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Conserved domains on  [gi|83287885|sp|Q9EP73|]
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RecName: Full=Programmed cell death 1 ligand 1; Short=PD-L1; Short=PDCD1 ligand 1; Short=Programmed death ligand 1; AltName: Full=B7 homolog 1; Short=B7-H1; AltName: CD_antigen=CD274; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
 21-130 4.52e-78

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.


:

Pssm-ID: 409539  Cd Length: 110  Bit Score: 232.51  E-value: 4.52e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  21 ITAPKDLYVVEYGSNVTMECRFPVERELDLLALVVYWEKEDEQVIQFVAGEEDLKPQHSNFRGRASLPKDQLLKGNAALQ 100
Cdd:cd20947   1 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 80

                        90       100       110
                ....*....|....*....|....*....|
gi 83287885 101 ITDVKLQDAGVYCCIISYGGADYKRITLKV 130
Cdd:cd20947  81 ITDVKLQDAGVYRCMISYGGADYKRITVKV 110
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 138-223 3.20e-12

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd20986:

Pssm-ID: 472250  Cd Length: 82  Bit Score: 61.20  E-value: 3.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885 138 NQRISVDPATSEHELICQAEGYPEAEVIWTNsdhqpVSGKRSVTTSRTEGMLLNVTSSLRVNATANDVFYCTFWRSqpgq 217
Cdd:cd20986   1 DTHILEVPGTGEVQLTCQARGYPLAEVSWQN-----VSVPANTSHTRTPEGLYQVTSVLRLKPQPGRNFSCMFWNA---- 71


                ....*.
gi 83287885 218 nHTAEL 223
Cdd:cd20986  72 -HMKEL 76
 
Name Accession Description Interval E-value
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
 21-130 4.52e-78

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.


Pssm-ID: 409539  Cd Length: 110  Bit Score: 232.51  E-value: 4.52e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  21 ITAPKDLYVVEYGSNVTMECRFPVERELDLLALVVYWEKEDEQVIQFVAGEEDLKPQHSNFRGRASLPKDQLLKGNAALQ 100
Cdd:cd20947   1 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 80

                        90       100       110
                ....*....|....*....|....*....|
gi 83287885 101 ITDVKLQDAGVYCCIISYGGADYKRITLKV 130
Cdd:cd20947  81 ITDVKLQDAGVYRCMISYGGADYKRITVKV 110
IgC1_PD-L2 cd20986
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ...
 138-223 3.20e-12

Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients.


Pssm-ID: 409578  Cd Length: 82  Bit Score: 61.20  E-value: 3.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885 138 NQRISVDPATSEHELICQAEGYPEAEVIWTNsdhqpVSGKRSVTTSRTEGMLLNVTSSLRVNATANDVFYCTFWRSqpgq 217
Cdd:cd20986   1 DTHILEVPGTGEVQLTCQARGYPLAEVSWQN-----VSVPANTSHTRTPEGLYQVTSVLRLKPQPGRNFSCMFWNA---- 71


                ....*.
gi 83287885 218 nHTAEL 223
Cdd:cd20986  72 -HMKEL 76
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 24-130 6.26e-07

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.34  E-value: 6.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885     24 PKDLYVVEyGSNVTMECRFPVERELdllalVVYWEKEDEQVIQFvageedlkpqhsnfRGRASLPKDqllKGNAALQITD 103
Cdd:smart00410   1 PPSVTVKE-GESVTLSCEASGSPPP-----EVTWYKQGGKLLAE--------------SGRFSVSRS---GSTSTLTISN 57

                           90       100
                   ....*....|....*....|....*...
gi 83287885    104 VKLQDAGVYCCIISYGGADYKR-ITLKV 130
Cdd:smart00410  58 VTPEDSGTYTCAATNSSGSASSgTTLTV 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 22-130 2.00e-06

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 45.53  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885    22 TAPKDLYVVEyGSNVTMECRFPVERELDLLalVVYWEK------EDEQVIQFVAGEEDLKPQhsnfrGRASLPKDQLlKG 95
Cdd:pfam07686   1 QTPREVTVAL-GGSVTLPCTYSSSMSEAST--SVYWYRqppgkgPTFLIAYYSNGSEEGVKK-----GRFSGRGDPS-NG 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 83287885    96 NAALQITDVKLQDAGVYCCIISYGGADY--KRITLKV 130
Cdd:pfam07686  72 DGSLTIQNLTLSDSGTYTCAVIPSGEGVfgKGTRLTV 108
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 151-225 2.13e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.41  E-value: 2.13e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83287885    151 ELICQAEGYPEAEVIWTNSDHQPVSGKRSVTTSRTEGmllnvTSSLRV-NATAND--VFYCTFWRSQPGQNHTAELII 225
Cdd:smart00410  13 TLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGS-----TSTLTIsNVTPEDsgTYTCAATNSSGSASSGTTLTV 85
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 151-209 1.75e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.39  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83287885   151 ELICQAEGYPEAEVIWTNSDHQPVSGKRSVTTSRTEGMLLNVTsslrvNATAND--VFYCT 209
Cdd:pfam13927  20 TLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTIS-----NVTRSDagTYTCV 75
 
Name Accession Description Interval E-value
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
 21-130 4.52e-78

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.


Pssm-ID: 409539  Cd Length: 110  Bit Score: 232.51  E-value: 4.52e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  21 ITAPKDLYVVEYGSNVTMECRFPVERELDLLALVVYWEKEDEQVIQFVAGEEDLKPQHSNFRGRASLPKDQLLKGNAALQ 100
Cdd:cd20947   1 VTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQ 80

                        90       100       110
                ....*....|....*....|....*....|
gi 83287885 101 ITDVKLQDAGVYCCIISYGGADYKRITLKV 130
Cdd:cd20947  81 ITDVKLQDAGVYRCMISYGGADYKRITVKV 110
IgV_PD-L2 cd20983
Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here ...
 19-130 1.37e-19

Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). Receptor-binding domain of PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients.


Pssm-ID: 409575  Cd Length: 100  Bit Score: 81.46  E-value: 1.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  19 FTITAPKDLYVVEYGSNVTMECRFPVERELDLLALVVYWEKEdeqviqfvagEEDLKPQhsnfRGRASLPKDQLLKGNAA 98
Cdd:cd20983   2 FTVTVPKELYTVDHGSNVTLECDFDTGEHVELGAIRASLQKV----------ENDTSLH----SERATLLEEQLPLGKAL 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 83287885  99 LQITDVKLQDAGVYCCIISYGGA-DYKRITLKV 130
Cdd:cd20983  68 FHIPSVQVRDAGQYRCLIIYGVAwDYKYLTLKV 100
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
 33-117 4.60e-18

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.


Pssm-ID: 409576  Cd Length: 110  Bit Score: 78.02  E-value: 4.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  33 GSNVTMECRFpvERELDLLALVVYWEKE-DEQVI-QFVAGEEDLKPQHSNFRGRASLPKDQLLKGNAALQITDVKLQDAG 110
Cdd:cd20984  12 GEDGILSCTF--TPDIKLSDIVIQWLKEgDSGLVhEFKEGKDELSRQSPMFRGRTSLFADQVHVGNASLRLKNVQLTDAG 89


                ....*..
gi 83287885 111 VYCCIIS 117
Cdd:cd20984  90 TYLCIIS 96
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
 24-134 6.47e-17

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: 74.95  E-value: 6.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  24 PKDLYVVEYGSNVTMECRFPVERELDLLALVVYWEKED--EQVIQFVAGEEDLKPQHSNFRGRASLPKDQLLKGNAALQI 101
Cdd:cd20934   3 PEDPVVALVGTDATLRCSFSPEPGFSLAQLSVFWQLTDtkQLVHSFTESQDQGRDQGSAYANRTALFPDLLAQGNASLRL 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 83287885 102 TDVKLQDAGVYCCIISYGGADYKRITLKVNAPY 134
Cdd:cd20934  83 QRVRVADEGSYTCFVSVQDFGSAAVSLQVAAPF 115
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 32-117 6.97e-14

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: 66.26  E-value: 6.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  32 YGSNVTMECRFPVERELdllalVVYWEKEDEQ--VIQFVAGEEDLKPQHSNFRGRASLPKDQLLKGNAALQITDVKLQDA 109
Cdd:cd16091  11 LSEDCILPCSFTPGSEV-----VIHWYKQDSDikVHSYYYGKDQLESQDQRYRNRTSLFKDQISNGNASLLLRRVQLQDE 85


                ....*...
gi 83287885 110 GVYCCIIS 117
Cdd:cd16091  86 GRYKCYTS 93
IgC1_PD-L2 cd20986
Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here ...
 138-223 3.20e-12

Immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2); The members here are composed of the immunoglobulin Constant 1 (IgC1) domain of Programmed death ligand 2 (PD-L2; also known as B7-DC or CD273). PD-L2 is a cell-surface ligand that competes with PD-L1 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the CD28/B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. PD-L2 has a higher affinity for PD-1 but is expressed at lower levels. PD-L2 interaction with PD-1 suppresses T cell proliferation, cytokine production and cytotoxic activity. PD-L2 is expressed on tumor cells, antigen-presenting cells or APCs (such as macrophages, B cells and dendritic cells), and a variety of other immune and nonimmune cells. Tumor expression of PD-L2 may contribute to tumor evasion of immune destruction by inactivating T cells. Thus, PD-L2 is a negative predictor for prognosis among solid cancer patients.


Pssm-ID: 409578  Cd Length: 82  Bit Score: 61.20  E-value: 3.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885 138 NQRISVDPATSEHELICQAEGYPEAEVIWTNsdhqpVSGKRSVTTSRTEGMLLNVTSSLRVNATANDVFYCTFWRSqpgq 217
Cdd:cd20986   1 DTHILEVPGTGEVQLTCQARGYPLAEVSWQN-----VSVPANTSHTRTPEGLYQVTSVLRLKPQPGRNFSCMFWNA---- 71


                ....*.
gi 83287885 218 nHTAEL 223
Cdd:cd20986  72 -HMKEL 76
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
 19-114 8.78e-08

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 49.50  E-value: 8.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  19 FTITAPKDLYVVEYGSNVTMECR-FPverELDLLALVVYW--EKEDEQVIQFVAGEEDLKPQHSNFRGRASLPKDQLLKG 95
Cdd:cd05713   1 FSVIGPTEPILALVGEDAELPCHlSP---KMSAEHMEVRWfrSQFSPVVHLYRDGQDQEEEQMPEYRGRTELLKDAIAEG 77

                        90
                ....*....|....*....
gi 83287885  96 NAALQITDVKLQDAGVYCC 114
Cdd:cd05713  78 SVALRIHNVRPSDEGQYTC 96
IgV_CD86 cd16087
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here ...
 40-116 1.41e-07

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). 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 CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family 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.


Pssm-ID: 409508  Cd Length: 108  Bit Score: 48.86  E-value: 1.41e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83287885  40 CRFPVERELDLLALVVYWEKEDEQVI-QFVAGEEDLKPQHSNFRGRASLPKDqllkgNAALQITDVKLQDAGVYCCII 116
Cdd:cd16087  15 CQFKNPQNISLSELVVFWQDQKKLVLyELYLGKEKLDNVNSKYIGRTSFDQE-----NWTLQLHNVQIKDQGTYQCFI 87
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 33-129 3.59e-07

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: 47.83  E-value: 3.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  33 GSNVTMECRFPVERE----LDLLALVVYWEKEDEQVIQFVAGE--EDLKPQHsnfRGRASLpKDQLLKGNAALQITDVKL 106
Cdd:cd20960  15 GENVTLPCHHQLGLEdqgtLDIEWLLLPSDKVEKVVITYSGDRvyNHYYPAL---KGRVAF-TSNDLSGDASLNISNLKL 90

                        90       100
                ....*....|....*....|....
gi 83287885 107 QDAGVYCC-IISYGGADYKRITLK 129
Cdd:cd20960  91 SDTGTYQCkVKKAPGYAWSKITLI 114
IgV_B7-H2 cd20935
Immunoglobulin Variable (IgV) domain of B7-H2 (B7 homolog 2); The members here are composed of ...
 33-116 4.98e-07

Immunoglobulin Variable (IgV) domain of B7-H2 (B7 homolog 2); The members here are composed of the immunoglobulin variable (IgV) domain of B7-H2 (B7 homolog 2 also known as ICOSL (inducible T cell costimulator ligand) or CD275). B7-H2 is a ligand for the T-cell-specific cell surface receptor ICOS and acts as a costimulatory signal for T-cell proliferation and cytokine secretion. The interaction of ICOS with ICOSL (B7-H2) regulates T cell activation and expansion, is involved in T cell dependent B cell activation, and T-helper cell differentiation. It is a member of the B7 family of immune regulatory proteins and shares homology with other B7 ligands, such as B7-1, B7-2, B7-H1 (PD-L1), PD-L2, and B7-H3. The extracellular domains of B7 proteins contain two Ig-like domains and all members have short cytoplasmic domains. These ligands are typically expressed on antigen presenting cells (such as macrophages, B cells and dendritic cells) and have the ability to regulate T-cell proliferation and function. Tumor cells are also capable of expressing the B7 family members in order to evade immune surveillance.


Pssm-ID: 409529  Cd Length: 113  Bit Score: 47.55  E-value: 4.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  33 GSNVTMECRFPVERELDLLALVVYWEKE--DEQVIQFVAGEEDLKPQHSNFRGRASLPKDQLLKGNAALQITDVKLQDAG 110
Cdd:cd20935   8 GSDVELSCICPEGSRFDLNDLYVYWQISesETVVTYHLPQNSSLENVDSHYRNRALLSLDSMKQGDFSLRLFNVTPQDEQ 87


                ....*.
gi 83287885 111 VYCCII 116
Cdd:cd20935  88 KFHCLV 93
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 24-130 6.26e-07

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 46.34  E-value: 6.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885     24 PKDLYVVEyGSNVTMECRFPVERELdllalVVYWEKEDEQVIQFvageedlkpqhsnfRGRASLPKDqllKGNAALQITD 103
Cdd:smart00410   1 PPSVTVKE-GESVTLSCEASGSPPP-----EVTWYKQGGKLLAE--------------SGRFSVSRS---GSTSTLTISN 57

                           90       100
                   ....*....|....*....|....*...
gi 83287885    104 VKLQDAGVYCCIISYGGADYKR-ITLKV 130
Cdd:smart00410  58 VTPEDSGTYTCAATNSSGSASSgTTLTV 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 22-130 2.00e-06

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


Pssm-ID: 462230  Cd Length: 109  Bit Score: 45.53  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885    22 TAPKDLYVVEyGSNVTMECRFPVERELDLLalVVYWEK------EDEQVIQFVAGEEDLKPQhsnfrGRASLPKDQLlKG 95
Cdd:pfam07686   1 QTPREVTVAL-GGSVTLPCTYSSSMSEAST--SVYWYRqppgkgPTFLIAYYSNGSEEGVKK-----GRFSGRGDPS-NG 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 83287885    96 NAALQITDVKLQDAGVYCCIISYGGADY--KRITLKV 130
Cdd:pfam07686  72 DGSLTIQNLTLSDSGTYTCAVIPSGEGVfgKGTRLTV 108
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
 21-130 2.71e-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 [Multi-domain]  Cd Length: 92  Bit Score: 44.81  E-value: 2.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  21 ITAPKDLY--VVEYGSNVTMECRFPVERELDllalvVYWEKEDEQVIQFVAGEEdlkpqhsnFRGRASLpkdqllkgnaa 98
Cdd:cd20970   3 ISTPQPSFtvTAREGENATFMCRAEGSPEPE-----ISWTRNGNLIIEFNTRYI--------VRENGTT----------- 58

                        90       100       110
                ....*....|....*....|....*....|....
gi 83287885  99 LQITDVKLQDAGVYCCIISYG--GADYKRITLKV 130
Cdd:cd20970  59 LTIRNIRRSDMGIYLCIASNGvpGSVEKRITLQV 92
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 20-117 1.99e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.17  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885    20 TITAPKDLYVVEYGSNVTMECR---FPVEReldllalvVYWEKEDEQVIQfvageedlkpqhsnfrgrASLPKDQLLKGN 96
Cdd:pfam13927   3 VITVSPSSVTVREGETVTLTCEatgSPPPT--------ITWYKNGEPISS------------------GSTRSRSLSGSN 56

                          90       100
                  ....*....|....*....|.
gi 83287885    97 AALQITDVKLQDAGVYCCIIS 117
Cdd:pfam13927  57 STLTISNVTRSDAGTYTCVAS 77
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 23-119 5.10e-05

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: 41.93  E-value: 5.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  23 APKDLYVVEYGSNVTMECRFPVERELDLLALV-VYWEK-----EDEQVIQFVAGeeDLKPQHSNFRGRASLPKDQllKGN 96
Cdd:cd05877   2 TVQAKVFSHRGGNVTLPCRYHYEPELSAPRKIrVKWTKlevdyAKEEDVLVAIG--TRHKSYGSYQGRVFLRRAD--DLD 77

                        90       100
                ....*....|....*....|...
gi 83287885  97 AALQITDVKLQDAGVYCCIISYG 119
Cdd:cd05877  78 ASLVITDLRLEDYGRYRCEVIDG 100
IgV_B7-H6 cd20981
Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the ...
 35-114 5.66e-05

Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H6 (also known as NCR3LG1). B7-H6 contains one IgV domain and one IgC domain (IgV-IgC) and belongs to the B7-family, which consists of structurally related cell-surface protein ligands which bind to receptors on lymphocytes that regulate immune responses. B7-H6 is a ligand of NKp30, which is a member of CD28 family and an activating receptor of natural killer (NK) cells. The expression of NKp30 has been found in most of NK cells, which is involved in the process of tumor cell killing and interaction with antigen presenting cells (APCs) such as dendritic cells. Studies showed that NK cells eliminate B7-H6-expressing tumor cells either directly via cytotoxicity or indirectly by cytokine secretion. For instance, chimeric NKp30-expressing T cells responded to B7-H6(+) tumor cells and those T cells produced IFN-gamma and killed B7-H6-expressing tumor cells in vivo. B7-H6 mRNA is not found in normal cells, while high expression of B7-H6 is found in certain type tumor cells, such as lymphoma, leukemia, ovarian cancer, brain tumors, breast cancers, and various sarcomas. Since B7-H6 can bind NKp30 to exert anti-tumor effects by NK cells, which are able to recognize the difference between cancer cells and normal cells, B7-H6 may serve as a promising target for cancer immunotherapy.


Pssm-ID: 409573  Cd Length: 114  Bit Score: 41.83  E-value: 5.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  35 NVTMECRFPVERELDLLALVVYWEKEDEQVIQFVAGEEDLKPQHSNFRGRASLPKDQLLKGNAALQITDVKLQDAGVYCC 114
Cdd:cd20981  18 NVTIFCNIFYSQPLNITSMGITWFRKSLTFDKEVKVFEFFGDHQKAFRPGAIVSPWRLKSGDASLQLPGVQLEEAGEYRC 97
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 21-130 9.06e-05

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: 41.46  E-value: 9.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  21 ITAPKDLYVVeYGSNVTMECRFPVERELD-------LLALVVYWE---KEDEQVIqFVAGEEDLKPQhSNFRGRASLPKD 90
Cdd:cd05900   1 IPLESPLRVV-LGSSLLIPCYFQDPIAKDpgaptvaPLSPRIKWSfisKEKESVL-LVATEGKVRVN-TEYLDRVSLPNY 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 83287885  91 QLLKGNAALQITDVKLQDAGVYCCIISYGGAD-YKRITLKV 130
Cdd:cd05900  78 PAIPSDATLEITELRSNDSGTYRCEVMHGIEDnYDTVEVQV 118
IgV_NKp30 cd20926
Immunoglobulin variable (IgV) domain of Natural Killer cell activating receptor NKp30 and ...
 18-114 1.09e-04

Immunoglobulin variable (IgV) domain of Natural Killer cell activating receptor NKp30 and similar domains; The members here are composed of the immunoglobulin variable region (IgV) of Natural Killer cell activating receptor NKp30 (also known as Natural Cytotoxicity triggering Receptor 3 (NCR3)) and similar domains. NKp30 Recognizes the N-Terminal IgV Domain of B7-H6. In humans, the activating natural cytotoxicity receptor NKp30 plays a major role in NK cell-mediated tumor cell lysis. NKp30 recognizes the cell-surface protein B7-H6, which is expressed on tumor, but not healthy, cells.


Pssm-ID: 409520  Cd Length: 112  Bit Score: 40.73  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  18 AFTITAPKDLYVVEyGSNVTMECRFPVERELDLLALVVYWEKEdeqviqfVAGEEDLKPQHSNFRGR-ASLPKDQLLKGN 96
Cdd:cd20926   1 ALWVSQPPEIRTLE-GSSAFLPCSFNASQGRLAIGSVTWFRDE-------VAPGKEVRNGTPEFRGRlAPLASSRFLRDH 72

                        90
                ....*....|....*....
gi 83287885  97 -AALQITDVKLQDAGVYCC 114
Cdd:cd20926  73 qAELHIWDVRGHDAGIYVC 91
IgV_VISTA cd20980
Immunoglobulin variable (IgV) domain of V-domain immunoglobulin suppressor of T cell ...
 21-116 1.14e-04

Immunoglobulin variable (IgV) domain of V-domain immunoglobulin suppressor of T cell activation (VISTA); The members here are composed of the immunoglobulin variable (IgV) domain of V-domain immunoglobulin suppressor of T cell activation (VISTA; also known as B7-H5, PD-1H, Gi24, Dies1, SISP1 and DD1alpha). VISTA is an immune checkpoint protein involved in the regulation of T cell activity and inhibits the T cell response against cancer. VISTA is a type I transmembrane protein with a single IgV domain with sequence homology to the IgV domains of the members of B7 family. VISTA is the only B7 family member that lacks an IgC domain. VISTA is primarily expressed in white blood cells and its transcription is partially controlled by p53. Similar to PD-1/PD-L1 and CTLA-4, a blockade of VISTA promotes tumor clearance by the immune system. Unlike the B7 family members, VISTA contains 10 beta-strands, instead of the nine that typically comprises of an IgV fold. Moreover, human VISTA contains the 21-residue extended loop between stands C and C', which does not align with any B7 family structure.


Pssm-ID: 409572  Cd Length: 147  Bit Score: 41.45  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  21 ITAPKDLYVVEYGSNVTMECRF--PVERELDLLALVVYWE---------KEDEQVIQFVAgeEDLKPQHSNFRGRAS--L 87
Cdd:cd20980   2 VATPYSLYVCPEGQNVTLTCRLlgPVDKGHDVTFYKTWYRssrgevqtcSERRPIRNLTF--QDLHLHHGGQAANTShdL 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 83287885  88 PKDQLLK------GNAALQITDVKLQDAGVYCCII 116
Cdd:cd20980  80 AQRHGLEsasdhhGNFSITMRNLTLLDSGLYCCLV 114
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 151-225 2.13e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 39.41  E-value: 2.13e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83287885    151 ELICQAEGYPEAEVIWTNSDHQPVSGKRSVTTSRTEGmllnvTSSLRV-NATAND--VFYCTFWRSQPGQNHTAELII 225
Cdd:smart00410  13 TLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGS-----TSTLTIsNVTPEDsgTYTCAATNSSGSASSGTTLTV 85
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 33-122 2.13e-04

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: 40.29  E-value: 2.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  33 GSNVTMECRF-----PVERELDLLALVVYWEK------EDEQVIQFVAGEEDLKpQHSNFRGRASLPKDQLLKGNAALQI 101
Cdd:cd05878  12 GTSVTLPCYFidpphPVTPSTAPLAPRIKWSKvsvdgkKEKEVVLLVATEGRVR-VNSAYQGRVSLPNYPAIPSDATLEV 90

                        90       100
                ....*....|....*....|.
gi 83287885 102 TDVKLQDAGVYCCIISYGGAD 122
Cdd:cd05878  91 QSLRASDSGLYRCEVMHGIED 111
IgV_CD33 cd05712
Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic ...
 19-112 2.27e-04

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.


Pssm-ID: 409377  Cd Length: 119  Bit Score: 40.07  E-value: 2.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  19 FTITAPKDLYVVEyGSNVTMECRFPVERELDLLALV-VYWEKE--DEQVIQFVAGEEDLKPQHSNFRGRASLPKDqLLKG 95
Cdd:cd05712   1 WGLQMPKSVTVQE-GLCVLIPCSFSYPADYWVSNPVhGYWYRGgpYPKYRPPVATNNRTREVHESTQGRFRLLGD-PGKK 78

                        90
                ....*....|....*..
gi 83287885  96 NAALQITDVKLQDAGVY 112
Cdd:cd05712  79 NCSLSISDARPEDSGKY 95
IgV_TIM-3_like cd20982
Immunoglobulin Variable (IgV) domain of T cell Immunoglobulin Domain and Mucin Domain 3 (Tim-3) ...
 28-132 2.53e-04

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: 39.75  E-value: 2.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  28 YVVEYGSNVTMECRFPVERELDLLAlvVYWEKEDEQVIQFV-----AGEEDLKPQHSNfrgRASLpKDQLLKGNAALQIT 102
Cdd:cd20982   3 YRAEVGHNAYLPCSYTTAAPGNLVP--VCWGKGACPVSYCGnvllrTDERDVTYQKSS---RYQL-KGDFSKGDVSLTIE 76

                        90       100       110
                ....*....|....*....|....*....|.
gi 83287885 103 DVKLQDAGVYCCIISYGGA-DYKRITLKVNA 132
Cdd:cd20982  77 NVTLADSGIYCCRIQIPGImNDEKFNLKLVI 107
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 33-122 4.80e-04

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: 39.12  E-value: 4.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  33 GSNVTMECRF---PVERELDLLALVVYWEK------EDEQVIQFVAGEEDLKPQHSnFRGRASLPKDQLLKGNAALQITD 103
Cdd:cd05714  12 GGNVTLPCKFyrdPTAFGSGIHKIRIKWTKltsdsgYLKEVDVLVAMGNVVYHKKT-YGGRVSVPLKPGSDSDASLVITD 90

                        90
                ....*....|....*....
gi 83287885 104 VKLQDAGVYCCIISYGGAD 122
Cdd:cd05714  91 LTASDYGLYRCEVIEGIED 109
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 80-131 1.39e-03

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: 38.02  E-value: 1.39e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 83287885  80 NFRGRASLPKDQLLKGNAALQITDVKLQDAGVYCCIISYGGADYK-RITLKVN 131
Cdd:cd05901  72 EYMGRVSVPSHPEDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQdTVSLDVS 124
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 21-114 1.59e-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 [Multi-domain]  Cd Length: 98  Bit Score: 37.24  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  21 ITAPKDlYVVEYGSNVTMECRFPVERELdllalVVYWEKEDEQVIQFVAgeedlKPQHSNFRGRASLPKDqllkgnaaLQ 100
Cdd:cd05726   3 VVKPRD-QVVALGRTVTFQCETKGNPQP-----AIFWQKEGSQNLLFPY-----QPPQPSSRFSVSPTGD--------LT 63

                        90
                ....*....|....
gi 83287885 101 ITDVKLQDAGVYCC 114
Cdd:cd05726  64 ITNVQRSDVGYYIC 77
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 151-209 1.75e-03

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 36.39  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 83287885   151 ELICQAEGYPEAEVIWTNSDHQPVSGKRSVTTSRTEGMLLNVTsslrvNATAND--VFYCT 209
Cdd:pfam13927  20 TLTCEATGSPPPTITWYKNGEPISSGSTRSRSLSGSNSTLTIS-----NVTRSDagTYTCV 75
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 24-124 3.18e-03

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.


Pssm-ID: 409355 [Multi-domain]  Cd Length: 111  Bit Score: 36.54  E-value: 3.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  24 PKDLyVVEYGSNVTMECRFPVERELDllalVVYWEKEDE-QVIQFVAGEEDLKPQHS-----NFRGRASLPKDqllkgnA 97
Cdd:cd00099   5 PRSL-SVQEGESVTLSCEVSSSFSST----YIYWYRQKPgQGPEFLIYLSSSKGKTKggvpgRFSGSRDGTSS------F 73

                        90       100
                ....*....|....*....|....*..
gi 83287885  98 ALQITDVKLQDAGVYCCIISYGGADYK 124
Cdd:cd00099  74 SLTISNLQPEDSGTYYCAVSESGGTDK 100
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 24-128 3.64e-03

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: 36.02  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885    24 PKDLYVVEYGSNVTMECRFpverELDLLALVVYWEKEDEQVIqfvagEEDLKPQHSNFRGRASLpkdqllkgnaalQITD 103
Cdd:pfam00047   2 APPTVTVLEGDSATLTCSA----STGSPGPDVTWSKEGGTLI-----ESLKVKHDNGRTTQSSL------------LISN 60

                          90       100
                  ....*....|....*....|....*.
gi 83287885   104 VKLQDAGVYCCIISY-GGADYKRITL 128
Cdd:pfam00047  61 VTKEDAGTYTCVVNNpGGSATLSTSL 86
IgV_CD80 cd16086
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here ...
 36-116 5.35e-03

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: 35.89  E-value: 5.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  36 VTMECRFPVERElDLLALVVYWEKEDEQVIQFVAGEEDLKPQHSNfRGRASLPKdqllkgNAALQITDVKLQDAGVYCCI 115
Cdd:cd16086  12 ALLSCDYNVSVD-ELAQVRIYWQKDDKMVLTIISGDVKVWPEYKN-RTLFDITN------NLSIVILALRLSDRGTYTCV 83


                .
gi 83287885 116 I 116
Cdd:cd16086  84 V 84
IgV_CD2_like_N cd05775
N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; ...
 54-130 5.45e-03

N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; The members here are composed of the N-terminal immunoglobulin (Ig)-like domain (or domain 1) of T-cell surface antigen Clusters of Differentiation (CD) 2 and similar proteins. CD2 is a T-cell specific surface glycoprotein and is critically important for mediating adhesion between T cells and antigen-presenting cells or between cytolytic T cells and target cells. CD2 is located on chromosome 1 at 1p13 in humans and on chromosome 3 in mice. CD2 contains an extracellular domain with two or Ig-like domains, a single transmembrane segment, and a cytoplasmic region rich in proline and basic residues.


Pssm-ID: 409431  Cd Length: 98  Bit Score: 35.79  E-value: 5.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  54 VVYWEKEDEQVIQFVAGEedlKPQHSN-FRGRASLPKdqllkGNAALQITDVKLQDAGVYCCIISY--GGADYKRITLKV 130
Cdd:cd05775  26 EIKWKKTKDKIVEWENNI---GPTYFGsFKDRVLLDK-----ESGSLTIKNLTKEDSGTYELEITStnGKVLSSKFTLEV 97
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 36-117 7.25e-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 [Multi-domain]  Cd Length: 70  Bit Score: 34.61  E-value: 7.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885  36 VTMECRFPVERELdllalVVYWEKEDEQVIQfvageedlkpqhsnfrgrASLPKDQLLKGNAALQITDVKLQDAGVYCCI 115
Cdd:cd00096   1 VTLTCSASGNPPP-----TITWYKNGKPLPP------------------SSRDSRRSELGNGTLTISNVTLEDSGTYTCV 57


                ..
gi 83287885 116 IS 117
Cdd:cd00096  58 AS 59
IGv smart00406
Immunoglobulin V-Type;
30-114 9.27e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 34.67  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83287885     30 VEYGSNVTMECRFPVERELDLLALVVYWEKEDEQVIQfvageedlkpqhSNFRGRASLPKDqLLKGNAALQITDVKLQDA 109
Cdd:smart00406   8 FSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSSYYQ------------ESYKGRFTISKD-TSKNDVSLTISNLRVEDT 74


                   ....*
gi 83287885    110 GVYCC 114
Cdd:smart00406  75 GTYYC 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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