 8.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   33 ASQGKSVTLPCTYHTSTSSREglIQWDKLLLTHTERVVIWPFSNKNYIHGElYKNRVSISNNAeQSDASITIDQLTMADN 112
Cdd:cd05887  11 AVWGKNVSLKCLIEVNETITQ--ISWEKIHGKSSQTVAVHHPQYGISIQGE-YQGRVSFKNYS-LNDATITLHNVGFSDS 86
                        90       100
                ....*....|....*....|....*.
gi 2842765  113 GTYECSVSLMSdlEGNTKSRVRLLVL 138
Cdd:cd05887  87 GKYICKAVTFP--LGNAQSSTTVTVL 110
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
24-118 9.72e-04

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: 38.09  E-value: 9.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   24 VETPQDVLRASQGKSVTLPCTYHTStssrEGLIQ--WDKLLLTHTERVVIWPFSNKNYIHGElYKNRVSIsNNAEQSDAS 101
Cdd:cd05846   1 VVVHTGDTRAVLGGNATLSCNLTLP----EEVLQvtWQKIKASSPENIVTYSKKYGVKIQPS-YVRRISF-TSSGLNSTS 74
                        90
                ....*....|....*..
gi 2842765  102 ITIDQLTMADNGTYECS 118
Cdd:cd05846  75 ITIWNVTLEDEGCYKCL 91
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
22-119 1.05e-03

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggrecan has a wide distribution in connective tissue and extracellular matrices. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409481  Cd Length: 123  Bit Score: 38.38  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   22 ISVETPqdvLRASQGKSVTLPCTYHTSTSSREGL---------IQWDKLLlTHTERVVIWPFSNKNYIHGElYKNRVSIS 92
Cdd:cd05900   1 IPLESP---LRVVLGSSLLIPCYFQDPIAKDPGAptvaplsprIKWSFIS-KEKESVLLVATEGKVRVNTE-YLDRVSLP 75
                        90       100
                ....*....|....*....|....*...
gi 2842765   93 N-NAEQSDASITIDQLTMADNGTYECSV 119
Cdd:cd05900  76 NyPAIPSDATLEITELRSNDSGTYRCEV 103
IgI_NrCAM cd05874
Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); ...
157-223 1.13e-03

Immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule); member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the first immunoglobulin (Ig)-like domain of NrCAM (Ng (neuronglia) CAM-related cell adhesion molecule). NrCAM belongs to the L1 subfamily of cell adhesion molecules (CAMs) and is comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region, and an intracellular domain. NrCAM is primarily expressed in the nervous system.


Pssm-ID: 409458  Cd Length: 95  Bit Score: 37.66  E-value: 1.13e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2842765  157 NIQLTCQSKeGSPTPQYSWKR----YNILNQEQPLAQPASGQPV--SLKNISTDT-SGYYICTSSNEEGTQFCN 223
Cdd:cd05874  18 NIVIQCEAK-GKPPPSFSWTRngthFDIDKDPKVTMKPNTGTLVinIMNGEKAEAyEGVYQCTARNERGAAVSN 90
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
154-218 1.35e-03

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 37.15  E-value: 1.35e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2842765  154 IGNNIQLTCQSkEGSPTPQYSWkryniLNQEQPLAQPASGQP------VSLKNISTDTSGYYICTSSNEEG 218
Cdd:cd05856  18 VGSSVRLKCVA-SGNPRPDITW-----LKDNKPLTPPEIGENkkkkwtLSLKNLKPEDSGKYTCHVSNRAG 82
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
26-119 1.47e-03

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: 37.38  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   26 TPQDVLRASQGKSVTLPCTY-HTSTSSREGLIQWDKLllTHTERVviwpfSNKNYIHGElyknRVSISNNAEQSDASITI 104
Cdd:cd05716   2 VGPEVVTGVEGGSVTIQCPYpPKYASSRKYWCKWGSE--GCQTLV-----SSEGVVPGG----RISLTDDPDNGVFTVTL 70
                        90
                ....*....|....*
gi 2842765  105 DQLTMADNGTYECSV 119
Cdd:cd05716  71 NQLRKEDAGWYWCGV 85
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
158-220 1.52e-03

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.


Pssm-ID: 409353  Cd Length: 70  Bit Score: 36.54  E-value: 1.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2842765  158 IQLTCQSkEGSPTPQYSWKRYNILNQEQPLAQPASGQPVS---LKNISTDTSGYYICTSSNEEGTQ 220
Cdd:cd00096   1 VTLTCSA-SGNPPPTITWYKNGKPLPPSSRDSRRSELGNGtltISNVTLEDSGTYTCVASNSAGGS 65
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
154-218 1.68e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 404734  Cd Length: 76  Bit Score: 36.61  E-value: 1.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2842765    154 IGNNIQLTCQSKeGSPTPQYSWKRynilnQEQPLAQpasGQPVSLKNISTDTSGYYICTSSNEEG 218
Cdd:pfam13895  13 EGEPVTLTCSAP-GNPPANYTWYK-----GGSALNS---SPNFFILAVSAEDSGTYTCVARNGRG 68
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
22-117 2.09e-03

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: 37.17  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   22 ISVETPQDVlRASQGKSVTLPCTYHT-STSSREGLIQWDKLLlTHTERVVIWPFSNKNYIHGELYKnRVSISNNAEQSDA 100
Cdd:cd20989   1 VRVQVPPEV-RGFLGGSVTLPCHLLPpNMVTHVSQVTWQRHD-EHGSVAVFHPKQGPSFPESERLS-FVAARLGAELRNA 77
                        90
                ....*....|....*..
gi 2842765  101 SITIDQLTMADNGTYEC 117
Cdd:cd20989  78 SLAMFGLRVEDEGNYTC 94
IgI_VEGFR_like cd05742
Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and ...
22-120 2.58e-03

Immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and similar proteins; member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig)-like domain of vascular endothelial growth factor (VEGF) receptor (R) and related proteins. The VEGFRs have an extracellular component with seven Ig-like domains, a transmembrane segment, and an intracellular tyrosine kinase domain interrupted by a kinase-insert domain. The VEGFR family consists of three members: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1) and VEGFR-3 (Flt-4). VEGF-A interacts with both VEGFR-1 and VEGFR-2. VEGFR-1 binds strongest to VEGF; VEGF-2 binds more weakly. VEGFR-3 appears not to bind VEGF, but binds other members of the VEGF family (VEGF-C and -D). VEGFRs bind VEGFs with high affinity with the IG-like domains. VEGF-A is important to the growth and maintenance of vascular endothelial cells and to the development of new blood- and lymphatic-vessels in physiological and pathological states. VEGFR-2 is a major mediator of the mitogenic, angiogenic, and microvascular permeability-enhancing effects of VEGF-A. VEGFR-1 may play an inhibitory part in these processes by binding VEGF and interfering with its interaction with VEGFR-2. VEGFR-1 has a signaling role in mediating monocyte chemotaxis. VEGFR-1 and VEGFR-2 may mediate a chemotactic and a survival signal in hematopoietic stem cells or leukemia cells. VEGFR-3 has been shown to be involved in tumor angiogenesis and growth. This group also contains alpha-type platelet-derived growth factor receptor precursor (PDGFR)-alpha (CD140a), and PDGFR-beta (CD140b). PDGFRs alpha and beta have an extracellular component with five Ig-like domains, a transmembrane segment, and a cytoplasmic portion that has protein tyrosine kinase activity.


Pssm-ID: 409404  Cd Length: 102  Bit Score: 36.75  E-value: 2.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   22 ISVETPQDVLRasQGKSVTLPCTYHTSTSSREGLiQWD-------KLLLTHTERVVIWPFSNKnyihgelyknRVSIsnn 94
Cdd:cd05742   5 LSPNAEPTVLP--QGETLVLNCTANVNLNEVVDF-QWTypsekegKLALLKPDIKVDWSEPGE----------FVST--- 68
                        90       100
                ....*....|....*....|....*.
gi 2842765   95 aeqsdasITIDQLTMADNGTYECSVS 120
Cdd:cd05742  69 -------LTIPEATLKDSGTYTCAAR 87
Ig4_L1-NrCAM_like cd04978
Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), ...
154-229 2.86e-03

Fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related); The members here are composed of the fourth immunoglobulin (Ig)-like domain of L1, Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM (Ng-CAM-related). These proteins belong to the L1 subfamily of cell adhesion molecules (CAMs) and are comprised of an extracellular region having six Ig-like domains and five fibronectin type III domains, a transmembrane region and an intracellular domain. These molecules are primarily expressed in the nervous system. L1 is associated with an X-linked recessive disorder, X-linked hydrocephalus, MASA syndrome, or spastic paraplegia type 1, that involves abnormalities of axonal growth.


Pssm-ID: 409367  Cd Length: 89  Bit Score: 36.27  E-value: 2.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2842765  154 IGNNIQLTCQSkEGSPTPQYSWKRYNILNQEQPLAQP--ASGQPVSLKNISTDTSGYYICTSSNEEGTQFCNITVAVR 229
Cdd:cd04978  13 PGETGELICEA-EGNPQPTITWRLNGVPIEPAPEDMRrtVDGRTLIFSNLQPNDTAVYQCNASNVHGYLLANAFLHVL 89
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
155-218 2.96e-03

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399  Cd Length: 93  Bit Score: 36.47  E-value: 2.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2842765  155 GNNIQLTCQSkEGSPTPQYSWKRYNI-LNQEQP--LAQPASGQPVSLKNISTDTSGYYICTSSNEEG 218
Cdd:cd05736  15 GVEASLRCHA-EGIPLPRVQWLKNGMdINPKLSkqLTLIANGSELHISNVRYEDTGAYTCIAKNEGG 80
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
155-219 5.26e-03

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391  Cd Length: 98  Bit Score: 35.70  E-value: 5.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2842765  155 GNNIQLTCQSKeGSPTPQYSWKR---YNILNQEQPLaQPASGQPVS------LKNISTDTSGYYICTSSNEEGT 219
Cdd:cd05726  14 GRTVTFQCETK-GNPQPAIFWQKegsQNLLFPYQPP-QPSSRFSVSptgdltITNVQRSDVGYYICQALNVAGS 85
IgI_NCAM-1_like cd05732
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar ...
148-218 5.51e-03

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1) and similar proteins; The members here are composed of the fourth immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. Also included in this group is NCAM-2 (also known as OCAM/mamFas II and RNCAM) NCAM-2 is differentially expressed in the developing and mature olfactory epithelium (OE). One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 409395  Cd Length: 96  Bit Score: 35.58  E-value: 5.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765  148 IEGETII-GNNIQLTCQSkEGSPTPQYSWKRY--NILNQEQPL------AQPASGQPVSLKNISTDTSGYYICTSSNEEG 218
Cdd:cd05732   8 LENQTAVeLEQITLTCEA-EGDPIPEITWRRAtrGISFEEGDLdgrivvRGHARVSSLTLKDVQLTDAGRYDCEASNRIG 86
IgI_M-protein_C cd05891
C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily ...
155-228 8.25e-03

C-terminal immunoglobulin (Ig)-like domain of M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of M-protein (also known as myomesin-2). M-protein is a structural protein localized to the M-band, a transverse structure in the center of the sarcomere, and is a candidate for M-band bridges. M-protein is modular consisting mainly of repetitive IG-like and fibronectin type III (FnIII) domains and has a muscle-type specific expression pattern. M-protein is present in fast fibers.


Pssm-ID: 143299  Cd Length: 92  Bit Score: 35.27  E-value: 8.25e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2842765  155 GNNIQLTCqSKEGSPTPQYSWKRYN--ILNQEQPLAQPASGQPVSL--KNISTDTSGYYICTSSNEEGTQFCNITVAV 228
Cdd:cd05891  16 GKTLNLTC-TVFGNPDPEVIWFKNDqdIELSEHYSVKLEQGKYASLtiKGVTSEDSGKYSINVKNKYGGETVDVTVSV 92
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
36-137 8.30e-03

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 35.44  E-value: 8.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765   36 GKSVTLPCTYhtsTSSREGLIQWDKLlltHTERVVIWPFSNKNYI--HGELYKNRVSISNNAEQS-DASITIDQLTMADN 112
Cdd:cd16091  12 SEDCILPCSF---TPGSEVVIHWYKQ---DSDIKVHSYYYGKDQLesQDQRYRNRTSLFKDQISNgNASLLLRRVQLQDE 85
                        90       100
                ....*....|....*....|....*
gi 2842765  113 GTYECSVslmSDLEGNTKSRVRLLV 137
Cdd:cd16091  86 GRYKCYT---STIIGNQESFVNLKV 107
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
23-120 8.47e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 404760  Cd Length: 79  Bit Score: 34.81  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765     23 SVETPQDVLRASQGKSVTLPCTYHTSTSSReglIQWDKlllthtervviwpfSNKNYIHGELYKNRVSISNNAeqsdaSI 102
Cdd:pfam13927   3 VITVSPSSVVVVEGESVTLTCEATGGPPPT---ITWYK--------------NGEEILSGSTSDRISLSGSNS-----TL 60
                          90
                  ....*....|....*...
gi 2842765    103 TIDQLTMADNGTYECSVS 120
Cdd:pfam13927  61 TISNVTRSDSGTYTCVAS 78
IgI_Myomesin_like_C cd05737
C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of ...
155-228 8.65e-03

C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the C-terminal immunoglobulin (Ig)-like domain of myomesin and M-protein (also known as myomesin-2). Myomesin and M-protein are both structural proteins localized to the M-band, a transverse structure in the center of the sarcomere, and are candidates for M-band bridges. Both proteins are modular, consisting mainly of repetitive Ig-like and fibronectin type III (FnIII) domains. Myomesin is expressed in all types of vertebrate striated muscle; M-protein has a muscle-type specific expression pattern. Myomesin is present in both slow and fast fibers; M-protein is present only in fast fibers. It has been suggested that myomesin acts as a molecular spring with alternative splicing as a means of modifying its elasticity.


Pssm-ID: 319300  Cd Length: 92  Bit Score: 34.87  E-value: 8.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765  155 GNNIQLTCqSKEGSPTPQYSWkryniLNQEQPLAQ---------PASGQPVSLKNISTDTSGYYICTSSNEEGTQFCNIT 225
Cdd:cd05737  16 GKTLNLTC-NVWGDPPPEVSW-----LKNDQALAFldhcnlkveAGRTVYFTINGVSSEDSGKYGLVVKNKYGSETSDVT 89

                ...
gi 2842765  226 VAV 228
Cdd:cd05737  90 VSV 92
IgI_2_Robo cd05724
Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
151-219 9.92e-03

Second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of the Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, and Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit-2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409389  Cd Length: 87  Bit Score: 34.68  E-value: 9.92e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2842765  151 ETIIGNNIQLTCQSKEGSPTPQYSWKRYNI-LNQEQPLAQPASGQPVSLKNISTDTSGYYICTSSNEEGT 219
Cdd:cd05724   8 QVAVGEMAVLECSPPRGHPEPTVSWRKDGQpLNLDNERVRIVDDGNLLIAEARKSDEGTYKCVATNMVGE 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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