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Conserved domains on  [gi|17537005|ref|NP_496688|]
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C-type LECtin [Caenorhabditis elegans]

Protein Classification

C-type lectin and CUB domain-containing protein( domain architecture ID 10637005)

C-type lectin and CUB (for complement C1r/C1s, Uegf, Bmp1) domain-containing protein; C-type lectin domain binds carbohydrate in a calcium-dependent manner, whereas CUB domain is found almost exclusively in extracellular and plasma membrane-associated proteins, many of which are developmentally regulated

Gene Ontology:  GO:0005509|GO:0030246
PubMed:  8510165|28876846

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 309-415 8.31e-29

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 109.04  E-value: 8.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 309 CNSSVMAPSE--ITSPHFPYNYYNSDFCSYQISTLGSYNVLLRFSTFDTEK----VNDVVTVYDGDSTNDPVIGVYAGSF 382
Cdd:cd00041   1 CGGTLTASTSgtISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 17537005 383 YPFTVISTGNKMLVTFKTDKSNTRQGFSGRITS 415
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 27-153 3.37e-26

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: 102.29  E-value: 3.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005     27 CTSGFTLINGKCLRIFVDVSTHTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNAN--LFWMGLYCFDSDvSKCLWDDA 104
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdYYWIGLSDPDSN-GSWQWSDG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 17537005    105 TGSaEVYDNFAAGFPHIALGNCVYYSVQGalaGMWLSSDCNDRRSFICE 153
Cdd:smart00034  80 SGP-VSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 162-283 3.33e-19

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: 83.03  E-value: 3.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005    162 CPYN---YNGFCYTFHNTASTYTKGQKICEQECGNLASIHSANENRYIMTFGGRATKEDLL-LGGMWP-ADDVYNWVDGS 236
Cdd:smart00034   1 CPSGwisYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYwIGLSDPdSNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17537005    237 -LWEYENFDPINVRDSV--CVIMSNGDsrpialGMWYSGECKNEYSVVCK 283
Cdd:smart00034  81 gPVSYSNWAPGEPNNSSgdCVVLSTSG------GKWNDVSCTSKLPFVCE 124
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 309-415 8.31e-29

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 109.04  E-value: 8.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 309 CNSSVMAPSE--ITSPHFPYNYYNSDFCSYQISTLGSYNVLLRFSTFDTEK----VNDVVTVYDGDSTNDPVIGVYAGSF 382
Cdd:cd00041   1 CGGTLTASTSgtISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 17537005 383 YPFTVISTGNKMLVTFKTDKSNTRQGFSGRITS 415
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 27-153 3.37e-26

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: 102.29  E-value: 3.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005     27 CTSGFTLINGKCLRIFVDVSTHTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNAN--LFWMGLYCFDSDvSKCLWDDA 104
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdYYWIGLSDPDSN-GSWQWSDG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 17537005    105 TGSaEVYDNFAAGFPHIALGNCVYYSVQGalaGMWLSSDCNDRRSFICE 153
Cdd:smart00034  80 SGP-VSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 318-412 3.74e-24

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 95.92  E-value: 3.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005    318 EITSPHFPYNYYNSDFCSYQISTLGSYNVLLRFSTFDTEKVN----DVVTVYDGDSTNDPVIGVYAGSFYPFTVIST-GN 392
Cdd:smart00042   2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                           90       100
                   ....*....|....*....|
gi 17537005    393 KMLVTFKTDKSNTRQGFSGR 412
Cdd:smart00042  82 SLTLTFVSDSSVQKRGFSAR 101
CUB pfam00431
CUB domain;
315-410 2.53e-20

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 85.42  E-value: 2.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005   315 APSEITSPHFPYNYYNSDFCSYQISTLGSYNVLLRFSTFDTEKV----NDVVTVYDGDSTNDPVIGVYAGSFYPFTVIST 390
Cdd:pfam00431   8 SSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgYDYVEIRDGPSASSPLLGRFCGSGIPEDIVSS 87

                          90       100
                  ....*....|....*....|
gi 17537005   391 GNKMLVTFKTDKSNTRQGFS 410
Cdd:pfam00431  88 SNQMTIKFVSDASVQKRGFK 107
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 162-283 3.33e-19

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: 83.03  E-value: 3.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005    162 CPYN---YNGFCYTFHNTASTYTKGQKICEQECGNLASIHSANENRYIMTFGGRATKEDLL-LGGMWP-ADDVYNWVDGS 236
Cdd:smart00034   1 CPSGwisYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYwIGLSDPdSNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17537005    237 -LWEYENFDPINVRDSV--CVIMSNGDsrpialGMWYSGECKNEYSVVCK 283
Cdd:smart00034  81 gPVSYSNWAPGEPNNSSgdCVVLSTSG------GKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 37-153 2.32e-17

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: 77.66  E-value: 2.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005  37 KCLRIFVDVSTHTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNANL-FWMGLYCFDSDvSKCLWDDATGSAEvYDNFA 115
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSE-GTWKWSDGSPLVD-YTNWA 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17537005 116 AGFPHIA-LGNCVYYSVQGalAGMWLSSDCNDRRSFICE 153
Cdd:cd00037  79 PGEPNPGgSEDCVVLSSSS--DGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 169-284 4.89e-16

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: 73.81  E-value: 4.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 169 FCYTFHNTASTYTKGQKICEQECGNLASIHSANENRYIMTFGGRATKEDLLLGGMWPADD-VYNWVDGS-LWEYENFD-- 244
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEgTWKWSDGSpLVDYTNWApg 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17537005 245 -PINVRDSVCVIMSNGDSrpialGMWYSGECKNEYSVVCKR 284
Cdd:cd00037  81 ePNPGGSEDCVVLSSSSD-----GKWNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 47-153 6.15e-11

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 59.03  E-value: 6.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005    47 THTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNANLFWMGLycFDSDVSKCL-WDDatGSAEVYDNFAAGFPHIA-LG 124
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGL--TDRKNEGTWkWVD--GSPVNYTNWAPEPNNNGeNE 78

                          90       100
                  ....*....|....*....|....*....
gi 17537005   125 NCVYYSvqgALAGMWLSSDCNDRRSFICE 153
Cdd:pfam00059  79 DCVELS---SSSGKWNDENCNSKNPFVCE 104
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 25-154 1.60e-07

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: 53.93  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005     25 PVCTSGFTLI--NGKCLRIFVDVSTHTAAEKTCKGY-GATLVTVKN-SIDNRAIADFTGNNANLFWMGLYCFDS-DVSKC 99
Cdd:TIGR00864  316 PHCPKDGEIFeeNGHCFQIVPEEAAWLDAQEQCLARaGAALAIVDNdALQNFLARKVTHSLDRGVWIGFSDVNGaEKGPA 395

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17537005    100 LWDDATgSAEVYDNFAAGFPHIALGN-CVYYSVQGalagmWLSSD-CNDRRSFICEL 154
Cdd:TIGR00864  396 HQGEAF-EAEECEEGLAGEPHPARAEhCVRLDPRG-----QCNSDlCNAPHAYVCEL 446
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 179-284 2.89e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 40.15  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005   179 TYTKGQKICEQECGNLASIHSANENRYIMTFGGRATK------EDLLLGGMWpaddvyNWVDGSLWEYENFD--PINVRD 250
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKyfwiglTDRKNEGTW------KWVDGSPVNYTNWApePNNNGE 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 17537005   251 SV-CVIMSNGDsrpialGMWYSGECKNEYSVVCKR 284
Cdd:pfam00059  77 NEdCVELSSSS------GKWNDENCNSKNPFVCEK 105
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 27-152 2.55e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 38.31  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005   27 CTSGFTLINGKCLRIFVDVSTHTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNAnlFWMGlycfdsDVSKCLWDDatg 106
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQD--LWIG------IEKKKGDDD--- 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 17537005  107 SAEVYDNFAAGfPHIalGNCVYYSVQGalagmWLSSDCNDRRSFIC 152
Cdd:PHA03097 115 DREVLDKVVKP-PKS--GKCAYLKDKT-----IISSNCNATKGWIC 152
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 309-415 8.31e-29

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 109.04  E-value: 8.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 309 CNSSVMAPSE--ITSPHFPYNYYNSDFCSYQISTLGSYNVLLRFSTFDTEK----VNDVVTVYDGDSTNDPVIGVYAGSF 382
Cdd:cd00041   1 CGGTLTASTSgtISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 17537005 383 YPFTVISTGNKMLVTFKTDKSNTRQGFSGRITS 415
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 27-153 3.37e-26

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: 102.29  E-value: 3.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005     27 CTSGFTLINGKCLRIFVDVSTHTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNAN--LFWMGLYCFDSDvSKCLWDDA 104
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdYYWIGLSDPDSN-GSWQWSDG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 17537005    105 TGSaEVYDNFAAGFPHIALGNCVYYSVQGalaGMWLSSDCNDRRSFICE 153
Cdd:smart00034  80 SGP-VSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 318-412 3.74e-24

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 95.92  E-value: 3.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005    318 EITSPHFPYNYYNSDFCSYQISTLGSYNVLLRFSTFDTEKVN----DVVTVYDGDSTNDPVIGVYAGSFYPFTVIST-GN 392
Cdd:smart00042   2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVISSsSN 81

                           90       100
                   ....*....|....*....|
gi 17537005    393 KMLVTFKTDKSNTRQGFSGR 412
Cdd:smart00042  82 SLTLTFVSDSSVQKRGFSAR 101
CUB pfam00431
CUB domain;
315-410 2.53e-20

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 85.42  E-value: 2.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005   315 APSEITSPHFPYNYYNSDFCSYQISTLGSYNVLLRFSTFDTEKV----NDVVTVYDGDSTNDPVIGVYAGSFYPFTVIST 390
Cdd:pfam00431   8 SSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHdecgYDYVEIRDGPSASSPLLGRFCGSGIPEDIVSS 87

                          90       100
                  ....*....|....*....|
gi 17537005   391 GNKMLVTFKTDKSNTRQGFS 410
Cdd:pfam00431  88 SNQMTIKFVSDASVQKRGFK 107
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 162-283 3.33e-19

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: 83.03  E-value: 3.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005    162 CPYN---YNGFCYTFHNTASTYTKGQKICEQECGNLASIHSANENRYIMTFGGRATKEDLL-LGGMWP-ADDVYNWVDGS 236
Cdd:smart00034   1 CPSGwisYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYwIGLSDPdSNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17537005    237 -LWEYENFDPINVRDSV--CVIMSNGDsrpialGMWYSGECKNEYSVVCK 283
Cdd:smart00034  81 gPVSYSNWAPGEPNNSSgdCVVLSTSG------GKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 37-153 2.32e-17

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: 77.66  E-value: 2.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005  37 KCLRIFVDVSTHTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNANL-FWMGLYCFDSDvSKCLWDDATGSAEvYDNFA 115
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSE-GTWKWSDGSPLVD-YTNWA 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17537005 116 AGFPHIA-LGNCVYYSVQGalAGMWLSSDCNDRRSFICE 153
Cdd:cd00037  79 PGEPNPGgSEDCVVLSSSS--DGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 169-284 4.89e-16

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: 73.81  E-value: 4.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 169 FCYTFHNTASTYTKGQKICEQECGNLASIHSANENRYIMTFGGRATKEDLLLGGMWPADD-VYNWVDGS-LWEYENFD-- 244
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEgTWKWSDGSpLVDYTNWApg 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17537005 245 -PINVRDSVCVIMSNGDSrpialGMWYSGECKNEYSVVCKR 284
Cdd:cd00037  81 ePNPGGSEDCVVLSSSSD-----GKWNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 47-153 6.15e-11

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 59.03  E-value: 6.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005    47 THTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNANLFWMGLycFDSDVSKCL-WDDatGSAEVYDNFAAGFPHIA-LG 124
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGL--TDRKNEGTWkWVD--GSPVNYTNWAPEPNNNGeNE 78

                          90       100
                  ....*....|....*....|....*....
gi 17537005   125 NCVYYSvqgALAGMWLSSDCNDRRSFICE 153
Cdd:pfam00059  79 DCVELS---SSSGKWNDENCNSKNPFVCE 104
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 36-152 1.61e-09

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 55.15  E-value: 1.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005  36 GKCLRIFVDVSTHTAAEKTCKG-YGATLVTVKN-SIDNRAIADFTGNNANLFWMG--LYCfDSDVSKCLWDDatGSAEVY 111
Cdd:cd03598   1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIHSfAFNYRVQRLVSTLNQAQVWIGgiITG-KGRCRRFSWVD--GSVWNY 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17537005 112 DNFAAGFPHIALGNCVYYSVQGalaGMWLSSDCNDRRSFIC 152
Cdd:cd03598  78 AYWAPGQPGNRRGHCVELCTRG---GHWRRAHCKLRRPFIC 115
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 27-153 4.26e-09

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 54.32  E-value: 4.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005  27 CTSGfTLINGKCLRIFVDVSTHTAAEKTCKGYGATLVTVKNSIDNRAIADF---TGNNANLFWMGLycfdSD-VSKCLWD 102
Cdd:cd03596   1 CLKG-TKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYvkaSVPGNWEVWLGI----NDmVAEGKWV 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17537005 103 DATGSAEVYDNFAAGFPHIALG----NCVYYSvqGALAGMWLSSDCNDRRSFICE 153
Cdd:cd03596  76 DVNGSPISYFNWEREITAQPDGgkreNCVALS--SSAQGKWFDEDCRREKPYVCE 128
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 166-283 4.52e-08

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: 51.59  E-value: 4.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 166 YNGFCYTFHNTASTYTKGqkicEQEC---------GNLASIHSANENRYIMTFGGRATKEDlLLGGMW------PADDVY 230
Cdd:cd03589   8 FGGYCYRFFGDRLTWEEA----ELRCrsfsipgliAHLVSIHSQEENDFVYDLFESSRGPD-TPYGLWiglhdrTSEGPF 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17537005 231 NWVDGSLWEYENFDPINVRDSV----CVIMSngdSRPIALGMWYSGECKNEYSVVCK 283
Cdd:cd03589  83 EWTDGSPVDFTKWAGGQPDNYGgnedCVQMW---RRGDAGQSWNDMPCDAVFPYICK 136
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 25-154 1.60e-07

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: 53.93  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005     25 PVCTSGFTLI--NGKCLRIFVDVSTHTAAEKTCKGY-GATLVTVKN-SIDNRAIADFTGNNANLFWMGLYCFDS-DVSKC 99
Cdd:TIGR00864  316 PHCPKDGEIFeeNGHCFQIVPEEAAWLDAQEQCLARaGAALAIVDNdALQNFLARKVTHSLDRGVWIGFSDVNGaEKGPA 395

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 17537005    100 LWDDATgSAEVYDNFAAGFPHIALGN-CVYYSVQGalagmWLSSD-CNDRRSFICEL 154
Cdd:TIGR00864  396 HQGEAF-EAEECEEGLAGEPHPARAEhCVRLDPRG-----QCNSDlCNAPHAYVCEL 446
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 170-282 2.52e-07

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: 48.99  E-value: 2.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 170 CYTFHNTASTYTKGQKICeQEC--GNLASIHSANENRYIMTFGGRATKEDLLLGGM---WPADDVYNWVDGSLWEYENFD 244
Cdd:cd03598   3 CYRFVKSPRTFRDAQVIC-RRCyrGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIitgKGRCRRFSWVDGSVWNYAYWA 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17537005 245 PIN--VRDSVCVIMSNGDsrpialGMWYSGECKNEYSVVC 282
Cdd:cd03598  82 PGQpgNRRGHCVELCTRG------GHWRRAHCKLRRPFIC 115
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 171-284 5.53e-07

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: 48.14  E-value: 5.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 171 YTFHNTASTYTKGQKICEQECGNLASIHSANENRYImtFGGRATkedLLLGGMW----PADDVYNWVD--GSLWEYENF- 243
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALL--NGFALK---YNLGYYWidgnDINNEGTWVDtdKKELEYKNWa 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17537005 244 --DPINVRDSVCVIMSNGDSrpialGMWYSGECKNEYSVVCKR 284
Cdd:cd03592  78 pgEPNNGRNENCLEIYIKDN-----GKWNDEPCSKKKSAICYT 115
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 41-152 2.80e-06

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: 45.83  E-value: 2.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005  41 IFVDVS-THTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNANLFWMGLYcFDSDvskcLWDDATGSAEVYDNFAAGFP 119
Cdd:cd03602   4 YLVNESkTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLY-RDVD----SWRWSDGSESSFRNWNTFQP 78

                        90       100       110
                ....*....|....*....|....*....|...
gi 17537005 120 HIAlGNCVYYSVQGAlagmWLSSDCNDRRSFIC 152
Cdd:cd03602  79 FGQ-GDCATMYSSGR----WYAALCSALKPFIC 106
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 170-283 8.09e-06

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: 45.65  E-value: 8.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 170 CYT---FHNTA--STYTKGQKICEQECGNLASIHSANENRYIMTF--GGRATKEDLLLgGMWPAD----------DVYNW 232
Cdd:cd03595  12 CYKiayFQDSRrrLNFEEARQACREDGGELLSIESENEQKLIERFiqTLRASDGDFWI-GLRRSSqynvtssacsSLYYW 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17537005 233 VDGSLWEYEN--FDPINVRDSVCVIMSNGDSRPIALG-----MWYSGECKNEYSVVCK 283
Cdd:cd03595  91 LDGSISTFRNwyVDEPSCGSEVCVVMYHQPSAPAGQGgpylfQWNDDNCNMKNNFICK 148
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 47-153 1.13e-05

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: 44.29  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005  47 THTAAEKTCKGYGATLVTVKNSIDNRAIADFTGN-NANLFWMGLycfdSDVSK-CLWDDATGSAEVYDNFAAGFPHIALG 124
Cdd:cd03592  11 TFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKyNLGYYWIDG----NDINNeGTWVDTDKKELEYKNWAPGEPNNGRN 86

                        90       100       110
                ....*....|....*....|....*....|..
gi 17537005 125 -NCV--YYSvqgaLAGMWLSSDCNDRRSFICE 153
Cdd:cd03592  87 eNCLeiYIK----DNGKWNDEPCSKKKSAICY 114
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 36-153 2.29e-05

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: 43.47  E-value: 2.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005  36 GKCLRIFVDVSTHTAAEKTCKGYGATLVTvknsIDNRAIADFTGNN--ANLFWMGLYcFDSDVSKCLWDDatGSAevydn 113
Cdd:cd03593  10 NKCYYFSMEKKTWNESKEACSSKNSSLLK----IDDEEELEFLQSQigSSSYWIGLS-REKSEKPWKWID--GSP----- 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17537005 114 FAAGF---PHIALGNCVYYSVQGAlagmwLSSDCNDRRSFICE 153
Cdd:cd03593  78 LNNLFnirGSTKSGNCAYLSSTGI-----YSEDCSTKKRWICE 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 179-284 2.89e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 40.15  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005   179 TYTKGQKICEQECGNLASIHSANENRYIMTFGGRATK------EDLLLGGMWpaddvyNWVDGSLWEYENFD--PINVRD 250
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKyfwiglTDRKNEGTW------KWVDGSPVNYTNWApePNNNGE 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 17537005   251 SV-CVIMSNGDsrpialGMWYSGECKNEYSVVCKR 284
Cdd:pfam00059  77 NEdCVELSSSS------GKWNDENCNSKNPFVCEK 105
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 27-152 2.55e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 38.31  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005   27 CTSGFTLINGKCLRIFVDVSTHTAAEKTCKGYGATLVTVKNSIDNRAIADFTGNNAnlFWMGlycfdsDVSKCLWDDatg 106
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQD--LWIG------IEKKKGDDD--- 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 17537005  107 SAEVYDNFAAGfPHIalGNCVYYSVQGalagmWLSSDCNDRRSFIC 152
Cdd:PHA03097 115 DREVLDKVVKP-PKS--GKCAYLKDKT-----IISSNCNATKGWIC 152
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 166-283 5.53e-03

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: 36.97  E-value: 5.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537005 166 YNGFCYTFHNTASTYTKGQKICEQ--ECGNLASIHSANEN----RYIMTFGGRatKEDLLLGGMWPA-DDVYNWVDGSLW 238
Cdd:cd03594   8 YKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAaaiaSLISSYQKA--YQPVWIGLHDPQqSRGWEWSDGSKL 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 17537005 239 EYENF--DPINVRDSVCVIMsngdSRPIALGMWYSGECKNEYSVVCK 283
Cdd:cd03594  86 DYRSWdrNPPYARGGYCAEL----SRSTGFLKWNDANCEERNPFICK 128
 
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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