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Conserved domains on  [gi|31982256|ref|NP_839986|]
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hyaluronan and proteoglycan link protein 3 precursor [Mus musculus]

Protein Classification

immunoglobulin domain-containing family protein; immunoglobulin domain-containing protein( domain architecture ID 10147181)

immunoglobulin (Ig) domain-containing family protein is a member of a large superfamily containing cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins; immunoglobulin domains are typically divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets| immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and/or pattern recognition

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 52-168 3.40e-67

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: 207.18  E-value: 3.40e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  52 ETTEESLFSHQGASVTLPCHYHYEPALASPRHVRVKWWKLSENGAPEQDVLVVIGQRHRSFGDYQGRVQLRQDKQQEVSL 131
Cdd:cd05877   1 ETVQAKVFSHRGGNVTLPCRYHYEPELSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDASL 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 31982256 132 ELRDLRLEDSGRYRCEVIDGLEDESGLVELELRGVVF 168
Cdd:cd05877  81 VITDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 166-260 7.63e-60

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: 187.63  E-value: 7.63e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 166 VVFPYQSREGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGGLGLAPGVRSY 245
Cdd:cd03518   1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTVPGLRSY 80

                        90
                ....*....|....*
gi 31982256 246 GQRHHRLHRYDVFCF 260
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 ...
 267-356 9.87e-53

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: 169.53  E-value: 9.87e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 267 RVYYLENPKKLTLLEAREACQEDGAQISTVGQLFAAWKFRGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTFGFPD 346
Cdd:cd03519   1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSFGFPD 80

                        90
                ....*....|.
gi 31982256 347 P-HTRYGVYCY 356
Cdd:cd03519  81 KkHKLYGVYCY 91
 
Name Accession Description Interval E-value
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 52-168 3.40e-67

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: 207.18  E-value: 3.40e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  52 ETTEESLFSHQGASVTLPCHYHYEPALASPRHVRVKWWKLSENGAPEQDVLVVIGQRHRSFGDYQGRVQLRQDKQQEVSL 131
Cdd:cd05877   1 ETVQAKVFSHRGGNVTLPCRYHYEPELSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDASL 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 31982256 132 ELRDLRLEDSGRYRCEVIDGLEDESGLVELELRGVVF 168
Cdd:cd05877  81 VITDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 166-260 7.63e-60

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: 187.63  E-value: 7.63e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 166 VVFPYQSREGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGGLGLAPGVRSY 245
Cdd:cd03518   1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTVPGLRSY 80

                        90
                ....*....|....*
gi 31982256 246 GQRHHRLHRYDVFCF 260
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 ...
 267-356 9.87e-53

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: 169.53  E-value: 9.87e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 267 RVYYLENPKKLTLLEAREACQEDGAQISTVGQLFAAWKFRGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTFGFPD 346
Cdd:cd03519   1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSFGFPD 80

                        90
                ....*....|.
gi 31982256 347 P-HTRYGVYCY 356
Cdd:cd03519  81 KkHKLYGVYCY 91
Xlink pfam00193
Extracellular link domain;
166-260 2.60e-43

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 145.02  E-value: 2.60e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256   166 VVFPYQSReGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGGLGlaPGVRSY 245
Cdd:pfam00193   1 GVFHLESP-GRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM--PGVRQY 77

                          90
                  ....*....|....*
gi 31982256   246 GQRHHRLHRYDVFCF 260
Cdd:pfam00193  78 GFRDPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
265-356 7.00e-40

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 136.32  E-value: 7.00e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256    265 KGRVYYLE--NPKKLTLLEAREACQEDGAQISTVGQLFAAWKfRGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTF 342
Cdd:smart00445   1 DGGVFHVEknGRYKLTFAEAREACRAQGATLATVGQLYAAWQ-DGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVRQY 79

                           90
                   ....*....|....
gi 31982256    343 GFPDPHTRYGVYCY 356
Cdd:smart00445  80 GFPDPTSRYDAYCF 93
Xlink pfam00193
Extracellular link domain;
267-356 2.81e-39

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 134.62  E-value: 2.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256   267 RVYYLENPK--KLTLLEAREACQEDGAQISTVGQLFAAWKfRGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTFGF 344
Cdd:pfam00193   1 GVFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWK-AGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVRQYGF 79

                          90
                  ....*....|...
gi 31982256   345 PDPHT-RYGVYCY 356
Cdd:pfam00193  80 RDPLSeRYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
164-261 5.51e-37

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 128.61  E-value: 5.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256    164 RGVVFPYQSReGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGGLGlaPGVR 243
Cdd:smart00445   1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNL--PGVR 77

                           90
                   ....*....|....*...
gi 31982256    244 SYGQRhHRLHRYDVFCFA 261
Cdd:smart00445  78 QYGFP-DPTSRYDAYCFN 94
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 53-150 3.49e-12

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: 62.48  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256    53 TTEESLFSHQGASVTLPCHYhyePALASPRHVRVKWWKLSENGAPEQDVLVVIGQRHRSFgdYQGRVQLRQDKQQ-EVSL 131
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTY---SSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGV--KKGRFSGRGDPSNgDGSL 75

                          90
                  ....*....|....*....
gi 31982256   132 ELRDLRLEDSGRYRCEVID 150
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAVIP 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 63-162 2.60e-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: 2.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256     63 GASVTLPCHYHYEPalasprHVRVKWWKlsengapeQDVLVVIgqrhrsfgdYQGRVQLRQDKQQeVSLELRDLRLEDSG 142
Cdd:smart00410   9 GESVTLSCEASGSP------PPEVTWYK--------QGGKLLA---------ESGRFSVSRSGST-STLTISNVTPEDSG 64

                           90       100
                   ....*....|....*....|
gi 31982256    143 RYRCEVIDGLEDESGLVELE 162
Cdd:smart00410  65 TYTCAATNSSGSASSGTTLT 84
 
Name Accession Description Interval E-value
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 52-168 3.40e-67

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: 207.18  E-value: 3.40e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  52 ETTEESLFSHQGASVTLPCHYHYEPALASPRHVRVKWWKLSENGAPEQDVLVVIGQRHRSFGDYQGRVQLRQDKQQEVSL 131
Cdd:cd05877   1 ETVQAKVFSHRGGNVTLPCRYHYEPELSAPRKIRVKWTKLEVDYAKEEDVLVAIGTRHKSYGSYQGRVFLRRADDLDASL 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 31982256 132 ELRDLRLEDSGRYRCEVIDGLEDESGLVELELRGVVF 168
Cdd:cd05877  81 VITDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 166-260 7.63e-60

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: 187.63  E-value: 7.63e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 166 VVFPYQSREGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGGLGLAPGVRSY 245
Cdd:cd03518   1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTVPGLRSY 80

                        90
                ....*....|....*
gi 31982256 246 GQRHHRLHRYDVFCF 260
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 ...
 267-356 9.87e-53

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: 169.53  E-value: 9.87e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 267 RVYYLENPKKLTLLEAREACQEDGAQISTVGQLFAAWKFRGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTFGFPD 346
Cdd:cd03519   1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKFHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSFGFPD 80

                        90
                ....*....|.
gi 31982256 347 P-HTRYGVYCY 356
Cdd:cd03519  81 KkHKLYGVYCY 91
Xlink pfam00193
Extracellular link domain;
166-260 2.60e-43

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 145.02  E-value: 2.60e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256   166 VVFPYQSReGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGGLGlaPGVRSY 245
Cdd:pfam00193   1 GVFHLESP-GRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM--PGVRQY 77

                          90
                  ....*....|....*
gi 31982256   246 GQRHHRLHRYDVFCF 260
Cdd:pfam00193  78 GFRDPLSERYDAYCY 92
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 ...
 268-356 2.50e-41

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: 140.14  E-value: 2.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 268 VYYLENPKKLTLLEAREACQEDGAQISTVGQLFAAWKfRGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTF----- 342
Cdd:cd03520   2 VFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWR-QGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLyrfpn 80

                        90
                ....*....|....*.
gi 31982256 343 --GFPDPHTRYGVYCY 356
Cdd:cd03520  81 qtGFPDPHSRFDAYCF 96
LINK smart00445
Link (Hyaluronan-binding);
265-356 7.00e-40

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 136.32  E-value: 7.00e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256    265 KGRVYYLE--NPKKLTLLEAREACQEDGAQISTVGQLFAAWKfRGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTF 342
Cdd:smart00445   1 DGGVFHVEknGRYKLTFAEAREACRAQGATLATVGQLYAAWQ-DGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVRQY 79

                           90
                   ....*....|....
gi 31982256    343 GFPDPHTRYGVYCY 356
Cdd:smart00445  80 GFPDPTSRYDAYCF 93
Xlink pfam00193
Extracellular link domain;
267-356 2.81e-39

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 134.62  E-value: 2.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256   267 RVYYLENPK--KLTLLEAREACQEDGAQISTVGQLFAAWKfRGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTFGF 344
Cdd:pfam00193   1 GVFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWK-AGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVRQYGF 79

                          90
                  ....*....|...
gi 31982256   345 PDPHT-RYGVYCY 356
Cdd:pfam00193  80 RDPLSeRYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
164-261 5.51e-37

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 128.61  E-value: 5.51e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256    164 RGVVFPYQSReGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGGLGlaPGVR 243
Cdd:smart00445   1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNL--PGVR 77

                           90
                   ....*....|....*...
gi 31982256    244 SYGQRhHRLHRYDVFCFA 261
Cdd:smart00445  78 QYGFP-DPTSRYDAYCFN 94
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 166-260 2.90e-34

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: 121.37  E-value: 2.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 166 VVFPYQSREGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGglGLAPGVRSY 245
Cdd:cd01102   1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCG--GRNPGVRSY 78

                        90
                ....*....|....*
gi 31982256 246 GQRHHRlHRYDVFCF 260
Cdd:cd01102  79 GNPAPS-GRYDAYCF 92
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 267-356 1.46e-31

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: 114.44  E-value: 1.46e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 267 RVYYLEN---PKKLTLLEAREACQEDGAQISTVGQLFAAWKFrGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTFG 343
Cdd:cd01102   1 VVFHLESqngRYKLTFAEAALACKARGAHLATPGQLEAAWQD-GFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSYG 79

                        90
                ....*....|...
gi 31982256 344 FPDPHTRYGVYCY 356
Cdd:cd01102  80 NPAPSGRYDAYCF 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 ...
 166-260 1.91e-29

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: 109.03  E-value: 1.91e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 166 VVFPYQSREGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPC-GGLGLAPGVRS 244
Cdd:cd03517   1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCyGDMDGFPGVRN 80

                        90
                ....*....|....*.
gi 31982256 245 YGQRHHRlHRYDVFCF 260
Cdd:cd03517  81 YGVRDPD-ELYDVYCY 95
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 57-168 2.17e-25

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: 99.21  E-value: 2.17e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  57 SLFSHQGASVTLPCHYHYEP-ALASPRH-VRVKWWKLSENGA--PEQDVLVVIGQRHRSFGDYQGRVQL--RQDKQQEVS 130
Cdd:cd05714   6 KVFSHLGGNVTLPCKFYRDPtAFGSGIHkIRIKWTKLTSDSGylKEVDVLVAMGNVVYHKKTYGGRVSVplKPGSDSDAS 85

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 31982256 131 LELRDLRLEDSGRYRCEVIDGLEDESGLVELELRGVVF 168
Cdd:cd05714  86 LVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
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 ...
 178-260 1.32e-23

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: 93.53  E-value: 1.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 178 QLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGglGLAPGVRSYGQRHHR------ 251
Cdd:cd03520  10 KFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCG--GGLPGVRTLYRFPNQtgfpdp 87


                ....*....
gi 31982256 252 LHRYDVFCF 260
Cdd:cd03520  88 HSRFDAYCF 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 ...
 167-260 2.31e-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: 92.53  E-value: 2.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 167 VFPYQSREGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGGLGLapGVRSYG 246
Cdd:cd03515   2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHV--GIVDYG 79

                        90
                ....*....|....
gi 31982256 247 QRHHRLHRYDVFCF 260
Cdd:cd03515  80 PRLNLSERWDAYCY 93
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 179-260 6.37e-23

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: 91.33  E-value: 6.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 179 LNFHEAQQACQEQGAMVATFEQLFRAWE-EGLDWCNAGWLQDASVQYPIVLPRQPCGglGLAPGVRSYGQRHHRLHRYDV 257
Cdd:cd03519  11 LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCG--PLEPGVRSFGFPDKKHKLYGV 88


                ...
gi 31982256 258 FCF 260
Cdd:cd03519  89 YCY 91
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 63-168 8.47e-23

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: 92.30  E-value: 8.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  63 GASVTLPCHY----HYEPALASPRHVRVKWWKLSENGAPEQDVLVVIGQ--RHRSFGDYQGRVQLRQ--DKQQEVSLELR 134
Cdd:cd05878  12 GTSVTLPCYFidppHPVTPSTAPLAPRIKWSKVSVDGKKEKEVVLLVATegRVRVNSAYQGRVSLPNypAIPSDATLEVQ 91

                        90       100       110
                ....*....|....*....|....*....|....
gi 31982256 135 DLRLEDSGRYRCEVIDGLEDESGLVELELRGVVF 168
Cdd:cd05878  92 SLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 268-356 1.10e-22

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: 90.93  E-value: 1.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 268 VYYLENPKK--LTLLEAREACQEDGAQISTVGQLFAAWkFRGLDRCDAGWLADGSARYPIVHPRLNCGPPE---PGVRTF 342
Cdd:cd03517   3 FHYRDATARyaLTFPRAQRACLDISAQIATPEQLLAAY-EDGFEQCDAGWLADQTVRYPIQTPREGCYGDMdgfPGVRNY 81

                        90
                ....*....|....
gi 31982256 343 GFPDPHTRYGVYCY 356
Cdd:cd03517  82 GVRDPDELYDVYCY 95
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 65-168 3.91e-18

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: 79.49  E-value: 3.91e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  65 SVTLPCHYHYEPALASPRHV-RVKWWKLSEN-GAPEQDVLVVIGQRHRSFGDYQGRVQL--RQDKQQEVSLELRDLRLED 140
Cdd:cd05902  14 SVLLPCVFTLPPSASSPPEGpRIKWTKLSTSgGQQQRPVLVARDNVVRVAKAFQGRVSLpgYPKNRYNASLVLSRLRYSD 93

                        90       100
                ....*....|....*....|....*...
gi 31982256 141 SGRYRCEVIDGLEDESGLVELELRGVVF 168
Cdd:cd05902  94 SGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 65-168 5.07e-16

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: 73.84  E-value: 5.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  65 SVTLPCHYHYEPAL-----ASPRHVRVKWWKL--SENGAPEQDVLVVIGQRH--RSFGDYQGRVQL--RQDKQQEVSLEL 133
Cdd:cd05901  14 SVVLPCRFSTLPTLppsynITSEFLRIKWTKIqvDKNGKDHKETTVLVAQNGiiKIGQEYMGRVSVpsHPEDQGDASLTI 93

                        90       100       110
                ....*....|....*....|....*....|....*
gi 31982256 134 RDLRLEDSGRYRCEVIDGLEDESGLVELELRGVVF 168
Cdd:cd05901  94 VKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
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 ...
 268-356 1.35e-15

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: 71.34  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 268 VYYLENPK---KLTLLEAREACQEDGAQISTVGQLFAAWKFrGLDRCDAGWLADGSARYPIVHPRLNCGPPEPGVRTFGF 344
Cdd:cd03515   2 VFHLRSRSgkyKLTYTEAKAACEAEGAHLATYSQLSAAQQL-GFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGIVDYGP 80

                        90
                ....*....|...
gi 31982256 345 P-DPHTRYGVYCY 356
Cdd:cd03515  81 RlNLSERWDAYCY 93
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 63-168 1.98e-14

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: 69.20  E-value: 1.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  63 GASVTLPCHY----HYEPALAS--PRHVRVKWWKLSENgaPEQDVLVVIGQRHRSFGDYQGRVQLRQDK--QQEVSLELR 134
Cdd:cd05900  12 GSSLLIPCYFqdpiAKDPGAPTvaPLSPRIKWSFISKE--KESVLLVATEGKVRVNTEYLDRVSLPNYPaiPSDATLEIT 89

                        90       100       110
                ....*....|....*....|....*....|....
gi 31982256 135 DLRLEDSGRYRCEVIDGLEDESGLVELELRGVVF 168
Cdd:cd05900  90 ELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 53-150 3.49e-12

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: 62.48  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256    53 TTEESLFSHQGASVTLPCHYhyePALASPRHVRVKWWKLSENGAPEQDVLVVIGQRHRSFgdYQGRVQLRQDKQQ-EVSL 131
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTY---SSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGV--KKGRFSGRGDPSNgDGSL 75

                          90
                  ....*....|....*....
gi 31982256   132 ELRDLRLEDSGRYRCEVID 150
Cdd:pfam07686  76 TIQNLTLSDSGTYTCAVIP 94
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 63-162 2.60e-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: 2.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256     63 GASVTLPCHYHYEPalasprHVRVKWWKlsengapeQDVLVVIgqrhrsfgdYQGRVQLRQDKQQeVSLELRDLRLEDSG 142
Cdd:smart00410   9 GESVTLSCEASGSP------PPEVTWYK--------QGGKLLA---------ESGRFSVSRSGST-STLTISNVTPEDSG 64

                           90       100
                   ....*....|....*....|
gi 31982256    143 RYRCEVIDGLEDESGLVELE 162
Cdd:smart00410  65 TYTCAATNSSGSASSGTTLT 84
IGv smart00406
Immunoglobulin V-Type;
65-148 9.51e-09

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 51.61  E-value: 9.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256     65 SVTLPCHYHYepalASPRHVRVKWWKLSENGAPEqdVLVVIGQRHRSFGD--YQGRVQLRQDKQQE-VSLELRDLRLEDS 141
Cdd:smart00406   1 SVTLSCKFSG----STFSSYYVSWVRQPPGKGLE--WLGYIGSNGSSYYQesYKGRFTISKDTSKNdVSLTISNLRVEDT 74


                   ....*..
gi 31982256    142 GRYRCEV 148
Cdd:smart00406  75 GTYYCAV 81
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 172-262 3.37e-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: 52.08  E-value: 3.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256 172 SREGRYQLNFHEAQQACQEQGAMVATFEQLFRAWEEGLDWCNAGWLQDASVQYPIVLPRQPCGglglAPGVRSYGQRHHR 251
Cdd:cd03516  12 EKNGRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCG----KNGTGVYILNSNL 87

                        90
                ....*....|.
gi 31982256 252 LHRYDVFCFAA 262
Cdd:cd03516  88 SSRYDAYCYNS 98
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 63-179 4.68e-07

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: 47.83  E-value: 4.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  63 GASVTLPCHYhyepalASPRHVR---VKWWKLsenGAPEQDVLVVIgqrHRSFG-----DYQGRVQLRQDKQQ--EVSLE 132
Cdd:cd05718  14 GGSVTLPCSL------TSPGTTKitqVTWMKI---GAGSSQNVAVF---HPQYGpsvpnPYAERVEFLAARLGlrNATLR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 31982256 133 LRDLRLEDSGRYRCEVidgledesglvelelrgVVFPYQSREGRYQL 179
Cdd:cd05718  82 IRNLRVEDEGNYICEF-----------------ATFPQGNRQGTTWL 111
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 49-148 5.10e-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: 5.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  49 LVVETTEESLFSHQGASVTLPCHYHYEPALASPRHVRvkwWKLSENGAPEQDVLVVIGQRhrSFGDY----QGRVQL-RQ 123
Cdd:cd20960   1 LLITSAQTEIKKVAGENVTLPCHHQLGLEDQGTLDIE---WLLLPSDKVEKVVITYSGDR--VYNHYypalKGRVAFtSN 75

                        90       100
                ....*....|....*....|....*
gi 31982256 124 DKQQEVSLELRDLRLEDSGRYRCEV 148
Cdd:cd20960  76 DLSGDASLNISNLKLSDTGTYQCKV 100
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
 65-148 1.04e-06

Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the immunoglobulin variable (IgV) region of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also known as Z39Ig and V-set and Ig domain-containing 4 (VSIG4) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. Like all members of this family, the CRIg domain contains two beta-sheets: one composed of strands A', G, F, C, C' and C", and the other of strands B, E and D. The complement system is an important part of the innate immune system and is required for removal of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles. It is also a potent inhibitor of the alternative pathway convertases and a negative regulator of T cell activation. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409510  Cd Length: 117  Bit Score: 47.13  E-value: 1.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  65 SVTLPCHYHYEPALAsprHVRVKWWKLSENGApeqdvlVVIGQRHRSfGD------YQGRVQLRQDKQQEVSLELRDLRL 138
Cdd:cd16089  16 SVNLPCTYVPEEGYT---QVLVKWLVQRDSDP------VTIFLRDSS-GDhiqqakYRGRLEVSKDTPGDVSLQLDTLEM 85

                        90
                ....*....|
gi 31982256 139 EDSGRYRCEV 148
Cdd:cd16089  86 DDRGHYTCQV 95
IgV_VCBP cd20963
Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set ...
 61-148 7.78e-06

Immunoglobulin Variable region-containing chitin-binding proteins; an immunoglobulin V-set domain; The members here are composed of the immunoglobulin variable (IgV) region-containing chitin-binding proteins (VCBPs). VCBPs are secreted, immune-type molecules that have been identified in both amphioxus and sea squirt (Ciona intestinalis). VCBPs, which consist of a leader peptide, two tandem N-terminal immunoglobulin V-type domains and a single C-terminal chitin-binding domain, belong to a multigene family encoding secreted proteins. The VCBPs were identified first in the cephalochordate Branchiostoma floridae and show structural similarities with V-type domains of immunoglobulins and T cell receptors, suggesting that VCBPs represent a unique gut-associated form of innate immune proteins. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other.


Pssm-ID: 409555  Cd Length: 123  Bit Score: 44.53  E-value: 7.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  61 HQGASVTLPCHYHYEPALASPRhvrVKWWKLSengAPEQDVLVVIGQRH---------RSFGDYQGRVQLRQDKQQevSL 131
Cdd:cd20963  15 TWGNRVELPCSYTISPAAQPPT---ITWLKGI---SVDRAEVVFKGFKYwnetsssgeVYFGDYAGRASVASLTQP--TL 86

                        90
                ....*....|....*..
gi 31982256 132 ELRDLRLEDSGRYRCEV 148
Cdd:cd20963  87 VLTDLKFDDWGRYWCRV 103
IgV cd00099
Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin ...
 51-151 1.18e-05

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: 43.86  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  51 VETTEESLFSHQGASVTLPCHYHYepalaSPRHVRVKWWKLSENGAPEQdVLVVIGQRHRSFGDYQGRVQLRQDKQQEVS 130
Cdd:cd00099   1 VTQSPRSLSVQEGESVTLSCEVSS-----SFSSTYIYWYRQKPGQGPEF-LIYLSSSKGKTKGGVPGRFSGSRDGTSSFS 74

                        90       100
                ....*....|....*....|.
gi 31982256 131 LELRDLRLEDSGRYRCEVIDG 151
Cdd:cd00099  75 LTISNLQPEDSGTYYCAVSES 95
IgV_CD33 cd05712
Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic ...
 63-151 1.46e-05

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: 43.92  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  63 GASVTLPCHYHYEPALASPRHVRVKWWKLSENgaPEQDVLVVIGQRHRSFGD-YQGRVQLRQDKQQEV-SLELRDLRLED 140
Cdd:cd05712  14 GLCVLIPCSFSYPADYWVSNPVHGYWYRGGPY--PKYRPPVATNNRTREVHEsTQGRFRLLGDPGKKNcSLSISDARPED 91

                        90
                ....*....|.
gi 31982256 141 SGRYRCEVIDG 151
Cdd:cd05712  92 SGKYFFRVERG 102
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
 63-161 4.72e-05

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: 42.18  E-value: 4.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  63 GASVTLPCHYHyePALaSPRHVRVKWWK--------LSENGapeQDvlvvigQRHRSFGDYQGRVQLRQD--KQQEVSLE 132
Cdd:cd05713  15 GEDAELPCHLS--PKM-SAEHMEVRWFRsqfspvvhLYRDG---QD------QEEEQMPEYRGRTELLKDaiAEGSVALR 82

                        90       100
                ....*....|....*....|....*....
gi 31982256 133 LRDLRLEDSGRYRCEVIDGLEDESGLVEL 161
Cdd:cd05713  83 IHNVRPSDEGQYTCFFRSGSFYEEATLEL 111
IgV_pIgR_like cd05716
Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The ...
 53-146 8.41e-05

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: 41.23  E-value: 8.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  53 TTEESLFSHQGASVTLPCHY--HYepalaspRHVRVKWWKLSENG-APEQDvlvvigqrhrSFGDYQ-GRVQLRQDKQQ- 127
Cdd:cd05716   2 VGPEVVTGVEGGSVTIQCPYppKY-------ASSRKYWCKWGSEGcQTLVS----------SEGVVPgGRISLTDDPDNg 64

                        90
                ....*....|....*....
gi 31982256 128 EVSLELRDLRLEDSGRYRC 146
Cdd:cd05716  65 VFTVTLNQLRKEDAGWYWC 83
IgV_B7-H6 cd20981
Immunoglobulin variable (IgV) domain of B7-H6; The members here are composed of the ...
 65-163 1.06e-04

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: 41.06  E-value: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  65 SVTLPCHYHYEPALaSPRHVRVKWWKLSENGAPEQDVLVVIGQRHRSFGDyQGRVQLRQDKQQEVSLELRDLRLEDSGRY 144
Cdd:cd20981  18 NVTIFCNIFYSQPL-NITSMGITWFRKSLTFDKEVKVFEFFGDHQKAFRP-GAIVSPWRLKSGDASLQLPGVQLEEAGEY 95

                        90
                ....*....|....*....
gi 31982256 145 RCEVIDGLEDESGLVELEL 163
Cdd:cd20981  96 RCEVVVTPLKAQGTVQLEV 114
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 51-163 2.03e-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: 40.21  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  51 VETTEESLFSHQGASVTLPCHYHYEPAlaSPRhvrVKWWKLsengapEQDVLVVIGQRHRSFGDYQGRVQLrqdkqQEVS 130
Cdd:cd20946   2 VPSSQQVVTVVENQEVILSCKTPKKTS--SPR---VEWKKL------QRDVTFVVFQNNKIQGDYKGRAEI-----LGTN 65

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 31982256 131 LELRDLRLEDSGRYRCEVI---DGLEDESGLVELEL 163
Cdd:cd20946  66 ITIKNVTRSDSGKYRCEVSarsDGQNLGEVTVTLEV 101
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 48-148 3.18e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.09  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256    48 KLVVETTEESLFSHQGASVTLPCHYHYEPalasprHVRVKWWKlseNGAPEQDvlvvigqrhrsfgdyqGRVQLRQDKQQ 127
Cdd:pfam13927   1 KPVITVSPSSVTVREGETVTLTCEATGSP------PPTITWYK---NGEPISS----------------GSTRSRSLSGS 55

                          90       100
                  ....*....|....*....|.
gi 31982256   128 EVSLELRDLRLEDSGRYRCEV 148
Cdd:pfam13927  56 NSTLTISNVTRSDAGTYTCVA 76
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 66-148 5.32e-04

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: 38.08  E-value: 5.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  66 VTLPCHYHYEPAlasprhVRVKWWKlseNGAPeqdvLVVIGQRHRSFGDYQGrvqlrqdkqqevSLELRDLRLEDSGRYR 145
Cdd:cd00096   1 VTLTCSASGNPP------PTITWYK---NGKP----LPPSSRDSRRSELGNG------------TLTISNVTLEDSGTYT 55


                ...
gi 31982256 146 CEV 148
Cdd:cd00096  56 CVA 58
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 63-147 8.09e-04

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409581  Cd Length: 112  Bit Score: 38.71  E-value: 8.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  63 GASVTLPCHyhyepaLASPRHV----RVKWWKLSENGapeqdvlvVIGQRHRSFG-DYQG-------RVQLRQDkQQEVS 130
Cdd:cd20989  14 GGSVTLPCH------LLPPNMVthvsQVTWQRHDEHG--------SVAVFHPKQGpSFPEserlsfvAARLGAE-LRNAS 78

                        90
                ....*....|....*..
gi 31982256 131 LELRDLRLEDSGRYRCE 147
Cdd:cd20989  79 LAMFGLRVEDEGNYTCE 95
IgV_TCR_alpha cd04983
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) alpha chain and similar ...
 51-151 1.74e-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: 37.64  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  51 VETTEESLFSHQGASVTLPCHYhyePALASPRhvrVKWWKLSENGAPEQDVLVVIGQRHRSFGDYqgRVQLrQDKQQEVS 130
Cdd:cd04983   1 VTQSPQSLSVQEGENVTLNCNY---STSTFYY---LFWYRQYPGQGPQFLIYISSDSGNKKKGRF--SATL-DKSRKSSS 71

                        90       100
                ....*....|....*....|.
gi 31982256 131 LELRDLRLEDSGRYRCEVIDG 151
Cdd:cd04983  72 LHISAAQLSDSAVYFCALSES 92
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 57-148 2.22e-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: 36.79  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256    57 SLFSHQGASVTLPCHYHYEPALASprhvrVKWWKlsENGAPEQDVLVVIGQ-RHRSFgdyqgrvqlrqdkqqevSLELRD 135
Cdd:pfam00047   5 TVTVLEGDSATLTCSASTGSPGPD-----VTWSK--EGGTLIESLKVKHDNgRTTQS-----------------SLLISN 60

                          90
                  ....*....|...
gi 31982256   136 LRLEDSGRYRCEV 148
Cdd:pfam00047  61 VTKEDAGTYTCVV 73
IgV_TCR_gamma cd04982
Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) gamma chain; The members here ...
 51-146 2.71e-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: 37.34  E-value: 2.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  51 VETTEESLFSHQGASVTLPCHYHYEPALASPRHvrvkWWKLSENGAPEQDVLVVI-GQRHRSFGDYQGRVQLRQDKQQEV 129
Cdd:cd04982   1 LEQPQLSITREESKSVTISCKVSGIDFSTTYIH----WYRQKPGQALERLLYVSStSAVRKDSGKTKNKFEARKDVGKST 76

                        90
                ....*....|....*...
gi 31982256 130 S-LELRDLRLEDSGRYRC 146
Cdd:cd04982  77 StLTITNLEKEDSATYYC 94
IgV_1_Nectin-3_like cd05887
First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor ...
 63-149 5.44e-03

First immunoglobulin variable (IgV) domain of nectin-3 (also known as poliovirus receptor related protein 3), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-3 (also known as poliovirus receptor related protein 3 (PVRL3) or cluster of differentiation (CD) 113). Nectin-3 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which participate in adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. For example, during spermatid development, the nectin-3,-2 trans-interaction is required for the formation of Sertoli cell-spermatid junctions in testis, and during morphogenesis of the ciliary body, the nectin-3,-1 trans-interaction is important for apex-apex adhesion between the pigment and non-pigment layers of the ciliary epithelia. Nectins also heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls); nectin-3 for example, trans-interacts with Necl-5, regulating cell movement and proliferation. Other proteins with which nectin-3 interacts include the actin filament-binding protein, afadin, integrin alpha-beta3, Par-3, and PDGF receptor; its interaction with PDGF receptor regulates the latter's signaling for anti-apoptosis.


Pssm-ID: 409470  Cd Length: 110  Bit Score: 36.45  E-value: 5.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  63 GASVTLPCHYHYEPALAsprhvRVKWWKLSENGApeqdvlVVIGQRHRSFG-----DYQGRVQLRQDKQQEVSLELRDLR 137
Cdd:cd05887  14 GKNVSLKCLIEVNETIT-----QISWEKIHGKSS------QTVAVHHPQYGisiqgEYQGRVSFKNYSLNDATITLHNVG 82

                        90
                ....*....|..
gi 31982256 138 LEDSGRYRCEVI 149
Cdd:cd05887  83 FSDSGKYICKAV 94
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
 63-148 6.05e-03

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: 36.43  E-value: 6.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  63 GASVTLPCHYHYEPALaSPRHVRVkWWKLSENGAPEQDVLVVIGQRHRSFGDYQGRVQLRQDK--QQEVSLELRDLRLED 140
Cdd:cd20934  12 GTDATLRCSFSPEPGF-SLAQLSV-FWQLTDTKQLVHSFTESQDQGRDQGSAYANRTALFPDLlaQGNASLRLQRVRVAD 89


                ....*...
gi 31982256 141 SGRYRCEV 148
Cdd:cd20934  90 EGSYTCFV 97
IgV_1_MRC-OX-2_like cd05846
First immunoglobulin (Ig) variable (V) domain of rat MRC OX-2 antigen, and similar domains; ...
 50-147 6.83e-03

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: 35.78  E-value: 6.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982256  50 VVETTEESLFSHQgaSVTLPChyhyepALASPRHVR-VKWWKLSENGapeQDVLVVIGQRH--RSFGDYQGRVQLRQDKQ 126
Cdd:cd05846   2 VVHTGDTRAVLGG--NATLSC------NLTLPEEVLqVTWQKIKASS---PENIVTYSKKYgvKIQPSYVRRISFTSSGL 70

                        90       100
                ....*....|....*....|.
gi 31982256 127 QEVSLELRDLRLEDSGRYRCE 147
Cdd:cd05846  71 NSTSITIWNVTLEDEGCYKCL 91
 
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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