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Conserved domains on  [gi|116875858|ref|NP_031450|]
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aggrecan core protein isoform 2 precursor [Mus musculus]

Protein Classification

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 ...
 1922-2045 1.71e-94

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: 300.65  E-value: 1.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQWIGLNDRTIEGDFRWSDGHSLQFE 2001
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 116875858 2002 KWRPNQPDNFFATGEDCVVMIWHERGEWNDVPCNYQLPFTCKKG 2045
Cdd:cd03588    81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 33-155 3.12e-71

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: 234.06  E-value: 3.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   33 IPQPSPLKVLLGSSLTIPCYFIDPMHPVTTAPSTAPLTPRIKWSRVSKEKEVVLLVATEGQVRVNSIYQDKVSLPNYPAI 112
Cdd:cd05900     1 IPLESPLRVVLGSSLLIPCYFQDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 116875858  113 PSDATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVF 155
Cdd:cd05900    81 PSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 153-247 3.53e-61

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: 204.18  E-value: 3.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  153 IVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRT 232
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 116875858  233 YGIRDTNETYDVYCF 247
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 254-349 1.04e-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: 202.93  E-value: 1.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  254 EVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYLHAN 333
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 116875858  334 QTGYPDPSSRYDAICY 349
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 ...
 588-683 4.81e-57

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: 192.53  E-value: 4.81e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  588 EVFFATRLEQFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRTVYLYPN 667
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 116875858  668 QTGLPDPLSKHHAFCF 683
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 ...
 487-581 1.72e-52

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: 179.53  E-value: 1.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  487 VVFHYRPGSTRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKDSSPGVRT 566
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 116875858  567 YGVRPSSETYDVYCY 581
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 2049-2105 1.75e-10

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: 58.24  E-value: 1.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116875858 2049 CGDPPVVEHARTLGqKKDRYEISSLVRYQCTEGFVQRHVPTIRCQPSGHWEEPRITC 2105
Cdd:cd00033     1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 689-1027 3.03e-07

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  689 APSPGEEGGSTPTSPSDIEdwIVTQVGPGVDAVPLEpktTEVPYFTTEPRKQTEWEPAYTPVGTSPQPGIPPTWLPTLPA 768
Cdd:PHA03307   24 PPATPGDAADDLLSGSQGQ--LVSDSAELAAVTVVA---GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  769 AEEHTESPSASEEPSASAVPSTSEepytssfavpsmtelPGSGEASGAPDLSGDFTGSGDASGRLDSSGQPSGGIESGLP 848
Cdd:PHA03307   99 SPAREGSPTPPGPSSPDPPPPTPP---------------PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  849 SGDLDSSGLSPTVSSGLPVESGSASGDGEVPWSHTPTvgrLPSGGESPEGSASASGTGDLSGLPSGGEITETSTSGAEET 928
Cdd:PHA03307  164 SDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPA---AASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  929 SGLPSGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSETSTSGiediSVLPT--GGESLETSASGVG 1006
Cdd:PHA03307  241 SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP----SPSPSspGSGPAPSSPRASS 316

                         330       340
                  ....*....|....*....|.
gi 116875858 1007 DLSGLPSGGESLETSASGAED 1027
Cdd:PHA03307  317 SSSSSRESSSSSTSSSSESSR 337
COG4625 super family cl34793
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 1080-1568 6.84e-07

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


The actual alignment was detected with superfamily member COG4625:

Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 54.78  E-value: 6.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1080 TSASGIEDISVFPTEAEGLDTSASGGYVSGIPSGGDGTETSASGVEDVSGLPSGGEGLETSASGVEDLGPSTRDSLETSA 1159
Cdd:COG4625     4 GGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1160 SGVDVTGFPSGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTP 1239
Cdd:COG4625    84 GGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1240 EVNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGEL 1319
Cdd:COG4625   164 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1320 DSSADISGLPSGTELSGQASGSPDSSGETSGFFDVSGQPFGSSGVSEETSGIPEISGQPSGTPDTTATSGVTELNELSSG 1399
Cdd:COG4625   244 GGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1400 QPDVSGDGSGILFGSGQSSGITSVSGETSGISDLSGQPSGFPVFSGTATRTPDLASGTISGSGESSGITFVDTSFVEVTP 1479
Cdd:COG4625   324 GGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGG 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1480 TTFREEEGLGSVELSGFPSGETELSGTSGTVDVSEQSSGAIDSSGLTSPTPEFSGLPSGVAEVSGEFSGVETGSSLPSGA 1559
Cdd:COG4625   404 GAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNT 483


                  ....*....
gi 116875858 1560 FDGSGLVSG 1568
Cdd:COG4625   484 YTGTTTVNG 492
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1922-2045 1.71e-94

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: 300.65  E-value: 1.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQWIGLNDRTIEGDFRWSDGHSLQFE 2001
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 116875858 2002 KWRPNQPDNFFATGEDCVVMIWHERGEWNDVPCNYQLPFTCKKG 2045
Cdd:cd03588    81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 33-155 3.12e-71

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: 234.06  E-value: 3.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   33 IPQPSPLKVLLGSSLTIPCYFIDPMHPVTTAPSTAPLTPRIKWSRVSKEKEVVLLVATEGQVRVNSIYQDKVSLPNYPAI 112
Cdd:cd05900     1 IPLESPLRVVLGSSLLIPCYFQDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 116875858  113 PSDATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVF 155
Cdd:cd05900    81 PSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 153-247 3.53e-61

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: 204.18  E-value: 3.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  153 IVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRT 232
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 116875858  233 YGIRDTNETYDVYCF 247
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 254-349 1.04e-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: 202.93  E-value: 1.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  254 EVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYLHAN 333
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 116875858  334 QTGYPDPSSRYDAICY 349
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 ...
 588-683 4.81e-57

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: 192.53  E-value: 4.81e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  588 EVFFATRLEQFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRTVYLYPN 667
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 116875858  668 QTGLPDPLSKHHAFCF 683
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 ...
 487-581 1.72e-52

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: 179.53  E-value: 1.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  487 VVFHYRPGSTRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKDSSPGVRT 566
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 116875858  567 YGVRPSSETYDVYCY 581
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
Xlink pfam00193
Extracellular link domain;
487-581 6.39e-45

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 157.73  E-value: 6.39e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   487 VVFHYRPGStRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKdssPGVRT 566
Cdd:pfam00193    1 GVFHLESPG-RYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 116875858   567 YGVR-PSSETYDVYCY 581
Cdd:pfam00193   77 YGFRdPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
151-248 9.56e-45

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 157.12  E-value: 9.56e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    151 KGIVFHYRAIsTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGdkdEFPGV 230
Cdd:smart00445    1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                            90
                    ....*....|....*...
gi 116875858    231 RTYGIRDTNETYDVYCFA 248
Cdd:smart00445   77 RQYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
154-247 1.21e-44

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 156.58  E-value: 1.21e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   154 VFHYRAiSTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:pfam00193    2 VFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQY 77

                           90
                   ....*....|....*
gi 116875858   234 GIRD-TNETYDVYCF 247
Cdd:pfam00193   78 GFRDpLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
252-350 4.14e-44

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 155.19  E-value: 4.14e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    252 EGEVFYATS--PEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRtvy 329
Cdd:smart00445    1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 116875858    330 lhanQTGYPDPSSRYDAICYT 350
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
586-684 6.62e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 149.03  E-value: 6.62e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    586 EGEVFF--ATRLEQFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRtvy 663
Cdd:smart00445    1 DGGVFHveKNGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 116875858    664 lypnQTGLPDPLSKHHAFCFR 684
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
254-349 1.76e-41

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 147.72  E-value: 1.76e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   254 EVFYATSPE--KFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRtvylh 331
Cdd:pfam00193    1 GVFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 116875858   332 anQTGYPDP-SSRYDAICY 349
Cdd:pfam00193   76 --QYGFRDPlSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
486-581 1.52e-40

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 145.18  E-value: 1.52e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    486 GVVFHYRPGsTRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKdssPGVR 565
Cdd:smart00445    2 GGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNL---PGVR 77

                            90
                    ....*....|....*.
gi 116875858    566 TYGVRPSSETYDVYCY 581
Cdd:smart00445   78 QYGFPDPTSRYDAYCF 93
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1922-2043 7.86e-40

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: 144.28  E-value: 7.86e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNK-----NAQDYQWIGLNDRTIEGDFRWSDGH 1996
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASllknsGSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 116875858   1997 SL-QFEKWRPNQPDNffaTGEDCVVMiWHERGEWNDVPCNYQLPFTCK 2043
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVL-STSGGKWNDVSCTSKLPFVCE 124
Xlink pfam00193
Extracellular link domain;
588-683 5.24e-39

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 140.79  E-value: 5.24e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   588 EVFFATRLEQ--FTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRtvyly 665
Cdd:pfam00193    1 GVFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 116875858   666 pnQTGLPDPLS-KHHAFCF 683
Cdd:pfam00193   76 --QYGFRDPLSeRYDAYCY 92
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1940-2044 1.33e-25

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 102.94  E-value: 1.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  1940 RETWVDAERRCREQQSHLSSIVTPEEQEFVN---KNAQDYQWIGLNDRTIEGDFRWSDGHSLQFEKWRPNQPDNffATGE 2016
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSstlKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENE 78

                           90       100
                   ....*....|....*....|....*...
gi 116875858  2017 DCVVMIWhERGEWNDVPCNYQLPFTCKK 2044
Cdd:pfam00059   79 DCVELSS-SSGKWNDENCNSKNPFVCEK 105
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 2049-2105 1.75e-10

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: 58.24  E-value: 1.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116875858 2049 CGDPPVVEHARTLGqKKDRYEISSLVRYQCTEGFVQRHVPTIRCQPSGHWEEPRITC 2105
Cdd:cd00033     1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 35-150 2.50e-09

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: 56.70  E-value: 2.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    35 QPSPLKVLLGSSLTIPCYFidpmhpvttAPSTAPLTPRIKWSRVSKEKEVVLLVATEGQVRVNSIYQDKVSLPNYPaIPS 114
Cdd:pfam07686    2 TPREVTVALGGSVTLPCTY---------SSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGRFSGRGDP-SNG 71

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 116875858   115 DATLEIQNLRSNDSGIYRCEV-MHGIEDSEATLEVIV 150
Cdd:pfam07686   72 DGSLTIQNLTLSDSGTYTCAViPSGEGVFGKGTRLTV 108
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 2049-2105 3.91e-08

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: 51.37  E-value: 3.91e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 116875858   2049 CGDPPVVEHARTLGqKKDRYEISSLVRYQCTEGFVQRHVPTIRCQPSGHWEEPRITC 2105
Cdd:smart00032    1 CPPPPDIENGTVTS-SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
2049-2105 8.40e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.58  E-value: 8.40e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116875858  2049 CGDPPVVEHARtLGQKKDRYEISSLVRYQCTEGFVQRHVPTIRCQPSGHWEEPRITC 2105
Cdd:pfam00084    1 CPPPPDIPNGK-VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 36-150 1.32e-07

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.97  E-value: 1.32e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858     36 PSPLKVLLGSSLTIPCyfidpmhpvttaPSTAPLTPRIKWSRVSKEKevvllvategqvrvnSIYQDKVSLPNYPaipSD 115
Cdd:smart00410    1 PPSVTVKEGESVTLSC------------EASGSPPPEVTWYKQGGKL---------------LAESGRFSVSRSG---ST 50

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 116875858    116 ATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIV 150
Cdd:smart00410   51 STLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 689-1027 3.03e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  689 APSPGEEGGSTPTSPSDIEdwIVTQVGPGVDAVPLEpktTEVPYFTTEPRKQTEWEPAYTPVGTSPQPGIPPTWLPTLPA 768
Cdd:PHA03307   24 PPATPGDAADDLLSGSQGQ--LVSDSAELAAVTVVA---GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  769 AEEHTESPSASEEPSASAVPSTSEepytssfavpsmtelPGSGEASGAPDLSGDFTGSGDASGRLDSSGQPSGGIESGLP 848
Cdd:PHA03307   99 SPAREGSPTPPGPSSPDPPPPTPP---------------PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  849 SGDLDSSGLSPTVSSGLPVESGSASGDGEVPWSHTPTvgrLPSGGESPEGSASASGTGDLSGLPSGGEITETSTSGAEET 928
Cdd:PHA03307  164 SDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPA---AASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  929 SGLPSGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSETSTSGiediSVLPT--GGESLETSASGVG 1006
Cdd:PHA03307  241 SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP----SPSPSspGSGPAPSSPRASS 316

                         330       340
                  ....*....|....*....|.
gi 116875858 1007 DLSGLPSGGESLETSASGAED 1027
Cdd:PHA03307  317 SSSSSRESSSSSTSSSSESSR 337
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 1080-1568 6.84e-07

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 54.78  E-value: 6.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1080 TSASGIEDISVFPTEAEGLDTSASGGYVSGIPSGGDGTETSASGVEDVSGLPSGGEGLETSASGVEDLGPSTRDSLETSA 1159
Cdd:COG4625     4 GGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1160 SGVDVTGFPSGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTP 1239
Cdd:COG4625    84 GGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1240 EVNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGEL 1319
Cdd:COG4625   164 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1320 DSSADISGLPSGTELSGQASGSPDSSGETSGFFDVSGQPFGSSGVSEETSGIPEISGQPSGTPDTTATSGVTELNELSSG 1399
Cdd:COG4625   244 GGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1400 QPDVSGDGSGILFGSGQSSGITSVSGETSGISDLSGQPSGFPVFSGTATRTPDLASGTISGSGESSGITFVDTSFVEVTP 1479
Cdd:COG4625   324 GGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGG 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1480 TTFREEEGLGSVELSGFPSGETELSGTSGTVDVSEQSSGAIDSSGLTSPTPEFSGLPSGVAEVSGEFSGVETGSSLPSGA 1559
Cdd:COG4625   404 GAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNT 483


                  ....*....
gi 116875858 1560 FDGSGLVSG 1568
Cdd:COG4625   484 YTGTTTVNG 492
PRK15319 PRK15319
fibronectin-binding autotransporter adhesin ShdA;
1171-1630 2.59e-06

fibronectin-binding autotransporter adhesin ShdA;


Pssm-ID: 185219 [Multi-domain]  Cd Length: 2039  Bit Score: 53.16  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1171 RGDPETSVSGVGDDFsglpsGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTPEVNGFPSGFSG 1250
Cdd:PRK15319  628 QGDGTLILSNTGNDY-----GDTEIDGGILAAKDAAALGTGDVTIAESATLALSQGTLDNNVTGEGQIVKSGSDELIVTG 702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1251 E--YSGADIGSGPSSGLPDFSGLPSGfptvSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGELDSSADISGl 1328
Cdd:PRK15319  703 DnnYSGGTTISGGTLTADHADSLGSG----DVDNSGVLKVGEGELENILSGSGSLVKTGTGELTLSGDNTYSGGTTITG- 777

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1329 psGTELSGQA----SGSPDSSGETS-GFFDVSGQPFGSSGVSEETSGIPEISGQPSGTPDTTATSGV---TELNELSSGQ 1400
Cdd:PRK15319  778 --GTLTADHAdslgSGDIDNSGVLKvGEGDLENTLSGSGSLVKTGTGELTLSGGNDYSGGTTIIGGTltaDHADSLGSGD 855

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1401 PDVS-------GDGSGILFGSGqsSGITSVSGE--TSGISDLSGqpsGFPVFSGT--ATRTPDLASGTIS-------GSG 1462
Cdd:PRK15319  856 IDNSgvlqvgeGELKNTLFGSG--SLVKTGTGEltLNGDNDYSG---GTTIDDGVliADHADSLGTGAVAnsgvlqvGEG 930

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1463 ESSGITFVDTSFVEVtpttfreeeGLGSVELSG---FPSGETELSGTSGTVDVSEQSSGAIDSSGLtsptpefsgLPSGV 1539
Cdd:PRK15319  931 ELKNTLSGSGSLVKT---------GTGELTLSGdnsYSGGTTIIGGTLIADHADSLGTGAVANSGV---------LQVGE 992

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1540 AEVSGEFSGveTGSSLPSG----AFDGSGLVSGFPTVSlvDRTLVESITQAPTAQEAGEGPSGILEFSGAH--SGTPDIS 1613
Cdd:PRK15319  993 GELENTLSG--SGSLVKTGtgelTLGGDNSYSGDTTIA--DGTLIAANVNALGSGNIDNSGTLMLDANGAFelANITTHS 1068

                         490
                  ....*....|....*..
gi 116875858 1614 GELSGSLDLSTLQSGQM 1630
Cdd:PRK15319 1069 GATTALAAGSTLDAGQL 1085
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 820-1313 8.59e-06

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 51.32  E-value: 8.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  820 SGDFTGSGDASGRLDSSGQPSGGIESGLPSGDLDSSGLSPTVSSGLPVESGSASGDGevpwshtpTVGRLPSGGESPEGS 899
Cdd:COG4625     1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGG--------GTGGGGGGGGGGGGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  900 ASASGTGDLSGLPSGGEITETSTSGAEETSGLPSGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSE 979
Cdd:COG4625    73 GAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  980 TSTSGIEDISVLPTGGESLETSASGVGDLSGLPSGGESLETSASGAEDVTQLPTERGGLETSASGVEDITVLPTGRESLE 1059
Cdd:COG4625   153 GGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1060 TSASGVEDVSGLPSGREGLETSASGIEDISVFPTEAEGLDTSASGGYVSGIPSGGDGTETSASGVEDVSGLPSGGEGLET 1139
Cdd:COG4625   233 GGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGG 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1140 SASGVEDLGPSTRDSLETSASGVDVTGFPSGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSA 1219
Cdd:COG4625   313 GGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGG 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1220 SGALDFGKLPPGTLGSGQTPEVNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTSSELEG 1299
Cdd:COG4625   393 GGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSG 472

                         490
                  ....*....|....
gi 116875858 1300 RGTIGISGSGEVSG 1313
Cdd:COG4625   473 AGTLTLTGNNTYTG 486
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1911-1997 1.13e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 45.49  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1911 ETESTVADQEQCEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVN--KNAQDYqWIGLNDRTIEG 1988
Cdd:PHA02642   77 DTQEPTIKYVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKryKDSSDH-WIGLNRESSNH 155


                  ....*....
gi 116875858 1989 DFRWSDGHS 1997
Cdd:PHA02642  156 PWKWADNSN 164
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 727-1041 1.96e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.37  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   727 TTEVPYFTTEPRKQTEwePAYTPVGTSPQPGIPPTWLPTLPAAEEHTESPSASEEPSASAVPSTSEEPYTSSFAVPSMTE 806
Cdd:pfam05109  445 TTGLPSSTHVPTNLTA--PASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   807 lPGSGEASGAPDLSGDFTGSGDASGRLDS----SGQPSGGIESGLPSGDLDSSG-LSPTVSSGLPVESGSASGDGEVP-- 879
Cdd:pfam05109  523 -PTPAVTTPTPNATSPTLGKTSPTSAVTTptpnATSPTPAVTTPTPNATIPTLGkTSPTSAVTTPTPNATSPTVGETSpq 601

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   880 ----------WSHTPTVGRLPSGGESP----EGSASASGTGDLSGLPSggEITETSTSGAEE---------TSGLPSGGD 936
Cdd:pfam05109  602 anttnhtlggTSSTPVVTSPPKNATSAvttgQHNITSSSTSSMSLRPS--SISETLSPSTSDnstshmpllTSAHPTGGE 679

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   937 GLE----TSTSGVDDVSGIPTGREGLETSASGVEDLSglPSGEEGSETSTSGIEDISVL----PTGGESLETSASGVGDL 1008
Cdd:pfam05109  680 NITqvtpASTSTHHVSTSSPAPRPGTTSQASGPGNSS--TSTKPGEVNVTKGTPPKNATspqaPSGQKTAVPTVTSTGGK 757

                          330       340       350
                   ....*....|....*....|....*....|...
gi 116875858  1009 SGLPSGGEslETSASGAEDVTQLPTERGGLETS 1041
Cdd:pfam05109  758 ANSTTGGK--HTTGHGARTSTEPTTDYGGDSTT 788
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 1931-2043 1.98e-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: 43.53  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  1931 GHCYRHFHDRETWVDAERRCREQ-QSHLSSIVTPEEQEF----VNKNAQDYQWIGLND-RTIE-GDFRWSDGHSLQ-FEK 2002
Cdd:TIGR00864  329 GHCFQIVPEEAAWLDAQEQCLARaGAALAIVDNDALQNFlarkVTHSLDRGVWIGFSDvNGAEkGPAHQGEAFEAEeCEE 408

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 116875858  2003 WRPNQPDnfFATGEDCVVMiwHERGEWNDVPCNYQLPFTCK 2043
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 ...
 1922-2045 1.71e-94

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: 300.65  E-value: 1.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQWIGLNDRTIEGDFRWSDGHSLQFE 2001
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 116875858 2002 KWRPNQPDNFFATGEDCVVMIWHERGEWNDVPCNYQLPFTCKKG 2045
Cdd:cd03588    81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 33-155 3.12e-71

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: 234.06  E-value: 3.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   33 IPQPSPLKVLLGSSLTIPCYFIDPMHPVTTAPSTAPLTPRIKWSRVSKEKEVVLLVATEGQVRVNSIYQDKVSLPNYPAI 112
Cdd:cd05900     1 IPLESPLRVVLGSSLLIPCYFQDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 116875858  113 PSDATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVF 155
Cdd:cd05900    81 PSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 153-247 3.53e-61

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: 204.18  E-value: 3.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  153 IVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRT 232
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 116875858  233 YGIRDTNETYDVYCF 247
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 254-349 1.04e-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: 202.93  E-value: 1.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  254 EVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYLHAN 333
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 116875858  334 QTGYPDPSSRYDAICY 349
Cdd:cd03520    81 QTGFPDPHSRFDAYCF 96
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 33-155 3.72e-57

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: 193.99  E-value: 3.72e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   33 IPQPSPLKVLLGSSLTIPCYFIDPMHPVTtaPSTAPLTPRIKWSRVS----KEKEVVLLVATEGQVRVNSIYQDKVSLPN 108
Cdd:cd05878     1 IPQSSPVRVLLGTSVTLPCYFIDPPHPVT--PSTAPLAPRIKWSKVSvdgkKEKEVVLLVATEGRVRVNSAYQGRVSLPN 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 116875858  109 YPAIPSDATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVF 155
Cdd:cd05878    79 YPAIPSDATLEVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
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 ...
 588-683 4.81e-57

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: 192.53  E-value: 4.81e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  588 EVFFATRLEQFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRTVYLYPN 667
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 116875858  668 QTGLPDPLSKHHAFCF 683
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 ...
 487-581 1.72e-52

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: 179.53  E-value: 1.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  487 VVFHYRPGSTRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKDSSPGVRT 566
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 116875858  567 YGVRPSSETYDVYCY 581
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
Xlink pfam00193
Extracellular link domain;
487-581 6.39e-45

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 157.73  E-value: 6.39e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   487 VVFHYRPGStRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKdssPGVRT 566
Cdd:pfam00193    1 GVFHLESPG-RYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 116875858   567 YGVR-PSSETYDVYCY 581
Cdd:pfam00193   77 YGFRdPLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
151-248 9.56e-45

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 157.12  E-value: 9.56e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    151 KGIVFHYRAIsTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGdkdEFPGV 230
Cdd:smart00445    1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                            90
                    ....*....|....*...
gi 116875858    231 RTYGIRDTNETYDVYCFA 248
Cdd:smart00445   77 RQYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
154-247 1.21e-44

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 156.58  E-value: 1.21e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   154 VFHYRAiSTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:pfam00193    2 VFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQY 77

                           90
                   ....*....|....*
gi 116875858   234 GIRD-TNETYDVYCF 247
Cdd:pfam00193   78 GFRDpLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
252-350 4.14e-44

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 155.19  E-value: 4.14e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    252 EGEVFYATS--PEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRtvy 329
Cdd:smart00445    1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 116875858    330 lhanQTGYPDPSSRYDAICYT 350
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
586-684 6.62e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 149.03  E-value: 6.62e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    586 EGEVFF--ATRLEQFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRtvy 663
Cdd:smart00445    1 DGGVFHveKNGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 116875858    664 lypnQTGLPDPLSKHHAFCFR 684
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 1922-2043 1.07e-41

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: 150.20  E-value: 1.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCRE-----QQSHLSSIVTPEEQEFV-------NKNAQDYQ-WIGLNDRTIEG 1988
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVydlfessRGPDTPYGlWIGLHDRTSEG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 116875858 1989 DFRWSDGHSLQFEKWRPNQPDNFFAtGEDCVVMiWHER---GEWNDVPCNYQLPFTCK 2043
Cdd:cd03589    81 PFEWTDGSPVDFTKWAGGQPDNYGG-NEDCVQM-WRRGdagQSWNDMPCDAVFPYICK 136
Xlink pfam00193
Extracellular link domain;
254-349 1.76e-41

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 147.72  E-value: 1.76e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   254 EVFYATSPE--KFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRtvylh 331
Cdd:pfam00193    1 GVFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 116875858   332 anQTGYPDP-SSRYDAICY 349
Cdd:pfam00193   76 --QYGFRDPlSERYDAYCY 92
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 1922-2044 8.51e-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: 147.07  E-value: 8.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQ--DYQWIGLNDRTIEGDFRWSDGHSLQ 1999
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSgnRSYWIGLSDEETEGEWKWVDGTPLN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 116875858 2000 FEK--WRPNQPDNFFATGEDCVVmIWHERGEWNDVPCNYQLPFTCKK 2044
Cdd:cd03590    81 SSKtfWHPGEPNNWGGGGEDCAE-LVYDSGGWNDVPCNLEYRWICEK 126
LINK smart00445
Link (Hyaluronan-binding);
486-581 1.52e-40

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 145.18  E-value: 1.52e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    486 GVVFHYRPGsTRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKdssPGVR 565
Cdd:smart00445    2 GGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNL---PGVR 77

                            90
                    ....*....|....*.
gi 116875858    566 TYGVRPSSETYDVYCY 581
Cdd:smart00445   78 QYGFPDPTSRYDAYCF 93
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1922-2043 7.86e-40

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: 144.28  E-value: 7.86e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNK-----NAQDYQWIGLNDRTIEGDFRWSDGH 1996
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASllknsGSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 116875858   1997 SL-QFEKWRPNQPDNffaTGEDCVVMiWHERGEWNDVPCNYQLPFTCK 2043
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVL-STSGGKWNDVSCTSKLPFVCE 124
Xlink pfam00193
Extracellular link domain;
588-683 5.24e-39

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 140.79  E-value: 5.24e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   588 EVFFATRLEQ--FTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRtvyly 665
Cdd:pfam00193    1 GVFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 116875858   666 pnQTGLPDPLS-KHHAFCF 683
Cdd:pfam00193   76 --QYGFRDPLSeRYDAYCY 92
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 254-349 4.33e-38

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: 137.94  E-value: 4.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  254 EVFYATS---PEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVyl 330
Cdd:cd01102     1 VVFHLESqngRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSY-- 78

                          90
                  ....*....|....*....
gi 116875858  331 hanqtGYPDPSSRYDAICY 349
Cdd:cd01102    79 -----GNPAPSGRYDAYCF 92
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 1932-2044 1.10e-37

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: 137.75  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1932 HCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQ----WIGLNDRTIEGDFRWSDGHS-LQFEKWRPN 2006
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssdvWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 116875858 2007 QPDNffATGEDCVVMIWHERGEWNDVPCNYQLPFTCKK 2044
Cdd:cd00037    81 EPNP--GGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 154-247 1.66e-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: 127.92  E-value: 1.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  154 VFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:cd01102     2 VFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN---PGVRSY 78

                          90
                  ....*....|....
gi 116875858  234 GIRDTNETYDVYCF 247
Cdd:cd01102    79 GNPAPSGRYDAYCF 92
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 487-581 2.62e-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: 127.15  E-value: 2.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  487 VVFHYRPGSTRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKdssPGVRT 566
Cdd:cd01102     1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN---PGVRS 77

                          90
                  ....*....|....*
gi 116875858  567 YGVRPSSETYDVYCY 581
Cdd:cd01102    78 YGNPAPSGRYDAYCF 92
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 487-581 3.54e-33

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: 124.08  E-value: 3.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  487 VVFHYRPGSTRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCvGDKDSSPGVRT 566
Cdd:cd03518     1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPC-GGKRTVPGLRS 79

                          90
                  ....*....|....*.
gi 116875858  567 YGVR-PSSETYDVYCY 581
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 ...
 153-247 8.64e-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: 8.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  153 IVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCyGDKDEFPGVRT 232
Cdd:cd03518     1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPC-GGKRTVPGLRS 79

                          90
                  ....*....|....*.
gi 116875858  233 YGIRDTNET-YDVYCF 247
Cdd:cd03518    80 YGERDKMLSrYDAFCF 95
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 588-683 4.51e-30

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: 115.21  E-value: 4.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  588 EVFFATR---LEQFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRTVyl 664
Cdd:cd01102     1 VVFHLESqngRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSY-- 78

                          90
                  ....*....|....*....
gi 116875858  665 ypnqtGLPDPLSKHHAFCF 683
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 ...
 588-683 1.36e-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: 110.98  E-value: 1.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  588 EVFFATRLEQFTFQEARAFCAAQNATLASTGQLYAAWS-QGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRTVylyp 666
Cdd:cd03519     1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF---- 76

                          90
                  ....*....|....*...
gi 116875858  667 nqtGLPDPLSKHH-AFCF 683
Cdd:cd03519    77 ---GFPDKKHKLYgVYCY 91
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 254-349 2.99e-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: 109.82  E-value: 2.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  254 EVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQ-GGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVylha 332
Cdd:cd03519     1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF---- 76

                          90
                  ....*....|....*...
gi 116875858  333 nqtGYPDPSSR-YDAICY 349
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 ...
 597-683 7.76e-28

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: 109.05  E-value: 7.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  597 QFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDK--PGVRTVylypnqtGLPDP 674
Cdd:cd03518    13 NLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRtvPGLRSY-------GERDK 85

                          90
                  ....*....|
gi 116875858  675 -LSKHHAFCF 683
Cdd:cd03518    86 mLSRYDAFCF 95
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 38-155 6.32e-26

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: 104.53  E-value: 6.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   38 PLKVLLGSSLTIPCYFIdpMHPvttAPSTAPLTPRIKWSRVSK---EKEVVLLVATEGQVRVNSIYQDKVSLPNYPAIPS 114
Cdd:cd05902     6 PVRRPLSSSVLLPCVFT--LPP---SASSPPEGPRIKWTKLSTsggQQQRPVLVARDNVVRVAKAFQGRVSLPGYPKNRY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 116875858  115 DATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVF 155
Cdd:cd05902    81 NASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1940-2044 1.33e-25

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 102.94  E-value: 1.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  1940 RETWVDAERRCREQQSHLSSIVTPEEQEFVN---KNAQDYQWIGLNDRTIEGDFRWSDGHSLQFEKWRPNQPDNffATGE 2016
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSstlKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENE 78

                           90       100
                   ....*....|....*....|....*...
gi 116875858  2017 DCVVMIWhERGEWNDVPCNYQLPFTCKK 2044
Cdd:pfam00059   79 DCVELSS-SSGKWNDENCNSKNPFVCEK 105
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 1922-2043 5.36e-24

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: 99.37  E-value: 5.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCRE--QQSHLSSIVTPEEQEFVNK------NAQDYQWIGLNDRTIEGDFRWS 1993
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASlissyqKAYQPVWIGLHDPQQSRGWEWS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 116875858 1994 DGHSLQFEKWRPNQPdnfFATGEDCVVMiWHERG--EWNDVPCNYQLPFTCK 2043
Cdd:cd03594    81 DGSKLDYRSWDRNPP---YARGGYCAEL-SRSTGflKWNDANCEERNPFICK 128
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 38-155 8.11e-24

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: 98.44  E-value: 8.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   38 PLKVLLGSSLTIPCYF-IDPmhpvtTAPSTAPLTPRIKWSRVSKE----KEVVLLVATEGQVRVNSIYQDKVSLPNYPAI 112
Cdd:cd05714     6 KVFSHLGGNVTLPCKFyRDP-----TAFGSGIHKIRIKWTKLTSDsgylKEVDVLVAMGNVVYHKKTYGGRVSVPLKPGS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 116875858  113 PSDATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVF 155
Cdd:cd05714    81 DSDASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 263-349 3.91e-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: 95.57  E-value: 3.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  263 KFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLL--GVRTVylhanqtGYPDP 340
Cdd:cd03518    13 NLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTvpGLRSY-------GERDK 85

                          90
                  ....*....|
gi 116875858  341 S-SRYDAICY 349
Cdd:cd03518    86 MlSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 486-581 2.14e-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: 93.26  E-value: 2.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  486 GVVFHYRPGStrysLTFEEAQQACMHTGAVIASPEQLQAAYE-AGYEQCDAGWLQDQTVRYPIVSPRTPCVGdkdSSPGV 564
Cdd:cd03519     1 GVFYLLHPGK----LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGP---LEPGV 73

                          90
                  ....*....|....*...
gi 116875858  565 RTYGV-RPSSETYDVYCY 581
Cdd:cd03519    74 RSFGFpDKKHKLYGVYCY 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 ...
 488-581 3.67e-22

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


Pssm-ID: 239592  Cd Length: 93  Bit Score: 92.53  E-value: 3.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  488 VFHYRPGSTRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCvgdKDSSPGVRTY 567
Cdd:cd03515     2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANC---GFGHVGIVDY 78

                          90
                  ....*....|....*
gi 116875858  568 GVRP-SSETYDVYCY 581
Cdd:cd03515    79 GPRLnLSERWDAYCY 93
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 37-155 1.36e-21

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: 92.33  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   37 SPLKVLLGSSLTIPCYFIdpmhPVTTAPSTAPLTP---RIKWSRVSKE------KEVVLLVATEGQVRVNSIYQDKVSLP 107
Cdd:cd05901     5 SRVHGSLSGSVVLPCRFS----TLPTLPPSYNITSeflRIKWTKIQVDkngkdhKETTVLVAQNGIIKIGQEYMGRVSVP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 116875858  108 NYPAIPSDATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVF 155
Cdd:cd05901    81 SHPEDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 1940-2042 1.82e-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: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1940 RETWVDAERRCREQQSHLSSIVTPEE----QEFVNKnAQDYQWIGLNDRTIEGDFRWSDGHSLQFEKWRPNQPDNFFAtG 2015
Cdd:cd03591    10 EKNFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVKK-GNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNNAGG-G 87

                          90       100
                  ....*....|....*....|....*..
gi 116875858 2016 EDCVVMIwhERGEWNDVPCNYQLPFTC 2042
Cdd:cd03591    88 EDCVEMY--TSGKWNDVACNLTRLFVC 112
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 ...
 255-349 3.39e-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: 3.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  255 VFYATSPE---KFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYLH 331
Cdd:cd03515     2 VFHLRSRSgkyKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGIVDYGPR 81

                          90
                  ....*....|....*...
gi 116875858  332 ANQtgypdpSSRYDAICY 349
Cdd:cd03515    82 LNL------SERWDAYCY 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 ...
 154-247 2.35e-18

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: 81.74  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  154 VFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:cd03515     2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGH---VGIVDY 78

                          90
                  ....*....|....*
gi 116875858  234 GIR-DTNETYDVYCF 247
Cdd:cd03515    79 GPRlNLSERWDAYCY 93
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 166-247 4.55e-18

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: 80.93  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  166 LDFDRAQRACLQNSAIIATPEQLQAAYE-DGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTYGIRD-TNETYD 243
Cdd:cd03519    11 LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLE---PGVRSFGFPDkKHKLYG 87


                  ....
gi 116875858  244 VYCF 247
Cdd:cd03519    88 VYCY 91
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 1932-2036 9.92e-18

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: 80.93  E-value: 9.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1932 HCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQ--WIGLNDRTIEGDFRWSDGHSLQFEKWRPNQPD 2009
Cdd:cd03603     1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGasWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80

                          90       100
                  ....*....|....*....|....*....
gi 116875858 2010 NFFATGEDCVVM--IWHERGEWNDVPCNY 2036
Cdd:cd03603    81 NNGGGNEDYAAInhFPGISGKWNDLANSY 109
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 1936-2042 1.13e-17

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: 80.50  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1936 HFHD-RETWVDAERRCREQQSHLSSIVTPEEQEFVNKNA----QDYQWIGLNDRTIEGdfRW--SDGHSLQFEKWRPNQP 2008
Cdd:cd03592     4 HYSTeKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFAlkynLGYYWIDGNDINNEG--TWvdTDKKELEYKNWAPGEP 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 116875858 2009 DNffATGEDCVVMIWHERGEWNDVPCNYQLPFTC 2042
Cdd:cd03592    82 NN--GRNENCLEIYIKDNGKWNDEPCSKKKSAIC 113
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 44-155 7.00e-17

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: 78.52  E-value: 7.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   44 GSSLTIPC-YFIDPmhpvttaPSTAPLTPRIKWSRVSK--EKEVVLLVATEGQVRVNSIYQDKVSLPNypAIPSDATLEI 120
Cdd:cd05877    12 GGNVTLPCrYHYEP-------ELSAPRKIRVKWTKLEVdyAKEEDVLVAIGTRHKSYGSYQGRVFLRR--ADDLDASLVI 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 116875858  121 QNLRSNDSGIYRCEVMHGIEDSEATLEVIVKGIVF 155
Cdd:cd05877    83 TDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
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 ...
 597-683 1.18e-13

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: 68.64  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  597 QFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRTVYLYPNQTGLPDpls 676
Cdd:cd03515    13 KLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGIVDYGPRLNLSERWD--- 89


                  ....*..
gi 116875858  677 khhAFCF 683
Cdd:cd03515    90 ---AYCY 93
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 1922-1995 1.80e-13

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: 68.90  E-value: 1.80e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116875858 1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNA-QDYQWIGLNDRTIEGDFRWSDG 1995
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 ...
 1942-2042 1.52e-12

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: 65.86  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1942 TWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQ---DYQWIGLNDRTIEgdFRWSDGHSLQFEKWRPNQPDNffatGEDC 2018
Cdd:cd03602    11 TWSEAQQYCRENYTDLATVQNQEDNALLSNLSRvsnSAAWIGLYRDVDS--WRWSDGSESSFRNWNTFQPFG----QGDC 84

                          90       100
                  ....*....|....*....|....
gi 116875858 2019 VVMIwhERGEWNDVPCNYQLPFTC 2042
Cdd:cd03602    85 ATMY--SSGRWYAALCSALKPFIC 106
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 1922-2042 4.37e-11

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: 62.41  E-value: 4.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1922 CEEGwTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQE--------FVNKNAQdyQWIGLNDRTIEGDFRWS 1993
Cdd:cd03596     1 CLKG-TKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDalrdyvkaSVPGNWE--VWLGINDMVAEGKWVDV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 116875858 1994 DGHSLQFEKWR---PNQPDNffATGEDCVVMIWHERGEWNDVPCNYQLPFTC 2042
Cdd:cd03596    78 NGSPISYFNWEreiTAQPDG--GKRENCVALSSSAQGKWFDEDCRREKPYVC 127
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 2049-2105 1.75e-10

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: 58.24  E-value: 1.75e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116875858 2049 CGDPPVVEHARTLGqKKDRYEISSLVRYQCTEGFVQRHVPTIRCQPSGHWEEPRITC 2105
Cdd:cd00033     1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 488-581 1.86e-10

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: 60.94  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  488 VFHYRPGStRYSLTFEEAQQACMHTGAVIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKdssPGVRTY 567
Cdd:cd03516     8 VFLVEKNG-RYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNG---TGVYIL 83

                          90
                  ....*....|....
gi 116875858  568 GVrPSSETYDVYCY 581
Cdd:cd03516    84 NS-NLSSRYDAYCY 96
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 1919-2043 2.10e-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: 61.06  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1919 QEQCEEGwtkFQGHCYR--HFHD---RETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQ------WIGL------ 1981
Cdd:cd03595     1 QRICRRG---TEKPCYKiaYFQDsrrRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRasdgdfWIGLrrssqy 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116875858 1982 --NDRTIEGDFRWSDGHSLQFEKWRPNQPDNFFatgEDCVVMIW----------HERGEWNDVPCNYQLPFTCK 2043
Cdd:cd03595    78 nvTSSACSSLYYWLDGSISTFRNWYVDEPSCGS---EVCVVMYHqpsapagqggPYLFQWNDDNCNMKNNFICK 148
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 35-150 2.50e-09

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: 56.70  E-value: 2.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    35 QPSPLKVLLGSSLTIPCYFidpmhpvttAPSTAPLTPRIKWSRVSKEKEVVLLVATEGQVRVNSIYQDKVSLPNYPaIPS 114
Cdd:pfam07686    2 TPREVTVALGGSVTLPCTY---------SSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGRFSGRGDP-SNG 71

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 116875858   115 DATLEIQNLRSNDSGIYRCEV-MHGIEDSEATLEVIV 150
Cdd:pfam07686   72 DGSLTIQNLTLSDSGTYTCAViPSGEGVFGKGTRLTV 108
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 1931-2042 2.94e-09

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: 56.69  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1931 GHCYRHFHDRETWVDAERRCRE-QQSHLSSI----VTPEEQEFVNKNAQDYQWIG--LNDRTIEGDFRWSDGHSLQFEKW 2003
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIhsfaFNYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYW 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 116875858 2004 RPNQPDNffaTGEDCVVMIWHErGEWNDVPCNYQLPFTC 2042
Cdd:cd03598    81 APGQPGN---RRGHCVELCTRG-GHWRRAHCKLRRPFIC 115
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 1978-2044 3.72e-09

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: 56.39  E-value: 3.72e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1978 WIGLND-RTIEGDFRWSDGHSL--QFEKWRPNQPDNfFATGEDCvVMIWHERGEWNDVPCNYQLPFTCKK 2044
Cdd:cd03601    52 WVGADNlQDGEYDFLWNDGVSLptDSDLWAPNEPSN-PQSRQLC-VQLWSKYNLLDDEYCGRAKRVICEK 119
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 2049-2105 3.91e-08

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: 51.37  E-value: 3.91e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 116875858   2049 CGDPPVVEHARTLGqKKDRYEISSLVRYQCTEGFVQRHVPTIRCQPSGHWEEPRITC 2105
Cdd:smart00032    1 CPPPPDIENGTVTS-SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
2049-2105 8.40e-08

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 50.58  E-value: 8.40e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116875858  2049 CGDPPVVEHARtLGQKKDRYEISSLVRYQCTEGFVQRHVPTIRCQPSGHWEEPRITC 2105
Cdd:pfam00084    1 CPPPPDIPNGK-VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 36-150 1.32e-07

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


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 50.97  E-value: 1.32e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858     36 PSPLKVLLGSSLTIPCyfidpmhpvttaPSTAPLTPRIKWSRVSKEKevvllvategqvrvnSIYQDKVSLPNYPaipSD 115
Cdd:smart00410    1 PPSVTVKEGESVTLSC------------EASGSPPPEVTWYKQGGKL---------------LAESGRFSVSRSG---ST 50

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 116875858    116 ATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIV 150
Cdd:smart00410   51 STLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 264-353 2.14e-07

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


Pssm-ID: 239593  Cd Length: 144  Bit Score: 52.08  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  264 FTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVrtVYLHANQtgypdpSSR 343
Cdd:cd03516    19 LNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGTGV--YILNSNL------SSR 90

                          90
                  ....*....|
gi 116875858  344 YDAICYTGED 353
Cdd:cd03516    91 YDAYCYNSSD 100
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 689-1027 3.03e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.95  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  689 APSPGEEGGSTPTSPSDIEdwIVTQVGPGVDAVPLEpktTEVPYFTTEPRKQTEWEPAYTPVGTSPQPGIPPTWLPTLPA 768
Cdd:PHA03307   24 PPATPGDAADDLLSGSQGQ--LVSDSAELAAVTVVA---GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  769 AEEHTESPSASEEPSASAVPSTSEepytssfavpsmtelPGSGEASGAPDLSGDFTGSGDASGRLDSSGQPSGGIESGLP 848
Cdd:PHA03307   99 SPAREGSPTPPGPSSPDPPPPTPP---------------PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  849 SGDLDSSGLSPTVSSGLPVESGSASGDGEVPWSHTPTvgrLPSGGESPEGSASASGTGDLSGLPSGGEITETSTSGAEET 928
Cdd:PHA03307  164 SDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPA---AASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  929 SGLPSGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSETSTSGiediSVLPT--GGESLETSASGVG 1006
Cdd:PHA03307  241 SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP----SPSPSspGSGPAPSSPRASS 316

                         330       340
                  ....*....|....*....|.
gi 116875858 1007 DLSGLPSGGESLETSASGAED 1027
Cdd:PHA03307  317 SSSSSRESSSSSTSSSSESSR 337
IGv smart00406
Immunoglobulin V-Type;
46-135 4.51e-07

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 49.30  E-value: 4.51e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858     46 SLTIPCYFidpmhpvttAPSTAPLTpRIKWSRVSKEKEVVLLVA--TEGQVRVNSIYQDKVSLPNYPAiPSDATLEIQNL 123
Cdd:smart00406    1 SVTLSCKF---------SGSTFSSY-YVSWVRQPPGKGLEWLGYigSNGSSYYQESYKGRFTISKDTS-KNDVSLTISNL 69

                            90
                    ....*....|..
gi 116875858    124 RSNDSGIYRCEV 135
Cdd:smart00406   70 RVEDTGTYYCAV 81
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 1080-1568 6.84e-07

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 54.78  E-value: 6.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1080 TSASGIEDISVFPTEAEGLDTSASGGYVSGIPSGGDGTETSASGVEDVSGLPSGGEGLETSASGVEDLGPSTRDSLETSA 1159
Cdd:COG4625     4 GGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1160 SGVDVTGFPSGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTP 1239
Cdd:COG4625    84 GGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1240 EVNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGEL 1319
Cdd:COG4625   164 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1320 DSSADISGLPSGTELSGQASGSPDSSGETSGFFDVSGQPFGSSGVSEETSGIPEISGQPSGTPDTTATSGVTELNELSSG 1399
Cdd:COG4625   244 GGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1400 QPDVSGDGSGILFGSGQSSGITSVSGETSGISDLSGQPSGFPVFSGTATRTPDLASGTISGSGESSGITFVDTSFVEVTP 1479
Cdd:COG4625   324 GGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGG 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1480 TTFREEEGLGSVELSGFPSGETELSGTSGTVDVSEQSSGAIDSSGLTSPTPEFSGLPSGVAEVSGEFSGVETGSSLPSGA 1559
Cdd:COG4625   404 GAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNT 483


                  ....*....
gi 116875858 1560 FDGSGLVSG 1568
Cdd:COG4625   484 YTGTTTVNG 492
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 849-1723 9.91e-07

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 54.39  E-value: 9.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  849 SGDLDSSGLSPTVSSGLPVESGSASGDGEVPWSHTPTvGRLPSGGESPEGSASASGTGDLSGLPSGGEITETSTSGAEET 928
Cdd:COG3210   754 AGTLSIGLTANTTASGTTLTLANANGNTSAGATLDNA-GAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTG 832

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  929 SGLPSGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSETSTSGIEDISVLPTGGESLETSASGVGDL 1008
Cdd:COG3210   833 TGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAV 912

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1009 SGLPSGGESLETSASGAEDVTQlpterggleTSASGVEDITVLPTGRESLETSASGVEDVSGLPSGREGLETSASGIEDI 1088
Cdd:COG3210   913 LATVTATGTGGGGLTGGNAAAG---------GTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANS 983

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1089 SVFPTEAEGLDTSASGGYVSGIPSGGDGTETSASGVEDVSGLPSGGEGLETSASGVEDLGPSTRDSLETSASGVDVTGFP 1168
Cdd:COG3210   984 AGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTA 1063

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1169 SGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAedlsglpsgkeDLVGSASGALDFGKLPPGTLGSGQTPEVNGFPSGF 1248
Cdd:COG3210  1064 SGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGI-----------TNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGT 1132

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1249 SGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGELDSSADISGL 1328
Cdd:COG3210  1133 STASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIG 1212

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1329 PSGTELSGQASGSPDSSGETSGFFDVSGQPFGSSGVSEETSGIPEISGQPSGTPDTTATSGVTELNELSSGQPDVSGDGS 1408
Cdd:COG3210  1213 TTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTS 1292

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1409 GILFGSGQSSGITSVSGETSGISDLSGQPSGFPVFSGTATRTPDLASGTISGSGESSGITFVDTSFVEVTPTTFREEEGL 1488
Cdd:COG3210  1293 ATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAG 1372

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1489 GSVELSGFPSGETELSGTSGTVDVSEQSSGAIDSSGLTSPTPEFSGLPSGVAEVSGEFSGVETGSSLPSGAFDGSGLVSG 1568
Cdd:COG3210  1373 SLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGN 1452

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1569 FPTVSLVDRTLVESITQAPTAQEAGEGPSGILEFSGAHSGTPDISGELSGSLDLSTLQSGQMETSTETPSSPYFSGDFSS 1648
Cdd:COG3210  1453 ADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYG 1532

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116875858 1649 TTDVSGESIAATTGSGESSGLPEVTLNTSELVEGVTEPTVSQELGHGPSMTYTPRLFEASGDASASGDLGGAVTN 1723
Cdd:COG3210  1533 GSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNA 1607
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 664-957 1.78e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 53.64  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  664 LYPNQTGLPDPLSKHHAFCFRGVSVAPSPGEEGGSTPTSPSDIEDWIVTQVGPGVDAVPLEPKTTEVPYFTTEPRKQTEW 743
Cdd:PHA03307   36 LSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPD 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  744 EPAYTPVGTSPQPGIPPTWLPTLP---------------AAEEHTESPSASEEPSASAVPStseepytssfAVPSMTELP 808
Cdd:PHA03307  116 PPPPTPPPASPPPSPAPDLSEMLRpvgspgpppaasppaAGASPAAVASDAASSRQAALPL----------SSPEETARA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  809 GSGEASGAPDLSGDFTGSGDASGRLDSSGQPSGGIESGLPSGDLDSSGLSPTVSSGLPVESGSASGDGEVPWSH-----T 883
Cdd:PHA03307  186 PSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRpapitL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  884 PTVGRLPSGGESPEG----SASASGTGDLSGLPS----GGEITETSTSGAEETSGLPSGGDGLETSTSGVDDVSGIPTGR 955
Cdd:PHA03307  266 PTRIWEASGWNGPSSrpgpASSSSSPRERSPSPSpsspGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGP 345


                  ..
gi 116875858  956 EG 957
Cdd:PHA03307  346 SP 347
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 933-1473 2.06e-06

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 53.24  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  933 SGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSETSTSGIEDISVLPTGGESLETSASGVGDLSGLP 1012
Cdd:COG4625     4 GGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1013 SGGESLETSASGAEDVTQLPTERGGLETSASGVEDITVLPTGRESLETSASGVEDVSGLPSGREGLETSASGIEDISVFP 1092
Cdd:COG4625    84 GGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1093 TEAEGLDTSASGGYVSGIPSGGDGTETSASGVEDVSGLPSGGegleTSASGVEDLGPSTRDSLETSASGVDVTGFPSGRG 1172
Cdd:COG4625   164 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGG----GGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1173 DPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTPEVNGFPSGFSGEY 1252
Cdd:COG4625   240 GGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1253 SGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGELDSSADISGLPSGT 1332
Cdd:COG4625   320 GGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGG 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1333 ELSGQASGSPDSSGETSGFFDVSGQPFGSSGVSEETSGIPEISGQPSGTPDTTATSGVTELNELSSGQPDVSGDGSGILF 1412
Cdd:COG4625   400 GGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLT 479

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116875858 1413 GSGQSSGITSVSG--------ETSGISDLSGQPSGFPVFSGTATRTPDLASGTISGSGESSGITFVDTS 1473
Cdd:COG4625   480 GNNTYTGTTTVNGggnytqsaGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLAGGYAPGTTYTILAVA 548
PRK15319 PRK15319
fibronectin-binding autotransporter adhesin ShdA;
1171-1630 2.59e-06

fibronectin-binding autotransporter adhesin ShdA;


Pssm-ID: 185219 [Multi-domain]  Cd Length: 2039  Bit Score: 53.16  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1171 RGDPETSVSGVGDDFsglpsGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTPEVNGFPSGFSG 1250
Cdd:PRK15319  628 QGDGTLILSNTGNDY-----GDTEIDGGILAAKDAAALGTGDVTIAESATLALSQGTLDNNVTGEGQIVKSGSDELIVTG 702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1251 E--YSGADIGSGPSSGLPDFSGLPSGfptvSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGELDSSADISGl 1328
Cdd:PRK15319  703 DnnYSGGTTISGGTLTADHADSLGSG----DVDNSGVLKVGEGELENILSGSGSLVKTGTGELTLSGDNTYSGGTTITG- 777

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1329 psGTELSGQA----SGSPDSSGETS-GFFDVSGQPFGSSGVSEETSGIPEISGQPSGTPDTTATSGV---TELNELSSGQ 1400
Cdd:PRK15319  778 --GTLTADHAdslgSGDIDNSGVLKvGEGDLENTLSGSGSLVKTGTGELTLSGGNDYSGGTTIIGGTltaDHADSLGSGD 855

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1401 PDVS-------GDGSGILFGSGqsSGITSVSGE--TSGISDLSGqpsGFPVFSGT--ATRTPDLASGTIS-------GSG 1462
Cdd:PRK15319  856 IDNSgvlqvgeGELKNTLFGSG--SLVKTGTGEltLNGDNDYSG---GTTIDDGVliADHADSLGTGAVAnsgvlqvGEG 930

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1463 ESSGITFVDTSFVEVtpttfreeeGLGSVELSG---FPSGETELSGTSGTVDVSEQSSGAIDSSGLtsptpefsgLPSGV 1539
Cdd:PRK15319  931 ELKNTLSGSGSLVKT---------GTGELTLSGdnsYSGGTTIIGGTLIADHADSLGTGAVANSGV---------LQVGE 992

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1540 AEVSGEFSGveTGSSLPSG----AFDGSGLVSGFPTVSlvDRTLVESITQAPTAQEAGEGPSGILEFSGAH--SGTPDIS 1613
Cdd:PRK15319  993 GELENTLSG--SGSLVKTGtgelTLGGDNSYSGDTTIA--DGTLIAANVNALGSGNIDNSGTLMLDANGAFelANITTHS 1068

                         490
                  ....*....|....*..
gi 116875858 1614 GELSGSLDLSTLQSGQM 1630
Cdd:PRK15319 1069 GATTALAAGSTLDAGQL 1085
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 1134-1670 5.92e-06

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 51.70  E-value: 5.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1134 GEGLETSASGVEDLGPSTRDSLETSASGVDVTGFPSGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKE 1213
Cdd:COG4625     1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1214 DLVGSASGALDFGKLPPGTLGSGQTPEVNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATT 1293
Cdd:COG4625    81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1294 SSELEGRGTIGISGSGEVSGLPLGELDSSADISGLPSGTELSGQASGSPDSSGETSGFFDVSGQPFGSSGVSEETSGIPE 1373
Cdd:COG4625   161 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1374 ISGQPSGTPDTTATSGVTELNELSSGQPDVSGDGSGILFGSGQSSGITSVSGETSGISDLSGQPSGFPVFSGTATRTpDL 1453
Cdd:COG4625   241 GGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG-GG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1454 ASGTISGSGESSGITFVDTSFVEVTPTTFREEEGLGSVELSGFPSGETELSGTSGTVDVSEQSSGAIDSSGLTSPTPEFS 1533
Cdd:COG4625   320 GGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGG 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1534 GLPSGVAEVSGEFSGVETGSSLPSGAFDGSGLVSGFPTVSLVDRTLVESITQAPTAQEAGEGPSGILEFSGAHSGTPDIS 1613
Cdd:COG4625   400 GGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLT 479

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116875858 1614 GELSGSLDLSTLQSGqmeTSTETPSSPYFSGDFSSTTDVSGESIAATTGSGESSGLP 1670
Cdd:COG4625   480 GNNTYTGTTTVNGGG---NYTQSAGSTLAVEVDAANSDRLVVTGTATLNGGTVVVLA 533
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 597-683 6.35e-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: 47.84  E-value: 6.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  597 QFTFQEARAFCAAQNATLASTGQLYAAWSQGLDKCYAGWLADGTLRYPIITPRPACGGDKPGVRTvylypnqtgLPDPLS 676
Cdd:cd03516    18 SLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGTGVYI---------LNSNLS 88


                  ....*...
gi 116875858  677 KHH-AFCF 683
Cdd:cd03516    89 SRYdAYCY 96
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 820-1313 8.59e-06

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 51.32  E-value: 8.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  820 SGDFTGSGDASGRLDSSGQPSGGIESGLPSGDLDSSGLSPTVSSGLPVESGSASGDGevpwshtpTVGRLPSGGESPEGS 899
Cdd:COG4625     1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGG--------GTGGGGGGGGGGGGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  900 ASASGTGDLSGLPSGGEITETSTSGAEETSGLPSGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSE 979
Cdd:COG4625    73 GAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  980 TSTSGIEDISVLPTGGESLETSASGVGDLSGLPSGGESLETSASGAEDVTQLPTERGGLETSASGVEDITVLPTGRESLE 1059
Cdd:COG4625   153 GGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1060 TSASGVEDVSGLPSGREGLETSASGIEDISVFPTEAEGLDTSASGGYVSGIPSGGDGTETSASGVEDVSGLPSGGEGLET 1139
Cdd:COG4625   233 GGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGG 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1140 SASGVEDLGPSTRDSLETSASGVDVTGFPSGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSA 1219
Cdd:COG4625   313 GGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGG 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1220 SGALDFGKLPPGTLGSGQTPEVNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTSSELEG 1299
Cdd:COG4625   393 GGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSG 472

                         490
                  ....*....|....
gi 116875858 1300 RGTIGISGSGEVSG 1313
Cdd:COG4625   473 AGTLTLTGNNTYTG 486
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 43-135 2.05e-05

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 45.52  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   43 LGSSLTIPCYFidpmhpvtTAPSTAPLTpRIKWSRV-SKEKEVVLLVATEGQVRVNSIYQDKVSLPNYPAIPSDATLEIQ 121
Cdd:cd05718    13 LGGSVTLPCSL--------TSPGTTKIT-QVTWMKIgAGSSQNVAVFHPQYGPSVPNPYAERVEFLAARLGLRNATLRIR 83

                          90
                  ....*....|....
gi 116875858  122 NLRSNDSGIYRCEV 135
Cdd:cd05718    84 NLRVEDEGNYICEF 97
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 1001-1905 5.30e-05

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 48.61  E-value: 5.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1001 SASGVGDLSGLPSGGESLETSASGAEDVTQLPTERGGLETSASGVEDITVLPTGRESLETSASGVEDVSGLPSGREGLET 1080
Cdd:COG3210   805 TAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGV 884

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1081 SASGIEDISVFPTEAEGLDTSASGGYVSGIPSGGDGTETSASGVEDVSGLPSGGEGLETSASGVEDLGPSTRDSLETSAS 1160
Cdd:COG3210   885 ATSTGTANAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAG 964

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1161 GVDVTGfpSGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTPE 1240
Cdd:COG3210   965 DTGASS--AAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGG 1042

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1241 VNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGELD 1320
Cdd:COG3210  1043 QNGVGVNASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVG 1122

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1321 SSADISGLPSGTELSGQASGSPDSSGETSGFFDVSGQPFGSSGVSEETSGipeisgqpsGTPDTTATSGVTELNELSSGQ 1400
Cdd:COG3210  1123 GTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAA---------TTTTTGSAINGGADSAATEGT 1193

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1401 PDVSGDGSGILFGSGQSSGITSVSGETSGISDLSGQPSGFPVFSGTATRTPDLASGTISGSGESSGITFVDTSFVEVTPT 1480
Cdd:COG3210  1194 AGTDLKGGDSTGGSTTTIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTV 1273

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1481 TFREEEGLGSVELSGFPSGETELSGTSGTVDVSEQSSGAIDSSGLTSPTPEFSGLPSGVAEVSGEFSGVETGSSLPSGAF 1560
Cdd:COG3210  1274 AGNAGATATGSTVDIGSTSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLN 1353

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1561 DGSGLVSGFPTVSLVDRTLVESITQAPTAQEAGEGPSGILEFSGAHSGTPDISGELSGSLDLSTLQSGQMETSTETPSSP 1640
Cdd:COG3210  1354 GGNGATDSAAGAGSGGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTG 1433

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1641 YFSGDFSSTTDVSGESIAATTGSGESSGLPEVTLNTSELVEGVTEPTVSQELGHGPSMTYTPRLFEASGDASASGDLGGA 1720
Cdd:COG3210  1434 TGGTGNTTGTSVAGAGGGNADASAINTGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAG 1513

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1721 VTNFPGSGIEASVPEASSDLSAYPEAGVGVSAAPEASSKLSEFPDLHGITSAFHETDLEMTTPSTEVNSNPWTFQEGTRE 1800
Cdd:COG3210  1514 GTTAEVAKASLEGGEGTYGGSSVAEAGTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGN 1593

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1801 GSAAPEVSGESSTTSDIDTGTSGVPSATPMASGDRTEISGEWSDHTSEVNVAISSTITESEWAQPTRYPTETLQEIESPN 1880
Cdd:COG3210  1594 TATLTLSLAEGTNAEYGGTTNVTSGTAGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLT 1673

                         890       900
                  ....*....|....*....|....*
gi 116875858 1881 PSYSGEETQTAETTMSLTDAPTLSS 1905
Cdd:COG3210  1674 DATLAGLGGATTAAAGNVATGDTAP 1698
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 1930-2043 9.20e-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: 44.34  E-value: 9.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1930 QGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNK--NAQDYQ--------WIGLN---------DRTIEGdF 1990
Cdd:cd03600     3 SDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLllAAGPGRhgrgslrlWIGLQreprqcsdpSLPLRG-F 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116875858 1991 RWSDGHS-LQFEKWrPNQPDNfFATGEDCVVM----IWHERGEWNDVPCNYQLP-FTCK 2043
Cdd:cd03600    82 SWVTGDQdTDFSNW-LQEPAG-TCTSPRCVALsaagSTPDNLKWKDGPCSARADgYLCK 138
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1911-1997 1.13e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 45.49  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1911 ETESTVADQEQCEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVN--KNAQDYqWIGLNDRTIEG 1988
Cdd:PHA02642   77 DTQEPTIKYVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKryKDSSDH-WIGLNRESSNH 155


                  ....*....
gi 116875858 1989 DFRWSDGHS 1997
Cdd:PHA02642  156 PWKWADNSN 164
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 1922-2010 2.13e-04

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: 43.34  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1922 CEEGWTKFQGHCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQ--------WIGLndRTIEGDFR-W 1992
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQmtkqkltpWVGL--RKINVSYWcW 78

                          90       100
                  ....*....|....*....|...
gi 116875858 1993 SD-----GHSLQfekWRPNQPDN 2010
Cdd:cd03597    79 EDmspftNTTLQ---WLPGEPSD 98
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
 883-1470 2.69e-04

Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 46.30  E-value: 2.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  883 TPTVGRLPSGGESPEGSASASGTGDLSGLPSGGEITETSTSGAEETSGLPSGGDGLETSTSGVDDVSGIPTGREGleTSA 962
Cdd:COG5295    17 VASGASTTASGSSATVTSAAQSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGAGSGGTSATAASSVASGGASAA--TAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  963 SGVEDLSGLPSGEEGSETSTSGIEDISVLPTGGESLETSASGVGDLSGLPSGGESLETSASGAEDVTQLPTERGGLETSA 1042
Cdd:COG5295    95 STGTGNTAGTAATVAGAASSGSATNAGASAGASAAAAAGSTAAAGGAAASTGGSSAAGGSNTATATGSSTANAATAAAGA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1043 SGVEDITVLPTGRESLETSASGVEDVSGLPSGREGLETSASGIEDISVFPTEAEGLDTSASGGYVS--GIPSGGDGTETS 1120
Cdd:COG5295   175 TSTSASGSSSGASGAAAASAATGASAGGTASAAASASSSATGTSASVGVNAGAATGSAASAGGSASagAASGNATTASAS 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1121 ASGVEDVSGLPSGGEGLETSASGVEDLGPSTRDSLETSASGVDVTGFPSGRGDPETSVSGVGDDFSGLPSGKEGLETSAS 1200
Cdd:COG5295   255 SVSGSAVAAGTASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGAAALGSAGGSSGVGT 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1201 GAEDLSGLPSGKEDLVG-SASGALDFGKLPPGTLGSGQTPEVNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVS 1279
Cdd:COG5295   335 ASGASAAAATNDGTANGaGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSGGSSTGASAGGGASAA 414

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1280 LVDSTLVEVITATTSSELEGRGTIGISGSGEVSGlplgelDSSADISGLPSGTELSGQASGSPDSSGETSGFFDVSGQPF 1359
Cdd:COG5295   415 GGAAAGSAAAGTSSNTSAVGASNGASGTSSSASS------AGAAGGGTAGAGGAANVGAATTAASAAATAAAATSSAAIA 488

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1360 GSSGVSEETSGIPEISGQPSGTPDTTATSGVTELNELSSGQPDVSGDGSGILFGSGQSSGITSVSGETSGISDLSGQPSG 1439
Cdd:COG5295   489 GATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATAGSAGGGAAAAAGGGSTTAATGTNSVAVGNNTATGANS 568

                         570       580       590
                  ....*....|....*....|....*....|.
gi 116875858 1440 fpvfsgTATRTPDLASGTISGSGESSGITFV 1470
Cdd:COG5295   569 ------VALGAGSVASGANSVSVGAAGAENV 593
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
 44-148 4.96e-04

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


Pssm-ID: 409539  Cd Length: 110  Bit Score: 41.46  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   44 GSSLTIPCYFidpmhPVTTAPSTAPLTprIKWSRvsKEKEVVLLVATEGQVRV-NSIYQDKVSLPNYPAIPSDATLEIQN 122
Cdd:cd20947    13 GSNMTIECKF-----PVEKQLDLAALI--VYWEM--EDKNIIQFVHGEEDLKVqHSSYRQRARLLKDQLSLGNAALQITD 83

                          90       100
                  ....*....|....*....|....*..
gi 116875858  123 LRSNDSGIYRCEVMHGIED-SEATLEV 148
Cdd:cd20947    84 VKLQDAGVYRCMISYGGADyKRITVKV 110
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 488-550 5.89e-04

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: 41.07  E-value: 5.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116875858  488 VFHYRPGSTRYSLTFEEAQQACMHTGAVIASPEQLQ-AAYEAGYEQCDAGWLQDQTVRYPIVSP 550
Cdd:cd03521     2 LFVLELENGSQGLGLRAARQSCASLGARLASAAELRrAVVECFFSACARGWLADGTVGTTVCNP 65
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 154-247 5.91e-04

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: 42.06  E-value: 5.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  154 VFHYRAiSTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:cd03516     8 VFLVEK-NGRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNG---TGVYIL 83

                          90
                  ....*....|....
gi 116875858  234 GIRDTNEtYDVYCF 247
Cdd:cd03516    84 NSNLSSR-YDAYCY 96
IgV_CD2_like_N cd05775
N-terminal immunoglobulin (Ig)-like domain of T-cell surface antigen CD2, and similar domains; ...
 58-149 9.21e-04

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


Pssm-ID: 409431  Cd Length: 98  Bit Score: 40.41  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   58 HPVTTAPSTAPLT-PRIKWSRvsKEKEVVLLVATEGqVRVNSIYQDKVSLPNypaipSDATLEIQNLRSNDSGIYRCEVM 136
Cdd:cd05775    11 GNVTLTISSLQDDiDEIKWKK--TKDKIVEWENNIG-PTYFGSFKDRVLLDK-----ESGSLTIKNLTKEDSGTYELEIT 82

                          90
                  ....*....|....*.
gi 116875858  137 H---GIEDSEATLEVI 149
Cdd:cd05775    83 StngKVLSSKFTLEVL 98
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 1922-2044 9.72e-04

C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS); CLECT_DGCR2_like: C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DGS is also known velo-cardio-facial syndrome (VCFS). DGS is a genetic abnormality that results in malformations of the heart, face, and limbs and is associated with schizophrenia and depressive disorders. DGCR2 is a candidate for involvement in the pathogenesis of DGS since the DGCR2 gene lies within the minimal DGS critical region (MDGRC) of 22q11, which when deleted gives rise to DGS, and the DGCR2 gene is in close proximity to the balanced translocation breakpoint in a DGS patient having a balanced translocation.


Pssm-ID: 153069  Cd Length: 153  Bit Score: 41.83  E-value: 9.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1922 CEEGWTKFQG--HCYRHFHDRETWVDAERRCREQQSHLSSIVTPEEQEFVNKNAQDYQ------------WIGLN----- 1982
Cdd:cd03599     1 CPSGWHHYEGtaSCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILAQEWDFDervfgrkdqckfWVGYQyvitn 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116875858 1983 -DRTIEGdfRWSDGHSLQFEKWRPnqPDNFFATG---EDCVV-----------MIWHERGEWNDVPCNYQLPFTCKK 2044
Cdd:cd03599    81 rNHSLEG--RWEVAYKGSMEVFLP--PEPIFATGmstNDNVFcaqlqcfqipsLRERGLHSWHAENCYEKSSFLCKR 153
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
930-1111 1.28e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 44.00  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  930 GLPSGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSETSTSGIEDISVLPTGGESLETSASGVGDLS 1009
Cdd:PRK15387  239 ALPPELRTLEVSGNQLTSLPVLPPGLLELSIFSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGLQELSVSDNQLASLP 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1010 GLPSGGESLETSASGAEDVTQLPTERGGLETSASGVEDITVLPTGRESLETSASGVEDVSGLPSGREGLETSASGIEDIS 1089
Cdd:PRK15387  319 ALPSELCKLWAYNNQLTSLPTLPSGLQELSVSDNQLASLPTLPSELYKLWAYNNRLTSLPALPSGLKELIVSGNRLTSLP 398

                         170       180
                  ....*....|....*....|..
gi 116875858 1090 VFPTEAEGLdtSASGGYVSGIP 1111
Cdd:PRK15387  399 VLPSELKEL--MVSGNRLTSLP 418
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 1169-1619 1.44e-03

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


Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 43.78  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1169 SGRGDPETSVSGVGDDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTPEVNGFPSGF 1248
Cdd:COG3468     3 SGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1249 SGEYSGADIGSGPSSGLPDFSGLpSGFPTVSLVDSTLVEVITATTSSELEGRGTIGISGSGEVSGLPLGELDSSADISGL 1328
Cdd:COG3468    83 GTGGNSTGGGGGNSGTGGTGGGG-GGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1329 PSGTELSGQASGSPDSSGETSGFFdVSGQPFGSSGVSEETSGIPEISGQPSGTPDTTATSGVTELNELSSGQPDVSGDGS 1408
Cdd:COG3468   162 GSGGGGSGGGGGAGGGGGGGAGGS-GGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1409 GILFGSGQSSGITSVSGETSGISDLSGQPSGFPVFSGTATRTpdlASGTISGSGESSGITFVDTSFVEVTPTTFREEEGL 1488
Cdd:COG3468   241 GGGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANG---GGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1489 GSVELSGFPSGETELSGTSGTVDVSEQSSGAIDSSGLTSptpefsglpSGVAEVSGEFSGVETGSSLPSGAFDGSGLVSG 1568
Cdd:COG3468   318 GGSNAGGGSGGGGGGGGGGGGGGTTLNGAGSAGGGTGAA---------LAGTGGSGSGGGGGGGSGGGGGAGGGGANTGS 388

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 116875858 1569 FPTVSLVDRTLVESITqaptaqeAGEGPSGILEFSGAHSGTPDISGELSGS 1619
Cdd:COG3468   389 DGVGTGLTTGGTGNNG-------GGGVGGGGGGGLTLTGGTLTVNGNYTGN 432
I-set pfam07679
Immunoglobulin I-set domain;
35-150 1.59e-03

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 39.55  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858    35 QPSPLKVLLGSSLTIPCYfidpmhpVTTAPstaplTPRIKWSRvskeKEVVLLVATEGQVRVNsiyqdkvslpnypaiPS 114
Cdd:pfam07679    6 KPKDVEVQEGESARFTCT-------VTGTP-----DPEVSWFK----DGQPLRSSDRFKVTYE---------------GG 54

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 116875858   115 DATLEIQNLRSNDSGIYRCEVMHGIEDSEATLEVIV 150
Cdd:pfam07679   55 TYTLTISNVQPDDSGKYTCVATNSAGEAEASAELTV 90
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 885-1308 1.68e-03

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


Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 43.78  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  885 TVGRLPSGGESPEGSASASGTGDLSGLPSGGEITETSTSGAEETSGLPSGGDGLETSTSGVDDVSGIPTGREGLETSASG 964
Cdd:COG3468    25 GTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGNSTGGGGGNSGTGGTGGG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  965 VEDLSGLPSGEEGSETSTSGiedisvlpTGGESLETSASGVGDLSGLPSGGESLETSASGAEDVTQLPTERGGLETSASG 1044
Cdd:COG3468   105 GGGGGSGNGGGGGGGGGGGG--------TGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGGSGGGGGAGG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1045 VEDITVLPTGRESLETSASGVEDVSGLPSGREGLETSASGIEDISVFPTEAEGLDTSASGGYVSGIPSGGDGTETSASGV 1124
Cdd:COG3468   177 GGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAGGTGGGGLTGG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1125 EDVSGLPSGGEGLETSASGVEDLGPSTRDSLETSASGVDVTGFPSGRGDPETSVSGVGDDFSGlpsgkegletSASGAED 1204
Cdd:COG3468   257 GAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGG----------SNAGGGS 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1205 LSGlpSGKEDLVGSASGALDFGKLPPGTLGSGQTPEVNGFPSGFSGEYSGADIGSGPSSGLPDFSGLPSGFPTVSLVDST 1284
Cdd:COG3468   327 GGG--GGGGGGGGGGGTTLNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTTGGTGNNG 404

                         410       420
                  ....*....|....*....|....
gi 116875858 1285 LVEVITATTSSELEGRGTIGISGS 1308
Cdd:COG3468   405 GGGVGGGGGGGLTLTGGTLTVNGN 428
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 727-1041 1.96e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 43.37  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   727 TTEVPYFTTEPRKQTEwePAYTPVGTSPQPGIPPTWLPTLPAAEEHTESPSASEEPSASAVPSTSEEPYTSSFAVPSMTE 806
Cdd:pfam05109  445 TTGLPSSTHVPTNLTA--PASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATS 522

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   807 lPGSGEASGAPDLSGDFTGSGDASGRLDS----SGQPSGGIESGLPSGDLDSSG-LSPTVSSGLPVESGSASGDGEVP-- 879
Cdd:pfam05109  523 -PTPAVTTPTPNATSPTLGKTSPTSAVTTptpnATSPTPAVTTPTPNATIPTLGkTSPTSAVTTPTPNATSPTVGETSpq 601

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   880 ----------WSHTPTVGRLPSGGESP----EGSASASGTGDLSGLPSggEITETSTSGAEE---------TSGLPSGGD 936
Cdd:pfam05109  602 anttnhtlggTSSTPVVTSPPKNATSAvttgQHNITSSSTSSMSLRPS--SISETLSPSTSDnstshmpllTSAHPTGGE 679

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858   937 GLE----TSTSGVDDVSGIPTGREGLETSASGVEDLSglPSGEEGSETSTSGIEDISVL----PTGGESLETSASGVGDL 1008
Cdd:pfam05109  680 NITqvtpASTSTHHVSTSSPAPRPGTTSQASGPGNSS--TSTKPGEVNVTKGTPPKNATspqaPSGQKTAVPTVTSTGGK 757

                          330       340       350
                   ....*....|....*....|....*....|...
gi 116875858  1009 SGLPSGGEslETSASGAEDVTQLPTERGGLETS 1041
Cdd:pfam05109  758 ANSTTGGK--HTTGHGARTSTEPTTDYGGDSTT 788
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 1931-2043 1.98e-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: 43.53  E-value: 1.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  1931 GHCYRHFHDRETWVDAERRCREQ-QSHLSSIVTPEEQEF----VNKNAQDYQWIGLND-RTIE-GDFRWSDGHSLQ-FEK 2002
Cdd:TIGR00864  329 GHCFQIVPEEAAWLDAQEQCLARaGAALAIVDNDALQNFlarkVTHSLDRGVWIGFSDvNGAEkGPAHQGEAFEAEeCEE 408

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 116875858  2003 WRPNQPDnfFATGEDCVVMiwHERGEWNDVPCNYQLPFTCK 2043
Cdd:TIGR00864  409 GLAGEPH--PARAEHCVRL--DPRGQCNSDLCNAPHAYVCE 445
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
907-1093 2.30e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 43.23  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  907 DLSGLPS-GGEITETSTSGAEETS--GLPSGGDGLETSTSGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSETSTS 983
Cdd:PRK15387  233 NLTSLPAlPPELRTLEVSGNQLTSlpVLPPGLLELSIFSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGLQELSVSDN 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  984 GIEDISVLPTGGESLETSASGVGDLSGLPSGGESLETSASGAEDVTQLPTERGGLETSASGVEDITVLPTGRESLETSAS 1063
Cdd:PRK15387  313 QLASLPALPSELCKLWAYNNQLTSLPTLPSGLQELSVSDNQLASLPTLPSELYKLWAYNNRLTSLPALPSGLKELIVSGN 392

                         170       180       190
                  ....*....|....*....|....*....|
gi 116875858 1064 GVEDVSGLPSGREGLETSASGIEDISVFPT 1093
Cdd:PRK15387  393 RLTSLPVLPSELKELMVSGNRLTSLPMLPS 422
PHA03369 PHA03369
capsid maturational protease; Provisional
 733-1058 3.85e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 42.29  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  733 FTTEPRKQTEWEPAYTPVGTSPQPGIPPTWLPTLPAAEEHTESPSASEEPSASAVPSTSEEPYTSSFAVPSMTELPGSGE 812
Cdd:PHA03369  335 FSTINGLKAHNEILKTASLTAPSRVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTAYPPVPQFCGDPG 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  813 ASGAPDLSGDFTGSGDasgrldssgQPSGGIESGLPSGDLDSSGLSPTVSSGLPVESGSA---SGDGEVPWSHTPTVGRL 889
Cdd:PHA03369  415 LVSPYNPQSPGTSYGP---------EPVGPVPPQPTNPYVMPISMANMVYPGHPQEHGHErkrKRGGELKEELIETLKLV 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  890 PSGGESPEGSASASGTGDLSGLPSGGEITETSTSGAEETSGLPSggDGLETSTSGVDDVSGIPTGREGLETSASGVEDLS 969
Cdd:PHA03369  486 KKLKEEQESLAKELEATAHKSEIKKIAESEFKNAGAKTAAANIE--PNCSADAAAPATKRARPETKTELEAVVRFPYQIR 563

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  970 GLPSGE-EGSETSTSGIEDISVLPTGGESLE-------TSASGVGDLSGLPSGGESLETSASGAEDVTQLPTERGGLETS 1041
Cdd:PHA03369  564 NMESPAfVHSFTSTTLAAAAGQGSDTAEALAgaietllTQASAQPAGLSLPAPAVPVNASTPASTPPPLAPQEPPQPGTS 643

                         330
                  ....*....|....*..
gi 116875858 1042 ASGVEdiTVLPTGRESL 1058
Cdd:PHA03369  644 APSLE--TSLPQQKPVL 658
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 783-1308 4.12e-03

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 42.46  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  783 SASAVPSTSEEPYTSSFAVPSMTELPGSGEASGAPDLSGDFTGSGDASGRLDSSGQPSGGIESGLPSGDLDSSGLSPTVS 862
Cdd:COG4625    22 AGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  863 SGLPVESGSASGDGEVpwSHTPTVGRLPSGGESPEGSASASGTGDLSGLPSGGEITETSTSGAEETSGLPSGGDGLETST 942
Cdd:COG4625   102 GGGGGGGGGGGGGGGG--SAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGG 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  943 SGVDDVSGIPTGREGLETSASGVEDLSGLPSGEEGSETSTSGIEDISVLPTGGESLETSASGVGDLSGLPSGGESLETSA 1022
Cdd:COG4625   180 GGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNG 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1023 SGAEDVTQLPTERGGLETSASGVEDITVLPTGRESLETSASGVEDVSGLPSGREGLETSASGIEDISVFPTEAEGLDTSA 1102
Cdd:COG4625   260 GGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGG 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1103 SGGYVSGIPSGGDGTeTSASGvedvsglpsggegleTSASGVEDLGPSTRDSLETSASGVDVTGFPSGRGDPETSVSGVG 1182
Cdd:COG4625   340 SGGAGAGGGGAGGGG-AGGGG---------------GGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGG 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858 1183 DDFSGLPSGKEGLETSASGAEDLSGLPSGKEDLVGSASGALDFGKLPPGTLGSGQTPEVNGFpSGFSGEYSGADIGSGPS 1262
Cdd:COG4625   404 GAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGA-GGGSGSGAGTLTLTGNN 482

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 116875858 1263 SGLPDFSGLPSGFPTVSlVDSTLVEVITATTSSELEGRGTIGISGS 1308
Cdd:COG4625   483 TYTGTTTVNGGGNYTQS-AGSTLAVEVDAANSDRLVVTGTATLNGG 527
IgV_CD80 cd16086
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here ...
 72-135 4.91e-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: 38.59  E-value: 4.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116875858   72 RIKWSrvsKEKEVVLLVaTEGQVRVNSIYQDKvslpNYPAIPSDATLEIQNLRSNDSGIYRCEV 135
Cdd:cd16086    29 RIYWQ---KDDKMVLTI-ISGDVKVWPEYKNR----TLFDITNNLSIVILALRLSDRGTYTCVV 84
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 266-348 6.49e-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: 37.99  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116875858  266 FQEAANECRRLGARLATTGQLYLAWQG-GMDMCSAGWLADRSVRYPIskARPNCGGNLLGVR-TVYLHANqtgyPDPSSR 343
Cdd:cd03521    16 LRAARQSCASLGARLASAAELRRAVVEcFFSACARGWLADGTVGTTV--CNPVVAEALKAVDvKVEIETN----PIPFAH 89


                  ....*
gi 116875858  344 YDAIC 348
Cdd:cd03521    90 YNALC 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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