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Conserved domains on  [gi|1375383923|sp|P16112|]
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RecName: Full=Aggrecan core protein; AltName: Full=Cartilage-specific proteoglycan core protein; Short=CSPCP; AltName: Full=Chondroitin sulfate proteoglycan core protein 1; Short=Chondroitin sulfate proteoglycan 1; Contains: RecName: Full=Aggrecan core protein 2; Flags: Precursor

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 ...
 2320-2443 3.18e-97

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: 308.74  E-value: 3.18e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPMQFE 2399
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1375383923 2400 NWRPNQPDNFFAAGEDCVVMIWHEKGEWNDVPCNYHLPFTCKKG 2443
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 33-155 1.03e-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: 235.60  E-value: 1.03e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   33 IPQPSPLRVLLGTSLTIPCYFIDPMHPVTTAPSTAPLAPRIKWSRVSKEKEVVLLVATEGRVRVNSAYQDKVSLPNYPAI 112
Cdd:cd05900      1 IPLESPLRVVLGSSLLIPCYFQDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1375383923  113 PSDATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVF 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 2.19e-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: 204.95  E-value: 2.19e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  153 IVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRT 232
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1375383923  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 1.21e-60

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239597  Cd Length: 96  Bit Score: 202.93  E-value: 1.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  254 EVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYVHAN 333
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1375383923  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 ...
 579-674 3.70e-59

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239597  Cd Length: 96  Bit Score: 198.69  E-value: 3.70e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  579 EVFFATRLEQFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTVYLYPN 658
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1375383923  659 QTGLPDPLSRHHAFCF 674
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 ...
 478-572 4.37e-53

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239594  Cd Length: 95  Bit Score: 181.07  E-value: 4.37e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  478 VVFHYRPGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKDSSPGVRT 557
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1375383923  558 YGVRPSTETYDVYCF 572
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 2447-2503 2.01e-11

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: 60.94  E-value: 2.01e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1375383923 2447 CGEPPVVEHARTFGqKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGHWEEPQITC 2503
Cdd:cd00033      1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2283-2313 1.19e-06

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


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.86  E-value: 1.19e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1375383923 2283 CAEE-PCGA-GTCKETEGHVICLCPPGYTGEHC 2313
Cdd:cd00054      5 CASGnPCQNgGTCVNTVGSYRCSCPPGYTGRNC 37
PRK15387 super family cl33133
type III secretion system effector E3 ubiquitin transferase SspH2;
1433-1614 1.04e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


The actual alignment was detected with superfamily member PRK15387:

Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 44.38  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1433 PSGEVLETTAPGVEEISGLPSGeVLETS--TSAVGDLSGLPSGGEVLEISVSGVEDISGLPSG-EVVETSASGIEDVSEL 1509
Cdd:PRK15387   242 PELRTLEVSGNQLTSLPVLPPG-LLELSifSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGlQELSVSDNQLASLPAL 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1510 PSGE-GLETSASGVEDLSRLPSGEEVLEISASGFGDLSGLPSGGEGLETSASEVgTDLSGLPSGREGLETSASGAEDLSG 1588
Cdd:PRK15387   321 PSELcKLWAYNNQLTSLPTLPSGLQELSVSDNQLASLPTLPSELYKLWAYNNRL-TSLPALPSGLKELIVSGNRLTSLPV 399

                          170       180
                   ....*....|....*....|....*.
gi 1375383923 1589 LPSGKEDLVGSASGDLDLGKLPSGTL 1614
Cdd:PRK15387   400 LPSELKELMVSGNRLTSLPMLPSGLL 425
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 716-975 2.82e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  716 EETTAVPSGETTAilEFTTEPENQTEWEPAYTPVGTSPLPGilPTWPPTGAATEESTEGPSATEVPSASEEPSPSEVPFP 795
Cdd:PHA03307    62 CDRFEPPTGPPPG--PGTEAPANESRSTPTWSLSTLAPASP--AREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEM 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  796 SEEPSPSEEPFPSVRPFPSVE-------------------LFPSEEPFPSkEPSPSEEPSASEEPYTPSPPVPSWTELPS 856
Cdd:PHA03307   138 LRPVGSPGPPPAASPPAAGASpaavasdaassrqaalplsSPEETARAPS-SPPAEPPPSTPPAAASPRPPRRSSPISAS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  857 SGEESGAPDVSGDFTGSGDVSGHLDFSGQLSGDRASGLPSGDLDSSGLTSTV---GSG--------LPVESGLPSGDEER 925
Cdd:PHA03307   217 ASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRiweASGwngpssrpGPASSSSSPRERSP 296

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1375383923  926 IEWPSTPTVGELPSGAEILE--GSASGVGDLSGLPSGEVLETSASGVGDLSG 975
Cdd:PHA03307   297 SPSPSSPGSGPAPSSPRASSssSSSRESSSSSTSSSSESSRGAAVSPGPSPS 348
TamB super family cl34519
Autotransporter translocation and assembly protein TamB [Intracellular trafficking, secretion, ...
 1511-2016 3.44e-03

Autotransporter translocation and assembly protein TamB [Intracellular trafficking, secretion, and vesicular transport];


The actual alignment was detected with superfamily member COG2911:

Pssm-ID: 442155 [Multi-domain]  Cd Length: 766  Bit Score: 42.72  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1511 SGEGLETSASGVEDLsRLPSGEEVLEISasgfGDLSGLPSGGEgLETSASEVGtDLSGLPSGREGlETSASGAEDLSGLP 1590
Cdd:COG2911     77 DAEGLDLASSALDDL-DLRSGGNRLTLS----GNLSAASLDGD-LDLDAPDLA-DLAALLPGLAG-SLSGDGLDSLSLDA 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1591 SGKEdlvgsASGDLDLGKlpSGTLGSGQAPETSGLPSGFSGEYSGVDLGSGPPSGLPDFSGLPSGFPTVSLVDSTLvevv 1670
Cdd:COG2911    149 DGTL-----AQHRLDLDA--KGEPASLSLALSGGLDRDDGGTLSRLDFLNTGRWGLAAPATLSYDDGRVTLGPLCL---- 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1671 taSTASELEGRGTIG--ISGAGEISGLPSSELdisgrASGLPSGTELSGQASGSPDVSG-----------EIPGLFGVSG 1737
Cdd:COG2911    218 --AGGGSLCLSGTLGgtLDLQLRLKNLPLALL-----NPFLPDDLGLSGTLNGDADLSGglanpqgdaslSLSGDLTLND 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1738 QPSGFPDTSGETSGVTELSG--------LSSGQPGiSGEASGVLYGTSQPFGITDLSGE-TSGVPDLSgqpsglpGFSGA 1808
Cdd:COG2911    291 GLGGLPLGLGDLTLNARLANgrltldltLDGGGLG-TLSLSGSVPLADGLPPSAPLDGNlRLDNLDLA-------LLNPL 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1809 TSGVPDLVSGTTSGSGESSG----------ITFVDTSL-VEVAPTTFKEEEGL-----GSVELSGL----PSGEADLSGK 1868
Cdd:COG2911    363 LPGVLERLSGQLNGDLRLSGtlaapqlngqLTLDDGRLkLPALGVRLTDINLRlrfdgDRLTLDGLtadsGGGTLTLSGT 442

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1869 SGMVDVSGQFSGTVDSSGFT-SQTPEFSGLPSGIAEVSGESSRAEIGSSL--PSGAYYGSGTPSSFPTVS----LVDRTL 1941
Cdd:COG2911    443 VDLDGLSWPADLTLKGDNLRvLNPPDYTATVSGDLTLTGTPDGPTLSGNVtvPRARITLPELPPSAVSLSddvvVVNRPP 522

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1942 VESVTQAPTAQ--------EAGE-----GP------SGILELSGAHSGAPDMSGE---HSGFLDLSG----LQSGLIEPS 1995
Cdd:COG2911    523 EPVPEEEAAGLpldldlnvNLGDdvrvrGFgldarlGGDLRLTGTPGGAPRLTGEinlVRGRYNAYGqrltIERGSITFN 602

                          570       580
                   ....*....|....*....|.
gi 1375383923 1996 GEPPgTPYFsgDFASTTNVSG 2016
Cdd:COG2911    603 GPPL-DPYL--DIEAVRTVDD 620
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 2320-2443 3.18e-97

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: 308.74  E-value: 3.18e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPMQFE 2399
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1375383923 2400 NWRPNQPDNFFAAGEDCVVMIWHEKGEWNDVPCNYHLPFTCKKG 2443
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 33-155 1.03e-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: 235.60  E-value: 1.03e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   33 IPQPSPLRVLLGTSLTIPCYFIDPMHPVTTAPSTAPLAPRIKWSRVSKEKEVVLLVATEGRVRVNSAYQDKVSLPNYPAI 112
Cdd:cd05900      1 IPLESPLRVVLGSSLLIPCYFQDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1375383923  113 PSDATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVF 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 2.19e-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: 204.95  E-value: 2.19e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  153 IVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRT 232
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1375383923  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 1.21e-60

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239597  Cd Length: 96  Bit Score: 202.93  E-value: 1.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  254 EVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYVHAN 333
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1375383923  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 ...
 579-674 3.70e-59

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239597  Cd Length: 96  Bit Score: 198.69  E-value: 3.70e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  579 EVFFATRLEQFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTVYLYPN 658
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1375383923  659 QTGLPDPLSRHHAFCF 674
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 ...
 478-572 4.37e-53

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239594  Cd Length: 95  Bit Score: 181.07  E-value: 4.37e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  478 VVFHYRPGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKDSSPGVRT 557
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1375383923  558 YGVRPSTETYDVYCF 572
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
Xlink pfam00193
Extracellular link domain;
478-572 1.48e-45

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 159.66  E-value: 1.48e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  478 VVFHYRpGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKdssPGVRT 557
Cdd:pfam00193    1 GVFHLE-SPGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 1375383923  558 YGVRPST-ETYDVYCF 572
Cdd:pfam00193   77 YGFRDPLsERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
151-248 6.86e-45

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 157.89  E-value: 6.86e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   151 KGIVFHYRAIsTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGdkdEFPGV 230
Cdd:smart00445    1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                            90
                    ....*....|....*...
gi 1375383923   231 RTYGIRDTNETYDVYCFA 248
Cdd:smart00445   77 RQYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
154-247 7.11e-45

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 157.73  E-value: 7.11e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  154 VFHYRAiSTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:pfam00193    2 VFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQY 77

                           90
                   ....*....|....*
gi 1375383923  234 GIRD-TNETYDVYCF 247
Cdd:pfam00193   78 GFRDpLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
252-350 6.40e-44

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 155.19  E-value: 6.40e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   252 EGEVFYATS--PEKFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRtvy 329
Cdd:smart00445    1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 1375383923   330 vhanQTGYPDPSSRYDAICYT 350
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
577-675 1.84e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.96  E-value: 1.84e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   577 EGEVFF--ATRLEQFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRtvy 654
Cdd:smart00445    1 DGGVFHveKNGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 1375383923   655 lypnQTGLPDPLSRHHAFCFR 675
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
254-349 2.59e-42

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 150.42  E-value: 2.59e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  254 EVFYATSPE--KFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRtvyvh 331
Cdd:pfam00193    1 GVFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 1375383923  332 anQTGYPDP-SSRYDAICY 349
Cdd:pfam00193   76 --QYGFRDPlSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
477-572 3.45e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.19  E-value: 3.45e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   477 GVVFHYRPGpTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKdssPGVR 556
Cdd:smart00445    2 GGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNL---PGVR 77

                            90
                    ....*....|....*.
gi 1375383923   557 TYGVRPSTETYDVYCF 572
Cdd:smart00445   78 QYGFPDPTSRYDAYCF 93
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2320-2441 2.41e-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: 146.21  E-value: 2.41e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFV-----NNNAQDYQWIGLNDRTIEGDFRWSDGH 2394
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllkNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1375383923  2395 PM-QFENWRPNQPDNffaAGEDCVVMiWHEKGEWNDVPCNYHLPFTCK 2441
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVL-STSGGKWNDVSCTSKLPFVCE 124
Xlink pfam00193
Extracellular link domain;
579-674 1.07e-37

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 137.32  E-value: 1.07e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  579 EVFFATRLEQ--FTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRtvyly 656
Cdd:pfam00193    1 GVFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 1375383923  657 pnQTGLPDPLS-RHHAFCF 674
Cdd:pfam00193   76 --QYGFRDPLSeRYDAYCY 92
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 2338-2442 1.68e-26

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 105.64  E-value: 1.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2338 RETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSDGHPMQFENWRPNQPDNffAAGE 2414
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNkyfWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENE 78

                           90       100
                   ....*....|....*....|....*...
gi 1375383923 2415 DCVVMIWhEKGEWNDVPCNYHLPFTCKK 2442
Cdd:pfam00059   79 DCVELSS-SSGKWNDENCNSKNPFVCEK 105
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 2447-2503 2.01e-11

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: 60.94  E-value: 2.01e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1375383923 2447 CGEPPVVEHARTFGqKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGHWEEPQITC 2503
Cdd:cd00033      1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
2447-2503 2.91e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.81  E-value: 2.91e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1375383923 2447 CGEPPVVEHARtFGQKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGHWEEPQITC 2503
Cdd:pfam00084    1 CPPPPDIPNGK-VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 2447-2503 8.38e-09

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: 53.68  E-value: 8.38e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1375383923  2447 CGEPPVVEHARTFGqKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGHWEEPQITC 2503
Cdd:smart00032    1 CPPPPDIENGTVTS-SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 35-150 5.72e-08

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: 52.85  E-value: 5.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   35 QPSPLRVLLGTSLTIPCYFidpmhpvttAPSTAPLAPRIKWSRVSKEKEVVLLVATEGRVRVNSAYQDKVSLPNYPaIPS 114
Cdd:pfam07686    2 TPREVTVALGGSVTLPCTY---------SSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGRFSGRGDP-SNG 71

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1375383923  115 DATLEVQSLRSNDSGVYRCEV-MHGIEDSEATLEVVV 150
Cdd:pfam07686   72 DGSLTIQNLTLSDSGTYTCAViPSGEGVFGKGTRLTV 108
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2283-2313 1.19e-06

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.86  E-value: 1.19e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1375383923 2283 CAEE-PCGA-GTCKETEGHVICLCPPGYTGEHC 2313
Cdd:cd00054      5 CASGnPCQNgGTCVNTVGSYRCSCPPGYTGRNC 37
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2283-2312 1.64e-06

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 46.61  E-value: 1.64e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1375383923 2283 CAEEPC-GAGTCKETEGHVICLCPPGYTGEH 2312
Cdd:pfam00008    1 CAPNPCsNGGTCVDTPGGYTCICPEGYTGKR 31
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 36-150 2.03e-06

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: 47.89  E-value: 2.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923    36 PSPLRVLLGTSLTIPCyfidpmhPVTTAPStaplaPRIKWSRVSKEkevvlLVATEGRVRVNSAyqdkvslpnypaiPSD 115
Cdd:smart00410    1 PPSVTVKEGESVTLSC-------EASGSPP-----PEVTWYKQGGK-----LLAESGRFSVSRS-------------GST 50

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1375383923   116 ATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVV 150
Cdd:smart00410   51 STLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
EGF smart00181
Epidermal growth factor-like domain;
2283-2313 5.39e-05

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 42.12  E-value: 5.39e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1375383923  2283 CAEE-PCGAGTCKETEGHVICLCPPGYTG-EHC 2313
Cdd:smart00181    2 CASGgPCSNGTCINTPGSYTCSCPPGYTGdKRC 34
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 2312-2441 7.35e-04

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: 45.46  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2312 HCNIDQEVCEEgwnkyQGHCYRHFPDRETWVDAERRCREQ-QSHLSSIVTPEEQEF----VNNNAQDYQWIGLND-RTIE 2385
Cdd:TIGR00864  317 HCPKDGEIFEE-----NGHCFQIVPEEAAWLDAQEQCLARaGAALAIVDNDALQNFlarkVTHSLDRGVWIGFSDvNGAE 391

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1375383923 2386 -GDFRWSDGHPMQ-FENWRPNQPDnfFAAGEDCVVMiwHEKGEWNDVPCNYHLPFTCK 2441
Cdd:TIGR00864  392 kGPAHQGEAFEAEeCEEGLAGEPH--PARAEHCVRL--DPRGQCNSDLCNAPHAYVCE 445
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
1433-1614 1.04e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 44.38  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1433 PSGEVLETTAPGVEEISGLPSGeVLETS--TSAVGDLSGLPSGGEVLEISVSGVEDISGLPSG-EVVETSASGIEDVSEL 1509
Cdd:PRK15387   242 PELRTLEVSGNQLTSLPVLPPG-LLELSifSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGlQELSVSDNQLASLPAL 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1510 PSGE-GLETSASGVEDLSRLPSGEEVLEISASGFGDLSGLPSGGEGLETSASEVgTDLSGLPSGREGLETSASGAEDLSG 1588
Cdd:PRK15387   321 PSELcKLWAYNNQLTSLPTLPSGLQELSVSDNQLASLPTLPSELYKLWAYNNRL-TSLPALPSGLKELIVSGNRLTSLPV 399

                          170       180
                   ....*....|....*....|....*.
gi 1375383923 1589 LPSGKEDLVGSASGDLDLGKLPSGTL 1614
Cdd:PRK15387   400 LPSELKELMVSGNRLTSLPMLPSGLL 425
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 716-975 2.82e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  716 EETTAVPSGETTAilEFTTEPENQTEWEPAYTPVGTSPLPGilPTWPPTGAATEESTEGPSATEVPSASEEPSPSEVPFP 795
Cdd:PHA03307    62 CDRFEPPTGPPPG--PGTEAPANESRSTPTWSLSTLAPASP--AREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEM 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  796 SEEPSPSEEPFPSVRPFPSVE-------------------LFPSEEPFPSkEPSPSEEPSASEEPYTPSPPVPSWTELPS 856
Cdd:PHA03307   138 LRPVGSPGPPPAASPPAAGASpaavasdaassrqaalplsSPEETARAPS-SPPAEPPPSTPPAAASPRPPRRSSPISAS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  857 SGEESGAPDVSGDFTGSGDVSGHLDFSGQLSGDRASGLPSGDLDSSGLTSTV---GSG--------LPVESGLPSGDEER 925
Cdd:PHA03307   217 ASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRiweASGwngpssrpGPASSSSSPRERSP 296

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1375383923  926 IEWPSTPTVGELPSGAEILE--GSASGVGDLSGLPSGEVLETSASGVGDLSG 975
Cdd:PHA03307   297 SPSPSSPGSGPAPSSPRASSssSSSRESSSSSTSSSSESSRGAAVSPGPSPS 348
TamB COG2911
Autotransporter translocation and assembly protein TamB [Intracellular trafficking, secretion, ...
 1511-2016 3.44e-03

Autotransporter translocation and assembly protein TamB [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442155 [Multi-domain]  Cd Length: 766  Bit Score: 42.72  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1511 SGEGLETSASGVEDLsRLPSGEEVLEISasgfGDLSGLPSGGEgLETSASEVGtDLSGLPSGREGlETSASGAEDLSGLP 1590
Cdd:COG2911     77 DAEGLDLASSALDDL-DLRSGGNRLTLS----GNLSAASLDGD-LDLDAPDLA-DLAALLPGLAG-SLSGDGLDSLSLDA 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1591 SGKEdlvgsASGDLDLGKlpSGTLGSGQAPETSGLPSGFSGEYSGVDLGSGPPSGLPDFSGLPSGFPTVSLVDSTLvevv 1670
Cdd:COG2911    149 DGTL-----AQHRLDLDA--KGEPASLSLALSGGLDRDDGGTLSRLDFLNTGRWGLAAPATLSYDDGRVTLGPLCL---- 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1671 taSTASELEGRGTIG--ISGAGEISGLPSSELdisgrASGLPSGTELSGQASGSPDVSG-----------EIPGLFGVSG 1737
Cdd:COG2911    218 --AGGGSLCLSGTLGgtLDLQLRLKNLPLALL-----NPFLPDDLGLSGTLNGDADLSGglanpqgdaslSLSGDLTLND 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1738 QPSGFPDTSGETSGVTELSG--------LSSGQPGiSGEASGVLYGTSQPFGITDLSGE-TSGVPDLSgqpsglpGFSGA 1808
Cdd:COG2911    291 GLGGLPLGLGDLTLNARLANgrltldltLDGGGLG-TLSLSGSVPLADGLPPSAPLDGNlRLDNLDLA-------LLNPL 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1809 TSGVPDLVSGTTSGSGESSG----------ITFVDTSL-VEVAPTTFKEEEGL-----GSVELSGL----PSGEADLSGK 1868
Cdd:COG2911    363 LPGVLERLSGQLNGDLRLSGtlaapqlngqLTLDDGRLkLPALGVRLTDINLRlrfdgDRLTLDGLtadsGGGTLTLSGT 442

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1869 SGMVDVSGQFSGTVDSSGFT-SQTPEFSGLPSGIAEVSGESSRAEIGSSL--PSGAYYGSGTPSSFPTVS----LVDRTL 1941
Cdd:COG2911    443 VDLDGLSWPADLTLKGDNLRvLNPPDYTATVSGDLTLTGTPDGPTLSGNVtvPRARITLPELPPSAVSLSddvvVVNRPP 522

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1942 VESVTQAPTAQ--------EAGE-----GP------SGILELSGAHSGAPDMSGE---HSGFLDLSG----LQSGLIEPS 1995
Cdd:COG2911    523 EPVPEEEAAGLpldldlnvNLGDdvrvrGFgldarlGGDLRLTGTPGGAPRLTGEinlVRGRYNAYGqrltIERGSITFN 602

                          570       580
                   ....*....|....*....|.
gi 1375383923 1996 GEPPgTPYFsgDFASTTNVSG 2016
Cdd:COG2911    603 GPPL-DPYL--DIEAVRTVDD 620
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 2320-2392 6.10e-03

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 40.48  E-value: 6.10e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVN--NNAQDYqWIGLNDRTIEGDFRWSD 2392
Cdd:PHA02642    88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKryKDSSDH-WIGLNRESSNHPWKWAD 161
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 2320-2443 3.18e-97

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: 308.74  E-value: 3.18e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPMQFE 2399
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1375383923 2400 NWRPNQPDNFFAAGEDCVVMIWHEKGEWNDVPCNYHLPFTCKKG 2443
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 33-155 1.03e-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: 235.60  E-value: 1.03e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   33 IPQPSPLRVLLGTSLTIPCYFIDPMHPVTTAPSTAPLAPRIKWSRVSKEKEVVLLVATEGRVRVNSAYQDKVSLPNYPAI 112
Cdd:cd05900      1 IPLESPLRVVLGSSLLIPCYFQDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1375383923  113 PSDATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVF 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 2.19e-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: 204.95  E-value: 2.19e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  153 IVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRT 232
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1375383923  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 1.21e-60

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239597  Cd Length: 96  Bit Score: 202.93  E-value: 1.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  254 EVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYVHAN 333
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1375383923  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 2.38e-60

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: 203.23  E-value: 2.38e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   33 IPQPSPLRVLLGTSLTIPCYFIDPMHPVTtaPSTAPLAPRIKWSRVS----KEKEVVLLVATEGRVRVNSAYQDKVSLPN 108
Cdd:cd05878      1 IPQSSPVRVLLGTSVTLPCYFIDPPHPVT--PSTAPLAPRIKWSKVSvdgkKEKEVVLLVATEGRVRVNSAYQGRVSLPN 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1375383923  109 YPAIPSDATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVF 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 ...
 579-674 3.70e-59

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239597  Cd Length: 96  Bit Score: 198.69  E-value: 3.70e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  579 EVFFATRLEQFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTVYLYPN 658
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1375383923  659 QTGLPDPLSRHHAFCF 674
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 ...
 478-572 4.37e-53

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239594  Cd Length: 95  Bit Score: 181.07  E-value: 4.37e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  478 VVFHYRPGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKDSSPGVRT 557
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1375383923  558 YGVRPSTETYDVYCF 572
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
Xlink pfam00193
Extracellular link domain;
478-572 1.48e-45

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 159.66  E-value: 1.48e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  478 VVFHYRpGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKdssPGVRT 557
Cdd:pfam00193    1 GVFHLE-SPGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 1375383923  558 YGVRPST-ETYDVYCF 572
Cdd:pfam00193   77 YGFRDPLsERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
151-248 6.86e-45

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 157.89  E-value: 6.86e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   151 KGIVFHYRAIsTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGdkdEFPGV 230
Cdd:smart00445    1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                            90
                    ....*....|....*...
gi 1375383923   231 RTYGIRDTNETYDVYCFA 248
Cdd:smart00445   77 RQYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
154-247 7.11e-45

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 157.73  E-value: 7.11e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  154 VFHYRAiSTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:pfam00193    2 VFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQY 77

                           90
                   ....*....|....*
gi 1375383923  234 GIRD-TNETYDVYCF 247
Cdd:pfam00193   78 GFRDpLSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
252-350 6.40e-44

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 155.19  E-value: 6.40e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   252 EGEVFYATS--PEKFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRtvy 329
Cdd:smart00445    1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 1375383923   330 vhanQTGYPDPSSRYDAICYT 350
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
577-675 1.84e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.96  E-value: 1.84e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   577 EGEVFF--ATRLEQFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRtvy 654
Cdd:smart00445    1 DGGVFHveKNGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 1375383923   655 lypnQTGLPDPLSRHHAFCFR 675
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
254-349 2.59e-42

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 150.42  E-value: 2.59e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  254 EVFYATSPE--KFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRtvyvh 331
Cdd:pfam00193    1 GVFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 1375383923  332 anQTGYPDP-SSRYDAICY 349
Cdd:pfam00193   76 --QYGFRDPlSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
477-572 3.45e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.19  E-value: 3.45e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   477 GVVFHYRPGpTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKdssPGVR 556
Cdd:smart00445    2 GGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNL---PGVR 77

                            90
                    ....*....|....*.
gi 1375383923   557 TYGVRPSTETYDVYCF 572
Cdd:smart00445   78 QYGFPDPTSRYDAYCF 93
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 2320-2441 5.27e-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: 148.27  E-value: 5.27e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCRE-----QQSHLSSIVTPEEQEFV-------NNNAQDYQ-WIGLNDRTIEG 2386
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVydlfessRGPDTPYGlWIGLHDRTSEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1375383923 2387 DFRWSDGHPMQFENWRPNQPDNFFaAGEDCVVMiWHEK---GEWNDVPCNYHLPFTCK 2441
Cdd:cd03589     81 PFEWTDGSPVDFTKWAGGQPDNYG-GNEDCVQM-WRRGdagQSWNDMPCDAVFPYICK 136
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 2320-2441 2.41e-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: 146.21  E-value: 2.41e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFV-----NNNAQDYQWIGLNDRTIEGDFRWSDGH 2394
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllkNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1375383923  2395 PM-QFENWRPNQPDNffaAGEDCVVMiWHEKGEWNDVPCNYHLPFTCK 2441
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVL-STSGGKWNDVSCTSKLPFVCE 124
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 2320-2442 8.08e-40

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: 144.37  E-value: 8.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVN--NNAQDYQWIGLNDRTIEGDFRWSDGHPMQ 2397
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISkiLSGNRSYWIGLSDEETEGEWKWVDGTPLN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1375383923 2398 --FENWRPNQPDNFFAAGEDCVVmIWHEKGEWNDVPCNYHLPFTCKK 2442
Cdd:cd03590     81 ssKTFWHPGEPNNWGGGGEDCAE-LVYDSGGWNDVPCNLEYRWICEK 126
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 254-349 5.63e-39

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: 141.02  E-value: 5.63e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  254 EVFYATS---PEKFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYV 330
Cdd:cd01102      1 VVFHLESqngRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSYGN 80

                           90
                   ....*....|....*....
gi 1375383923  331 hanqtgyPDPSSRYDAICY 349
Cdd:cd01102     81 -------PAPSGRYDAYCF 92
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 2330-2442 2.24e-38

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: 140.06  E-value: 2.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2330 HCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQ----WIGLNDRTIEGDFRWSDGHP-MQFENWRPN 2404
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssdvWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1375383923 2405 QPDNffAAGEDCVVMIWHEKGEWNDVPCNYHLPFTCKK 2442
Cdd:cd00037     81 EPNP--GGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
Xlink pfam00193
Extracellular link domain;
579-674 1.07e-37

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 137.32  E-value: 1.07e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  579 EVFFATRLEQ--FTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRtvyly 656
Cdd:pfam00193    1 GVFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR----- 75

                           90
                   ....*....|....*....
gi 1375383923  657 pnQTGLPDPLS-RHHAFCF 674
Cdd:pfam00193   76 --QYGFRDPLSeRYDAYCY 92
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 154-247 9.00e-35

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


Pssm-ID: 238534  Cd Length: 92  Bit Score: 128.69  E-value: 9.00e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  154 VFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:cd01102      2 VFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN---PGVRSY 78

                           90
                   ....*....|....
gi 1375383923  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 ...
 478-572 3.37e-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: 3.37e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  478 VVFHYRPGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKdssPGVRT 557
Cdd:cd01102      1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN---PGVRS 77

                           90
                   ....*....|....*
gi 1375383923  558 YGVRPSTETYDVYCF 572
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 ...
 478-572 3.82e-34

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: 127.16  E-value: 3.82e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  478 VVFHYRPGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCvGDKDSSPGVRT 557
Cdd:cd03518      1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPC-GGKRTVPGLRS 79

                           90
                   ....*....|....*.
gi 1375383923  558 YGVR-PSTETYDVYCF 572
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 5.57e-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: 120.99  E-value: 5.57e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  153 IVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCyGDKDEFPGVRT 232
Cdd:cd03518      1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPC-GGKRTVPGLRS 79

                           90
                   ....*....|....*.
gi 1375383923  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 ...
 579-674 1.79e-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: 116.75  E-value: 1.79e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  579 EVFFATR---LEQFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTVyl 655
Cdd:cd01102      1 VVFHLESqngRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSY-- 78

                           90
                   ....*....|....*....
gi 1375383923  656 ypnqtGLPDPLSRHHAFCF 674
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 ...
 254-349 2.87e-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: 110.21  E-value: 2.87e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  254 EVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQ-AGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVyvha 332
Cdd:cd03519      1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF---- 76

                           90
                   ....*....|....*...
gi 1375383923  333 nqtGYPDPSSR-YDAICY 349
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 ...
 579-674 4.19e-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: 4.19e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  579 EVFFATRLEQFTFQEALEFCESHNATLATTGQLYAAWS-RGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTVylyp 657
Cdd:cd03519      1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF---- 76

                           90
                   ....*....|....*...
gi 1375383923  658 nqtGLPDPLSRHH-AFCF 674
Cdd:cd03519     77 ---GFPDKKHKLYgVYCY 91
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 38-155 1.80e-27

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: 109.15  E-value: 1.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   38 PLRVLLGTSLTIPCYFIdpMHPvttAPSTAPLAPRIKWSRVSK---EKEVVLLVATEGRVRVNSAYQDKVSLPNYPAIPS 114
Cdd:cd05902      6 PVRRPLSSSVLLPCVFT--LPP---SASSPPEGPRIKWTKLSTsggQQQRPVLVARDNVVRVAKAFQGRVSLPGYPKNRY 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1375383923  115 DATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVF 155
Cdd:cd05902     81 NASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 588-674 3.49e-27

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: 107.13  E-value: 3.49e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  588 QFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDK--PGVRTVylypnqtGLPDP 665
Cdd:cd03518     13 NLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRtvPGLRSY-------GERDK 85

                           90
                   ....*....|
gi 1375383923  666 -LSRHHAFCF 674
Cdd:cd03518     86 mLSRYDAFCF 95
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 2338-2442 1.68e-26

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 105.64  E-value: 1.68e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2338 RETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSDGHPMQFENWRPNQPDNffAAGE 2414
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNkyfWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENE 78

                           90       100
                   ....*....|....*....|....*...
gi 1375383923 2415 DCVVMIWhEKGEWNDVPCNYHLPFTCKK 2442
Cdd:pfam00059   79 DCVELSS-SSGKWNDENCNSKNPFVCEK 105
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 38-155 1.50e-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: 100.75  E-value: 1.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   38 PLRVLLGTSLTIPCYF-IDPmhpvtTAPSTAPLAPRIKWSRVSKE----KEVVLLVATEGRVRVNSAYQDKVSLPNYPAI 112
Cdd:cd05714      6 KVFSHLGGNVTLPCKFyRDP-----TAFGSGIHKIRIKWTKLTSDsgylKEVDVLVAMGNVVYHKKTYGGRVSVPLKPGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1375383923  113 PSDATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVF 155
Cdd:cd05714     81 DSDASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 2320-2441 3.15e-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: 100.14  E-value: 3.15e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCRE--QQSHLSSIVTPEEQ----EFVNN--NAQDYQWIGLNDRTIEGDFRWS 2391
Cdd:cd03594      1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAaaiaSLISSyqKAYQPVWIGLHDPQQSRGWEWS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1375383923 2392 DGHPMQFENWRPNQPdnfFAAGEDCVVMiWHEKG--EWNDVPCNYHLPFTCK 2441
Cdd:cd03594     81 DGSKLDYRSWDRNPP---YARGGYCAEL-SRSTGflKWNDANCEERNPFICK 128
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 5.38e-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: 95.19  E-value: 5.38e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  263 KFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLL--GVRTVyvhanqtGYPDP 340
Cdd:cd03518     13 NLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTvpGLRSY-------GERDK 85

                           90
                   ....*....|
gi 1375383923  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 ...
 477-572 2.70e-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: 2.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  477 GVVFHYRPGPtrysLTFEEAQQACLRTGAVIASPEQLQAAYE-AGYEQCDAGWLRDQTVRYPIVSPRTPCVGdkdSSPGV 555
Cdd:cd03519      1 GVFYLLHPGK----LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGP---LEPGV 73

                           90
                   ....*....|....*...
gi 1375383923  556 RTYGV-RPSTETYDVYCF 572
Cdd:cd03519     74 RSFGFpDKKHKLYGVYCY 91
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 37-155 9.53e-22

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: 93.10  E-value: 9.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   37 SPLRVLLGTSLTIPCYFID-PMHPVTTAPSTAPLapRIKWSRVSKE------KEVVLLVATEGRVRVNSAYQDKVSLPNY 109
Cdd:cd05901      5 SRVHGSLSGSVVLPCRFSTlPTLPPSYNITSEFL--RIKWTKIQVDkngkdhKETTVLVAQNGIIKIGQEYMGRVSVPSH 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1375383923  110 PAIPSDATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVF 155
Cdd:cd05901     83 PEDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 2338-2440 2.22e-21

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: 91.59  E-value: 2.22e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2338 RETWVDAERRCREQQSHLSSIVTPEE----QEFVNNnAQDYQWIGLNDRTIEGDFRWSDGHPMQFENWRPNQPDNfFAAG 2413
Cdd:cd03591     10 EKNFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVKK-GNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNN-AGGG 87

                           90       100
                   ....*....|....*....|....*..
gi 1375383923 2414 EDCVVMIwhEKGEWNDVPCNYHLPFTC 2440
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 ...
 479-572 7.71e-20

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


Pssm-ID: 239592  Cd Length: 93  Bit Score: 86.36  E-value: 7.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  479 VFHYRPGPTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCvgdKDSSPGVRTY 558
Cdd:cd03515      2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANC---GFGHVGIVDY 78

                           90
                   ....*....|....*
gi 1375383923  559 GVRP-STETYDVYCF 572
Cdd:cd03515     79 GPRLnLSERWDAYCY 93
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 2330-2434 1.18e-19

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: 86.71  E-value: 1.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2330 HCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQ--WIGLNDRTIEGDFRWSDGHPMQFENWRPNQPD 2407
Cdd:cd03603      1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGasWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80

                           90       100
                   ....*....|....*....|....*....
gi 1375383923 2408 NFFAAGEDCVVM--IWHEKGEWNDVPCNY 2434
Cdd:cd03603     81 NNGGGNEDYAAInhFPGISGKWNDLANSY 109
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 255-349 1.30e-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: 85.59  E-value: 1.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  255 VFYATSPE---KFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYVH 331
Cdd:cd03515      2 VFHLRSRSgkyKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGIVDYGPR 81

                           90
                   ....*....|....*...
gi 1375383923  332 ANQtgypdpSSRYDAICY 349
Cdd:cd03515     82 LNL------SERWDAYCY 93
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 2340-2434 2.89e-19

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: 85.50  E-value: 2.89e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2340 TWVDAERRCREQQSHLSSIVTPEEQEFVNNNA----QDYQWIGLNDRTIEGdfRW--SDGHPMQFENWRPNQPDNffAAG 2413
Cdd:cd03592     11 TFNEAVKYCKSRGTDLVAIQNAEENALLNGFAlkynLGYYWIDGNDINNEG--TWvdTDKKELEYKNWAPGEPNN--GRN 86

                           90       100
                   ....*....|....*....|.
gi 1375383923 2414 EDCVVMIWHEKGEWNDVPCNY 2434
Cdd:cd03592     87 ENCLEIYIKDNGKWNDEPCSK 107
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 154-247 2.01e-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: 82.13  E-value: 2.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  154 VFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:cd03515      2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGH---VGIVDY 78

                           90
                   ....*....|....*
gi 1375383923  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 6.84e-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: 80.54  E-value: 6.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  166 LDFDRAQRACLQNSAIIATPEQLQAAYE-DGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTYGIRD-TNETYD 243
Cdd:cd03519     11 LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLE---PGVRSFGFPDkKHKLYG 87


                   ....
gi 1375383923  244 VYCF 247
Cdd:cd03519     88 VYCY 91
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 44-155 6.17e-16

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: 75.82  E-value: 6.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   44 GTSLTIPC-YFIDPmhpvttaPSTAPLAPRIKWSRVSK--EKEVVLLVATEGRVRVNSAYQDKVSLPNypAIPSDATLEV 120
Cdd:cd05877     12 GGNVTLPCrYHYEP-------ELSAPRKIRVKWTKLEVdyAKEEDVLVAIGTRHKSYGSYQGRVFLRR--ADDLDASLVI 82

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1375383923  121 QSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVF 155
Cdd:cd05877     83 TDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 2320-2442 1.72e-14

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 71.98  E-value: 1.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFV-NNNAQDYQWIGLNDRTIEGDFRWSDGHPmqF 2398
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLqSQIGSSSYWIGLSREKSEKPWKWIDGSP--L 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1375383923 2399 ENWRPNQPDNffaAGEDCVVMiwhEKGEWNDVPCNYHLPFTCKK 2442
Cdd:cd03593     79 NNLFNIRGST---KSGNCAYL---SSTGIYSEDCSTKKRWICEK 116
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 ...
 588-674 8.78e-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: 66.33  E-value: 8.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  588 QFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTVYLYPNQTGLPDpls 667
Cdd:cd03515     13 KLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGIVDYGPRLNLSERWD--- 89


                   ....*..
gi 1375383923  668 rhhAFCF 674
Cdd:cd03515     90 ---AYCY 93
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 2340-2440 1.72e-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: 1.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2340 TWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQ---DYQWIGLNDRTIEgdFRWSDGHPMQFENWRPNQPDNffaaGEDC 2416
Cdd:cd03602     11 TWSEAQQYCRENYTDLATVQNQEDNALLSNLSRvsnSAAWIGLYRDVDS--WRWSDGSESSFRNWNTFQPFG----QGDC 84

                           90       100
                   ....*....|....*....|....*
gi 1375383923 2417 VVM-IWhekGEWNDVPCNYHLPFTC 2440
Cdd:cd03602     85 ATMySS---GRWYAALCSALKPFIC 106
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 2317-2441 6.09e-12

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: 65.68  E-value: 6.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2317 QEVCEEGWNKyqgHCYR--HFPD---RETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQ------WIGL------ 2379
Cdd:cd03595      1 QRICRRGTEK---PCYKiaYFQDsrrRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRasdgdfWIGLrrssqy 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375383923 2380 --NDRTIEGDFRWSDGHPMQFENWRPNQPDnffAAGEDCVVMiWHE-------KG----EWNDVPCNYHLPFTCK 2441
Cdd:cd03595     78 nvTSSACSSLYYWLDGSISTFRNWYVDEPS---CGSEVCVVM-YHQpsapagqGGpylfQWNDDNCNMKNNFICK 148
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 2329-2440 6.83e-12

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: 64.39  E-value: 6.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2329 GHCYRHFPDRETWVDAERRCRE-QQSHLSSI----VTPEEQEFVNNNAQDYQWIG--LNDRTIEGDFRWSDGHPMQFENW 2401
Cdd:cd03598      1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIhsfaFNYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1375383923 2402 RPNQPDNffaAGEDCVVMIWHEkGEWNDVPCNYHLPFTC 2440
Cdd:cd03598     81 APGQPGN---RRGHCVELCTRG-GHWRRAHCKLRRPFIC 115
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 2326-2440 1.02e-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: 64.33  E-value: 1.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2326 KYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQE--------FVNNNAQdyQWIGLNDRTIEGDFRWSDGHPMQ 2397
Cdd:cd03596      6 KIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDalrdyvkaSVPGNWE--VWLGINDMVAEGKWVDVNGSPIS 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1375383923 2398 FENWR---PNQPDNffAAGEDCVVMIWHEKGEWNDVPCNYHLPFTC 2440
Cdd:cd03596     84 YFNWEreiTAQPDG--GKRENCVALSSSAQGKWFDEDCRREKPYVC 127
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 2447-2503 2.01e-11

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: 60.94  E-value: 2.01e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1375383923 2447 CGEPPVVEHARTFGqKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGHWEEPQITC 2503
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 ...
 479-572 8.84e-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: 59.40  E-value: 8.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  479 VFHYRPGpTRYSLTFEEAQQACLRTGAVIASPEQLQAAYEAGYEQCDAGWLRDQTVRYPIVSPRTPCVGDKdssPGVRTY 558
Cdd:cd03516      8 VFLVEKN-GRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNG---TGVYIL 83

                           90
                   ....*....|....
gi 1375383923  559 GVrPSTETYDVYCF 572
Cdd:cd03516     84 NS-NLSSRYDAYCY 96
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 2376-2442 1.40e-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: 57.93  E-value: 1.40e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2376 WIGLND-RTIEGDFRWSDGH--PMQFENWRPNQPDNFfAAGEDCVvMIWHEKGEWNDVPCNYHLPFTCKK 2442
Cdd:cd03601     52 WVGADNlQDGEYDFLWNDGVslPTDSDLWAPNEPSNP-QSRQLCV-QLWSKYNLLDDEYCGRAKRVICEK 119
Sushi pfam00084
Sushi repeat (SCR repeat);
2447-2503 2.91e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 54.81  E-value: 2.91e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1375383923 2447 CGEPPVVEHARtFGQKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGHWEEPQITC 2503
Cdd:pfam00084    1 CPPPPDIPNGK-VSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 2447-2503 8.38e-09

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: 53.68  E-value: 8.38e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1375383923  2447 CGEPPVVEHARTFGqKKDRYEINSLVRYQCTEGFVQRHMPTIRCQPSGHWEEPQITC 2503
Cdd:smart00032    1 CPPPPDIENGTVTS-SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 35-150 5.72e-08

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: 52.85  E-value: 5.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   35 QPSPLRVLLGTSLTIPCYFidpmhpvttAPSTAPLAPRIKWSRVSKEKEVVLLVATEGRVRVNSAYQDKVSLPNYPaIPS 114
Cdd:pfam07686    2 TPREVTVALGGSVTLPCTY---------SSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGRFSGRGDP-SNG 71

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1375383923  115 DATLEVQSLRSNDSGVYRCEV-MHGIEDSEATLEVVV 150
Cdd:pfam07686   72 DGSLTIQNLTLSDSGTYTCAViPSGEGVFGKGTRLTV 108
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 264-353 1.05e-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: 53.23  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  264 FTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGvrtVYVHANQTgypdpSSR 343
Cdd:cd03516     19 LNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGTG---VYILNSNL-----SSR 90

                           90
                   ....*....|
gi 1375383923  344 YDAICYTGED 353
Cdd:cd03516     91 YDAYCYNSSD 100
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 2283-2313 1.19e-06

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 46.86  E-value: 1.19e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1375383923 2283 CAEE-PCGA-GTCKETEGHVICLCPPGYTGEHC 2313
Cdd:cd00054      5 CASGnPCQNgGTCVNTVGSYRCSCPPGYTGRNC 37
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 2328-2441 1.52e-06

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: 49.74  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2328 QGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNN--NAQDYQ--------WIGLN---------DRTIEGdF 2388
Cdd:cd03600      3 SDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLllAAGPGRhgrgslrlWIGLQreprqcsdpSLPLRG-F 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1375383923 2389 RW-SDGHPMQFENWrPNQPDNFFAAgEDCVVM----IWHEKGEWNDVPCNYHLP-FTCK 2441
Cdd:cd03600     82 SWvTGDQDTDFSNW-LQEPAGTCTS-PRCVALsaagSTPDNLKWKDGPCSARADgYLCK 138
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 2283-2312 1.64e-06

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 46.61  E-value: 1.64e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1375383923 2283 CAEEPC-GAGTCKETEGHVICLCPPGYTGEH 2312
Cdd:pfam00008    1 CAPNPCsNGGTCVDTPGGYTCICPEGYTGKR 31
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 36-150 2.03e-06

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: 47.89  E-value: 2.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923    36 PSPLRVLLGTSLTIPCyfidpmhPVTTAPStaplaPRIKWSRVSKEkevvlLVATEGRVRVNSAyqdkvslpnypaiPSD 115
Cdd:smart00410    1 PPSVTVKEGESVTLSC-------EASGSPP-----PEVTWYKQGGK-----LLAESGRFSVSRS-------------GST 50

                            90       100       110
                    ....*....|....*....|....*....|....*
gi 1375383923   116 ATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVV 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 ...
 588-683 2.35e-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: 49.38  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  588 QFTFQEALEFCESHNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTvylypnqtgLPDPLS 667
Cdd:cd03516     18 SLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGTGVYI---------LNSNLS 88

                           90
                   ....*....|....*..
gi 1375383923  668 -RHHAFCFRGiSAVPSP 683
Cdd:cd03516     89 sRYDAYCYNS-SDTWIN 104
IGv smart00406
Immunoglobulin V-Type;
46-135 3.24e-06

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 46.99  E-value: 3.24e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923    46 SLTIPCYFidpmHPVTTAPSTaplaprIKWSRVSKEKEVVLLVA--TEGRVRVNSAYQDKVSLPNYPAiPSDATLEVQSL 123
Cdd:smart00406    1 SVTLSCKF----SGSTFSSYY------VSWVRQPPGKGLEWLGYigSNGSSYYQESYKGRFTISKDTS-KNDVSLTISNL 69

                            90
                    ....*....|..
gi 1375383923   124 RSNDSGVYRCEV 135
Cdd:smart00406   70 RVEDTGTYYCAV 81
EGF smart00181
Epidermal growth factor-like domain;
2283-2313 5.39e-05

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 42.12  E-value: 5.39e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 1375383923  2283 CAEE-PCGAGTCKETEGHVICLCPPGYTG-EHC 2313
Cdd:smart00181    2 CASGgPCSNGTCINTPGSYTCSCPPGYTGdKRC 34
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 2320-2408 9.62e-05

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


Pssm-ID: 153067  Cd Length: 129  Bit Score: 44.50  E-value: 9.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQ--------WIGLndRTIEGDFR-W 2390
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQmtkqkltpWVGL--RKINVSYWcW 78

                           90       100
                   ....*....|....*....|..
gi 1375383923 2391 SDGHPmqFEN----WRPNQPDN 2408
Cdd:cd03597     79 EDMSP--FTNttlqWLPGEPSD 98
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 2283-2313 1.30e-04

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


Pssm-ID: 238010  Cd Length: 36  Bit Score: 41.31  E-value: 1.30e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1375383923 2283 CAEE-PCGA-GTCKETEGHVICLCPPGYTGE-HC 2313
Cdd:cd00053      2 CAASnPCSNgGTCVNTPGSYRCVCPPGYTGDrSC 35
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 2320-2442 2.96e-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: 43.37  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2320 CEEGWNKYQG--HCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVNNNAQDYQ------------WIGLN----- 2380
Cdd:cd03599      1 CPSGWHHYEGtaSCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILAQEWDFDervfgrkdqckfWVGYQyvitn 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375383923 2381 -DRTIEGdfRWSDGHPMQFENWRPNQP---------DNFFAAGEDCV---VMIWHEKGEWNDVPCNYHLPFTCKK 2442
Cdd:cd03599     81 rNHSLEG--RWEVAYKGSMEVFLPPEPifatgmstnDNVFCAQLQCFqipSLRERGLHSWHAENCYEKSSFLCKR 153
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 154-247 4.34e-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: 42.83  E-value: 4.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  154 VFHYRAiSTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKdefPGVRTY 233
Cdd:cd03516      8 VFLVEK-NGRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNG---TGVYIL 83

                           90
                   ....*....|....
gi 1375383923  234 GIRDTNEtYDVYCF 247
Cdd:cd03516     84 NSNLSSR-YDAYCY 96
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 43-135 5.60e-04

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


Pssm-ID: 409383  Cd Length: 113  Bit Score: 41.66  E-value: 5.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   43 LGTSLTIPCYFIDPMHPVTTapstaplapRIKWSRV-SKEKEVVLLVATEGRVRVNSAYQDKVSLPNYPAIPSDATLEVQ 121
Cdd:cd05718     13 LGGSVTLPCSLTSPGTTKIT---------QVTWMKIgAGSSQNVAVFHPQYGPSVPNPYAERVEFLAARLGLRNATLRIR 83

                           90
                   ....*....|....
gi 1375383923  122 SLRSNDSGVYRCEV 135
Cdd:cd05718     84 NLRVEDEGNYICEF 97
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 2312-2441 7.35e-04

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: 45.46  E-value: 7.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 2312 HCNIDQEVCEEgwnkyQGHCYRHFPDRETWVDAERRCREQ-QSHLSSIVTPEEQEF----VNNNAQDYQWIGLND-RTIE 2385
Cdd:TIGR00864  317 HCPKDGEIFEE-----NGHCFQIVPEEAAWLDAQEQCLARaGAALAIVDNDALQNFlarkVTHSLDRGVWIGFSDvNGAE 391

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1375383923 2386 -GDFRWSDGHPMQ-FENWRPNQPDnfFAAGEDCVVMiwHEKGEWNDVPCNYHLPFTCK 2441
Cdd:TIGR00864  392 kGPAHQGEAFEAEeCEEGLAGEPH--PARAEHCVRL--DPRGQCNSDLCNAPHAYVCE 445
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
1433-1614 1.04e-03

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 44.38  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1433 PSGEVLETTAPGVEEISGLPSGeVLETS--TSAVGDLSGLPSGGEVLEISVSGVEDISGLPSG-EVVETSASGIEDVSEL 1509
Cdd:PRK15387   242 PELRTLEVSGNQLTSLPVLPPG-LLELSifSNPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGlQELSVSDNQLASLPAL 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1510 PSGE-GLETSASGVEDLSRLPSGEEVLEISASGFGDLSGLPSGGEGLETSASEVgTDLSGLPSGREGLETSASGAEDLSG 1588
Cdd:PRK15387   321 PSELcKLWAYNNQLTSLPTLPSGLQELSVSDNQLASLPTLPSELYKLWAYNNRL-TSLPALPSGLKELIVSGNRLTSLPV 399

                          170       180
                   ....*....|....*....|....*.
gi 1375383923 1589 LPSGKEDLVGSASGDLDLGKLPSGTL 1614
Cdd:PRK15387   400 LPSELKELMVSGNRLTSLPMLPSGLL 425
EGF_CA smart00179
Calcium-binding EGF-like domain;
2283-2313 1.89e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.00  E-value: 1.89e-03
                            10        20        30
                    ....*....|....*....|....*....|....
gi 1375383923  2283 CAEE-PCG-AGTCKETEGHVICLCPPGYT-GEHC 2313
Cdd:smart00179    5 CASGnPCQnGGTCVNTVGSYRCECPPGYTdGRNC 38
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
 44-148 2.34e-03

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: 39.91  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   44 GTSLTIPCYFidpmhPVTTAPSTAPLAprIKWSRvsKEKEVVLLVATEGRVRV-NSAYQDKVSLPNYPAIPSDATLEVQS 122
Cdd:cd20947     13 GSNMTIECKF-----PVEKQLDLAALI--VYWEM--EDKNIIQFVHGEEDLKVqHSSYRQRARLLKDQLSLGNAALQITD 83

                           90       100
                   ....*....|....*....|....*..
gi 1375383923  123 LRSNDSGVYRCEVMHGIED-SEATLEV 148
Cdd:cd20947     84 VKLQDAGVYRCMISYGGADyKRITVKV 110
IgV_1_Nectin-1_like cd05886
First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here ...
 43-134 2.69e-03

First immunoglobulin variable (IgV) domain of nectin-1, and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of nectin-1 (also known as poliovirus receptor related protein 1 (PVRL1) or cluster of differentiation (CD) 111). Nectin-1 belongs to the nectin family comprised of four transmembrane glycoproteins (nectins-1 through -4). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. In addition nectins heterophilically trans-interact with other CAMs such as nectin-like molecules (Necls), nectin-1 for example, has been shown to trans-interact with Necl-1. Nectins also interact with various other proteins, including the actin filament (F-actin)-binding protein, afadin. Mutation in the human nectin-1 gene is associated with cleft lip/palate ectodermal dysplasia syndrome (CLPED1). Nectin-1 is a major receptor for herpes simplex virus through interaction with the viral envelope glycoprotein D.


Pssm-ID: 409469  Cd Length: 113  Bit Score: 39.95  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923   43 LGTSLTIPCYFIDPMHPVTTApstaplapRIKWSRVSK-EKEVVLLVATEGRVRVNSAYQDKVSLPNyPAIpSDATLEVQ 121
Cdd:cd05886     13 IGTDVVLHCSFANPLPSVKIT--------QVTWQKSTNgSKQNVAIYNPSMGVSVLPPYRERVTFLN-PSF-TDGTIRLS 82

                           90
                   ....*....|...
gi 1375383923  122 SLRSNDSGVYRCE 134
Cdd:cd05886     83 RLELEDEGVYICE 95
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 479-541 2.78e-03

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


Pssm-ID: 239598  Cd Length: 95  Bit Score: 39.14  E-value: 2.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1375383923  479 VFHYRPGPTRYSLTFEEAQQACLRTGAVIASPEQLQ-AAYEAGYEQCDAGWLRDQTVRYPIVSP 541
Cdd:cd03521      2 LFVLELENGSQGLGLRAARQSCASLGARLASAAELRrAVVECFFSACARGWLADGTVGTTVCNP 65
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 716-975 2.82e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 2.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  716 EETTAVPSGETTAilEFTTEPENQTEWEPAYTPVGTSPLPGilPTWPPTGAATEESTEGPSATEVPSASEEPSPSEVPFP 795
Cdd:PHA03307    62 CDRFEPPTGPPPG--PGTEAPANESRSTPTWSLSTLAPASP--AREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEM 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  796 SEEPSPSEEPFPSVRPFPSVE-------------------LFPSEEPFPSkEPSPSEEPSASEEPYTPSPPVPSWTELPS 856
Cdd:PHA03307   138 LRPVGSPGPPPAASPPAAGASpaavasdaassrqaalplsSPEETARAPS-SPPAEPPPSTPPAAASPRPPRRSSPISAS 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  857 SGEESGAPDVSGDFTGSGDVSGHLDFSGQLSGDRASGLPSGDLDSSGLTSTV---GSG--------LPVESGLPSGDEER 925
Cdd:PHA03307   217 ASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRiweASGwngpssrpGPASSSSSPRERSP 296

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1375383923  926 IEWPSTPTVGELPSGAEILE--GSASGVGDLSGLPSGEVLETSASGVGDLSG 975
Cdd:PHA03307   297 SPSPSSPGSGPAPSSPRASSssSSSRESSSSSTSSSSESSRGAAVSPGPSPS 348
TamB COG2911
Autotransporter translocation and assembly protein TamB [Intracellular trafficking, secretion, ...
 1511-2016 3.44e-03

Autotransporter translocation and assembly protein TamB [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442155 [Multi-domain]  Cd Length: 766  Bit Score: 42.72  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1511 SGEGLETSASGVEDLsRLPSGEEVLEISasgfGDLSGLPSGGEgLETSASEVGtDLSGLPSGREGlETSASGAEDLSGLP 1590
Cdd:COG2911     77 DAEGLDLASSALDDL-DLRSGGNRLTLS----GNLSAASLDGD-LDLDAPDLA-DLAALLPGLAG-SLSGDGLDSLSLDA 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1591 SGKEdlvgsASGDLDLGKlpSGTLGSGQAPETSGLPSGFSGEYSGVDLGSGPPSGLPDFSGLPSGFPTVSLVDSTLvevv 1670
Cdd:COG2911    149 DGTL-----AQHRLDLDA--KGEPASLSLALSGGLDRDDGGTLSRLDFLNTGRWGLAAPATLSYDDGRVTLGPLCL---- 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1671 taSTASELEGRGTIG--ISGAGEISGLPSSELdisgrASGLPSGTELSGQASGSPDVSG-----------EIPGLFGVSG 1737
Cdd:COG2911    218 --AGGGSLCLSGTLGgtLDLQLRLKNLPLALL-----NPFLPDDLGLSGTLNGDADLSGglanpqgdaslSLSGDLTLND 290

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1738 QPSGFPDTSGETSGVTELSG--------LSSGQPGiSGEASGVLYGTSQPFGITDLSGE-TSGVPDLSgqpsglpGFSGA 1808
Cdd:COG2911    291 GLGGLPLGLGDLTLNARLANgrltldltLDGGGLG-TLSLSGSVPLADGLPPSAPLDGNlRLDNLDLA-------LLNPL 362

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1809 TSGVPDLVSGTTSGSGESSG----------ITFVDTSL-VEVAPTTFKEEEGL-----GSVELSGL----PSGEADLSGK 1868
Cdd:COG2911    363 LPGVLERLSGQLNGDLRLSGtlaapqlngqLTLDDGRLkLPALGVRLTDINLRlrfdgDRLTLDGLtadsGGGTLTLSGT 442

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1869 SGMVDVSGQFSGTVDSSGFT-SQTPEFSGLPSGIAEVSGESSRAEIGSSL--PSGAYYGSGTPSSFPTVS----LVDRTL 1941
Cdd:COG2911    443 VDLDGLSWPADLTLKGDNLRvLNPPDYTATVSGDLTLTGTPDGPTLSGNVtvPRARITLPELPPSAVSLSddvvVVNRPP 522

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1942 VESVTQAPTAQ--------EAGE-----GP------SGILELSGAHSGAPDMSGE---HSGFLDLSG----LQSGLIEPS 1995
Cdd:COG2911    523 EPVPEEEAAGLpldldlnvNLGDdvrvrGFgldarlGGDLRLTGTPGGAPRLTGEinlVRGRYNAYGqrltIERGSITFN 602

                          570       580
                   ....*....|....*....|.
gi 1375383923 1996 GEPPgTPYFsgDFASTTNVSG 2016
Cdd:COG2911    603 GPPL-DPYL--DIEAVRTVDD 620
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 266-348 3.72e-03

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


Pssm-ID: 239598  Cd Length: 95  Bit Score: 38.76  E-value: 3.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923  266 FQEAANECRRLGARLATTGQLYLAWQ-AGMDMCSAGWLADRSVRYPIskARPNCGGNLLGVRtvyVHANQTGYPDPSSRY 344
Cdd:cd03521     16 LRAARQSCASLGARLASAAELRRAVVeCFFSACARGWLADGTVGTTV--CNPVVAEALKAVD---VKVEIETNPIPFAHY 90


                   ....
gi 1375383923  345 DAIC 348
Cdd:cd03521     91 NALC 94
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
2290-2331 3.82e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 3.82e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1375383923  2290 AGTCKETEGHviCLCPPGYTGEHCnidqEVCEEG-WNKYQGHC 2331
Cdd:smart00180   10 SGTCDPDTGQ--CECKPNVTGRRC----DRCAPGyYGDGPPGC 46
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 2320-2392 6.10e-03

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 40.48  E-value: 6.10e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375383923 2320 CEEGWNKYQGHCYRHFPDRETWVDAERRCREQQSHLSSIVTPEEQEFVN--NNAQDYqWIGLNDRTIEGDFRWSD 2392
Cdd:PHA02642    88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKryKDSSDH-WIGLNRESSNHPWKWAD 161
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 2291-2323 7.51e-03

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 36.56  E-value: 7.51e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1375383923 2291 GTCKETEGHviCLCPPGYTGEHCnidqEVCEEG 2323
Cdd:pfam00053   11 DTCDPETGQ--CLCKPGVTGRHC----DRCKPG 37
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 1448-1880 9.74e-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: 41.47  E-value: 9.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1448 ISGLPSGEVLETSTSAVGDLSGLPSGGEVLEISVSGVEDISGLPSGEVVETSASGIEDVSELPSGEGLETSASGVEDLSR 1527
Cdd:COG3468      5 GGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1528 LPSGEEVLEISASGFGDLSGLPSGGEGLETSASEVGTDLSGLpsgreGLETSASGAEDLSGLPSGKEDLVGSASGDLDLG 1607
Cdd:COG3468     85 GGNSTGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTG-----GGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1608 KLPSGTLGSGQAPETSGLPSGFSGEYSGVDLGSGPPSGLPDFSGLPSGFPTVSLVDSTLVEVVTASTASELEGRGTIGIS 1687
Cdd:COG3468    160 GTGSGGGGSGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTGGGGGGGGGAGGATGGAGSGGNTGGGVG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1688 GAGEISGLPSSELDISGRASGLPSGTELSGQASGSPDVSGEI-PGLFGVSGQPSGFPDTSGETSGVTELSGLSSGQPGIS 1766
Cdd:COG3468    240 GGGGSAGGTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANgGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGG 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375383923 1767 GEASGVLYGTSQPFGITDLSGETSGVPDLSGqpSGLPGFSGATSGVPDLVSGTTSGSGESSGITFVDTSLVEVAPTTFKE 1846
Cdd:COG3468    320 SNAGGGSGGGGGGGGGGGGGGTTLNGAGSAG--GGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANTGSDGVGTGLTT 397

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1375383923 1847 EEGLGSVELSGLPSGEADLSGKSGMVDVSGQFSG 1880
Cdd:COG3468    398 GGTGNNGGGGVGGGGGGGLTLTGGTLTVNGNYTG 431
 
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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