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Conserved domains on  [gi|281604094|ref|NP_001164031|]
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versican core protein isoform 3 precursor [Rattus norvegicus]

Protein Classification

Ig_Versican and CLECT_CSPGs domain-containing protein( domain architecture ID 12945639)

protein containing domains Ig_Versican, Link_domain_CSPGs_modules_1_3, Link_domain_CSPGs_modules_2_4, and CLECT_CSPGs

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 ...
 1394-1517 4.18e-79

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: 256.35  E-value: 4.18e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1394 CDYGWHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFVNRVGHDYQWIGLNDKMFEHDFRWTDGSALQYE 1473
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 281604094 1474 NWRPNQPDSFFSAGEDCVVIIWHENGQWNDVPCNYHLTYTCKKG 1517
Cdd:cd03588    81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 26-152 1.88e-71

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: 234.47  E-value: 1.88e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   26 MEENPPVKGSLSGKVILPCHFSTLPTLPPDYN-TSEFLRIKWSKIEVDKNGKDIKETTVLVAQDGNIKIGQDYKGRVSVP 104
Cdd:cd05901     1 VRKSSRVHGSLSGSVVLPCRFSTLPTLPPSYNiTSEFLRIKWTKIQVDKNGKDHKETTVLVAQNGIIKIGQEYMGRVSVP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 281604094  105 THPDDVGDASLTMVKLRASDAGVYRCDVMYGIEDTQNTMSLAVDGVVF 152
Cdd:cd05901    81 SHPEDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
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 ...
 251-346 2.84e-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: 201.39  E-value: 2.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  251 DVFHITAPSKFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRTLYRFEN 330
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 281604094  331 QTCFPLPDSRFDAYCF 346
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 ...
 150-244 3.16e-58

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: 195.32  E-value: 3.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  150 VVFHYRAATSRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCYGDMMGKEGVRT 229
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 281604094  230 YGFRSPQETYDVYCY 244
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1352-1388 2.50e-11

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: 59.57  E-value: 2.50e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 281604094 1352 DFDECHS-NPCRNGATCVDGLNTFRCLCLPSYVGALCE 1388
Cdd:cd00054     1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1316-1350 1.44e-10

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: 57.65  E-value: 1.44e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 281604094 1316 DLCKT-NPCLNGGTCYPTETSYVCTCAPGYSGDQCE 1350
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1521-1577 2.46e-10

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


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 57.47  E-value: 2.46e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094 1521 CGQPPVVENAKTFGKmKPRYEINSLIRYHCKDGFIQRHLPTIRCLGNGRWAMPKITC 1577
Cdd:cd00033     1 CPPPPVPENGTVTGS-KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 766-1193 1.06e-04

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


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.22  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   766 ILTRLETDVPTSDEDVTSAHLTHSTlnvEVVTVLKWPGNEDNSTSKPLPPTERAGFTKSPPVSLS-TVGIVGKDKETPSF 844
Cdd:pfam05109  404 IITRTATNATTTTHKVIFSKAPEST---TTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGpTVSTADVTSPTPAG 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   845 TDGGDEytlSLDGTPKPLEKFSEE---DLTSGEFAVTIPTSISIDSAEKSTLGEPTTGDRVLSTTSTKDLVINATVEGSA 921
Cdd:pfam05109  481 TTSGAS---PVTPSPSPRDNGTESkapDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATS 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   922 LDEDMDASKPLFTATPFVHTSDVE---------ESAFVNYSSTQQPTTYVDISHTSPLSIIPKTEWSVSETSVPLEDEVL 992
Cdd:pfam05109  558 PTPAVTTPTPNATIPTLGKTSPTSavttptpnaTSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNIT 637

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   993 GKSDQD-TLEQTHLEATMSPEA----------LSTIEVTQGE--TQEEPQTPGIPFPALSSTAVMTKETTAFEEEGEGST 1059
Cdd:pfam05109  638 SSSTSSmSLRPSSISETLSPSTsdnstshmplLTSAHPTGGEniTQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSST 717

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  1060 YTLSEDRLMTD--------SEIVPSLETT--PVGTSYPGGAMTQQGVEMDTMVTQMSSIRPTVVL---STEPEVSYEAEG 1126
Cdd:pfam05109  718 STKPGEVNVTKgtppknatSPQAPSGQKTavPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYggdSTTPRTRYNATT 797

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094  1127 SSPMEFASTLKPFGTQVTQLVeetTEEGKKTPLDYTdlgsglfEQPRVTELPDFSMTPSDISVFTAI 1193
Cdd:pfam05109  798 YLPPSTSSKLRPRWTFTSPPV---TTAQATVPVPPT-------SQPRFSNLSMLVLQWASLAVLTLL 854
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1394-1517 4.18e-79

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: 256.35  E-value: 4.18e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1394 CDYGWHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFVNRVGHDYQWIGLNDKMFEHDFRWTDGSALQYE 1473
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 281604094 1474 NWRPNQPDSFFSAGEDCVVIIWHENGQWNDVPCNYHLTYTCKKG 1517
Cdd:cd03588    81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 26-152 1.88e-71

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: 234.47  E-value: 1.88e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   26 MEENPPVKGSLSGKVILPCHFSTLPTLPPDYN-TSEFLRIKWSKIEVDKNGKDIKETTVLVAQDGNIKIGQDYKGRVSVP 104
Cdd:cd05901     1 VRKSSRVHGSLSGSVVLPCRFSTLPTLPPSYNiTSEFLRIKWTKIQVDKNGKDHKETTVLVAQNGIIKIGQEYMGRVSVP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 281604094  105 THPDDVGDASLTMVKLRASDAGVYRCDVMYGIEDTQNTMSLAVDGVVF 152
Cdd:cd05901    81 SHPEDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
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 ...
 251-346 2.84e-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: 201.39  E-value: 2.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  251 DVFHITAPSKFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRTLYRFEN 330
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 281604094  331 QTCFPLPDSRFDAYCF 346
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 ...
 150-244 3.16e-58

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: 195.32  E-value: 3.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  150 VVFHYRAATSRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCYGDMMGKEGVRT 229
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 281604094  230 YGFRSPQETYDVYCY 244
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
Xlink pfam00193
Extracellular link domain;
150-244 1.65e-45

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 158.89  E-value: 1.65e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   150 VVFHYRAAtSRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCYGDMmgkEGVRT 229
Cdd:pfam00193    1 GVFHLESP-GRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 281604094   230 YGFRSPQ-ETYDVYCY 244
Cdd:pfam00193   77 YGFRDPLsERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
148-244 3.04e-44

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 155.19  E-value: 3.04e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094    148 DGVVFHYRAATsRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCYGdmmGKEGV 227
Cdd:smart00445    1 DGGVFHVEKNG-RYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                            90
                    ....*....|....*..
gi 281604094    228 RTYGFRSPQETYDVYCY 244
Cdd:smart00445   77 RQYGFPDPTSRYDAYCF 93
LINK smart00445
Link (Hyaluronan-binding);
249-347 4.96e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 149.03  E-value: 4.96e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094    249 DGDVFHITA--PSKFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRtly 326
Cdd:smart00445    1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 281604094    327 rfenQTCFPLPDSRFDAYCFK 347
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
252-346 6.49e-38

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 137.32  E-value: 6.49e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   252 VFHITAPS--KFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRtlyrfe 329
Cdd:pfam00193    2 VFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR------ 75

                           90
                   ....*....|....*...
gi 281604094   330 nQTCFPLPDS-RFDAYCF 346
Cdd:pfam00193   76 -QYGFRDPLSeRYDAYCY 92
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1394-1515 5.26e-37

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: 135.81  E-value: 5.26e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   1394 CDYGWHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFV-----NRVGHDYQWIGLNDKMFEHDFRWTDGS 1468
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllkNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 281604094   1469 -ALQYENWRPNQPDsffSAGEDCVViIWHENGQWNDVPCNYHLTYTCK 1515
Cdd:smart00034   81 gPVSYSNWAPGEPN---NSSGDCVV-LSTSGGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1412-1516 1.44e-24

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 99.47  E-value: 1.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  1412 RRTWDAAERECRLQGAHLTSILSHEEQMFVNRVGHDYQ---WIGLNDKMFEHDFRWTDGSALQYENWRPNQPDSffSAGE 1488
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNkyfWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENE 78

                           90       100
                   ....*....|....*....|....*...
gi 281604094  1489 DCVVIIWhENGQWNDVPCNYHLTYTCKK 1516
Cdd:pfam00059   79 DCVELSS-SSGKWNDENCNSKNPFVCEK 105
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 27-147 2.97e-12

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 64.79  E-value: 2.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094    27 EENPPVKGSLSGKVILPCHFSTlptlppdYNTSEFLRIKWSKievdknGKDIKETTVLVA-QDGNIKIGQDyKGRVSVPT 105
Cdd:pfam07686    1 QTPREVTVALGGSVTLPCTYSS-------SMSEASTSVYWYR------QPPGKGPTFLIAyYSNGSEEGVK-KGRFSGRG 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 281604094   106 HPDdVGDASLTMVKLRASDAGVYRCDVMY-GIEDTQNTMSLAV 147
Cdd:pfam07686   67 DPS-NGDGSLTIQNLTLSDSGTYTCAVIPsGEGVFGKGTRLTV 108
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1352-1388 2.50e-11

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: 59.57  E-value: 2.50e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 281604094 1352 DFDECHS-NPCRNGATCVDGLNTFRCLCLPSYVGALCE 1388
Cdd:cd00054     1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1316-1350 1.44e-10

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: 57.65  E-value: 1.44e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 281604094 1316 DLCKT-NPCLNGGTCYPTETSYVCTCAPGYSGDQCE 1350
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1521-1577 2.46e-10

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 57.47  E-value: 2.46e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094 1521 CGQPPVVENAKTFGKmKPRYEINSLIRYHCKDGFIQRHLPTIRCLGNGRWAMPKITC 1577
Cdd:cd00033     1 CPPPPVPENGTVTGS-KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
EGF_CA smart00179
Calcium-binding EGF-like domain;
1352-1388 2.90e-10

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 56.87  E-value: 2.90e-10
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 281604094   1352 DFDECHS-NPCRNGATCVDGLNTFRCLCLPSYV-GALCE 1388
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1318-1348 6.17e-09

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: 52.77  E-value: 6.17e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 281604094  1318 CKTNPCLNGGTCYPTETSYVCTCAPGYSGDQ 1348
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA smart00179
Calcium-binding EGF-like domain;
1316-1350 2.69e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 51.09  E-value: 2.69e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 281604094   1316 DLCKT-NPCLNGGTCYPTETSYVCTCAPGYS-GDQCE 1350
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 1521-1577 8.31e-08

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 50.22  E-value: 8.31e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094   1521 CGQPPVVENAKTFGKmKPRYEINSLIRYHCKDGFIQRHLPTIRCLGNGRWAMPKITC 1577
Cdd:smart00032    1 CPPPPDIENGTVTSS-SGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1356-1384 2.33e-07

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 48.15  E-value: 2.33e-07
                           10        20
                   ....*....|....*....|....*....
gi 281604094  1356 CHSNPCRNGATCVDGLNTFRCLCLPSYVG 1384
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
Sushi pfam00084
Sushi repeat (SCR repeat);
1521-1577 3.09e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 48.65  E-value: 3.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094  1521 CGQPPVVENAKTFGKmKPRYEINSLIRYHCKDGFIQRHLPTIRCLGNGRWAMPKITC 1577
Cdd:pfam00084    1 CPPPPDIPNGKVSAT-KNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
IGv smart00406
Immunoglobulin V-Type;
40-132 2.96e-06

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 46.61  E-value: 2.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094     40 VILPCHFSTlptlppdyNTSEFLRIKWSKievDKNGKdIKETTVLVAQDGNIKIGQDYKGRVSVPTHPDDvGDASLTMVK 119
Cdd:smart00406    2 VTLSCKFSG--------STFSSYYVSWVR---QPPGK-GLEWLGYIGSNGSSYYQESYKGRFTISKDTSK-NDVSLTISN 68

                            90
                    ....*....|...
gi 281604094    120 LRASDAGVYRCDV 132
Cdd:smart00406   69 LRVEDTGTYYCAV 81
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1393-1469 1.59e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 47.80  E-value: 1.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281604094 1393 TCDYGWHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFVNRVGHDY-QWIGLNDKMFEHDFRWTDGSA 1469
Cdd:PHA02642   87 TCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSdHWIGLNRESSNHPWKWADNSN 164
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 1383-1515 1.02e-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: 47.38  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  1383 VGALCEQDTETcdygwHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHE--EQMFVNRVGHDYQ---WIGLND-- 1455
Cdd:TIGR00864  314 SHPHCPKDGEI-----FEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDalQNFLARKVTHSLDrgvWIGFSDvn 388

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281604094  1456 KMFEHDFRWTDGSALQY-ENWRPnqPDSFFSAGEDCVVIiwHENGQWNDVPCNYHLTYTCK 1515
Cdd:TIGR00864  389 GAEKGPAHQGEAFEAEEcEEGLA--GEPHPARAEHCVRL--DPRGQCNSDLCNAPHAYVCE 445
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 766-1193 1.06e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.22  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   766 ILTRLETDVPTSDEDVTSAHLTHSTlnvEVVTVLKWPGNEDNSTSKPLPPTERAGFTKSPPVSLS-TVGIVGKDKETPSF 844
Cdd:pfam05109  404 IITRTATNATTTTHKVIFSKAPEST---TTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGpTVSTADVTSPTPAG 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   845 TDGGDEytlSLDGTPKPLEKFSEE---DLTSGEFAVTIPTSISIDSAEKSTLGEPTTGDRVLSTTSTKDLVINATVEGSA 921
Cdd:pfam05109  481 TTSGAS---PVTPSPSPRDNGTESkapDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATS 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   922 LDEDMDASKPLFTATPFVHTSDVE---------ESAFVNYSSTQQPTTYVDISHTSPLSIIPKTEWSVSETSVPLEDEVL 992
Cdd:pfam05109  558 PTPAVTTPTPNATIPTLGKTSPTSavttptpnaTSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNIT 637

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   993 GKSDQD-TLEQTHLEATMSPEA----------LSTIEVTQGE--TQEEPQTPGIPFPALSSTAVMTKETTAFEEEGEGST 1059
Cdd:pfam05109  638 SSSTSSmSLRPSSISETLSPSTsdnstshmplLTSAHPTGGEniTQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSST 717

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  1060 YTLSEDRLMTD--------SEIVPSLETT--PVGTSYPGGAMTQQGVEMDTMVTQMSSIRPTVVL---STEPEVSYEAEG 1126
Cdd:pfam05109  718 STKPGEVNVTKgtppknatSPQAPSGQKTavPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYggdSTTPRTRYNATT 797

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094  1127 SSPMEFASTLKPFGTQVTQLVeetTEEGKKTPLDYTdlgsglfEQPRVTELPDFSMTPSDISVFTAI 1193
Cdd:pfam05109  798 YLPPSTSSKLRPRWTFTSPPV---TTAQATVPVPPT-------SQPRFSNLSMLVLQWASLAVLTLL 854
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1394-1517 4.18e-79

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: 256.35  E-value: 4.18e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1394 CDYGWHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFVNRVGHDYQWIGLNDKMFEHDFRWTDGSALQYE 1473
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 281604094 1474 NWRPNQPDSFFSAGEDCVVIIWHENGQWNDVPCNYHLTYTCKKG 1517
Cdd:cd03588    81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 26-152 1.88e-71

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: 234.47  E-value: 1.88e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   26 MEENPPVKGSLSGKVILPCHFSTLPTLPPDYN-TSEFLRIKWSKIEVDKNGKDIKETTVLVAQDGNIKIGQDYKGRVSVP 104
Cdd:cd05901     1 VRKSSRVHGSLSGSVVLPCRFSTLPTLPPSYNiTSEFLRIKWTKIQVDKNGKDHKETTVLVAQNGIIKIGQEYMGRVSVP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 281604094  105 THPDDVGDASLTMVKLRASDAGVYRCDVMYGIEDTQNTMSLAVDGVVF 152
Cdd:cd05901    81 SHPEDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
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 ...
 251-346 2.84e-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: 201.39  E-value: 2.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  251 DVFHITAPSKFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRTLYRFEN 330
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 281604094  331 QTCFPLPDSRFDAYCF 346
Cdd:cd03520    81 QTGFPDPHSRFDAYCF 96
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 30-152 2.08e-59

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: 200.15  E-value: 2.08e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   30 PPVKGSLSGKVILPCHFSTLPTLPPDYNTSEFLRIKWSKIEVDknGKDIKETTVLVAQDGNIKIGQDYKGRVSVPTHPDD 109
Cdd:cd05878     5 SPVRVLLGTSVTLPCYFIDPPHPVTPSTAPLAPRIKWSKVSVD--GKKEKEVVLLVATEGRVRVNSAYQGRVSLPNYPAI 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 281604094  110 VGDASLTMVKLRASDAGVYRCDVMYGIEDTQNTMSLAVDGVVF 152
Cdd:cd05878    83 PSDATLEVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 150-244 3.16e-58

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: 195.32  E-value: 3.16e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  150 VVFHYRAATSRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCYGDMMGKEGVRT 229
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 281604094  230 YGFRSPQETYDVYCY 244
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 28-152 9.82e-56

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: 189.34  E-value: 9.82e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   28 ENPPVKGSLSGKVILPCHFSTLPTLPpdYNTSEFLRIKWSKIEVDKngKDIKETTVLVAQDGNIKIGQDYKGRVSVPTHP 107
Cdd:cd05714     3 ESAKVFSHLGGNVTLPCKFYRDPTAF--GSGIHKIRIKWTKLTSDS--GYLKEVDVLVAMGNVVYHKKTYGGRVSVPLKP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 281604094  108 DDVGDASLTMVKLRASDAGVYRCDVMYGIEDTQNTMSLAVDGVVF 152
Cdd:cd05714    79 GSDSDASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
Xlink pfam00193
Extracellular link domain;
150-244 1.65e-45

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 158.89  E-value: 1.65e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   150 VVFHYRAAtSRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCYGDMmgkEGVRT 229
Cdd:pfam00193    1 GVFHLESP-GRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 281604094   230 YGFRSPQ-ETYDVYCY 244
Cdd:pfam00193   77 YGFRDPLsERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
148-244 3.04e-44

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 155.19  E-value: 3.04e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094    148 DGVVFHYRAATsRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCYGdmmGKEGV 227
Cdd:smart00445    1 DGGVFHVEKNG-RYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                            90
                    ....*....|....*..
gi 281604094    228 RTYGFRSPQETYDVYCY 244
Cdd:smart00445   77 RQYGFPDPTSRYDAYCF 93
LINK smart00445
Link (Hyaluronan-binding);
249-347 4.96e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 149.03  E-value: 4.96e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094    249 DGDVFHITA--PSKFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRtly 326
Cdd:smart00445    1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                            90       100
                    ....*....|....*....|.
gi 281604094    327 rfenQTCFPLPDSRFDAYCFK 347
Cdd:smart00445   78 ----QYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
252-346 6.49e-38

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 137.32  E-value: 6.49e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   252 VFHITAPS--KFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRtlyrfe 329
Cdd:pfam00193    2 VFHLESPGryKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVR------ 75

                           90
                   ....*....|....*...
gi 281604094   330 nQTCFPLPDS-RFDAYCF 346
Cdd:pfam00193   76 -QYGFRDPLSeRYDAYCY 92
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 1394-1516 1.44e-37

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: 137.44  E-value: 1.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1394 CDYGWHKFQGQCYkYFAH-RRTWDAAERECRLQGAHLTSILSHEEQMFVNR--VGHDYQWIGLNDKMFEHDFRWTDGSAL 1470
Cdd:cd03590     1 CPTNWKSFQSSCY-FFSTeKKSWEESRQFCEDMGAHLVIINSQEEQEFISKilSGNRSYWIGLSDEETEGEWKWVDGTPL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 281604094 1471 Q--YENWRPNQPDSFFSAGEDCVViIWHENGQWNDVPCNYHLTYTCKK 1516
Cdd:cd03590    80 NssKTFWHPGEPNNWGGGGEDCAE-LVYDSGGWNDVPCNLEYRWICEK 126
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1394-1515 5.26e-37

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: 135.81  E-value: 5.26e-37
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   1394 CDYGWHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFV-----NRVGHDYQWIGLNDKMFEHDFRWTDGS 1468
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVasllkNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 281604094   1469 -ALQYENWRPNQPDsffSAGEDCVViIWHENGQWNDVPCNYHLTYTCK 1515
Cdd:smart00034   81 gPVSYSNWAPGEPN---NSSGDCVV-LSTSGGKWNDVSCTSKLPFVCE 124
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 150-244 1.24e-36

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


Pssm-ID: 238534  Cd Length: 92  Bit Score: 133.70  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  150 VVFHYRAATSRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCYGDmmgKEGVRT 229
Cdd:cd01102     1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGR---NPGVRS 77

                          90
                  ....*....|....*
gi 281604094  230 YGFRSPQETYDVYCY 244
Cdd:cd01102    78 YGNPAPSGRYDAYCF 92
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 1405-1516 4.39e-36

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: 133.13  E-value: 4.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1405 CYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFV----NRVGHDYQWIGLNDKMFEHDFRWTDGS-ALQYENWRPNQ 1479
Cdd:cd00037     2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLasllKKSSSSDVWIGLNDLSSEGTWKWSDGSpLVDYTNWAPGE 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 281604094 1480 PDSffSAGEDCVVIIWHENGQWNDVPCNYHLTYTCKK 1516
Cdd:cd00037    82 PNP--GGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 1394-1515 8.94e-36

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: 132.87  E-value: 8.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1394 CDYGWHKFQGQCYKYFAHRRTWDAAERECR------LQgAHLTSILSHEEQMFV-------NRVGHDYQ-WIGLNDKMFE 1459
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRsfsipgLI-AHLVSIHSQEENDFVydlfessRGPDTPYGlWIGLHDRTSE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281604094 1460 HDFRWTDGSALQYENWRPNQPDSFFSaGEDCvVIIWHEN---GQWNDVPCNYHLTYTCK 1515
Cdd:cd03589    80 GPFEWTDGSPVDFTKWAGGQPDNYGG-NEDC-VQMWRRGdagQSWNDMPCDAVFPYICK 136
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 150-244 3.19e-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: 126.77  E-value: 3.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  150 VVFHYRAATSRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCYGDMMgKEGVRT 229
Cdd:cd03518     1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRT-VPGLRS 79

                          90
                  ....*....|....*.
gi 281604094  230 YGFRSPQET-YDVYCY 244
Cdd:cd03518    80 YGERDKMLSrYDAFCF 95
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 252-346 4.22e-32

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: 120.60  E-value: 4.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  252 VFHITA---PSKFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRTLYrf 328
Cdd:cd01102     2 VFHLESqngRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSYG-- 79

                          90
                  ....*....|....*...
gi 281604094  329 enqtcFPLPDSRFDAYCF 346
Cdd:cd01102    80 -----NPAPSGRYDAYCF 92
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 30-152 1.68e-31

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: 119.94  E-value: 1.68e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   30 PPVKGSLSGKVILPCHFstlpTLPPDYN-TSEFLRIKWSKIEVDKNGKDIketTVLVAQDGNIKIGQDYKGRVSVPTHPD 108
Cdd:cd05902     5 PPVRRPLSSSVLLPCVF----TLPPSASsPPEGPRIKWTKLSTSGGQQQR---PVLVARDNVVRVAKAFQGRVSLPGYPK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 281604094  109 DVGDASLTMVKLRASDAGVYRCDVMYGIEDTQNTMSLAVDGVVF 152
Cdd:cd05902    78 NRYNASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 1394-1515 2.12e-26

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: 105.92  E-value: 2.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1394 CDYGWHKFQGQCYKYFAHRRTWDAAERECRL--QGAHLTSILSHEEQMFVNRVGHDYQ------WIGLNDKMFEHDFRWT 1465
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQkayqpvWIGLHDPQQSRGWEWS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281604094 1466 DGSALQYENWRPNQPdsfFSAGEDCVViIWHENG--QWNDVPCNYHLTYTCK 1515
Cdd:cd03594    81 DGSKLDYRSWDRNPP---YARGGYCAE-LSRSTGflKWNDANCEERNPFICK 128
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1412-1516 1.44e-24

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 99.47  E-value: 1.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  1412 RRTWDAAERECRLQGAHLTSILSHEEQMFVNRVGHDYQ---WIGLNDKMFEHDFRWTDGSALQYENWRPNQPDSffSAGE 1488
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNkyfWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENE 78

                           90       100
                   ....*....|....*....|....*...
gi 281604094  1489 DCVVIIWhENGQWNDVPCNYHLTYTCKK 1516
Cdd:pfam00059   79 DCVELSS-SSGKWNDENCNSKNPFVCEK 105
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 252-346 3.41e-24

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: 97.88  E-value: 3.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  252 VFHITAPSKFTFEEAEAECANRDARLATVGELHAAWR-NGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRTLyrfen 330
Cdd:cd03519     2 VFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF----- 76

                          90
                  ....*....|....*..
gi 281604094  331 qtCFPLPDSR-FDAYCF 346
Cdd:cd03519    77 --GFPDKKHKlYGVYCY 91
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 28-152 5.18e-23

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: 95.78  E-value: 5.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   28 ENPPVKGSLSGKVILPCHFSTLPTLPPDYNTSEFL--RIKWSKIEVDKngkdikETTVLVAQDGNIKIGQDYKGRVSVPT 105
Cdd:cd05900     3 LESPLRVVLGSSLLIPCYFQDPIAKDPGAPTVAPLspRIKWSFISKEK------ESVLLVATEGKVRVNTEYLDRVSLPN 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 281604094  106 HPDDVGDASLTMVKLRASDAGVYRCDVMYGIEDTQNTMSLAVDGVVF 152
Cdd:cd05900    77 YPAIPSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 260-346 8.54e-22

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: 91.33  E-value: 8.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  260 KFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLL--GVRTlYRFENQTcfplp 337
Cdd:cd03518    13 NLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKRTvpGLRS-YGERDKM----- 86


                  ....*....
gi 281604094  338 DSRFDAYCF 346
Cdd:cd03518    87 LSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 163-244 1.74e-21

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: 90.17  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  163 LNFESAQQACLDIGAVIATPEQLFAAYE-DGFEQCDAGWLSDQTVRYPIRAPREGCYGDmmgKEGVRTYGFRSPQE-TYD 240
Cdd:cd03519    11 LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPL---EPGVRSFGFPDKKHkLYG 87


                  ....
gi 281604094  241 VYCY 244
Cdd:cd03519    88 VYCY 91
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 151-244 1.85e-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: 87.52  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  151 VFHYRAATSRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCyGDmmGKEGVRTY 230
Cdd:cd03515     2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANC-GF--GHVGIVDY 78

                          90
                  ....*....|....*
gi 281604094  231 GFR-SPQETYDVYCY 244
Cdd:cd03515    79 GPRlNLSERWDAYCY 93
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 38-152 5.09e-20

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: 87.00  E-value: 5.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   38 GKVILPCHFSTLPTL--PPDYntseflRIKWSKIEVDkngkDIKETTVLVAQDGNIKIGQDYKGRVSVptHPDDVGDASL 115
Cdd:cd05877    13 GNVTLPCRYHYEPELsaPRKI------RVKWTKLEVD----YAKEEDVLVAIGTRHKSYGSYQGRVFL--RRADDLDASL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 281604094  116 TMVKLRASDAGVYRCDVMYGIEDTQNTMSLAVDGVVF 152
Cdd:cd05877    81 VITDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 1406-1508 5.70e-18

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 81.32  E-value: 5.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1406 YKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFVNRVGHDYQ--WIGLNDKMFEHDFRWTDGSALQYENWRPNQPDSF 1483
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGasWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNN 82

                          90       100
                  ....*....|....*....|....*..
gi 281604094 1484 FSAGEDCVVI--IWHENGQWNDVPCNY 1508
Cdd:cd03603    83 GGGNEDYAAInhFPGISGKWNDLANSY 109
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 1406-1514 5.74e-18

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


Pssm-ID: 153062  Cd Length: 115  Bit Score: 81.27  E-value: 5.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1406 YKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFVN----RVGHDYQWIGLNDKMFEhdFRW--TDGSALQYENWRPNQ 1479
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgfalKYNLGYYWIDGNDINNE--GTWvdTDKKELEYKNWAPGE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 281604094 1480 PDSffSAGEDCVVIIWHENGQWNDVPCNYHLTYTC 1514
Cdd:cd03592    81 PNN--GRNENCLEIYIKDNGKWNDEPCSKKKSAIC 113
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 1407-1514 6.00e-17

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: 78.11  E-value: 6.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1407 KYFA---HRRTWDAAERECRLQGAHLTSILSHEE----QMFVNRvGHDYQWIGLNDKMFEHDFRWTDGSALQYENWRPNQ 1479
Cdd:cd03591     2 KIFVtngEEKNFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVKK-GNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 281604094 1480 PDSFFSaGEDCVVIIwhENGQWNDVPCNYHLTYTC 1514
Cdd:cd03591    81 PNNAGG-GEDCVEMY--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 ...
 252-346 1.82e-15

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


Pssm-ID: 239592  Cd Length: 93  Bit Score: 73.27  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  252 VFHITAPS---KFTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRTLYRF 328
Cdd:cd03515     2 VFHLRSRSgkyKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGIVDYGPR 81

                          90
                  ....*....|....*...
gi 281604094  329 ENQTcfplpdSRFDAYCF 346
Cdd:cd03515    82 LNLS------ERWDAYCY 93
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 1394-1516 1.11e-13

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 68.90  E-value: 1.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1394 CDYGWHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFV-NRVGHDYQWIGLNDKMFEHDFRWTDGSALqy 1472
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLqSQIGSSSYWIGLSREKSEKPWKWIDGSPL-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 281604094 1473 enwrpnqPDSFFSAGED----CVVIiwHENGQWNDVpCNYHLTYTCKK 1516
Cdd:cd03593    79 -------NNLFNIRGSTksgnCAYL--SSTGIYSED-CSTKKRWICEK 116
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 1401-1515 1.96e-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: 66.45  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1401 FQGQCYK--YF---AHRRTWDAAERECRLQGAHLTSILSHEEQMFVNRVGHDYQ------WIGL---NDKMFEHD----- 1461
Cdd:cd03595     8 TEKPCYKiaYFqdsRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRasdgdfWIGLrrsSQYNVTSSacssl 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281604094 1462 FRWTDGSALQYENWRPNQPdsffSAGEDCVVIIWHENG-----------QWNDVPCNYHLTYTCK 1515
Cdd:cd03595    88 YYWLDGSISTFRNWYVDEP----SCGSEVCVVMYHQPSapagqggpylfQWNDDNCNMKNNFICK 148
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 27-147 2.97e-12

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 64.79  E-value: 2.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094    27 EENPPVKGSLSGKVILPCHFSTlptlppdYNTSEFLRIKWSKievdknGKDIKETTVLVA-QDGNIKIGQDyKGRVSVPT 105
Cdd:pfam07686    1 QTPREVTVALGGSVTLPCTYSS-------SMSEASTSVYWYR------QPPGKGPTFLIAyYSNGSEEGVK-KGRFSGRG 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 281604094   106 HPDdVGDASLTMVKLRASDAGVYRCDVMY-GIEDTQNTMSLAV 147
Cdd:pfam07686   67 DPS-NGDGSLTIQNLTLSDSGTYTCAVIPsGEGVFGKGTRLTV 108
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 1403-1514 7.80e-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: 63.62  E-value: 7.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1403 GQCYKYFAHRRTWDAAERECR-LQGAHLTSILS---HEE-QMFVNRVGHDYQWIG--LNDKMFEHDFRWTDGSALQYENW 1475
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRrCYRGNLASIHSfafNYRvQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYW 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 281604094 1476 RPNQPdsfFSAGEDCVVIIwHENGQWNDVPCNYHLTYTC 1514
Cdd:cd03598    81 APGQP---GNRRGHCVELC-TRGGHWRRAHCKLRRPFIC 115
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1352-1388 2.50e-11

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: 59.57  E-value: 2.50e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 281604094 1352 DFDECHS-NPCRNGATCVDGLNTFRCLCLPSYVGALCE 1388
Cdd:cd00054     1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1316-1350 1.44e-10

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: 57.65  E-value: 1.44e-10
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 281604094 1316 DLCKT-NPCLNGGTCYPTETSYVCTCAPGYSGDQCE 1350
Cdd:cd00054     3 DECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1521-1577 2.46e-10

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


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 57.47  E-value: 2.46e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094 1521 CGQPPVVENAKTFGKmKPRYEINSLIRYHCKDGFIQRHLPTIRCLGNGRWAMPKITC 1577
Cdd:cd00033     1 CPPPPVPENGTVTGS-KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
EGF_CA smart00179
Calcium-binding EGF-like domain;
1352-1388 2.90e-10

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 56.87  E-value: 2.90e-10
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 281604094   1352 DFDECHS-NPCRNGATCVDGLNTFRCLCLPSYV-GALCE 1388
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 159-244 3.06e-09

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


Pssm-ID: 239593  Cd Length: 144  Bit Score: 57.08  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  159 SRYTLNFESAQQACLDIGAVIATPEQLFAAYEDGFEQCDAGWLSDQTVRYPIRAPREGCygdmmGKEGVRTYGFRSP-QE 237
Cdd:cd03516    15 GRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLC-----GKNGTGVYILNSNlSS 89


                  ....*..
gi 281604094  238 TYDVYCY 244
Cdd:cd03516    90 RYDAYCY 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 ...
 1445-1516 3.30e-09

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


Pssm-ID: 153071  Cd Length: 119  Bit Score: 56.39  E-value: 3.30e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281604094 1445 GHDYqWIGLND-KMFEHDFRWTDGSAL--QYENWRPNQPDSFFSAgEDCVViIWHENGQWNDVPCNYHLTYTCKK 1516
Cdd:cd03601    48 GHGY-WVGADNlQDGEYDFLWNDGVSLptDSDLWAPNEPSNPQSR-QLCVQ-LWSKYNLLDDEYCGRAKRVICEK 119
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1318-1348 6.17e-09

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: 52.77  E-value: 6.17e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 281604094  1318 CKTNPCLNGGTCYPTETSYVCTCAPGYSGDQ 1348
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1321-1350 1.13e-08

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: 52.09  E-value: 1.13e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 281604094 1321 NPCLNGGTCYPTETSYVCTCAPGYSGDQ-CE 1350
Cdd:cd00053     6 NPCSNGGTCVNTPGSYRCVCPPGYTGDRsCE 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
1316-1350 2.69e-08

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 51.09  E-value: 2.69e-08
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 281604094   1316 DLCKT-NPCLNGGTCYPTETSYVCTCAPGYS-GDQCE 1350
Cdd:smart00179    3 DECASgNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 1400-1514 5.65e-08

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 53.16  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1400 KFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEqmfvNRVGHDYQ----------WIGLNDKMFEHDFRWTDGSA 1469
Cdd:cd03596     6 KIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDE----NDALRDYVkasvpgnwevWLGINDMVAEGKWVDVNGSP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 281604094 1470 LQYENWR---PNQPDSffSAGEDCVVIIWHENGQWNDVPCNYHLTYTC 1514
Cdd:cd03596    82 ISYFNWEreiTAQPDG--GKRENCVALSSSAQGKWFDEDCRREKPYVC 127
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 263-345 6.79e-08

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: 51.85  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  263 FEEAEAECANRDARLATVGEL-HAAWRNGFDQCDYGWLSDASVrhPVTVARAQCGGGLLGVRTLYRFENQtcfPLPDSRF 341
Cdd:cd03521    16 LRAARQSCASLGARLASAAELrRAVVECFFSACARGWLADGTV--GTTVCNPVVAEALKAVDVKVEIETN---PIPFAHY 90


                  ....
gi 281604094  342 DAYC 345
Cdd:cd03521    91 NALC 94
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 1412-1507 6.84e-08

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: 52.38  E-value: 6.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1412 RRTWDAAERECRLQGAHLTSILSHEEQ---MFVNRVGHDYQWIGLNDKMFEhdFRWTDGSALQYENWRPNQPDsffsAGE 1488
Cdd:cd03602     9 SKTWSEAQQYCRENYTDLATVQNQEDNallSNLSRVSNSAAWIGLYRDVDS--WRWSDGSESSFRNWNTFQPF----GQG 82

                          90
                  ....*....|....*....
gi 281604094 1489 DCVVIIwhENGQWNDVPCN 1507
Cdd:cd03602    83 DCATMY--SSGRWYAALCS 99
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 1521-1577 8.31e-08

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


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 50.22  E-value: 8.31e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094   1521 CGQPPVVENAKTFGKmKPRYEINSLIRYHCKDGFIQRHLPTIRCLGNGRWAMPKITC 1577
Cdd:smart00032    1 CPPPPDIENGTVTSS-SGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1356-1384 2.33e-07

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


Pssm-ID: 394967  Cd Length: 31  Bit Score: 48.15  E-value: 2.33e-07
                           10        20
                   ....*....|....*....|....*....
gi 281604094  1356 CHSNPCRNGATCVDGLNTFRCLCLPSYVG 1384
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTG 29
Sushi pfam00084
Sushi repeat (SCR repeat);
1521-1577 3.09e-07

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 48.65  E-value: 3.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094  1521 CGQPPVVENAKTFGKmKPRYEINSLIRYHCKDGFIQRHLPTIRCLGNGRWAMPKITC 1577
Cdd:pfam00084    1 CPPPPDIPNGKVSAT-KNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1355-1388 3.76e-07

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: 47.86  E-value: 3.76e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 281604094 1355 ECH-SNPCRNGATCVDGLNTFRCLCLPSYVGAL-CE 1388
Cdd:cd00053     1 ECAaSNPCSNGGTCVNTPGSYRCVCPPGYTGDRsCE 36
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 39-132 4.81e-07

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 50.14  E-value: 4.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   39 KVILPCHFstlpTL-PPDYNTsefLRIKWSKIEVDKNgkdikETTVLVAQDGNI--KIGQDYKGRVSVpTHPDDVGDASL 115
Cdd:cd20960    17 NVTLPCHH----QLgLEDQGT---LDIEWLLLPSDKV-----EKVVITYSGDRVynHYYPALKGRVAF-TSNDLSGDASL 83

                          90
                  ....*....|....*..
gi 281604094  116 TMVKLRASDAGVYRCDV 132
Cdd:cd20960    84 NISNLKLSDTGTYQCKV 100
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 1402-1515 6.27e-07

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: 50.51  E-value: 6.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094 1402 QGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFVNRV------GHDYQ----WIGLN--------DKMFEHDFR 1463
Cdd:cd03600     3 SDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLlaagpgRHGRGslrlWIGLQreprqcsdPSLPLRGFS 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281604094 1464 W-TDGSALQYENWrPNQPDSFFSAgEDCVVI----IWHENGQWNDVPCNYHLT-YTCK 1515
Cdd:cd03600    83 WvTGDQDTDFSNW-LQEPAGTCTS-PRCVALsaagSTPDNLKWKDGPCSARADgYLCK 138
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 252-347 8.90e-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: 50.15  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  252 VFHITAPSK--FTFEEAEAECANRDARLATVGELHAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRTLYRFE 329
Cdd:cd03516     8 VFLVEKNGRysLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGTGVYILNSNL 87

                          90
                  ....*....|....*...
gi 281604094  330 NqtcfplpdSRFDAYCFK 347
Cdd:cd03516    88 S--------SRYDAYCYN 97
IGv smart00406
Immunoglobulin V-Type;
40-132 2.96e-06

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 46.61  E-value: 2.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094     40 VILPCHFSTlptlppdyNTSEFLRIKWSKievDKNGKdIKETTVLVAQDGNIKIGQDYKGRVSVPTHPDDvGDASLTMVK 119
Cdd:smart00406    2 VTLSCKFSG--------STFSSYYVSWVR---QPPGK-GLEWLGYIGSNGSSYYQESYKGRFTISKDTSK-NDVSLTISN 68

                            90
                    ....*....|...
gi 281604094    120 LRASDAGVYRCDV 132
Cdd:smart00406   69 LRVEDTGTYYCAV 81
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 1323-1344 8.56e-06

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


Pssm-ID: 463660  Cd Length: 22  Bit Score: 43.86  E-value: 8.56e-06
                           10        20
                   ....*....|....*....|..
gi 281604094  1323 CLNGGTCYPTETSYVCTCAPGY 1344
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22
EGF smart00181
Epidermal growth factor-like domain;
1318-1350 1.46e-05

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 43.27  E-value: 1.46e-05
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 281604094   1318 CKT-NPCLNGgTCYPTETSYVCTCAPGYSGD-QCE 1350
Cdd:smart00181    2 CASgGPCSNG-TCINTPGSYTCSCPPGYTGDkRCE 35
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1393-1469 1.59e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 47.80  E-value: 1.59e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281604094 1393 TCDYGWHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFVNRVGHDY-QWIGLNDKMFEHDFRWTDGSA 1469
Cdd:PHA02642   87 TCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSdHWIGLNRESSNHPWKWADNSN 164
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 163-206 8.64e-05

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: 42.99  E-value: 8.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 281604094  163 LNFESAQQACLDIGAVIATPEQLFAAYED-GFEQCDAGWLSDQTV 206
Cdd:cd03521    14 LGLRAARQSCASLGARLASAAELRRAVVEcFFSACARGWLADGTV 58
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 29-132 8.78e-05

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


Pssm-ID: 409383  Cd Length: 113  Bit Score: 43.59  E-value: 8.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   29 NPPVKGSLSGKVILPCHFstlptLPPdyNTSEFLRIKWSKIevdkNGKDIKETTVLVAQDGnIKIGQDYKGRVSVPTHPD 108
Cdd:cd05718     6 PTEVTGFLGGSVTLPCSL-----TSP--GTTKITQVTWMKI----GAGSSQNVAVFHPQYG-PSVPNPYAERVEFLAARL 73

                          90       100
                  ....*....|....*....|....
gi 281604094  109 DVGDASLTMVKLRASDAGVYRCDV 132
Cdd:cd05718    74 GLRNATLRIRNLRVEDEGNYICEF 97
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 1361-1380 9.33e-05

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


Pssm-ID: 463660  Cd Length: 22  Bit Score: 40.78  E-value: 9.33e-05
                           10        20
                   ....*....|....*....|
gi 281604094  1361 CRNGATCVDGLNTFRCLCLP 1380
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPP 20
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 1383-1515 1.02e-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: 47.38  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  1383 VGALCEQDTETcdygwHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHE--EQMFVNRVGHDYQ---WIGLND-- 1455
Cdd:TIGR00864  314 SHPHCPKDGEI-----FEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDalQNFLARKVTHSLDrgvWIGFSDvn 388

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281604094  1456 KMFEHDFRWTDGSALQY-ENWRPnqPDSFFSAGEDCVVIiwHENGQWNDVPCNYHLTYTCK 1515
Cdd:TIGR00864  389 GAEKGPAHQGEAFEAEEcEEGLA--GEPHPARAEHCVRL--DPRGQCNSDLCNAPHAYVCE 445
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 766-1193 1.06e-04

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


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.22  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   766 ILTRLETDVPTSDEDVTSAHLTHSTlnvEVVTVLKWPGNEDNSTSKPLPPTERAGFTKSPPVSLS-TVGIVGKDKETPSF 844
Cdd:pfam05109  404 IITRTATNATTTTHKVIFSKAPEST---TTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGpTVSTADVTSPTPAG 480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   845 TDGGDEytlSLDGTPKPLEKFSEE---DLTSGEFAVTIPTSISIDSAEKSTLGEPTTGDRVLSTTSTKDLVINATVEGSA 921
Cdd:pfam05109  481 TTSGAS---PVTPSPSPRDNGTESkapDMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATS 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   922 LDEDMDASKPLFTATPFVHTSDVE---------ESAFVNYSSTQQPTTYVDISHTSPLSIIPKTEWSVSETSVPLEDEVL 992
Cdd:pfam05109  558 PTPAVTTPTPNATIPTLGKTSPTSavttptpnaTSPTVGETSPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNIT 637

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   993 GKSDQD-TLEQTHLEATMSPEA----------LSTIEVTQGE--TQEEPQTPGIPFPALSSTAVMTKETTAFEEEGEGST 1059
Cdd:pfam05109  638 SSSTSSmSLRPSSISETLSPSTsdnstshmplLTSAHPTGGEniTQVTPASTSTHHVSTSSPAPRPGTTSQASGPGNSST 717

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094  1060 YTLSEDRLMTD--------SEIVPSLETT--PVGTSYPGGAMTQQGVEMDTMVTQMSSIRPTVVL---STEPEVSYEAEG 1126
Cdd:pfam05109  718 STKPGEVNVTKgtppknatSPQAPSGQKTavPTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYggdSTTPRTRYNATT 797

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281604094  1127 SSPMEFASTLKPFGTQVTQLVeetTEEGKKTPLDYTdlgsglfEQPRVTELPDFSMTPSDISVFTAI 1193
Cdd:pfam05109  798 YLPPSTSSKLRPRWTFTSPPV---TTAQATVPVPPT-------SQPRFSNLSMLVLQWASLAVLTLL 854
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 1318-1347 1.56e-04

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 40.27  E-value: 1.56e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 281604094  1318 CKTNpclNGG-----TCYPTETSYVCTCAPGYSGD 1347
Cdd:pfam12947    1 CSDN---NGGchpnaTCTNTGGSFTCTCNDGYTGD 32
IgV_1_JAM1-like cd20946
First Ig-like domain of Junctional adhesion molecule-1 (JAM1)and similar domains; a member of ...
 40-132 2.16e-04

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


Pssm-ID: 409538  Cd Length: 102  Bit Score: 42.14  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   40 VILPCHFSTLPTLPpdyntseflRIKWSKIEvdkngkdiKETTVLVAQDGniKIGQDYKGRVSVPthpddvgDASLTMVK 119
Cdd:cd20946    17 VILSCKTPKKTSSP---------RVEWKKLQ--------RDVTFVVFQNN--KIQGDYKGRAEIL-------GTNITIKN 70

                          90
                  ....*....|...
gi 281604094  120 LRASDAGVYRCDV 132
Cdd:cd20946    71 VTRSDSGKYRCEV 83
IgV_CD80 cd16086
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here ...
 32-132 2.66e-04

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


Pssm-ID: 319335  Cd Length: 105  Bit Score: 42.05  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   32 VKGSLSGKVILPChfstlptlppDYNTS----EFLRIKWSKievdkngkdiKETTVLVAQDGNIKIGQDYKGRvsvpTHP 107
Cdd:cd16086     4 VTKSVKEKALLSC----------DYNVSvdelAQVRIYWQK----------DDKMVLTIISGDVKVWPEYKNR----TLF 59

                          90       100
                  ....*....|....*....|....*
gi 281604094  108 DDVGDASLTMVKLRASDAGVYRCDV 132
Cdd:cd16086    60 DITNNLSIVILALRLSDRGTYTCVV 84
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
 34-130 9.94e-04

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.


Pssm-ID: 409576  Cd Length: 110  Bit Score: 40.27  E-value: 9.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   34 GSLSGKVILPCHFStlptlpPDYNTSEfLRIKWSKIEVD------KNGKDikettVLVAQDgnikigQDYKGRVSVPTHP 107
Cdd:cd20984     9 GNIGEDGILSCTFT------PDIKLSD-IVIQWLKEGDSglvhefKEGKD-----ELSRQS------PMFRGRTSLFADQ 70

                          90       100
                  ....*....|....*....|...
gi 281604094  108 DDVGDASLTMVKLRASDAGVYRC 130
Cdd:cd20984    71 VHVGNASLRLKNVQLTDAGTYLC 93
EGF smart00181
Epidermal growth factor-like domain;
1355-1388 1.55e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 37.50  E-value: 1.55e-03
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 281604094   1355 ECHS-NPCRNGaTCVDGLNTFRCLCLPSYVGAL-CE 1388
Cdd:smart00181    1 ECASgGPCSNG-TCINTPGSYTCSCPPGYTGDKrCE 35
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 28-147 2.13e-03

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 39.29  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094   28 ENPPVKGSLSGKVILPCHFstlptlPPdynTSEFLrIKWSKIEVDK------NGKDikettVLVAQDgnikigQDYKGRV 101
Cdd:cd16091     3 SEVIVVCLLSEDCILPCSF------TP---GSEVV-IHWYKQDSDIkvhsyyYGKD-----QLESQD------QRYRNRT 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 281604094  102 SVPTHPDDVGDASLTMVKLRASDAGVYRCDVMYGIEDTQNTMSLAV 147
Cdd:cd16091    62 SLFKDQISNGNASLLLRRVQLQDEGRYKCYTSTIIGNQESFVNLKV 107
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 30-147 3.43e-03

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: 38.26  E-value: 3.43e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604094     30 PPVKGSLSGKVILPCHFSTLPTLppdyntseflRIKWskievdkngkdIKETTVLVAQDGNIKIGQDYkgrvsvpthpdd 109
Cdd:smart00410    2 PSVTVKEGESVTLSCEASGSPPP----------EVTW-----------YKQGGKLLAESGRFSVSRSG------------ 48

                            90       100       110
                    ....*....|....*....|....*....|....*...
gi 281604094    110 vGDASLTMVKLRASDAGVYRCDVMYGIEDTQNTMSLAV 147
Cdd:smart00410   49 -STSTLTISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 1394-1463 4.37e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 39.46  E-value: 4.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281604094 1394 CDYGWHKFQGQCYKYFAHRRTWDAAERECRLQGAHLTSILSHEEQMFVNRV--GHDYqWIGLNDKMFEHDFR 1463
Cdd:PHA03097   46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYkgGQDL-WIGIEKKKGDDDDR 116
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 1323-1349 6.56e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 35.79  E-value: 6.56e-03
                           10        20
                   ....*....|....*....|....*..
gi 281604094  1323 CLNGGTCYPTEtsYVCTCAPGYSGDQC 1349
Cdd:pfam07974    2 CSGRGTCVNQC--GKCVCDSGYQGATC 26
 
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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