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Conserved domains on  [gi|808358626|ref|NP_001256730|]
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C-type lectin domain-containing protein [Caenorhabditis elegans]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10636995)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

CATH:  3.10.100.10
Gene Ontology:  GO:0030246|GO:0120153
PubMed:  16336259|10508765
SCOP:  4002453

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 117-245 1.50e-24

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: 96.90  E-value: 1.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626   117 CTDGFTHINNKCWKLVTGPKSRADADKTCYDLGGsTLFSIRNDQENQALMEFVKDQ-KVENLWAGLICDRHgPAWCTWDL 195
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNSgSSDYYWIGLSDPDS-NGSWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 808358626   196 QSGTTaVYNNFADGWPSNEDKICNYFMTNGtqaGKWASASCTETMSFVCE 245
Cdd:smart00034  79 GSGPV-SYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 259-367 6.70e-20

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: 84.57  E-value: 6.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626   259 YDNYCYTPYFELKLSSEAQTFCASSGSNLVSIHSANENRFVYNIIPPGTETS---IGGVA-YSDDSLLWYDGTPPL-FTN 333
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDyywIGLSDpDSNGSWQWSDGSGPVsYSN 87

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 808358626   334 MIQLE----NGNCLFLYNDYVHWFGNNClTTKCHFVCK 367
Cdd:smart00034  88 WAPGEpnnsSGDCVVLSTSGGKWNDVSC-TSKLPFVCE 124
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 117-245 1.50e-24

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: 96.90  E-value: 1.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626   117 CTDGFTHINNKCWKLVTGPKSRADADKTCYDLGGsTLFSIRNDQENQALMEFVKDQ-KVENLWAGLICDRHgPAWCTWDL 195
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNSgSSDYYWIGLSDPDS-NGSWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 808358626   196 QSGTTaVYNNFADGWPSNEDKICNYFMTNGtqaGKWASASCTETMSFVCE 245
Cdd:smart00034  79 GSGPV-SYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 259-367 6.70e-20

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: 84.57  E-value: 6.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626   259 YDNYCYTPYFELKLSSEAQTFCASSGSNLVSIHSANENRFVYNIIPPGTETS---IGGVA-YSDDSLLWYDGTPPL-FTN 333
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDyywIGLSDpDSNGSWQWSDGSGPVsYSN 87

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 808358626   334 MIQLE----NGNCLFLYNDYVHWFGNNClTTKCHFVCK 367
Cdd:smart00034  88 WAPGEpnnsSGDCVVLSTSGGKWNDVSC-TSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 127-245 2.62e-15

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: 71.50  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 127 KCWKLVTGPKSRADADKTCYDLGGsTLFSIRNDQENQALMEFVKDQKVENLWAGLICDRHGPAWcTWDlqSGTTAV-YNN 205
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGG-HLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTW-KWS--DGSPLVdYTN 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 808358626 206 FADGWP-SNEDKICNYFmtNGTQAGKWASASCTETMSFVCE 245
Cdd:cd00037   77 WAPGEPnPGGSEDCVVL--SSSSDGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 262-368 1.42e-13

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: 66.49  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 262 YCYTPYFELKLSSEAQTFCASSGSNLVSIHSANENRFVYNIIPPGTETS--IGGV-AYSDDSLLWYDGTPPL-FTNMIQL 337
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvwIGLNdLSSEGTWKWSDGSPLVdYTNWAPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 808358626 338 E-----NGNCLFLYNDYV-HWFGNNClTTKCHFVCKR 368
Cdd:cd00037   81 EpnpggSEDCVVLSSSSDgKWNDVSC-SSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 135-245 1.25e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 49.40  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626  135 PKSRADADKTCYDLGGStLFSIRNDQENQALMEFVKDQKvENLWAGLICDRHGPAWcTWDlqSGTTAVYNNFADGWPSNE 214
Cdd:pfam00059   1 SKTWDEAREACRKLGGH-LVSINSAEELDFLSSTLKKSN-KYFWIGLTDRKNEGTW-KWV--DGSPVNYTNWAPEPNNNG 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 808358626  215 DKICNYFMTNGTqaGKWASASCTETMSFVCE 245
Cdd:pfam00059  76 ENEDCVELSSSS--GKWNDENCNSKNPFVCE 104
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 275-368 1.76e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 49.01  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626  275 EAQTFCASSGSNLVSIHSANENRFVYNIIP-PGTETSIG-GVAYSDDSLLWYDGTPPLFTNMIQL-----ENGNCLFLYN 347
Cdd:pfam00059   6 EAREACRKLGGHLVSINSAEELDFLSSTLKkSNKYFWIGlTDRKNEGTWKWVDGSPVNYTNWAPEpnnngENEDCVELSS 85

                          90       100
                  ....*....|....*....|.
gi 808358626  348 DYVHWFGNNClTTKCHFVCKR 368
Cdd:pfam00059  86 SSGKWNDENC-NSKNPFVCEK 105
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 125-246 8.98e-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: 41.61  E-value: 8.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626   125 NNKCWKLVTGPKSRADADKTCYDLGGSTLFSIRNDQENQALMEFVKDQKVENLWAGL-ICDRHGPAWCTW----DLQSGt 199
Cdd:TIGR00864  328 NGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFsDVNGAEKGPAHQgeafEAEEC- 406

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 808358626   200 tavyNNFADGWPS-NEDKICnyfmTNGTQAGKWASASCTETMSFVCEL 246
Cdd:TIGR00864  407 ----EEGLAGEPHpARAEHC----VRLDPRGQCNSDLCNAPHAYVCEL 446
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 117-245 1.50e-24

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: 96.90  E-value: 1.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626   117 CTDGFTHINNKCWKLVTGPKSRADADKTCYDLGGsTLFSIRNDQENQALMEFVKDQ-KVENLWAGLICDRHgPAWCTWDL 195
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNSgSSDYYWIGLSDPDS-NGSWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 808358626   196 QSGTTaVYNNFADGWPSNEDKICNYFMTNGtqaGKWASASCTETMSFVCE 245
Cdd:smart00034  79 GSGPV-SYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 259-367 6.70e-20

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: 84.57  E-value: 6.70e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626   259 YDNYCYTPYFELKLSSEAQTFCASSGSNLVSIHSANENRFVYNIIPPGTETS---IGGVA-YSDDSLLWYDGTPPL-FTN 333
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDyywIGLSDpDSNGSWQWSDGSGPVsYSN 87

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 808358626   334 MIQLE----NGNCLFLYNDYVHWFGNNClTTKCHFVCK 367
Cdd:smart00034  88 WAPGEpnnsSGDCVVLSTSGGKWNDVSC-TSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 127-245 2.62e-15

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: 71.50  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 127 KCWKLVTGPKSRADADKTCYDLGGsTLFSIRNDQENQALMEFVKDQKVENLWAGLICDRHGPAWcTWDlqSGTTAV-YNN 205
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGG-HLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTW-KWS--DGSPLVdYTN 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 808358626 206 FADGWP-SNEDKICNYFmtNGTQAGKWASASCTETMSFVCE 245
Cdd:cd00037   77 WAPGEPnPGGSEDCVVL--SSSSDGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 262-368 1.42e-13

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: 66.49  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 262 YCYTPYFELKLSSEAQTFCASSGSNLVSIHSANENRFVYNIIPPGTETS--IGGV-AYSDDSLLWYDGTPPL-FTNMIQL 337
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvwIGLNdLSSEGTWKWSDGSPLVdYTNWAPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 808358626 338 E-----NGNCLFLYNDYV-HWFGNNClTTKCHFVCKR 368
Cdd:cd00037   81 EpnpggSEDCVVLSSSSDgKWNDVSC-SSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 259-367 3.64e-09

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: 54.67  E-value: 3.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 259 YDNYCYTpYFELKLS-SEAQTFCASSGSN-----LVSIHSANENRFVYNIIPPGTETSIGGVA-------YSDDSLLWYD 325
Cdd:cd03589    8 FGGYCYR-FFGDRLTwEEAELRCRSFSIPgliahLVSIHSQEENDFVYDLFESSRGPDTPYGLwiglhdrTSEGPFEWTD 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 808358626 326 GTPPLFTNMI--QLENGNclfLYNDYVH----------WFGNNClTTKCHFVCK 367
Cdd:cd03589   87 GSPVDFTKWAggQPDNYG---GNEDCVQmwrrgdagqsWNDMPC-DAVFPYICK 136
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 274-352 3.52e-08

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: 51.27  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 274 SEAQTFCASSGSNLVSIHSANENRFVYNIIPPGTETSIGGV-AYSDDSLLWYDGTPPLFTNMIQLENGNCLFLYNDYVHW 352
Cdd:cd03603   13 EAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGASWIGASdAATEGTWKWSDGEESTYTNWGSGEPHNNGGGNEDYAAI 92
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 135-245 1.25e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 49.40  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626  135 PKSRADADKTCYDLGGStLFSIRNDQENQALMEFVKDQKvENLWAGLICDRHGPAWcTWDlqSGTTAVYNNFADGWPSNE 214
Cdd:pfam00059   1 SKTWDEAREACRKLGGH-LVSINSAEELDFLSSTLKKSN-KYFWIGLTDRKNEGTW-KWV--DGSPVNYTNWAPEPNNNG 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 808358626  215 DKICNYFMTNGTqaGKWASASCTETMSFVCE 245
Cdd:pfam00059  76 ENEDCVELSSSS--GKWNDENCNSKNPFVCE 104
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 275-368 1.76e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 49.01  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626  275 EAQTFCASSGSNLVSIHSANENRFVYNIIP-PGTETSIG-GVAYSDDSLLWYDGTPPLFTNMIQL-----ENGNCLFLYN 347
Cdd:pfam00059   6 EAREACRKLGGHLVSINSAEELDFLSSTLKkSNKYFWIGlTDRKNEGTWKWVDGSPVNYTNWAPEpnnngENEDCVELSS 85

                          90       100
                  ....*....|....*....|.
gi 808358626  348 DYVHWFGNNClTTKCHFVCKR 368
Cdd:pfam00059  86 SSGKWNDENC-NSKNPFVCEK 105
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 126-244 6.72e-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: 47.83  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 126 NKCWKLVTGPKSRADADKTCYDLGGSTLFSIRNDQENQALMEFVKDQKVENLWAGLICDRHGPAWCT-WdlQSGTTAVYN 204
Cdd:cd03598    1 GRCYRFVKSPRTFRDAQVICRRCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFsW--VDGSVWNYA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 808358626 205 NFADGWPSNEDKICNYFMTNGtqaGKWASASCTETMSFVC 244
Cdd:cd03598   79 YWAPGQPGNRRGHCVELCTRG---GHWRRAHCKLRRPFIC 115
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 117-245 6.79e-07

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: 47.75  E-value: 6.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 117 CTDGFTHINNKCWKLVTGPKSRADADKTCYDLG-GSTLFSIRNDQENQALMEFVKD--QKVENLWAGLICDRHGPAWcTW 193
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGpGAHLASIHSPAEAAAIASLISSyqKAYQPVWIGLHDPQQSRGW-EW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 808358626 194 dlQSGTTAVYNNFADGWPSNEDKICNYfMTNGTQAGKWASASCTETMSFVCE 245
Cdd:cd03594   80 --SDGSKLDYRSWDRNPPYARGGYCAE-LSRSTGFLKWNDANCEERNPFICK 128
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 255-368 7.67e-07

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: 47.68  E-value: 7.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 255 CEYNYDNY---CYtpYF--ELKLSSEAQTFCASSGSNLVSIHSANENRFVYNIIPPGTETSIG-GVAYSDDSLLWYDGTP 328
Cdd:cd03590    1 CPTNWKSFqssCY--FFstEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGlSDEETEGEWKWVDGTP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 808358626 329 PLFT---------NMIQLENGNCLFLYNDYVHWFGNNClTTKCHFVCKR 368
Cdd:cd03590   79 LNSSktfwhpgepNNWGGGGEDCAELVYDSGGWNDVPC-NLEYRWICEK 126
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 139-246 1.98e-06

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: 46.14  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 139 ADADKTCYDLGGsTLFSIRNDQENQALMEFVKdQKVENLWAGLIcdrhgpawctwDLQ--------SGTTAVYNNFADGW 210
Cdd:cd03591   14 DDAQKLCSEAGG-TLAMPRNAAENAAIASYVK-KGNTYAFIGIT-----------DLEtegqfvylDGGPLTYTNWKPGE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 808358626 211 PSN----EDkiCNYFMTNGtqagKWASASCTETMSFVCEL 246
Cdd:cd03591   81 PNNagggED--CVEMYTSG----KWNDVACNLTRLFVCEF 114
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 117-245 7.01e-05

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: 41.99  E-value: 7.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 117 CTDGfTHINNKCWKLVTGPKSRADADKTCYDLGGsTLFSIRNDQENQALMEFVKdQKVEN---LWAGlICDRHGPAwcTW 193
Cdd:cd03596    1 CLKG-TKIHKKCYLVSEETKHYHEASEDCIARGG-TLATPRDSDENDALRDYVK-ASVPGnweVWLG-INDMVAEG--KW 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 808358626 194 DLQSGTTAVYNNFADGWPSNED--KICNYFMTNGTQAGKWASASCTETMSFVCE 245
Cdd:cd03596   75 VDVNGSPISYFNWEREITAQPDggKRENCVALSSSAQGKWFDEDCRREKPYVCE 128
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 259-367 2.27e-04

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: 40.82  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 259 YDNYCYTpYFELKLS-SEAQTFCAS--SGSNLVSIHSANENRFVYNII----PPGTETSIG--------GVAYSDDSLLW 323
Cdd:cd03594    8 YKGNCYG-YFRQPLSwSDAELFCQKygPGAHLASIHSPAEAAAIASLIssyqKAYQPVWIGlhdpqqsrGWEWSDGSKLD 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 808358626 324 Y---DGTPPLftnmiqLENGNCLFLY--NDYVHWFGNNClTTKCHFVCK 367
Cdd:cd03594   87 YrswDRNPPY------ARGGYCAELSrsTGFLKWNDANC-EERNPFICK 128
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 274-366 6.50e-04

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: 38.89  E-value: 6.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 274 SEAQTFCASSGSNLVSIHSANENRFVYNIIPPGTETSIGGVAYSDDSLLWYDGTPPLFTNMIQLE---NGNCLFLYNdYV 350
Cdd:cd03602   13 SEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSWRWSDGSESSFRNWNTFQpfgQGDCATMYS-SG 91

                         90
                 ....*....|....*.
gi 808358626 351 HWFGNNCLTTKcHFVC 366
Cdd:cd03602   92 RWYAALCSALK-PFIC 106
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 125-246 8.98e-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: 41.61  E-value: 8.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626   125 NNKCWKLVTGPKSRADADKTCYDLGGSTLFSIRNDQENQALMEFVKDQKVENLWAGL-ICDRHGPAWCTW----DLQSGt 199
Cdd:TIGR00864  328 NGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFsDVNGAEKGPAHQgeafEAEEC- 406

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 808358626   200 tavyNNFADGWPS-NEDKICnyfmTNGTQAGKWASASCTETMSFVCEL 246
Cdd:TIGR00864  407 ----EEGLAGEPHpARAEHC----VRLDPRGQCNSDLCNAPHAYVCEL 446
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 153-244 1.14e-03

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: 38.12  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 153 LFSIRNDQENQALMEFVKDQKVEnLWAGLICDRhgpawCTWDLQSGTTAVYNNFADGWPSNeDKICNYFmtngTQAGKWA 232
Cdd:cd03602   26 LATVQNQEDNALLSNLSRVSNSA-AWIGLYRDV-----DSWRWSDGSESSFRNWNTFQPFG-QGDCATM----YSSGRWY 94

                         90
                 ....*....|..
gi 808358626 233 SASCTETMSFVC 244
Cdd:cd03602   95 AALCSALKPFIC 106
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 274-366 2.03e-03

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: 37.66  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 274 SEAQTFCASSGSNLVSIHSANENRFVYNIIPPGTETSIGGV---------AYSDDSLL----WYDGTPplftnmiqleNG 340
Cdd:cd03591   14 DDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGItdletegqfVYLDGGPLtytnWKPGEP----------NN 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 808358626 341 -----NCLFLYNDYvHWFGNNCLTTkCHFVC 366
Cdd:cd03591   84 agggeDCVEMYTSG-KWNDVACNLT-RLFVC 112
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 275-368 3.80e-03

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: 36.97  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 275 EAQTFCASSGSNLVSIHSANENRFVYNIIPP---------GTETSIGGV-AYSDDSLL----WYDGTPplftnmiqleNG 340
Cdd:cd03592   14 EAVKYCKSRGTDLVAIQNAEENALLNGFALKynlgyywidGNDINNEGTwVDTDKKELeyknWAPGEP----------NN 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 808358626 341 ----NCLFLY-NDYVHWFGNNClTTKCHFVCKR 368
Cdd:cd03592   84 grneNCLEIYiKDNGKWNDEPC-SKKKSAICYT 115
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 117-246 6.53e-03

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: 36.57  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358626 117 CTDGFTHINNKCWKLVTGPKSRADADKTC--YDLGG--STLFSIRNDQENQALMEFVK----DQKVENLWAGLIcDR--H 186
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCrsFSIPGliAHLVSIHSQEENDFVYDLFEssrgPDTPYGLWIGLH-DRtsE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808358626 187 GPawctWDLQSGTTAVYNNFA----DGWPSNEDkiCNYFMTNGTQAGKWASASCTETMSFVCEL 246
Cdd:cd03589   80 GP----FEWTDGSPVDFTKWAggqpDNYGGNED--CVQMWRRGDAGQSWNDMPCDAVFPYICKM 137
 
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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