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Conserved domains on  [gi|1832431027|ref|XP_033372871|]
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aggrecan core protein [Parus major]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 10308794)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1895-2018 1.15e-90

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, 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. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


:

Pssm-ID: 153058  Cd Length: 124  Bit Score: 289.86  E-value: 1.15e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDYQWIGLSDRAVENDFRWSDGHSLQYE 1974
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1832431027 1975 NWRPNQPDNFFSAGEDCVVMIWHEKGEWNDVPCNYHLPFTCKKG 2018
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 33-151 9.15e-65

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 cd05900:

Pssm-ID: 472250  Cd Length: 123  Bit Score: 215.57  E-value: 9.15e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   33 IPEQSPLRVILGSSLNIPCYFNIPEEQD----TSVMLTPRIKWSKLSNGTEVVLLVATGGKIRLNSEYREVISLPNYPAI 108
Cdd:cd05900      1 IPLESPLRVVLGSSLLIPCYFQDPIAKDpgapTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1832431027  109 PTDATLEIKALRSNHTGIYRCEVMYGIEDRQDTIEVLVKGIVF 151
Cdd:cd05900     81 PSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 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 ...
 250-345 1.21e-60

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: 202.54  E-value: 1.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  250 KVFYATAPEKFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVRTVYLYIN 329
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1832431027  330 QTGYPHPDSRYDAICY 345
Cdd:cd03520     81 QTGFPDPHSRFDAYCF 96
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 ...
 629-724 1.40e-59

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: 199.46  E-value: 1.40e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  629 DVFFATQPEQFTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRTVYQHHN 708
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1832431027  709 QTGFPDPLSRHHAFCF 724
Cdd:cd03520     81 QTGFPDPHSRFDAYCF 96
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 149-243 3.42e-59

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: 198.40  E-value: 3.42e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  149 IVFHYRAISTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGDKDEFPGVRT 228
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1832431027  229 YGVREPDETYDVYCY 243
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 528-622 5.91e-53

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: 180.68  E-value: 5.91e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  528 VVFHYRAATSRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCIGDKENTPGVRS 607
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1832431027  608 YGMRPASETYDVYCY 622
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 2022-2078 1.93e-12

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 63.64  E-value: 1.93e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832431027 2022 CGDPPAVENARTFGRKkERYEINSMVRYQCNQGYIQRHVPTIRCQPNGQWEEPRISC 2078
Cdd:cd00033      1 CPPPPVPENGTVTGSK-GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1853-1889 1.67e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 1.67e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1832431027 1853 DTDVCHS-SPCLNGATCVDGIDSFKCFCLPSYGGDLCE 1889
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
AidA super family cl34620
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 1033-1280 8.82e-05

Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];


The actual alignment was detected with superfamily member COG3468:

Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 47.63  E-value: 8.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1033 SGGAELSGLPSGLGASGETSGTHETSGLVDLSGLTSGIDGSSEASGITFVDVTLEEVTTAPpIIGAETKETLETSGLPSG 1112
Cdd:COG3468    196 GGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGG-GAAGTGGGGGGTGTGSGG 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1113 DEDGSGMVSGSLDISGEPSGDVDFGGSVSGVLEVSGYPSGVTDSSGDVSGVDVTSGLLSGEESGLTSGFPTVSLVDTTLV 1192
Cdd:COG3468    275 GGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTG 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1193 EAVTQTSVAQEVGEGPSGMIEISGFTSGDRGLSGEGSGSVETSGFPSGAGDLSGEPSGIPH---------ISGDFSGA-- 1261
Cdd:COG3468    355 AALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGGltltggtltVNGNYTGNng 434

                          250       260
                   ....*....|....*....|....*..
gi 1832431027 1262 -----TDLSGQSStVTD---ISGEASG 1280
Cdd:COG3468    435 tlvlnTVLGDDNS-PTDrlvVNGNTSG 460
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1895-2018 1.15e-90

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, 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. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 289.86  E-value: 1.15e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDYQWIGLSDRAVENDFRWSDGHSLQYE 1974
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1832431027 1975 NWRPNQPDNFFSAGEDCVVMIWHEKGEWNDVPCNYHLPFTCKKG 2018
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 33-151 9.15e-65

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: 215.57  E-value: 9.15e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   33 IPEQSPLRVILGSSLNIPCYFNIPEEQD----TSVMLTPRIKWSKLSNGTEVVLLVATGGKIRLNSEYREVISLPNYPAI 108
Cdd:cd05900      1 IPLESPLRVVLGSSLLIPCYFQDPIAKDpgapTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1832431027  109 PTDATLEIKALRSNHTGIYRCEVMYGIEDRQDTIEVLVKGIVF 151
Cdd:cd05900     81 PSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 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 ...
 250-345 1.21e-60

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: 202.54  E-value: 1.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  250 KVFYATAPEKFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVRTVYLYIN 329
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1832431027  330 QTGYPHPDSRYDAICY 345
Cdd:cd03520     81 QTGFPDPHSRFDAYCF 96
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 ...
 629-724 1.40e-59

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: 199.46  E-value: 1.40e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  629 DVFFATQPEQFTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRTVYQHHN 708
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1832431027  709 QTGFPDPLSRHHAFCF 724
Cdd:cd03520     81 QTGFPDPHSRFDAYCF 96
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 149-243 3.42e-59

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: 198.40  E-value: 3.42e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  149 IVFHYRAISTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGDKDEFPGVRT 228
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1832431027  229 YGVREPDETYDVYCY 243
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 528-622 5.91e-53

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: 180.68  E-value: 5.91e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  528 VVFHYRAATSRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCIGDKENTPGVRS 607
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1832431027  608 YGMRPASETYDVYCY 622
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
Xlink pfam00193
Extracellular link domain;
150-243 1.33e-44

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 156.58  E-value: 1.33e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  150 VFHYRAiSTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGDKdefPGVRTY 229
Cdd:pfam00193    2 VFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQY 77

                           90
                   ....*....|....*
gi 1832431027  230 GVREP-DETYDVYCY 243
Cdd:pfam00193   78 GFRDPlSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
627-725 1.49e-43

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 153.65  E-value: 1.49e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   627 KGDVFF--ATQPEQFTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRtvy 704
Cdd:smart00445    1 DGGVFHveKNGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 1832431027   705 qhhnQTGFPDPLSRHHAFCFR 725
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
147-244 1.52e-43

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 153.65  E-value: 1.52e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   147 KGIVFHYRAIsTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGdkdEFPGV 226
Cdd:smart00445    1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                            90
                    ....*....|....*...
gi 1832431027   227 RTYGVREPDETYDVYCYA 244
Cdd:smart00445   77 RQYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
528-622 3.00e-42

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 150.03  E-value: 3.00e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  528 VVFHYRAAtSRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCIGDKentPGVRS 607
Cdd:pfam00193    1 GVFHLESP-GRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 1832431027  608 YGMRPA-SETYDVYCY 622
Cdd:pfam00193   77 YGFRDPlSERYDAYCY 92
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1895-2016 6.92e-42

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 150.06  E-value: 6.92e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHA-----QDYQWIGLSDRAVENDFRWSDGH 1969
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgsSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1832431027  1970 SL-QYENWRPNQPDNffsAGEDCVVMiWHEKGEWNDVPCNYHLPFTCK 2016
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVL-STSGGKWNDVSCTSKLPFVCE 124
LINK smart00445
Link (Hyaluronan-binding);
248-345 1.27e-41

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 148.26  E-value: 1.27e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   248 QGKVFYATA--PEKFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVRtvy 325
Cdd:smart00445    1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|
gi 1832431027   326 lyinQTGYPHPDSRYDAICY 345
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCF 93
Xlink pfam00193
Extracellular link domain;
630-724 1.75e-40

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 145.02  E-value: 1.75e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  630 VFFATQPEQ--FTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRtvyqhh 707
Cdd:pfam00193    2 VFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR------ 75

                           90
                   ....*....|....*...
gi 1832431027  708 nQTGFPDPLS-RHHAFCF 724
Cdd:pfam00193   76 -QYGFRDPLSeRYDAYCY 92
Xlink pfam00193
Extracellular link domain;
250-345 9.30e-40

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 142.71  E-value: 9.30e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  250 KVFYATAPE--KFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVRtvyly 327
Cdd:pfam00193    1 GVFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 1832431027  328 inQTGYPHPDS-RYDAICY 345
Cdd:pfam00193   76 --QYGFRDPLSeRYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
527-622 1.28e-38

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 139.78  E-value: 1.28e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   527 GVVFHYRAATsRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCIGDKentPGVR 606
Cdd:smart00445    2 GGVFHVEKNG-RYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNL---PGVR 77

                            90
                    ....*....|....*.
gi 1832431027   607 SYGMRPASETYDVYCY 622
Cdd:smart00445   78 QYGFPDPTSRYDAYCF 93
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1913-2017 2.48e-26

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 104.87  E-value: 2.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1913 RETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDYQ---WIGLSDRAVENDFRWSDGHSLQYENWRPNQPDNffSAGE 1989
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNkyfWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENE 78

                           90       100
                   ....*....|....*....|....*...
gi 1832431027 1990 DCVVMIWhEKGEWNDVPCNYHLPFTCKK 2017
Cdd:pfam00059   79 DCVELSS-SSGKWNDENCNSKNPFVCEK 105
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 2022-2078 1.93e-12

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 63.64  E-value: 1.93e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832431027 2022 CGDPPAVENARTFGRKkERYEINSMVRYQCNQGYIQRHVPTIRCQPNGQWEEPRISC 2078
Cdd:cd00033      1 CPPPPVPENGTVTGSK-GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 2022-2078 3.23e-10

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 57.54  E-value: 3.23e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832431027  2022 CGDPPAVENARTFGRKkERYEINSMVRYQCNQGYIQRHVPTIRCQPNGQWEEPRISC 2078
Cdd:smart00032    1 CPPPPDIENGTVTSSS-GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
2022-2078 2.33e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.81  E-value: 2.33e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832431027 2022 CGDPPAVENARtFGRKKERYEINSMVRYQCNQGYIQRHVPTIRCQPNGQWEEPRISC 2078
Cdd:pfam00084    1 CPPPPDIPNGK-VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1853-1889 1.67e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 1.67e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1832431027 1853 DTDVCHS-SPCLNGATCVDGIDSFKCFCLPSYGGDLCE 1889
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1857-1886 2.15e-07

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 48.53  E-value: 2.15e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1832431027 1857 CHSSPCLNGATCVDGIDSFKCFCLPSYGGD 1886
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF_CA smart00179
Calcium-binding EGF-like domain;
1853-1889 7.57e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 7.57e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1832431027  1853 DTDVCHS-SPCLNGATCVDGIDSFKCFCLPSY-GGDLCE 1889
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 1033-1280 8.82e-05

Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 47.63  E-value: 8.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1033 SGGAELSGLPSGLGASGETSGTHETSGLVDLSGLTSGIDGSSEASGITFVDVTLEEVTTAPpIIGAETKETLETSGLPSG 1112
Cdd:COG3468    196 GGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGG-GAAGTGGGGGGTGTGSGG 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1113 DEDGSGMVSGSLDISGEPSGDVDFGGSVSGVLEVSGYPSGVTDSSGDVSGVDVTSGLLSGEESGLTSGFPTVSLVDTTLV 1192
Cdd:COG3468    275 GGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTG 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1193 EAVTQTSVAQEVGEGPSGMIEISGFTSGDRGLSGEGSGSVETSGFPSGAGDLSGEPSGIPH---------ISGDFSGA-- 1261
Cdd:COG3468    355 AALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGGltltggtltVNGNYTGNng 434

                          250       260
                   ....*....|....*....|....*..
gi 1832431027 1262 -----TDLSGQSStVTD---ISGEASG 1280
Cdd:COG3468    435 tlvlnTVLGDDNS-PTDrlvVNGNTSG 460
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1895-1970 9.88e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 45.88  E-value: 9.88e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDY-QWIGLSDRAVENDFRWSDGHS 1970
Cdd:PHA02642    88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSdHWIGLNRESSNHPWKWADNSN 164
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 36-146 1.59e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 1.59e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027    36 QSPLRVILGSSLNIPCYFNIPEeqdtsvmlTPRIKWSKlsNGTEvvlLVATGGKIRLNSEyrevislpnypaiPTDATLE 115
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSP--------PPEVTWYK--QGGK---LLAESGRFSVSRS-------------GSTSTLT 54

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1832431027   116 IKALRSNHTGIYRCEVMYGIEDRQDTIEVLV 146
Cdd:smart00410   55 ISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 35-146 3.04e-04

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: 42.06  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   35 EQSPLRVILGSSLNIPCYFNIPEEQDTsvmltPRIKWSKLSNGTEVVLLVATGGKIRLNSEYREVISLPNYPaIPTDATL 114
Cdd:pfam07686    2 TPREVTVALGGSVTLPCTYSSSMSEAS-----TSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGRFSGRGDP-SNGDGSL 75

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1832431027  115 EIKALRSNHTGIYRCEVMY-GIEDRQDTIEVLV 146
Cdd:pfam07686   76 TIQNLTLSDSGTYTCAVIPsGEGVFGKGTRLTV 108
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 1904-2016 3.64e-03

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 42.76  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1904 GHCYKHFEERETWMDAETRCRQH-QAHLSSIITPEEQEFVNS---HAQDYQ-WIGLSD--RAVENDFRWSDGHSLQY-EN 1975
Cdd:TIGR00864  329 GHCFQIVPEEAAWLDAQEQCLARaGAALAIVDNDALQNFLARkvtHSLDRGvWIGFSDvnGAEKGPAHQGEAFEAEEcEE 408

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1832431027 1976 WRPNQPDnfFSAGEDCVVMiwHEKGEWNDVPCNYHLPFTCK 2016
Cdd:TIGR00864  409 GLAGEPH--PARAEHCVRL--DPRGQCNSDLCNAPHAYVCE 445
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1895-2018 1.15e-90

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, 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. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 289.86  E-value: 1.15e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDYQWIGLSDRAVENDFRWSDGHSLQYE 1974
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1832431027 1975 NWRPNQPDNFFSAGEDCVVMIWHEKGEWNDVPCNYHLPFTCKKG 2018
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 33-151 9.15e-65

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: 215.57  E-value: 9.15e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   33 IPEQSPLRVILGSSLNIPCYFNIPEEQD----TSVMLTPRIKWSKLSNGTEVVLLVATGGKIRLNSEYREVISLPNYPAI 108
Cdd:cd05900      1 IPLESPLRVVLGSSLLIPCYFQDPIAKDpgapTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1832431027  109 PTDATLEIKALRSNHTGIYRCEVMYGIEDRQDTIEVLVKGIVF 151
Cdd:cd05900     81 PSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 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 ...
 250-345 1.21e-60

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: 202.54  E-value: 1.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  250 KVFYATAPEKFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVRTVYLYIN 329
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1832431027  330 QTGYPHPDSRYDAICY 345
Cdd:cd03520     81 QTGFPDPHSRFDAYCF 96
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 ...
 629-724 1.40e-59

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: 199.46  E-value: 1.40e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  629 DVFFATQPEQFTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRTVYQHHN 708
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1832431027  709 QTGFPDPLSRHHAFCF 724
Cdd:cd03520     81 QTGFPDPHSRFDAYCF 96
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 149-243 3.42e-59

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: 198.40  E-value: 3.42e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  149 IVFHYRAISTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGDKDEFPGVRT 228
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1832431027  229 YGVREPDETYDVYCY 243
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 528-622 5.91e-53

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: 180.68  E-value: 5.91e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  528 VVFHYRAATSRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCIGDKENTPGVRS 607
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1832431027  608 YGMRPASETYDVYCY 622
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
Xlink pfam00193
Extracellular link domain;
150-243 1.33e-44

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 156.58  E-value: 1.33e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  150 VFHYRAiSTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGDKdefPGVRTY 229
Cdd:pfam00193    2 VFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQY 77

                           90
                   ....*....|....*
gi 1832431027  230 GVREP-DETYDVYCY 243
Cdd:pfam00193   78 GFRDPlSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
627-725 1.49e-43

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 153.65  E-value: 1.49e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   627 KGDVFF--ATQPEQFTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRtvy 704
Cdd:smart00445    1 DGGVFHveKNGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 1832431027   705 qhhnQTGFPDPLSRHHAFCFR 725
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
147-244 1.52e-43

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 153.65  E-value: 1.52e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   147 KGIVFHYRAIsTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGdkdEFPGV 226
Cdd:smart00445    1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                            90
                    ....*....|....*...
gi 1832431027   227 RTYGVREPDETYDVYCYA 244
Cdd:smart00445   77 RQYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
528-622 3.00e-42

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 150.03  E-value: 3.00e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  528 VVFHYRAAtSRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCIGDKentPGVRS 607
Cdd:pfam00193    1 GVFHLESP-GRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 1832431027  608 YGMRPA-SETYDVYCY 622
Cdd:pfam00193   77 YGFRDPlSERYDAYCY 92
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1895-2016 6.92e-42

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 150.06  E-value: 6.92e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHA-----QDYQWIGLSDRAVENDFRWSDGH 1969
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgsSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1832431027  1970 SL-QYENWRPNQPDNffsAGEDCVVMiWHEKGEWNDVPCNYHLPFTCK 2016
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVL-STSGGKWNDVSCTSKLPFVCE 124
LINK smart00445
Link (Hyaluronan-binding);
248-345 1.27e-41

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 148.26  E-value: 1.27e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   248 QGKVFYATA--PEKFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVRtvy 325
Cdd:smart00445    1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|
gi 1832431027   326 lyinQTGYPHPDSRYDAICY 345
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCF 93
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 1895-2017 3.28e-41

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 148.22  E-value: 3.28e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQ--DYQWIGLSDRAVENDFRWSDGHSLQ 1972
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSgnRSYWIGLSDEETEGEWKWVDGTPLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1832431027 1973 --YENWRPNQPDNFFSAGEDCVVmIWHEKGEWNDVPCNYHLPFTCKK 2017
Cdd:cd03590     81 ssKTFWHPGEPNNWGGGGEDCAE-LVYDSGGWNDVPCNLEYRWICEK 126
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 33-151 1.54e-40

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: 146.22  E-value: 1.54e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   33 IPEQSPLRVILGSSLNIPCYFNIPEEQDTS--VMLTPRIKWSKLSNGT----EVVLLVATGGKIRLNSEYREVISLPNYP 106
Cdd:cd05878      1 IPQSSPVRVLLGTSVTLPCYFIDPPHPVTPstAPLAPRIKWSKVSVDGkkekEVVLLVATEGRVRVNSAYQGRVSLPNYP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1832431027  107 AIPTDATLEIKALRSNHTGIYRCEVMYGIEDRQDTIEVLVKGIVF 151
Cdd:cd05878     81 AIPSDATLEVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
Xlink pfam00193
Extracellular link domain;
630-724 1.75e-40

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 145.02  E-value: 1.75e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  630 VFFATQPEQ--FTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRtvyqhh 707
Cdd:pfam00193    2 VFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR------ 75

                           90
                   ....*....|....*...
gi 1832431027  708 nQTGFPDPLS-RHHAFCF 724
Cdd:pfam00193   76 -QYGFRDPLSeRYDAYCY 92
Xlink pfam00193
Extracellular link domain;
250-345 9.30e-40

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 142.71  E-value: 9.30e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  250 KVFYATAPE--KFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVRtvyly 327
Cdd:pfam00193    1 GVFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 1832431027  328 inQTGYPHPDS-RYDAICY 345
Cdd:pfam00193   76 --QYGFRDPLSeRYDAYCY 92
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 1905-2017 4.43e-39

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 141.99  E-value: 4.43e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1905 HCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDYQ----WIGLSDRAVENDFRWSDGHS-LQYENWRPN 1979
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssdvWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1832431027 1980 QPDNffSAGEDCVVMIWHEKGEWNDVPCNYHLPFTCKK 2017
Cdd:cd00037     81 EPNP--GGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
LINK smart00445
Link (Hyaluronan-binding);
527-622 1.28e-38

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 139.78  E-value: 1.28e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   527 GVVFHYRAATsRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCIGDKentPGVR 606
Cdd:smart00445    2 GGVFHVEKNG-RYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNL---PGVR 77

                            90
                    ....*....|....*.
gi 1832431027   607 SYGMRPASETYDVYCY 622
Cdd:smart00445   78 QYGFPDPTSRYDAYCF 93
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 1895-2016 5.97e-38

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 139.42  E-value: 5.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQ-----HQAHLSSIITPEEQEFV----NSHAQDYQ----WIGLSDRAVEN 1961
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVydlfESSRGPDTpyglWIGLHDRTSEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1832431027 1962 DFRWSDGHSLQYENWRPNQPDNFFSaGEDCVVMiWHEK---GEWNDVPCNYHLPFTCK 2016
Cdd:cd03589     81 PFEWTDGSPVDFTKWAGGQPDNYGG-NEDCVQM-WRRGdagQSWNDMPCDAVFPYICK 136
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 250-345 6.80e-36

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: 131.77  E-value: 6.80e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  250 KVFYATA---PEKFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVRTVyl 326
Cdd:cd01102      1 VVFHLESqngRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSY-- 78

                           90
                   ....*....|....*....
gi 1832431027  327 yinqtGYPHPDSRYDAICY 345
Cdd:cd01102     79 -----GNPAPSGRYDAYCF 92
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 528-622 9.18e-35

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: 128.69  E-value: 9.18e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  528 VVFHYRAATSRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCIGDKentPGVRS 607
Cdd:cd01102      1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN---PGVRS 77

                           90
                   ....*....|....*
gi 1832431027  608 YGMRPASETYDVYCY 622
Cdd:cd01102     78 YGNPAPSGRYDAYCF 92
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 150-243 4.09e-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: 126.76  E-value: 4.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  150 VFHYRAISTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGDKdefPGVRTY 229
Cdd:cd01102      2 VFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN---PGVRSY 78

                           90
                   ....*....|....
gi 1832431027  230 GVREPDETYDVYCY 243
Cdd:cd01102     79 GNPAPSGRYDAYCF 92
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 630-724 3.26e-33

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: 124.07  E-value: 3.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  630 VFFATQPEQFTFPEAQQYCESQNATLASVGQLHAAWK-QGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRTVyqhhn 708
Cdd:cd03519      2 VFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF----- 76

                           90
                   ....*....|....*..
gi 1832431027  709 qtGFPDPLSRHH-AFCF 724
Cdd:cd03519     77 --GFPDKKHKLYgVYCY 91
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 149-243 7.38e-32

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: 120.22  E-value: 7.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  149 IVFHYRAISTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCyGDKDEFPGVRT 228
Cdd:cd03518      1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPC-GGKRTVPGLRS 79

                           90
                   ....*....|....*.
gi 1832431027  229 YGVREPDET-YDVYCY 243
Cdd:cd03518     80 YGERDKMLSrYDAFCF 95
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 528-622 1.15e-31

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: 119.84  E-value: 1.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  528 VVFHYRAATSRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCiGDKENTPGVRS 607
Cdd:cd03518      1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPC-GGKRTVPGLRS 79

                           90
                   ....*....|....*.
gi 1832431027  608 YGMR-PASETYDVYCY 622
Cdd:cd03518     80 YGERdKMLSRYDAFCF 95
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 630-724 2.15e-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: 119.06  E-value: 2.15e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  630 VFFATQ---PEQFTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRTVyqh 706
Cdd:cd01102      2 VFHLESqngRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSY--- 78

                           90
                   ....*....|....*...
gi 1832431027  707 hnqtGFPDPLSRHHAFCF 724
Cdd:cd01102     79 ----GNPAPSGRYDAYCF 92
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 630-724 3.85e-31

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: 118.30  E-value: 3.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  630 VFFATQPE----QFTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGD--APGVRTV 703
Cdd:cd03518      1 VVFPYQPRlgryNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKrtVPGLRSY 80

                           90       100
                   ....*....|....*....|..
gi 1832431027  704 yqhhnqtGFPDP-LSRHHAFCF 724
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 ...
 250-345 5.83e-28

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: 109.05  E-value: 5.83e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  250 KVFYATAPEKFTFQEAFDKCRSLGARLATTGELYLAWK-DGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVRTVylyi 328
Cdd:cd03519      1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF---- 76

                           90
                   ....*....|....*...
gi 1832431027  329 nqtGYPHPDSR-YDAICY 345
Cdd:cd03519     77 ---GFPDKKHKlYGVYCY 91
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 1895-2016 5.69e-27

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 107.84  E-value: 5.69e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQ--AHLSSIITPEEQEFVNSHAQDYQ------WIGLSDRAVENDFRWS 1966
Cdd:cd03594      1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSYQkayqpvWIGLHDPQQSRGWEWS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1832431027 1967 DGHSLQYENWRPNQPdnfFSAGEDCVVMiWHEKG--EWNDVPCNYHLPFTCK 2016
Cdd:cd03594     81 DGSKLDYRSWDRNPP---YARGGYCAEL-SRSTGflKWNDANCEERNPFICK 128
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1913-2017 2.48e-26

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 104.87  E-value: 2.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1913 RETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDYQ---WIGLSDRAVENDFRWSDGHSLQYENWRPNQPDNffSAGE 1989
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNkyfWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENE 78

                           90       100
                   ....*....|....*....|....*...
gi 1832431027 1990 DCVVMIWhEKGEWNDVPCNYHLPFTCKK 2017
Cdd:pfam00059   79 DCVELSS-SSGKWNDENCNSKNPFVCEK 105
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 37-151 1.85e-23

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: 97.72  E-value: 1.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   37 SPLRVILGSSLNIPCYFNI-----PEEQDTSVMLtpRIKWSKLSNGT------EVVLLVATGGKIRLNSEYREVISLPNY 105
Cdd:cd05901      5 SRVHGSLSGSVVLPCRFSTlptlpPSYNITSEFL--RIKWTKIQVDKngkdhkETTVLVAQNGIIKIGQEYMGRVSVPSH 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1832431027  106 PAIPTDATLEIKALRSNHTGIYRCEVMYGIEDRQDTIEVLVKGIVF 151
Cdd:cd05901     83 PEDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 541-622 2.24e-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: 95.95  E-value: 2.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  541 FSFVQAQKACLENSAVIATPQQLQAAYE-AGFDQCDAGWLRDQTVRYPIVNPRNNCIGDKentPGVRSYGM-RPASETYD 618
Cdd:cd03519     11 LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLE---PGVRSFGFpDKKHKLYG 87


                   ....
gi 1832431027  619 VYCY 622
Cdd:cd03519     88 VYCY 91
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 38-151 3.36e-23

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: 96.83  E-value: 3.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   38 PLRVILGSSLNIPCYFNIPEEQDTSVMlTPRIKWSKLSNGT---EVVLLVATGGKIRLNSEYREVISLPNYPAIPTDATL 114
Cdd:cd05902      6 PVRRPLSSSVLLPCVFTLPPSASSPPE-GPRIKWTKLSTSGgqqQRPVLVARDNVVRVAKAFQGRVSLPGYPKNRYNASL 84

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1832431027  115 EIKALRSNHTGIYRCEVMYGIEDRQDTIEVLVKGIVF 151
Cdd:cd05902     85 VLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 259-345 5.99e-23

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: 94.80  E-value: 5.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  259 KFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGG-NLV-GVRTVylyinqtGYPHP 336
Cdd:cd03518     13 NLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGkRTVpGLRSY-------GERDK 85

                           90
                   ....*....|
gi 1832431027  337 D-SRYDAICY 345
Cdd:cd03518     86 MlSRYDAFCF 95
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 35-151 7.19e-23

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: 95.74  E-value: 7.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   35 EQSPLRVILGSSLNIPCYFNIPEEQDTSVMLTPRIKWSKLSNGT----EVVLLVATGGKIRLNSEYREVISLPNYPAIPT 110
Cdd:cd05714      3 ESAKVFSHLGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDSgylkEVDVLVAMGNVVYHKKTYGGRVSVPLKPGSDS 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1832431027  111 DATLEIKALRSNHTGIYRCEVMYGIEDRQDTIEVLVKGIVF 151
Cdd:cd05714     83 DASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 162-243 8.35e-22

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: 91.72  E-value: 8.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  162 LNFEKAKQACIQNSAVIATPEQLQAAYE-DGYEQCDAGWLADQTVRYPIHWPRERCYGDKdefPGVRTYGVrePDET--- 237
Cdd:cd03519     11 LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLE---PGVRSFGF--PDKKhkl 85


                   ....*.
gi 1832431027  238 YDVYCY 243
Cdd:cd03519     86 YGVYCY 91
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 ...
 529-622 1.03e-20

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: 88.67  E-value: 1.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  529 VFHYRAATSRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCiGDkeNTPGVRSY 608
Cdd:cd03515      2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANC-GF--GHVGIVDY 78

                           90
                   ....*....|....*
gi 1832431027  609 GMRP-ASETYDVYCY 622
Cdd:cd03515     79 GPRLnLSERWDAYCY 93
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 1912-2015 1.93e-20

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 88.51  E-value: 1.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1912 ERETWMDAETRCRQHQAHLSSIITPEE----QEFVNShAQDYQWIGLSDRAVENDFRWSDGHSLQYENWRPNQPDNFFSa 1987
Cdd:cd03591      9 EEKNFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVKK-GNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNNAGG- 86

                           90       100
                   ....*....|....*....|....*...
gi 1832431027 1988 GEDCVVMIwhEKGEWNDVPCNYHLPFTC 2015
Cdd:cd03591     87 GEDCVEMY--TSGKWNDVACNLTRLFVC 112
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 1905-2009 2.50e-20

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 88.25  E-value: 2.50e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1905 HCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDYQ--WIGLSDRAVENDFRWSDGHSLQYENWRPNQPD 1982
Cdd:cd03603      1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGasWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80

                           90       100
                   ....*....|....*....|....*....
gi 1832431027 1983 NFFSAGEDCVVM--IWHEKGEWNDVPCNY 2009
Cdd:cd03603     81 NNGGGNEDYAAInhFPGISGKWNDLANSY 109
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 ...
 150-243 3.92e-19

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: 84.05  E-value: 3.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  150 VFHYRAISTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGDKdefPGVRTY 229
Cdd:cd03515      2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGH---VGIVDY 78

                           90
                   ....*....|....*
gi 1832431027  230 GVR-EPDETYDVYCY 243
Cdd:cd03515     79 GPRlNLSERWDAYCY 93
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 1912-2009 8.71e-18

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 80.88  E-value: 8.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1912 ERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHA----QDYQWIGLSDRAVEndFRW--SDGHSLQYENWRPNQPDNff 1985
Cdd:cd03592      8 EKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFAlkynLGYYWIDGNDINNE--GTWvdTDKKELEYKNWAPGEPNN-- 83

                           90       100
                   ....*....|....*....|....
gi 1832431027 1986 SAGEDCVVMIWHEKGEWNDVPCNY 2009
Cdd:cd03592     84 GRNENCLEIYIKDNGKWNDEPCSK 107
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 ...
 251-345 2.37e-16

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: 75.96  E-value: 2.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  251 VFYATAPE---KFTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRYPISRARPNCGGNLVGVrtvyly 327
Cdd:cd03515      2 VFHLRSRSgkyKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGI------ 75

                           90
                   ....*....|....*...
gi 1832431027  328 INQTGYPHPDSRYDAICY 345
Cdd:cd03515     76 VDYGPRLNLSERWDAYCY 93
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 ...
 638-724 6.17e-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: 72.11  E-value: 6.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  638 QFTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVrTVYqhhnqtGFPDPLS 717
Cdd:cd03515     13 KLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGI-VDY------GPRLNLS 85


                   ....*...
gi 1832431027  718 -RHHAFCF 724
Cdd:cd03515     86 eRWDAYCY 93
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 1895-1968 4.44e-14

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 70.44  E-value: 4.44e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHA-QDYQWIGLSDRAVENDFRWSDG 1968
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIgSSSYWIGLSREKSEKPWKWIDG 75
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 1907-2015 2.23e-13

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 68.17  E-value: 2.23e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1907 YKHFEERETWMDAETRCRQHQAHLSSIITPEEQE------FVNSHAQdyqWIGLSDRAveNDFRWSDGHSLQYENWRPNQ 1980
Cdd:cd03602      3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNAllsnlsRVSNSAA---WIGLYRDV--DSWRWSDGSESSFRNWNTFQ 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1832431027 1981 PDNffsaGEDCVVM-IWhekGEWNDVPCNYHLPFTC 2015
Cdd:cd03602     78 PFG----QGDCATMySS---GRWYAALCSALKPFIC 106
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 44-151 2.61e-13

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: 68.12  E-value: 2.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   44 GSSLNIPC-YFNIPEEQDTSVMltpRIKWSKLSN--GTEVVLLVATGGKIRLNSEYREVISLPNypAIPTDATLEIKALR 120
Cdd:cd05877     12 GGNVTLPCrYHYEPELSAPRKI---RVKWTKLEVdyAKEEDVLVAIGTRHKSYGSYQGRVFLRR--ADDLDASLVITDLR 86

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1832431027  121 SNHTGIYRCEVMYGIEDRQDTIEVLVKGIVF 151
Cdd:cd05877     87 LEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 2022-2078 1.93e-12

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 63.64  E-value: 1.93e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832431027 2022 CGDPPAVENARTFGRKkERYEINSMVRYQCNQGYIQRHVPTIRCQPNGQWEEPRISC 2078
Cdd:cd00033      1 CPPPPVPENGTVTGSK-GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 1951-2017 2.24e-11

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 62.94  E-value: 2.24e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1951 WIGLSD-RAVENDFRWSDGHSL--QYENWRPNQPDNFFSAgEDCvVMIWHEKGEWNDVPCNYHLPFTCKK 2017
Cdd:cd03601     52 WVGADNlQDGEYDFLWNDGVSLptDSDLWAPNEPSNPQSR-QLC-VQLWSKYNLLDDEYCGRAKRVICEK 119
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 1904-2015 5.38e-11

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 61.70  E-value: 5.38e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1904 GHCYKHFEERETWMDAETRCRQ-HQAHLSSI----ITPEEQEFVNSHAQDYQWIG--LSDRAVENDFRWSDGHSLQYENW 1976
Cdd:cd03598      1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIhsfaFNYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1832431027 1977 RPNQPDNffsAGEDCVVMIWHEkGEWNDVPCNYHLPFTC 2015
Cdd:cd03598     81 APGQPGN---RRGHCVELCTRG-GHWRRAHCKLRRPFIC 115
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 2022-2078 3.23e-10

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 57.54  E-value: 3.23e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832431027  2022 CGDPPAVENARTFGRKkERYEINSMVRYQCNQGYIQRHVPTIRCQPNGQWEEPRISC 2078
Cdd:smart00032    1 CPPPPDIENGTVTSSS-GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 1895-2016 7.99e-10

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.


Pssm-ID: 153065  Cd Length: 149  Bit Score: 59.13  E-value: 7.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1895 CEEGwtkFQGHCYK--HFEE---RETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDYQ------WIGL---SDRAVE 1960
Cdd:cd03595      4 CRRG---TEKPCYKiaYFQDsrrRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRasdgdfWIGLrrsSQYNVT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832431027 1961 ND-----FRWSDGHSLQYENWRPNQPdnffSAG-EDCVVMiWHE-------KG----EWNDVPCNYHLPFTCK 2016
Cdd:cd03595     81 SSacsslYYWLDGSISTFRNWYVDEP----SCGsEVCVVM-YHQpsapagqGGpylfQWNDDNCNMKNNFICK 148
Sushi pfam00084
Sushi repeat (SCR repeat);
2022-2078 2.33e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.81  E-value: 2.33e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1832431027 2022 CGDPPAVENARtFGRKKERYEINSMVRYQCNQGYIQRHVPTIRCQPNGQWEEPRISC 2078
Cdd:pfam00084    1 CPPPPDIPNGK-VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 260-378 5.32e-09

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: 56.70  E-value: 5.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  260 FTFQEAFDKCRSLGARLATTGELYLAWKDGMDMCSAGWLADRSVRypISRARPN--CGGNLVGVRTVYLYINqtgyphpd 337
Cdd:cd03516     19 LNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVV--IPRIDPNplCGKNGTGVYILNSNLS-------- 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1832431027  338 SRYDAICYSGDDIESLVPGQFIDEIGSELgsaFTVQTVTQT 378
Cdd:cd03516     89 SRYDAYCYNSSDTWINSCLPEILTTDDPI---FITQTATDG 126
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1853-1889 1.67e-08

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 51.87  E-value: 1.67e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1832431027 1853 DTDVCHS-SPCLNGATCVDGIDSFKCFCLPSYGGDLCE 1889
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 1895-2015 2.45e-08

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 54.32  E-value: 2.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1895 CEEGwTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVnshaQDYQ----------WIGLSDRAVENDFR 1964
Cdd:cd03596      1 CLKG-TKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDAL----RDYVkasvpgnwevWLGINDMVAEGKWV 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1832431027 1965 WSDGHSLQYENWR---PNQPDnffsAG--EDCVVMIWHEKGEWNDVPCNYHLPFTC 2015
Cdd:cd03596     76 DVNGSPISYFNWEreiTAQPD----GGkrENCVALSSSAQGKWFDEDCRREKPYVC 127
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 638-761 9.83e-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: 53.23  E-value: 9.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  638 QFTFPEAQQYCESQNATLASVGQLHAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRTVYQHHNqtgfpdplS 717
Cdd:cd03516     18 SLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGTGVYILNSNLS--------S 89

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1832431027  718 RHHAFCFRAL-TPVEEEG--VTPFFEDVLATQVI-PGVEGVPSGEEVT 761
Cdd:cd03516     90 RYDAYCYNSSdTWINSCLpeILTTDDPIFITQTAtDGTRYNVSGSTHS 137
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1857-1886 2.15e-07

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 48.53  E-value: 2.15e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 1832431027 1857 CHSSPCLNGATCVDGIDSFKCFCLPSYGGD 1886
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
EGF_CA smart00179
Calcium-binding EGF-like domain;
1853-1889 7.57e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 47.24  E-value: 7.57e-07
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1832431027  1853 DTDVCHS-SPCLNGATCVDGIDSFKCFCLPSY-GGDLCE 1889
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 537-622 1.75e-06

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: 49.38  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  537 SRYAFSFVQAQKACLENSAVIATPQQLQAAYEAGFDQCDAGWLRDQTVRYPIVNPRNNCIgdkENTPGVRSYGMrPASET 616
Cdd:cd03516     15 GRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCG---KNGTGVYILNS-NLSSR 90


                   ....*.
gi 1832431027  617 YDVYCY 622
Cdd:cd03516     91 YDAYCY 96
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1859-1889 5.45e-06

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 44.77  E-value: 5.45e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1832431027 1859 SSPCLNGATCVDGIDSFKCFCLPSYGGDL-CE 1889
Cdd:cd00053      5 SNPCSNGGTCVNTPGSYRCVCPPGYTGDRsCE 36
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 1903-2016 1.20e-05

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 47.04  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1903 QGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNS----------HAQDYQWIGLSDRAVE--------NDFR 1964
Cdd:cd03600      3 SDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLllaagpgrhgRGSLRLWIGLQREPRQcsdpslplRGFS 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1832431027 1965 WSDGHS-LQYENWrPNQPDNFFSAgEDCVVM----IWHEKGEWNDVPCNYHLP-FTCK 2016
Cdd:cd03600     83 WVTGDQdTDFSNW-LQEPAGTCTS-PRCVALsaagSTPDNLKWKDGPCSARADgYLCK 138
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 150-243 1.26e-05

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: 47.07  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  150 VFHYRAiSTRYTLNFEKAKQACIQNSAVIATPEQLQAAYEDGYEQCDAGWLADQTVRYPIHWPRERCYGDKdefPGVRTY 229
Cdd:cd03516      8 VFLVEK-NGRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNG---TGVYIL 83

                           90
                   ....*....|....
gi 1832431027  230 GVREPDEtYDVYCY 243
Cdd:cd03516     84 NSNLSSR-YDAYCY 96
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 1895-1983 6.45e-05

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.


Pssm-ID: 153067  Cd Length: 129  Bit Score: 44.50  E-value: 6.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDYQ--------WIGLSDRAVENdFRWS 1966
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQmtkqkltpWVGLRKINVSY-WCWE 79

                           90       100
                   ....*....|....*....|..
gi 1832431027 1967 D-----GHSLQyenWRPNQPDN 1983
Cdd:cd03597     80 DmspftNTTLQ---WLPGEPSD 98
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 1033-1280 8.82e-05

Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 47.63  E-value: 8.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1033 SGGAELSGLPSGLGASGETSGTHETSGLVDLSGLTSGIDGSSEASGITFVDVTLEEVTTAPpIIGAETKETLETSGLPSG 1112
Cdd:COG3468    196 GGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGG-GAAGTGGGGGGTGTGSGG 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1113 DEDGSGMVSGSLDISGEPSGDVDFGGSVSGVLEVSGYPSGVTDSSGDVSGVDVTSGLLSGEESGLTSGFPTVSLVDTTLV 1192
Cdd:COG3468    275 GGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTG 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1193 EAVTQTSVAQEVGEGPSGMIEISGFTSGDRGLSGEGSGSVETSGFPSGAGDLSGEPSGIPH---------ISGDFSGA-- 1261
Cdd:COG3468    355 AALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNGGGGVGGGGGGGltltggtltVNGNYTGNng 434

                          250       260
                   ....*....|....*....|....*..
gi 1832431027 1262 -----TDLSGQSStVTD---ISGEASG 1280
Cdd:COG3468    435 tlvlnTVLGDDNS-PTDrlvVNGNTSG 460
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1895-1970 9.88e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 45.88  E-value: 9.88e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832431027 1895 CEEGWTKFQGHCYKHFEERETWMDAETRCRQHQAHLSSIITPEEQEFVNSHAQDY-QWIGLSDRAVENDFRWSDGHS 1970
Cdd:PHA02642    88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSdHWIGLNRESSNHPWKWADNSN 164
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 1862-1881 1.22e-04

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 40.78  E-value: 1.22e-04
                           10        20
                   ....*....|....*....|
gi 1832431027 1862 CLNGATCVDGIDSFKCFCLP 1881
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPP 20
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 1894-1968 1.52e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 44.09  E-value: 1.52e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832431027 1894 NCEEGWTKFQGHCYkHFEERETWMDAET-RCRQHQAHLSSIITPEEQEFVNSH--AQDYqWIGLSDRAVENDFRWSDG 1968
Cdd:PHA03097    45 NCRSGWVGYNNKCY-TFSENITNKHLAIeRCADMDGILTLIDDQKEVLFVSRYkgGQDL-WIGIEKKKGDDDDREVLD 120
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 36-146 1.59e-04

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 42.11  E-value: 1.59e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027    36 QSPLRVILGSSLNIPCYFNIPEeqdtsvmlTPRIKWSKlsNGTEvvlLVATGGKIRLNSEyrevislpnypaiPTDATLE 115
Cdd:smart00410    1 PPSVTVKEGESVTLSCEASGSP--------PPEVTWYK--QGGK---LLAESGRFSVSRS-------------GSTSTLT 54

                            90       100       110
                    ....*....|....*....|....*....|.
gi 1832431027   116 IKALRSNHTGIYRCEVMYGIEDRQDTIEVLV 146
Cdd:smart00410   55 ISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 35-146 3.04e-04

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: 42.06  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   35 EQSPLRVILGSSLNIPCYFNIPEEQDTsvmltPRIKWSKLSNGTEVVLLVATGGKIRLNSEYREVISLPNYPaIPTDATL 114
Cdd:pfam07686    2 TPREVTVALGGSVTLPCTYSSSMSEAS-----TSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGRFSGRGDP-SNGDGSL 75

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1832431027  115 EIKALRSNHTGIYRCEVMY-GIEDRQDTIEVLV 146
Cdd:pfam07686   76 TIQNLTLSDSGTYTCAVIPsGEGVFGKGTRLTV 108
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 262-344 1.21e-03

Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, it is highly similar to the link domain. The link domain is a hyaluronan-binding (HA) domain. KIAA0527 contains a single link module. The KIAA0527 gene was originally cloned from human brain tissue.


Pssm-ID: 239598  Cd Length: 95  Bit Score: 39.91  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  262 FQEAFDKCRSLGARLATTGELYLAWKD-GMDMCSAGWLADRSVRYPIsrARPNCGGNLVGVRtVYLYINQTgyPHPDSRY 340
Cdd:cd03521     16 LRAARQSCASLGARLASAAELRRAVVEcFFSACARGWLADGTVGTTV--CNPVVAEALKAVD-VKVEIETN--PIPFAHY 90


                   ....
gi 1832431027  341 DAIC 344
Cdd:cd03521     91 NALC 94
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
 46-147 1.31e-03

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: 40.59  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   46 SLNIPCYFnIPEEQDTSVMltprIKWSKL--SNGTEVVLLVATGGKIRLnSEYREVISLPNYPaiPTDATLEIKALRSNH 123
Cdd:cd16089     16 SVNLPCTY-VPEEGYTQVL----VKWLVQrdSDPVTIFLRDSSGDHIQQ-AKYRGRLEVSKDT--PGDVSLQLDTLEMDD 87

                           90       100
                   ....*....|....*....|....*....
gi 1832431027  124 TGIYRCEVMYGIED-----RQDTIEVLVK 147
Cdd:cd16089     88 RGHYTCQVTWQTPDgnlivREKTTELRVQ 116
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 31-130 1.41e-03

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


Pssm-ID: 409581  Cd Length: 112  Bit Score: 40.25  E-value: 1.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   31 VKIPEQSPLRviLGSSLNIPCYFNIPEEQDTSVMLTprikWSKLSNGTEVVLLVATGGKIRLNSEYREVISlPNYPAIPT 110
Cdd:cd20989      3 VQVPPEVRGF--LGGSVTLPCHLLPPNMVTHVSQVT----WQRHDEHGSVAVFHPKQGPSFPESERLSFVA-ARLGAELR 75

                           90       100
                   ....*....|....*....|
gi 1832431027  111 DATLEIKALRSNHTGIYRCE 130
Cdd:cd20989     76 NASLAMFGLRVEDEGNYTCE 95
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 641-723 1.69e-03

Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, it is highly similar to the link domain. The link domain is a hyaluronan-binding (HA) domain. KIAA0527 contains a single link module. The KIAA0527 gene was originally cloned from human brain tissue.


Pssm-ID: 239598  Cd Length: 95  Bit Score: 39.53  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027  641 FPEAQQYCESQNATLASVGQL-HAAWKQGLDRCYAGWLADGSLRYPIVSPRPACGGDAPGVRTvyqhHNQTGfPDPLSRH 719
Cdd:cd03521     16 LRAARQSCASLGARLASAAELrRAVVECFFSACARGWLADGTVGTTVCNPVVAEALKAVDVKV----EIETN-PIPFAHY 90


                   ....
gi 1832431027  720 HAFC 723
Cdd:cd03521     91 NALC 94
IGv smart00406
Immunoglobulin V-Type;
46-131 1.83e-03

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 39.29  E-value: 1.83e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027    46 SLNIPCYFNipeeqdTSVMLTPRIKWSKLSNGTEVVLLVA--TGGKIRLNSEYREVISLPNYPAiPTDATLEIKALRSNH 123
Cdd:smart00406    1 SVTLSCKFS------GSTFSSYYVSWVRQPPGKGLEWLGYigSNGSSYYQESYKGRFTISKDTS-KNDVSLTISNLRVED 73


                    ....*...
gi 1832431027   124 TGIYRCEV 131
Cdd:smart00406   74 TGTYYCAV 81
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 30-146 1.93e-03

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: 40.12  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   30 EVKIPEQSPLRviLGSSLNIPCYFNIPEeqdtSVMLTpRIKWSKLSNGTEVVllVAT-----GGKIRlnSEYREVISLPN 104
Cdd:cd05718      2 RVQVPTEVTGF--LGGSVTLPCSLTSPG----TTKIT-QVTWMKIGAGSSQN--VAVfhpqyGPSVP--NPYAERVEFLA 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1832431027  105 YPAIPTDATLEIKALRSNHTGIYRCE-VMYGIEDRQDTIEVLV 146
Cdd:cd05718     71 ARLGLRNATLRIRNLRVEDEGNYICEfATFPQGNRQGTTWLRV 113
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 162-205 3.41e-03

Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, it is highly similar to the link domain. The link domain is a hyaluronan-binding (HA) domain. KIAA0527 contains a single link module. The KIAA0527 gene was originally cloned from human brain tissue.


Pssm-ID: 239598  Cd Length: 95  Bit Score: 38.76  E-value: 3.41e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1832431027  162 LNFEKAKQACIQNSAVIATPEQLQAAYED-GYEQCDAGWLADQTV 205
Cdd:cd03521     14 LGLRAARQSCASLGARLASAAELRRAVVEcFFSACARGWLADGTV 58
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 1904-2016 3.64e-03

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 42.76  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027 1904 GHCYKHFEERETWMDAETRCRQH-QAHLSSIITPEEQEFVNS---HAQDYQ-WIGLSD--RAVENDFRWSDGHSLQY-EN 1975
Cdd:TIGR00864  329 GHCFQIVPEEAAWLDAQEQCLARaGAALAIVDNDALQNFLARkvtHSLDRGvWIGFSDvnGAEKGPAHQGEAFEAEEcEE 408

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1832431027 1976 WRPNQPDnfFSAGEDCVVMiwHEKGEWNDVPCNYHLPFTCK 2016
Cdd:TIGR00864  409 GLAGEPH--PARAEHCVRL--DPRGQCNSDLCNAPHAYVCE 445
IgV_CD80 cd16086
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here ...
 49-131 6.56e-03

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


Pssm-ID: 319335  Cd Length: 105  Bit Score: 38.20  E-value: 6.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832431027   49 IPCYFNIPEEQDTSVmltpRIKWSKlsnGTEVVLLVATGgKIRLNSEYREvislPNYPAIPTDATLEIKALRSNHTGIYR 128
Cdd:cd16086     14 LSCDYNVSVDELAQV----RIYWQK---DDKMVLTIISG-DVKVWPEYKN----RTLFDITNNLSIVILALRLSDRGTYT 81


                   ...
gi 1832431027  129 CEV 131
Cdd:cd16086     82 CVV 84
EGF smart00181
Epidermal growth factor-like domain;
1857-1889 9.94e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 35.57  E-value: 9.94e-03
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 1832431027  1857 CHS-SPCLNGaTCVDGIDSFKCFCLPSYGGDL-CE 1889
Cdd:smart00181    2 CASgGPCSNG-TCINTPGSYTCSCPPGYTGDKrCE 35
 
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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