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Conserved domains on  [gi|15042971|ref|NP_071314|]
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hyaluronan and proteoglycan link protein 2 precursor [Mus musculus]

Protein Classification

Link_domain_HAPLN_module_1 and Link_domain_HAPLN_module_2 domain-containing protein( domain architecture ID 10308845)

protein containing domains Ig, Link_domain_HAPLN_module_1, and Link_domain_HAPLN_module_2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 149-242 1.36e-58

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239595  Cd Length: 95  Bit Score: 183.78  E-value: 1.36e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 149 VVFPYQPSRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGHGR-PGIRSY 227
Cdd:cd03518   1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTvPGLRSY 80

                        90
                ....*....|....*
gi 15042971 228 GPRDRSRDRYDAFCF 242
Cdd:cd03518  81 GERDKMLSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 251-338 1.34e-48

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239596  Cd Length: 91  Bit Score: 158.36  E-value: 1.34e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 251 FFVPGRLTLSEAHAACRRRGAVVAKVGHLYAAWKFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPdPGVRSFGFPRPQQ 330
Cdd:cd03519   5 LLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLE-PGVRSFGFPDKKH 83


                ....*...
gi 15042971 331 ASYGTYCY 338
Cdd:cd03519  84 KLYGVYCY 91
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 46-151 1.21e-44

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 cd05877:

Pssm-ID: 472250  Cd Length: 117  Bit Score: 149.01  E-value: 1.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  46 IHSRRGATATLPCVL-----GTSPPSYKVRWSKVEPGELRETLILITNGLHARDYGLLGGRASLRRGHRLDASLIIKNVR 120
Cdd:cd05877   7 VFSHRGGNVTLPCRYhyepeLSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDASLVITDLR 86

                        90       100       110
                ....*....|....*....|....*....|.
gi 15042971 121 LEDEGRYRCELINGIEDESVALTLRLEGVVF 151
Cdd:cd05877  87 LEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
 
Name Accession Description Interval E-value
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 149-242 1.36e-58

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239595  Cd Length: 95  Bit Score: 183.78  E-value: 1.36e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 149 VVFPYQPSRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGHGR-PGIRSY 227
Cdd:cd03518   1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTvPGLRSY 80

                        90
                ....*....|....*
gi 15042971 228 GPRDRSRDRYDAFCF 242
Cdd:cd03518  81 GERDKMLSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 251-338 1.34e-48

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 158.36  E-value: 1.34e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 251 FFVPGRLTLSEAHAACRRRGAVVAKVGHLYAAWKFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPdPGVRSFGFPRPQQ 330
Cdd:cd03519   5 LLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLE-PGVRSFGFPDKKH 83


                ....*...
gi 15042971 331 ASYGTYCY 338
Cdd:cd03519  84 KLYGVYCY 91
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 46-151 1.21e-44

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: 149.01  E-value: 1.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  46 IHSRRGATATLPCVL-----GTSPPSYKVRWSKVEPGELRETLILITNGLHARDYGLLGGRASLRRGHRLDASLIIKNVR 120
Cdd:cd05877   7 VFSHRGGNVTLPCRYhyepeLSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDASLVITDLR 86

                        90       100       110
                ....*....|....*....|....*....|.
gi 15042971 121 LEDEGRYRCELINGIEDESVALTLRLEGVVF 151
Cdd:cd05877  87 LEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Xlink pfam00193
Extracellular link domain;
149-242 1.10e-43

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 145.41  E-value: 1.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971   149 VVFPYQpSRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGhGRPGIRSYG 228
Cdd:pfam00193   1 GVFHLE-SPGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGG-NMPGVRQYG 78

                          90
                  ....*....|....
gi 15042971   229 PRDRSRDRYDAFCF 242
Cdd:pfam00193  79 FRDPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
147-243 2.83e-35

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 123.61  E-value: 2.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971    147 EGVVFPYQPsRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGhGRPGIRS 226
Cdd:smart00445   1 DGGVFHVEK-NGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG-NLPGVRQ 78

                           90
                   ....*....|....*..
gi 15042971    227 YGPRDrSRDRYDAFCFT 243
Cdd:smart00445  79 YGFPD-PTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
250-338 6.51e-34

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 119.99  E-value: 6.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971   250 VFFVPGR----LTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSFGF 325
Cdd:pfam00193   2 VFHLESPgrykLTFQEAQAACAALGATLATPEQLYAAWK-AGLDTCDAGWLADGTVRYPITTPRPNCGG-NMPGVRQYGF 79

                          90
                  ....*....|...
gi 15042971   326 PRPQQASYGTYCY 338
Cdd:pfam00193  80 RDPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
248-339 4.07e-31

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 112.82  E-value: 4.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971    248 GQVFFV----PGRLTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSF 323
Cdd:smart00445   2 GGVFHVekngRYKLTFAEAREACRAQGATLATVGQLYAAWQ-DGFDTCDAGWLADGSVRYPIITPRPRCGG-NLPGVRQY 79

                           90
                   ....*....|....*.
gi 15042971    324 GFPRPqQASYGTYCYA 339
Cdd:smart00445  80 GFPDP-TSRYDAYCFN 94
IGv smart00406
Immunoglobulin V-Type;
53-130 1.33e-10

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 57.01  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971     53 TATLPC-VLGTSPPSYKVRWSKVEPGELRETLILITNGLHARDYGLLGGRASLRR-GHRLDASLIIKNVRLEDEGRYRCE 130
Cdd:smart00406   1 SVTLSCkFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSSYYQESYKGRFTISKdTSKNDVSLTISNLRVEDTGTYYCA 80
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 50-133 5.73e-10

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: 55.93  E-value: 5.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971    50 RGATATLPCVLGTSP--PSYKVRWSKVEPGELRETLILITNGLhaRDYGLLGGRASLRRGHRL-DASLIIKNVRLEDEGR 126
Cdd:pfam07686  10 LGGSVTLPCTYSSSMseASTSVYWYRQPPGKGPTFLIAYYSNG--SEEGVKKGRFSGRGDPSNgDGSLTIQNLTLSDSGT 87


                  ....*..
gi 15042971   127 YRCELIN 133
Cdd:pfam07686  88 YTCAVIP 94
 
Name Accession Description Interval E-value
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 149-242 1.36e-58

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239595  Cd Length: 95  Bit Score: 183.78  E-value: 1.36e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 149 VVFPYQPSRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGHGR-PGIRSY 227
Cdd:cd03518   1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTvPGLRSY 80

                        90
                ....*....|....*
gi 15042971 228 GPRDRSRDRYDAFCF 242
Cdd:cd03518  81 GERDKMLSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 251-338 1.34e-48

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 158.36  E-value: 1.34e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 251 FFVPGRLTLSEAHAACRRRGAVVAKVGHLYAAWKFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPdPGVRSFGFPRPQQ 330
Cdd:cd03519   5 LLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLE-PGVRSFGFPDKKH 83


                ....*...
gi 15042971 331 ASYGTYCY 338
Cdd:cd03519  84 KLYGVYCY 91
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 46-151 1.21e-44

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: 149.01  E-value: 1.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  46 IHSRRGATATLPCVL-----GTSPPSYKVRWSKVEPGELRETLILITNGLHARDYGLLGGRASLRRGHRLDASLIIKNVR 120
Cdd:cd05877   7 VFSHRGGNVTLPCRYhyepeLSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDASLVITDLR 86

                        90       100       110
                ....*....|....*....|....*....|.
gi 15042971 121 LEDEGRYRCELINGIEDESVALTLRLEGVVF 151
Cdd:cd05877  87 LEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Xlink pfam00193
Extracellular link domain;
149-242 1.10e-43

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 145.41  E-value: 1.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971   149 VVFPYQpSRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGhGRPGIRSYG 228
Cdd:pfam00193   1 GVFHLE-SPGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGG-NMPGVRQYG 78

                          90
                  ....*....|....
gi 15042971   229 PRDRSRDRYDAFCF 242
Cdd:pfam00193  79 FRDPLSERYDAYCY 92
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 149-242 6.27e-41

The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It is found in the CD44 receptor and in human TSG-6. TSG-6 is the protein product of the tumor necrosis factor-stimulated gene-6. TSG-6 has a strong anti-inflammatory effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. This group also contains the link domains of the chondroitin sulfate proteoglycan core proteins (CSPG) including aggrecan, versican, neurocan, and brevican and the link domains of the vertebrate HAPLN (HA and proteoglycan binding link) protein family. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates in which other CSPGs substitute for aggregan might contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN gene family are physically linked adjacent to CSPG genes. TSG-6 contains a single link module which supports high affinity binding with HA. The functional HA-binding domain of CD44 is an extended domain comprised of a link module flanked with N-and C- extensions. These extensions are essential for folding and functional activity. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of the CSPG aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) which contains link modules 3 and 4 which lack HA-binding activity. HAPLNs contain two contiguous link modules.


Pssm-ID: 238534  Cd Length: 92  Bit Score: 138.32  E-value: 6.27e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 149 VVFPYQPSRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGhGRPGIRSYG 228
Cdd:cd01102   1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGG-RNPGVRSYG 79

                        90
                ....*....|....
gi 15042971 229 PRDRSrDRYDAFCF 242
Cdd:cd01102  80 NPAPS-GRYDAYCF 92
LINK smart00445
Link (Hyaluronan-binding);
147-243 2.83e-35

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 123.61  E-value: 2.83e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971    147 EGVVFPYQPsRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGhGRPGIRS 226
Cdd:smart00445   1 DGGVFHVEK-NGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG-NLPGVRQ 78

                           90
                   ....*....|....*..
gi 15042971    227 YGPRDrSRDRYDAFCFT 243
Cdd:smart00445  79 YGFPD-PTSRYDAYCFN 94
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 249-338 5.55e-34

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan 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: 239597  Cd Length: 96  Bit Score: 120.50  E-value: 5.55e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 249 QVFFV--PGRLTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSF--- 323
Cdd:cd03520   1 EVFYAtaPEKFTFQEARAECRSLGAVLATTGQLYAAWR-QGLDQCDPGWLADGSVRYPISTPRPQCGG-GLPGVRTLyrf 78

                        90
                ....*....|....*....
gi 15042971 324 ----GFPRPqQASYGTYCY 338
Cdd:cd03520  79 pnqtGFPDP-HSRFDAYCF 96
Xlink pfam00193
Extracellular link domain;
250-338 6.51e-34

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 119.99  E-value: 6.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971   250 VFFVPGR----LTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSFGF 325
Cdd:pfam00193   2 VFHLESPgrykLTFQEAQAACAALGATLATPEQLYAAWK-AGLDTCDAGWLADGTVRYPITTPRPNCGG-NMPGVRQYGF 79

                          90
                  ....*....|...
gi 15042971   326 PRPQQASYGTYCY 338
Cdd:pfam00193  80 RDPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
248-339 4.07e-31

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 112.82  E-value: 4.07e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971    248 GQVFFV----PGRLTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSF 323
Cdd:smart00445   2 GGVFHVekngRYKLTFAEAREACRAQGATLATVGQLYAAWQ-DGFDTCDAGWLADGSVRYPIITPRPRCGG-NLPGVRQY 79

                           90
                   ....*....|....*.
gi 15042971    324 GFPRPqQASYGTYCYA 339
Cdd:smart00445  80 GFPDP-TSRYDAYCFN 94
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 257-338 6.28e-27

The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It is found in the CD44 receptor and in human TSG-6. TSG-6 is the protein product of the tumor necrosis factor-stimulated gene-6. TSG-6 has a strong anti-inflammatory effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. This group also contains the link domains of the chondroitin sulfate proteoglycan core proteins (CSPG) including aggrecan, versican, neurocan, and brevican and the link domains of the vertebrate HAPLN (HA and proteoglycan binding link) protein family. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates in which other CSPGs substitute for aggregan might contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN gene family are physically linked adjacent to CSPG genes. TSG-6 contains a single link module which supports high affinity binding with HA. The functional HA-binding domain of CD44 is an extended domain comprised of a link module flanked with N-and C- extensions. These extensions are essential for folding and functional activity. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of the CSPG aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) which contains link modules 3 and 4 which lack HA-binding activity. HAPLNs contain two contiguous link modules.


Pssm-ID: 238534  Cd Length: 92  Bit Score: 101.73  E-value: 6.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 257 LTLSEAHAACRRRGAVVAKVGHLYAAWKfSGLDQCDGGWLADGSVRFPITTPRPRCGGlPDPGVRSFGFPRPQQaSYGTY 336
Cdd:cd01102  14 LTFAEAALACKARGAHLATPGQLEAAWQ-DGFDVCTAGWLADGSVRYPIVTSRPNCGG-RNPGVRSYGNPAPSG-RYDAY 90


                ..
gi 15042971 337 CY 338
Cdd:cd01102  91 CF 92
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 149-242 1.60e-25

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with 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: 239594  Cd Length: 95  Bit Score: 98.25  E-value: 1.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 149 VVFPYQPSRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGH--GRPGIRS 226
Cdd:cd03517   1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDmdGFPGVRN 80

                        90
                ....*....|....*.
gi 15042971 227 YGPRDrSRDRYDAFCF 242
Cdd:cd03517  81 YGVRD-PDELYDVYCY 95
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 161-242 1.99e-25

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan 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: 239597  Cd Length: 96  Bit Score: 97.77  E-value: 1.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 161 QFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGhGRPGIRS-YGPRDRS-----R 234
Cdd:cd03520  10 KFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGG-GLPGVRTlYRFPNQTgfpdpH 88


                ....*...
gi 15042971 235 DRYDAFCF 242
Cdd:cd03520  89 SRFDAYCF 96
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 150-242 1.26e-23

This is the extracellular link domain of the type found in human TSG-6. The link domain is a hyaluronan (HA)-binding domain. TSG-6 is the protein product of tumor necrosis factor-stimulated gene-6. TSG-6 is up-regulated in inflammatory lesions and in the ovary during ovulation. It has a strong anti-inflammatory and chondroprotective effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. Also included in this group are the stabilins: stabilin-1 (FEEL-1, CLEVER-1) and stabilin-2 (FEEL-2). Stabilin-2 functions as the major liver and lymph node-scavenging receptor for HA and related glycosaminoglycans. Stabilin-2 is a scavenger receptor with a broad range of ligands including advanced glycation end (AGE) products, acetylated low density lipoprotein and procollagen peptides. In contrast, stabilin-1 does not bind HA, but binds acetylated low density lipoprotein and AGEs with lower affinity. As AGEs accumulate in vascular tissues during aging and diabetes, these receptors may be implicated in the pathologies of these states. Both stabilins are present in the early endocytic pathway in hepatic sinusoidal epithelium associating with clathrin/AP-2. Stabilin-1 is expressed in macrophages. Stabilin-2 is absent from the latter. In macrophages: stabilin-1 is involved in trafficking between early/sorting endosomes and the trans-Golgi network. Stabilin-1 has also been implicated in angiogenesis and possibly leucocyte trafficking. Both stabilins bind gram-positive and gram-negative bacteria. TSG-6 and stabilins contain a single link module which supports high affinity binding to HA.


Pssm-ID: 239592  Cd Length: 93  Bit Score: 92.91  E-value: 1.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 150 VFPYQPSRGRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCgGHGRPGIRSYGP 229
Cdd:cd03515   2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANC-GFGHVGIVDYGP 80

                        90
                ....*....|...
gi 15042971 230 RDRSRDRYDAFCF 242
Cdd:cd03515  81 RLNLSERWDAYCY 93
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 257-338 2.62e-21

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with 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: 239594  Cd Length: 95  Bit Score: 86.69  E-value: 2.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 257 LTLSEAHAACRRRGAVVAKVGHLYAAWkFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPD--PGVRSFGfPRPQQASYG 334
Cdd:cd03517  14 LTFPRAQRACLDISAQIATPEQLLAAY-EDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDgfPGVRNYG-VRDPDELYD 91


                ....
gi 15042971 335 TYCY 338
Cdd:cd03517  92 VYCY 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 148-242 1.74e-20

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 84.40  E-value: 1.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 148 GVVFPYQPSRgryqFNYFEAKRACEEQDGRLATYGQLYQAWT-EGLDWCNAGWLLEGSVRYPVLTARAPCGGHgRPGIRS 226
Cdd:cd03519   1 GVFYLLHPGK----LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPL-EPGVRS 75

                        90
                ....*....|....*.
gi 15042971 227 YGPRDRSRDRYDAFCF 242
Cdd:cd03519  76 FGFPDKKHKLYGVYCY 91
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 46-151 1.03e-19

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: 83.41  E-value: 1.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  46 IHSRRGATATLPCVLGTSPPSY-------KVRWSKVE--PGELRETLILITNGL---HARDYGllgGRASL--RRGHRLD 111
Cdd:cd05714   7 VFSHLGGNVTLPCKFYRDPTAFgsgihkiRIKWTKLTsdSGYLKEVDVLVAMGNvvyHKKTYG---GRVSVplKPGSDSD 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15042971 112 ASLIIKNVRLEDEGRYRCELINGIEDESVALTLRLEGVVF 151
Cdd:cd05714  84 ASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 51-151 7.50e-13

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: 64.56  E-value: 7.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  51 GATATLPCVLGTSP---PSY------KVRWSKVE--PGELRETLILITNGLHARDYGLLGGRASL-----RRGhrlDASL 114
Cdd:cd05878  12 GTSVTLPCYFIDPPhpvTPStaplapRIKWSKVSvdGKKEKEVVLLVATEGRVRVNSAYQGRVSLpnypaIPS---DATL 88

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15042971 115 IIKNVRLEDEGRYRCELINGIEDESVALTLRLEGVVF 151
Cdd:cd05878  89 EVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 46-151 1.93e-12

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: 63.44  E-value: 1.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  46 IHSRRGATATLPC---VLGTSPPSY-------KVRWSKVEPG----ELRETLILIT-NGL--HARDYGllgGRASL--RR 106
Cdd:cd05901   7 VHGSLSGSVVLPCrfsTLPTLPPSYnitseflRIKWTKIQVDkngkDHKETTVLVAqNGIikIGQEYM---GRVSVpsHP 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15042971 107 GHRLDASLIIKNVRLEDEGRYRCELINGIEDESVALTLRLEGVVF 151
Cdd:cd05901  84 EDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 35-151 1.22e-10

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: 58.41  E-value: 1.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  35 PHYLLPPIHEVihsrrgatatlPCVLGTSPPSYKVRWSKVEPGelRETLILITNGLHARDYGLLGGRASLRRGHRL--DA 112
Cdd:cd05900  18 PCYFQDPIAKD-----------PGAPTVAPLSPRIKWSFISKE--KESVLLVATEGKVRVNTEYLDRVSLPNYPAIpsDA 84

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15042971 113 SLIIKNVRLEDEGRYRCELINGIEDESVALTLRLEGVVF 151
Cdd:cd05900  85 TLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
IGv smart00406
Immunoglobulin V-Type;
53-130 1.33e-10

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 57.01  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971     53 TATLPC-VLGTSPPSYKVRWSKVEPGELRETLILITNGLHARDYGLLGGRASLRR-GHRLDASLIIKNVRLEDEGRYRCE 130
Cdd:smart00406   1 SVTLSCkFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSSYYQESYKGRFTISKdTSKNDVSLTISNLRVEDTGTYYCA 80
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 53-151 1.39e-10

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. 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. Unlike aggrecan which is widely distributed 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: 409483  Cd Length: 121  Bit Score: 57.92  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  53 TATLPCVLgTSPPSY-------KVRWSKVEPGELRETLILitngLHARDYGL-----LGGRASL--RRGHRLDASLIIKN 118
Cdd:cd05902  14 SVLLPCVF-TLPPSAssppegpRIKWTKLSTSGGQQQRPV----LVARDNVVrvakaFQGRVSLpgYPKNRYNASLVLSR 88

                        90       100       110
                ....*....|....*....|....*....|...
gi 15042971 119 VRLEDEGRYRCELINGIEDESVALTLRLEGVVF 151
Cdd:cd05902  89 LRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 256-338 4.50e-10

This is the extracellular link domain of the type found in human TSG-6. The link domain is a hyaluronan (HA)-binding domain. TSG-6 is the protein product of tumor necrosis factor-stimulated gene-6. TSG-6 is up-regulated in inflammatory lesions and in the ovary during ovulation. It has a strong anti-inflammatory and chondroprotective effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. Also included in this group are the stabilins: stabilin-1 (FEEL-1, CLEVER-1) and stabilin-2 (FEEL-2). Stabilin-2 functions as the major liver and lymph node-scavenging receptor for HA and related glycosaminoglycans. Stabilin-2 is a scavenger receptor with a broad range of ligands including advanced glycation end (AGE) products, acetylated low density lipoprotein and procollagen peptides. In contrast, stabilin-1 does not bind HA, but binds acetylated low density lipoprotein and AGEs with lower affinity. As AGEs accumulate in vascular tissues during aging and diabetes, these receptors may be implicated in the pathologies of these states. Both stabilins are present in the early endocytic pathway in hepatic sinusoidal epithelium associating with clathrin/AP-2. Stabilin-1 is expressed in macrophages. Stabilin-2 is absent from the latter. In macrophages: stabilin-1 is involved in trafficking between early/sorting endosomes and the trans-Golgi network. Stabilin-1 has also been implicated in angiogenesis and possibly leucocyte trafficking. Both stabilins bind gram-positive and gram-negative bacteria. TSG-6 and stabilins contain a single link module which supports high affinity binding to HA.


Pssm-ID: 239592  Cd Length: 93  Bit Score: 55.93  E-value: 4.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 256 RLTLSEAHAACRRRGAVVAKVGHLYAAWKFsGLDQCDGGWLADGSVRFPITTPRPRCgGLPDPGVRSFGFPRPQQASYGT 335
Cdd:cd03515  13 KLTYTEAKAACEAEGAHLATYSQLSAAQQL-GFHLCAAGWLAKGRVGYPIVFPSANC-GFGHVGIVDYGPRLNLSERWDA 90


                ...
gi 15042971 336 YCY 338
Cdd:cd03515  91 YCY 93
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 50-133 5.73e-10

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: 55.93  E-value: 5.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971    50 RGATATLPCVLGTSP--PSYKVRWSKVEPGELRETLILITNGLhaRDYGLLGGRASLRRGHRL-DASLIIKNVRLEDEGR 126
Cdd:pfam07686  10 LGGSVTLPCTYSSSMseASTSVYWYRQPPGKGPTFLIAYYSNG--SEEGVKKGRFSGRGDPSNgDGSLTIQNLTLSDSGT 87


                  ....*..
gi 15042971   127 YRCELIN 133
Cdd:pfam07686  88 YTCAVIP 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 49-145 2.48e-09

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: 53.66  E-value: 2.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971     49 RRGATATLPCVLgTSPPSYKVRWSKVEPGELREtlilitnglhardygllGGRASLRRGHRlDASLIIKNVRLEDEGRYR 128
Cdd:smart00410   7 KEGESVTLSCEA-SGSPPPEVTWYKQGGKLLAE-----------------SGRFSVSRSGS-TSTLTISNVTPEDSGTYT 67

                           90
                   ....*....|....*..
gi 15042971    129 CELINGIEDESVALTLR 145
Cdd:smart00410  68 CAATNSSGSASSGTTLT 84
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 158-244 6.79e-08

This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It also plays an important role in arteriogenesis. The functional HA-binding domain of CD44 is an extended domain comprised of a single link module flanked with N-and C- extensions. These extensions are essential for folding and for functional activity. This group also contains the cell surface retention sequence (CRS) binding protein-1 (CRSBP-1) and lymph vessel endothelial receptor-1 (LYVE-1). CRSBP-1 is a cell surface binding protein for the CRS motif of PDGF-BB (platelet-derived growth factor-BB) and is responsible for the cell surface retention of PDGF-BB in SSV-transformed cells. CRSBP-1 may play a role in autocrine regulation of cell growth mediated by CRS containing growth regulators. LYVE-1 is preferentially expressed on the lymphatic endothelium and is used as a molecular marker for the detection and characterization of lymphatic vessels in tumors.


Pssm-ID: 239593  Cd Length: 144  Bit Score: 50.92  E-value: 6.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 158 GRYQFNYFEAKRACEEQDGRLATYGQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGHGRpGIrsYGPRDRSRDRY 237
Cdd:cd03516  15 GRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGT-GV--YILNSNLSSRY 91


                ....*..
gi 15042971 238 DAFCFTS 244
Cdd:cd03516  92 DAYCYNS 98
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 50-129 1.93e-07

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: 48.87  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  50 RGATATLPCVLGTSPPSYKVRWSKVEPGELREtLILITNGLHARDYGLLGGRASLRRGHRLDASLIIKNVRLEDEGRYRC 129
Cdd:cd00099  12 EGESVTLSCEVSSSFSSTYIYWYRQKPGQGPE-FLIYLSSSKGKTKGGVPGRFSGSRDGTSSFSLTISNLQPEDSGTYYC 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 54-141 2.10e-06

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: 44.63  E-value: 2.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  54 ATLPCVLgTSPPSYKVRWSKVEPGELRETLILITNGLHardygllggraslrrghrlDASLIIKNVRLEDEGRYRCELIN 133
Cdd:cd00096   1 VTLTCSA-SGNPPPTITWYKNGKPLPPSSRDSRRSELG-------------------NGTLTISNVTLEDSGTYTCVASN 60


                ....*...
gi 15042971 134 GIEDESVA 141
Cdd:cd00096  61 SAGGSASA 68
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 49-133 1.37e-05

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 42.55  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971    49 RRGATATLPC-VLGTSPPSYkvRWSKvepgelretlilitNGLHardygLLGGRASLRRGHRLDASLIIKNVRLEDEGRY 127
Cdd:pfam13927  14 REGETVTLTCeATGSPPPTI--TWYK--------------NGEP-----ISSGSTRSRSLSGSNSTLTISNVTRSDAGTY 72


                  ....*.
gi 15042971   128 RCELIN 133
Cdd:pfam13927  73 TCVASN 78
I-set pfam07679
Immunoglobulin I-set domain;
35-144 7.91e-05

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 40.70  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971    35 PHYLLPPIHEVIHSrrGATATLPC-VLGTSPPSykVRWSKvepgelretlilitnglhardygllgGRASLRRGHRL--- 110
Cdd:pfam07679   1 PKFTQKPKDVEVQE--GESARFTCtVTGTPDPE--VSWFK--------------------------DGQPLRSSDRFkvt 50

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 15042971   111 ----DASLIIKNVRLEDEGRYRCELINGIEDESVALTL 144
Cdd:pfam07679  51 yeggTYTLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 51-131 8.07e-05

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: 41.28  E-value: 8.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  51 GATATLPCVLGTSPPSY--KVRWSKVEPGElrETLILI---TNGLH-----ARDYGLLGGRASLRrghrlDASLIIKNVR 120
Cdd:cd05718  14 GGSVTLPCSLTSPGTTKitQVTWMKIGAGS--SQNVAVfhpQYGPSvpnpyAERVEFLAARLGLR-----NATLRIRNLR 86

                        90
                ....*....|.
gi 15042971 121 LEDEGRYRCEL 131
Cdd:cd05718  87 VEDEGNYICEF 97
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 43-144 1.70e-04

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: 40.51  E-value: 1.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  43 HEVIHSRRGATATLPCVLGTSP---PSYKVRWSKVEPGELRETLILITNGlHARD--YGLLGGRASL----RRGhrlDAS 113
Cdd:cd20960   7 QTEIKKVAGENVTLPCHHQLGLedqGTLDIEWLLLPSDKVEKVVITYSGD-RVYNhyYPALKGRVAFtsndLSG---DAS 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 15042971 114 LIIKNVRLEDEGRYRCELINGIEDESVALTL 144
Cdd:cd20960  83 LNISNLKLSDTGTYQCKVKKAPGYAWSKITL 113
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 54-144 2.61e-04

First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of the V-set of IgSF domains; The members here are composed of the first Ig-like domain of Junctional Adhesion Molecule-1 (JAM1)and similar domains. JAM1 is an immunoglobulin superfamily (IgSF) protein with two Ig-like domains in its extracellular region; it plays a role in the formation of endothelial and epithelial tight junction and acts as a receptor for mammalian reovirus sigma-1. The IgSF is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. The two sheets are linked together by a conserved disulfide bond between B strand and F strand. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The first Ig-like domain of JAM1 is a member of the V-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C'-C" in the other.


Pssm-ID: 409538  Cd Length: 102  Bit Score: 39.83  E-value: 2.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  54 ATLPCVLGTSPPSYKVRWSKVepGELRETLILITNGLHardyGLLGGRASLrrghrLDASLIIKNVRLEDEGRYRCELI- 132
Cdd:cd20946  17 VILSCKTPKKTSSPRVEWKKL--QRDVTFVVFQNNKIQ----GDYKGRAEI-----LGTNITIKNVTRSDSGKYRCEVSa 85

                        90
                ....*....|....*.
gi 15042971 133 ----NGIEDESVALTL 144
Cdd:cd20946  86 rsdgQNLGEVTVTLEV 101
IgI_7_Dscam cd20954
Seventh immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar ...
 50-135 3.03e-04

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 [Multi-domain]  Cd Length: 96  Bit Score: 39.22  E-value: 3.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  50 RGATATLPC-VLGTSPPSykVRWSKV---EPGELREtlILITNGLHARDYGllggraslrrghrldaSLIIKNVRLEDEG 125
Cdd:cd20954  15 AGQDVMLHCqADGFPTPT--VTWKKAtgsTPGEYKD--LLYDPNVRILPNG----------------TLVFGHVQKENEG 74

                        90
                ....*....|
gi 15042971 126 RYRCELINGI 135
Cdd:cd20954  75 HYLCEAKNGI 84
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
 51-145 5.45e-04

Third 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 third 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: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 38.15  E-value: 5.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  51 GATATLPCVLGTSPPSyKVRWSKvEPGELREtlilitnglhardygllgGRASLRRghrlDASLIIKNVRLEDEGRYRCE 130
Cdd:cd05725  12 DDSAEFQCEVGGDPVP-TVRWRK-EDGELPK------------------GRYEILD----DHSLKIRKVTAGDMGSYTCV 67

                        90
                ....*....|....*
gi 15042971 131 LINGIEDESVALTLR 145
Cdd:cd05725  68 AENMVGKIEASATLT 82
IgV_PD-L2 cd20983
Immunoglobulin Variable (IgV) domain of Programmed death ligand 2 (PD-L2); The members here ...
 51-146 6.49e-04

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: 38.71  E-value: 6.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  51 GATATLPCVLGTSPPsykvrwskVEPGELRETLILITNglharDYGLLGGRASLRRGHRL--DASLIIKNVRLEDEGRYR 128
Cdd:cd20983  16 GSNVTLECDFDTGEH--------VELGAIRASLQKVEN-----DTSLHSERATLLEEQLPlgKALFHIPSVQVRDAGQYR 82

                        90
                ....*....|....*...
gi 15042971 129 CELINGIEDESVALTLRL 146
Cdd:cd20983  83 CLIIYGVAWDYKYLTLKV 100
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 51-130 8.07e-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: 38.48  E-value: 8.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  51 GATATLPCVLGTSPPSYKVRWSKVEpGELRETLilitnGLHARDYG--LLG---GRASLRRGHRLDASLIIKNVRLEDEG 125
Cdd:cd05846  13 GGNATLSCNLTLPEEVLQVTWQKIK-ASSPENI-----VTYSKKYGvkIQPsyvRRISFTSSGLNSTSITIWNVTLEDEG 86


                ....*
gi 15042971 126 RYRCE 130
Cdd:cd05846  87 CYKCL 91
IgV_L_lambda cd04984
Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of ...
 51-131 9.67e-04

Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409373  Cd Length: 105  Bit Score: 38.21  E-value: 9.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  51 GATATLPCVL-GTSPPSYKVRWSKVEPGELRETLILITN----GLHARDYGLLGGRaslrrghrlDASLIIKNVRLEDEG 125
Cdd:cd04984  13 GETVTITCTGsSGNISGNYVNWYQQKPGSAPRYLIYEDKhrpsGIPDRFSGSKSGN---------TASLTISGAQTEDEA 83


                ....*.
gi 15042971 126 RYRCEL 131
Cdd:cd04984  84 DYYCQV 89
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 40-129 1.32e-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: 37.76  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  40 PPIHEVIHSRRGATATLPCVLGTSPPSYKVRWSKVEPGelRETLILITNGLHArdygllGGRASLRRGHR-LDASLIIKN 118
Cdd:cd05716   1 SVGPEVVTGVEGGSVTIQCPYPPKYASSRKYWCKWGSE--GCQTLVSSEGVVP------GGRISLTDDPDnGVFTVTLNQ 72

                        90
                ....*....|.
gi 15042971 119 VRLEDEGRYRC 129
Cdd:cd05716  73 LRKEDAGWYWC 83
IgI_Perlecan_like cd05754
Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of ...
 49-129 1.36e-03

Immunoglobulin (Ig)-like domain found in Perlecan and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain found in Perlecan. Perlecan is a large multi-domain heparin sulfate proteoglycan, important in tissue development and organogenesis. Perlecan can be represented as 5 major portions; its fourth major portion (domain IV) is a tandem repeat of immunoglobulin-like domains (Ig2-Ig15) which can vary in size due to alternative splicing. Perlecan binds many cellular and extracellular ligands. Its domain IV region has many binding sites. Some of these have been mapped at the level of individual Ig-like domains, including a site restricted to the Ig5 domain for heparin/sulfatide, a site restricted to the Ig3 domain for nidogen-1 and nidogen-2, a site restricted to Ig4-5 for fibronectin, and sites restricted to Ig2 and to Ig13-15 for fibulin-2. 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: 409412  Cd Length: 85  Bit Score: 37.15  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  49 RRGATATLPCVLGTSPPSYKVRWSKVEpGELRETlilitnglhARDYgllGGRaslrrghrldasLIIKNVRLEDEGRYR 128
Cdd:cd05754  14 RPGADVSFICRAKSKSPAYTLVWTRVN-GTLPSR---------AMDF---NGI------------LTIRNVQLSDAGTYV 68


                .
gi 15042971 129 C 129
Cdd:cd05754  69 C 69
IgV_1_Nectin-4_like cd05888
First immunoglobulin (Ig) domain of nectin-4, and similar domains; The members here are ...
 51-132 1.81e-03

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: 37.57  E-value: 1.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  51 GATATLPCVLGTSPPSY--KVRWSKVEPGELRETLILITNGLHARDYGLLGGRASLRRGHR-LDASLIIKNVRLEDEGRY 127
Cdd:cd05888   8 GQDAKLPCFYRGDSGEQvgQVAWARVDAGEGAQEIALLHSKYGLHVFPAYEGRVEQPPPPRpADGSVLLRNAVQADEGEY 87


                ....*
gi 15042971 128 RCELI 132
Cdd:cd05888  88 ECRVS 92
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 111-129 1.99e-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: 37.37  E-value: 1.99e-03
                        10
                ....*....|....*....
gi 15042971 111 DASLIIKNVRLEDEGRYRC 129
Cdd:cd16091  72 NASLLLRRVQLQDEGRYKC 90
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 257-338 2.02e-03

This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It also plays an important role in arteriogenesis. The functional HA-binding domain of CD44 is an extended domain comprised of a single link module flanked with N-and C- extensions. These extensions are essential for folding and for functional activity. This group also contains the cell surface retention sequence (CRS) binding protein-1 (CRSBP-1) and lymph vessel endothelial receptor-1 (LYVE-1). CRSBP-1 is a cell surface binding protein for the CRS motif of PDGF-BB (platelet-derived growth factor-BB) and is responsible for the cell surface retention of PDGF-BB in SSV-transformed cells. CRSBP-1 may play a role in autocrine regulation of cell growth mediated by CRS containing growth regulators. LYVE-1 is preferentially expressed on the lymphatic endothelium and is used as a molecular marker for the detection and characterization of lymphatic vessels in tumors.


Pssm-ID: 239593  Cd Length: 144  Bit Score: 38.21  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971 257 LTLSEAHAACRRRGAVVAKVGHLYAAWKFsGLDQCDGGWLADGSVRFPITTPRPRCGGlpdPGVRSFGFPRPQQASYGTY 336
Cdd:cd03516  19 LNFTEAKEACRALGLTLASKAQVETALKF-GFETCRYGWVEDGFVVIPRIDPNPLCGK---NGTGVYILNSNLSSRYDAY 94


                ..
gi 15042971 337 CY 338
Cdd:cd03516  95 CY 96
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 49-131 2.71e-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: 36.40  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971    49 RRGATATLPCVLGTSPPSYKVRWSKVEPGELRETLILITNGLHArdygllggraslrrghrlDASLIIKNVRLEDEGRYR 128
Cdd:pfam00047   9 LEGDSATLTCSASTGSPGPDVTWSKEGGTLIESLKVKHDNGRTT------------------QSSLLISNVTKEDAGTYT 70


                  ...
gi 15042971   129 CEL 131
Cdd:pfam00047  71 CVV 73
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 51-131 5.85e-03

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 [Multi-domain]  Cd Length: 109  Bit Score: 36.09  E-value: 5.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  51 GATATLPCVLGTSPPSYkVRWSKVEPGELRETLILIT-NGLHARDYGLlggRASLRRGHRlDASLIIKNVRLEDEGRYRC 129
Cdd:cd04983  13 GENVTLNCNYSTSTFYY-LFWYRQYPGQGPQFLIYISsDSGNKKKGRF---SATLDKSRK-SSSLHISAAQLSDSAVYFC 87


                ..
gi 15042971 130 EL 131
Cdd:cd04983  88 AL 89
IgV_B7-H6 cd20981
Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the ...
 48-132 6.81e-03

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: 36.05  E-value: 6.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  48 SRRGATATLPCVLGTSPP----SYKVRWSKVEPGELRETLILITNGLHARDYgLLGGRASLRRGHRLDASLIIKNVRLED 123
Cdd:cd20981  13 TPLNDNVTIFCNIFYSQPlnitSMGITWFRKSLTFDKEVKVFEFFGDHQKAF-RPGAIVSPWRLKSGDASLQLPGVQLEE 91


                ....*....
gi 15042971 124 EGRYRCELI 132
Cdd:cd20981  92 AGEYRCEVV 100
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 50-129 9.65e-03

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigens as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens directly without antigen processing and recognize MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain the standard Ig superfamily V-set AGFCC'C"/DEB domain topology.


Pssm-ID: 409371  Cd Length: 117  Bit Score: 35.42  E-value: 9.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15042971  50 RGATATLPCVL-GTSPPSYKVRWSKVEPGELRETLILI-TNGLHARDYGLLGGRASLRRGHRLDAS-LIIKNVRLEDEGR 126
Cdd:cd04982  12 ESKSVTISCKVsGIDFSTTYIHWYRQKPGQALERLLYVsSTSAVRKDSGKTKNKFEARKDVGKSTStLTITNLEKEDSAT 91


                ...
gi 15042971 127 YRC 129
Cdd:cd04982  92 YYC 94
 
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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