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Conserved domains on  [gi|767917241|ref|XP_011509122|]
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secretory phospholipase A2 receptor isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
beta-trefoil_Ricin_PLA2R1 cd23410
ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor ...
38-156 2.18e-62

ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor (PLA2R1) and similar proteins; PLA2R1, also called PLA2-R, PLA2R, 180 kDa secretory phospholipase A2 receptor, C-type lectin domain family 13 member C (CLEC13C), or M-type receptor, is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine production during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. PLA2R1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


:

Pssm-ID: 467788  Cd Length: 118  Bit Score: 208.06  E-value: 2.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   38 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRC 117
Cdd:cd23410     1 KGMFILESESLKKCISADKSGLFLENCDQPSDSMLWKWVSRHRLFNLGSSMCLGLNLSYPQQPLGLFECDSTLRTLWWRC 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767917241  118 NRKMITGPLQYSVQVAHDnTVVASRKYIHKWISYGSGGG 156
Cdd:cd23410    81 NGKMLIGADQYKLTAVGS-KVVASRQSSHKWKPYGSQDE 118
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
378-502 2.77e-29

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: 113.85  E-value: 2.77e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASET-WIGLSSNKIPVSFEWSNDS 456
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYyWIGLSDPDSNGSWQWSDGS 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 767917241    457 S-VIFTNWHTLEPhifPNRSQLCVSAEQSEGHWKVKNCEERLFYICK 502
Cdd:smart00034   81 GpVSYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
242-356 2.00e-25

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: 102.31  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  242 CYQFNLlSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMS-SKTVEVWMGLNQLDEHAGWQWSDGTP-LNYLNWSPE 319
Cdd:cd00037     2 CYKFST-EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKkSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767917241  320 vNFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKK 356
Cdd:cd00037    81 -EPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
816-938 1.21e-23

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: 97.67  E-value: 1.21e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    816 WLFYQDAEYLFHTFASEWLNFEFVCSWLHSDLLTIHSAHEQEFIHSKIKALSKYGaSWWIGLQEERANDEFRWRDGTP-V 894
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGSWQWSDGSGpV 83
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 767917241    895 IYQNWDTGRErtvNNQSQRCGFISSITGLWGSEECSVSMPSICK 938
Cdd:smart00034   84 SYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1254-1378 4.36e-23

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: 96.13  E-value: 4.36e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   1254 WIKFKSNCYSFSTvlDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLeELFAFGSSVQMVWLNAQFDGNNETIKWFDGTP 1333
Cdd:smart00034    5 WISYGGKCYKFST--EKKTWEDAQAFCQSLGGHLASIHSEAENDFVA-SLLKNSGSSDYYWIGLSDPDSNGSWQWSDGSG 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 767917241   1334 TDQ-SNWgirKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFICK 1378
Cdd:smart00034   82 PVSySNW---APGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
171-219 2.74e-22

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 91.21  E-value: 2.74e-22
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 767917241    171 GNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWGFC 219
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
958-1097 1.12e-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: 89.20  E-value: 1.12e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    958 CPKGWLYFNYKCLLLNipkdpSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFIT--MNLFGQTTSVWIGLQNDDYET--- 1032
Cdd:smart00034    1 CPSGWISYGGKCYKFS-----TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGswq 75
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767917241   1033 WLNGKPVV-YSNWSPfdiinipshntTEVQKHIPLCALLSSNpnfhfTGKWYFEDCGKEgYGFVCE 1097
Cdd:smart00034   76 WSDGSGPVsYSNWAP-----------GEPNNSSGDCVVLSTS-----GGKWNDVSCTSK-LPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
664-797 4.48e-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: 84.57  E-value: 4.48e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    664 CYLDWESEPGlaSCFKVFHSEKvlmkrTWREAEAFCEEFGAHLASFAHIEEENFVNELLHskfNWTEERQFWIGFNKRNp 743
Cdd:smart00034    1 CPSGWISYGG--KCYKFSTEKK-----TWEDAQAFCQSLGGHLASIHSEAENDFVASLLK---NSGSSDYYWIGLSDPD- 69
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 767917241    744 lNAGSWEWSDRTPVVS-SFLDNTYFGEDARNCAVYKANKTLL-PLHCGSKREWICK 797
Cdd:smart00034   70 -SNGSWQWSDGSGPVSySNWAPGEPNNSSGDCVVLSTSGGKWnDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
515-644 3.79e-18

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: 81.88  E-value: 3.79e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    515 CQEGWERHGGFCYKIDTVLRSFDQASSgyYC---PPALVTITNRFEQAFITSLISSVVkmKDSYFWIALQDQNDTGEYTW 591
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQA--FCqslGGHLASIHSEAENDFVASLLKNSG--SSDYYWIGLSDPDSNGSWQW 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767917241    592 KpvgQKPEPVQYTHWNTHQPRYSGG-CVAMRGRhpLGRWEVKHCRHfKAMSLCK 644
Cdd:smart00034   77 S---DGSGPVSYSNWAPGEPNNSSGdCVVLSTS--GGKWNDVSCTS-KLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1116-1232 4.13e-18

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: 81.88  E-value: 4.13e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   1116 PNTLEYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYA--HWIGLFTTDNGLNFDWSDGTKS 1193
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGSGP 82
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 767917241   1194 -SFTFW-KDEESSLLGDCVFAD-SNGRWHSTACESFLqGAIC 1232
Cdd:smart00034   83 vSYSNWaPGEPNNSSGDCVVLStSGGKWNDVSCTSKL-PFVC 123
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_PLA2R1 cd23410
ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor ...
38-156 2.18e-62

ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor (PLA2R1) and similar proteins; PLA2R1, also called PLA2-R, PLA2R, 180 kDa secretory phospholipase A2 receptor, C-type lectin domain family 13 member C (CLEC13C), or M-type receptor, is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine production during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. PLA2R1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467788  Cd Length: 118  Bit Score: 208.06  E-value: 2.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   38 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRC 117
Cdd:cd23410     1 KGMFILESESLKKCISADKSGLFLENCDQPSDSMLWKWVSRHRLFNLGSSMCLGLNLSYPQQPLGLFECDSTLRTLWWRC 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767917241  118 NRKMITGPLQYSVQVAHDnTVVASRKYIHKWISYGSGGG 156
Cdd:cd23410    81 NGKMLIGADQYKLTAVGS-KVVASRQSSHKWKPYGSQDE 118
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
378-502 2.77e-29

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: 113.85  E-value: 2.77e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASET-WIGLSSNKIPVSFEWSNDS 456
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYyWIGLSDPDSNGSWQWSDGS 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 767917241    457 S-VIFTNWHTLEPhifPNRSQLCVSAEQSEGHWKVKNCEERLFYICK 502
Cdd:smart00034   81 GpVSYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
242-356 2.00e-25

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: 102.31  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  242 CYQFNLlSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMS-SKTVEVWMGLNQLDEHAGWQWSDGTP-LNYLNWSPE 319
Cdd:cd00037     2 CYKFST-EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKkSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767917241  320 vNFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKK 356
Cdd:cd00037    81 -EPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
229-355 1.81e-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: 99.98  E-value: 1.81e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    229 CDTIWEKDLNShiCYQFNLlSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTV--EVWMGLNQLDEHAGWQWS 306
Cdd:smart00034    1 CPSGWISYGGK--CYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdYYWIGLSDPDSNGSWQWS 77
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 767917241    307 DGTPL-NYLNWSPevNFEPFVEDHCGTFSSfMPSAWRSRDCESTLPYICK 355
Cdd:smart00034   78 DGSGPvSYSNWAP--GEPNNSSGDCVVLST-SGGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
388-503 4.43e-24

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: 98.46  E-value: 4.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  388 NCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASETWIGLSSNKIPVSFEWSNDSS-VIFTNWHTL 466
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767917241  467 EPhiFPNRSQLCVSAEQS-EGHWKVKNCEERLFYICKK 503
Cdd:cd00037    81 EP--NPGGSEDCVVLSSSsDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
816-938 1.21e-23

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: 97.67  E-value: 1.21e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    816 WLFYQDAEYLFHTFASEWLNFEFVCSWLHSDLLTIHSAHEQEFIHSKIKALSKYGaSWWIGLQEERANDEFRWRDGTP-V 894
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGSWQWSDGSGpV 83
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 767917241    895 IYQNWDTGRErtvNNQSQRCGFISSITGLWGSEECSVSMPSICK 938
Cdd:smart00034   84 SYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1254-1378 4.36e-23

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: 96.13  E-value: 4.36e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   1254 WIKFKSNCYSFSTvlDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLeELFAFGSSVQMVWLNAQFDGNNETIKWFDGTP 1333
Cdd:smart00034    5 WISYGGKCYKFST--EKKTWEDAQAFCQSLGGHLASIHSEAENDFVA-SLLKNSGSSDYYWIGLSDPDSNGSWQWSDGSG 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 767917241   1334 TDQ-SNWgirKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFICK 1378
Cdd:smart00034   82 PVSySNW---APGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
171-219 2.74e-22

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 91.21  E-value: 2.74e-22
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 767917241    171 GNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWGFC 219
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
958-1097 1.12e-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: 89.20  E-value: 1.12e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    958 CPKGWLYFNYKCLLLNipkdpSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFIT--MNLFGQTTSVWIGLQNDDYET--- 1032
Cdd:smart00034    1 CPSGWISYGGKCYKFS-----TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGswq 75
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767917241   1033 WLNGKPVV-YSNWSPfdiinipshntTEVQKHIPLCALLSSNpnfhfTGKWYFEDCGKEgYGFVCE 1097
Cdd:smart00034   76 WSDGSGPVsYSNWAP-----------GEPNNSSGDCVVLSTS-----GGKWNDVSCTSK-LPFVCE 124
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
172-219 1.82e-20

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 85.82  E-value: 1.82e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767917241  172 NTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWGFC 219
Cdd:cd00062     1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1260-1379 1.73e-19

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: 85.36  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1260 NCYSFSTvlDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEelFAFGSSVQMVWLNAQFDGNNETIKWFDGTPTDQ-SN 1338
Cdd:cd00037     1 SCYKFST--EKLTWEEAQEYCRSLGGHLASIHSEEENDFLAS--LLKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDyTN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767917241 1339 WGIRKPDTDyfKPHHCVALRI-PEGLWQLSPCQEKKGFICKM 1379
Cdd:cd00037    77 WAPGEPNPG--GSEDCVVLSSsSDGKWNDVSCSSKLPFICEK 116
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
824-939 2.38e-19

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: 84.98  E-value: 2.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  824 YLFHTFASEWLNFEFVCSWLHSDLLTIHSAHEQEFIHSKIKALSKYgaSWWIGLQEERANDEFRWRDGTP-VIYQNWDTG 902
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSS--DVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767917241  903 RERtvNNQSQRCGFIS-SITGLWGSEECSVSMPSICKR 939
Cdd:cd00037    81 EPN--PGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
664-797 4.48e-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: 84.57  E-value: 4.48e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    664 CYLDWESEPGlaSCFKVFHSEKvlmkrTWREAEAFCEEFGAHLASFAHIEEENFVNELLHskfNWTEERQFWIGFNKRNp 743
Cdd:smart00034    1 CPSGWISYGG--KCYKFSTEKK-----TWEDAQAFCQSLGGHLASIHSEAENDFVASLLK---NSGSSDYYWIGLSDPD- 69
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 767917241    744 lNAGSWEWSDRTPVVS-SFLDNTYFGEDARNCAVYKANKTLL-PLHCGSKREWICK 797
Cdd:smart00034   70 -SNGSWQWSDGSGPVSySNWAPGEPNNSSGDCVVLSTSGGKWnDVSCTSKLPFVCE 124
fn2 pfam00040
Fibronectin type II domain;
178-219 3.70e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.15  E-value: 3.70e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 767917241   178 CMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWGFC 219
Cdd:pfam00040    1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
515-644 3.79e-18

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: 81.88  E-value: 3.79e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    515 CQEGWERHGGFCYKIDTVLRSFDQASSgyYC---PPALVTITNRFEQAFITSLISSVVkmKDSYFWIALQDQNDTGEYTW 591
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQA--FCqslGGHLASIHSEAENDFVASLLKNSG--SSDYYWIGLSDPDSNGSWQW 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767917241    592 KpvgQKPEPVQYTHWNTHQPRYSGG-CVAMRGRhpLGRWEVKHCRHfKAMSLCK 644
Cdd:smart00034   77 S---DGSGPVSYSNWAPGEPNNSSGdCVVLSTS--GGKWNDVSCTS-KLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1116-1232 4.13e-18

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: 81.88  E-value: 4.13e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   1116 PNTLEYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYA--HWIGLFTTDNGLNFDWSDGTKS 1193
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGSGP 82
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 767917241   1194 -SFTFW-KDEESSLLGDCVFAD-SNGRWHSTACESFLqGAIC 1232
Cdd:smart00034   83 vSYSNWaPGEPNNSSGDCVVLStSGGKWNDVSCTSKL-PFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
676-798 1.23e-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: 79.97  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  676 SCFKVFHSekvlmKRTWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKfnwtEERQFWIGFNKRNplNAGSWEWSDRT 755
Cdd:cd00037     1 SCYKFSTE-----KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKS----SSSDVWIGLNDLS--SEGTWKWSDGS 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767917241  756 PVV--SSFLDNTYFGEDARNCAVYKANKTLL--PLHCGSKREWICKI 798
Cdd:cd00037    70 PLVdyTNWAPGEPNPGGSEDCVVLSSSSDGKwnDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
397-503 3.25e-17

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 78.67  E-value: 3.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   397 KTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASeTWIGLSSNKIPVSFEWSNDSSVIFTNWHTLEPHifPNRSQ 476
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY-FWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNN--NGENE 78
                           90       100
                   ....*....|....*....|....*..
gi 767917241   477 LCVSAEQSEGHWKVKNCEERLFYICKK 503
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
250-356 1.76e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 76.36  E-value: 1.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   250 SLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDh 329
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENED- 79
                           90       100
                   ....*....|....*....|....*..
gi 767917241   330 CGTFSSFMPSaWRSRDCESTLPYICKK 356
Cdd:pfam00059   80 CVELSSSSGK-WNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1126-1232 2.03e-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: 76.50  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1126 YKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAH-WIGLFTTDNGLNFDWSDGTK-SSFTFWKDEE- 1202
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvWIGLNDLSSEGTWKWSDGSPlVDYTNWAPGEp 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767917241 1203 -SSLLGDCVF--ADSNGRWHSTACESfLQGAIC 1232
Cdd:cd00037    83 nPGGSEDCVVlsSSSDGKWNDVSCSS-KLPFIC 114
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1133-1233 2.04e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 76.36  E-value: 2.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  1133 MTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFTFWKDEES--SLLGDCV 1210
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNnnGENEDCV 81
                           90       100
                   ....*....|....*....|....
gi 767917241  1211 -FADSNGRWHSTACESfLQGAICH 1233
Cdd:pfam00059   82 eLSSSSGKWNDENCNS-KNPFVCE 104
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
979-1098 2.97e-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: 76.12  E-value: 2.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  979 SSWKNWTHAQHFCAEEGGTLVAIESEVEQAFITMNL-FGQTTSVWIGLQNDDYE---TWLNGKPVV-YSNWSPfdiiNIP 1053
Cdd:cd00037     7 TEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkKSSSSDVWIGLNDLSSEgtwKWSDGSPLVdYTNWAP----GEP 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767917241 1054 SHNTTEvqkhipLCALLSSNPNfhftGKWYFEDCGKEgYGFVCEK 1098
Cdd:cd00037    83 NPGGSE------DCVVLSSSSD----GKWNDVSCSSK-LPFICEK 116
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
43-151 3.59e-15

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 73.31  E-value: 3.59e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241     43 IQSESLKKCIQA--GKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAPeQPLSLYECDSTLVSLRWRCNR- 119
Cdd:smart00458    1 IISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIKDTDLCLTANGNTG-STVTLYSCDGTNDNQYWEVNKd 79
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 767917241    120 KMITGP-LQYSVQVAHDNT--VVASRKYIH----KWISY 151
Cdd:smart00458   80 GTIRNPdSGKCLDVKDGNTgtKVILWTCSGnpnqKWIFE 118
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
982-1098 4.45e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.51  E-value: 4.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   982 KNWTHAQHFCAEEGGTLVAIESEVEQAFITMNLFGQTTSVWIGL---QNDDYETWLNGKPVVYSNWSPFDIINIPShntt 1058
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdrKNEGTWKWVDGSPVNYTNWAPEPNNNGEN---- 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 767917241  1059 evqkhiPLCALLSSNPnfhftGKWYFEDCGKEgYGFVCEK 1098
Cdd:pfam00059   78 ------EDCVELSSSS-----GKWNDENCNSK-NPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
833-939 2.15e-14

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 70.58  E-value: 2.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   833 WLNFEFVCSWLHSDLLTIHSAHEQEFIHSKIKalsKYGASWWIGLQEERANDEFRWRDGTPVIYQNWdtGRERTVNNQSQ 912
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTLK---KSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNW--APEPNNNGENE 78
                           90       100
                   ....*....|....*....|....*..
gi 767917241   913 RCGFISSITGLWGSEECSVSMPSICKR 939
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1270-1379 3.11e-14

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 70.20  E-value: 3.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  1270 SMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSvqmVWLNAQFDGNNETIKWFDGTPTDQSNWGiRKPDTDYF 1349
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY---FWIGLTDRKNEGTWKWVDGSPVNYTNWA-PEPNNNGE 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 767917241  1350 KPhHCVALRIPEGLWQLSPCQEKKGFICKM 1379
Cdd:pfam00059   77 NE-DCVELSSSSGKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
525-645 5.85e-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: 66.87  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  525 FCYKIDTVLRSFDQASSgyYC---PPALVTITNRFEQAFITSLISsvvKMKDSYFWIALQDQNDTGEYTWkpvGQKPEPV 601
Cdd:cd00037     1 SCYKFSTEKLTWEEAQE--YCrslGGHLASIHSEEENDFLASLLK---KSSSSDVWIGLNDLSSEGTWKW---SDGSPLV 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767917241  602 QYTHWNTHQPRYSGG--CVAMRgRHPLGRWEVKHCRHfKAMSLCKQ 645
Cdd:cd00037    73 DYTNWAPGEPNPGGSedCVVLS-SSSDGKWNDVSCSS-KLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
689-797 4.50e-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: 60.95  E-value: 4.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   689 KRTWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKfnwteERQFWIGFNKRNplNAGSWEWSDRTPVVSSFLDNtYFG 768
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKS-----NKYFWIGLTDRK--NEGTWKWVDGSPVNYTNWAP-EPN 72
                           90       100       110
                   ....*....|....*....|....*....|..
gi 767917241   769 EDARN--CAVY-KANKTLLPLHCGSKREWICK 797
Cdd:pfam00059   73 NNGENedCVELsSSSGKWNDENCNSKNPFVCE 104
PHA02642 PHA02642
C-type lectin-like protein; Provisional
944-1028 3.83e-08

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 55.51  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  944 LIEKKKDTPK---QHGTCPKGWLYFNYKCLLLNipkdpSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFitMNLFGQTTS 1020
Cdd:PHA02642   71 LMAFKSDTQEptiKYVTCPKGWIGFGYKCFYFS-----EDSKNWTFGNTFCTSLGATLVKVETEEELNF--LKRYKDSSD 143

                  ....*...
gi 767917241 1021 VWIGLQND 1028
Cdd:PHA02642  144 HWIGLNRE 151
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
549-645 2.68e-06

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 47.47  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   549 LVTITNRFEQAFItsliSSVVKMKDSYFWIALQDQNDTGEYTWkPVGqkpEPVQYTHWNTHQPRYSGG--CVAMrgRHPL 626
Cdd:pfam00059   18 LVSINSAEELDFL----SSTLKKSNKYFWIGLTDRKNEGTWKW-VDG---SPVNYTNWAPEPNNNGENedCVEL--SSSS 87
                           90
                   ....*....|....*....
gi 767917241   627 GRWEVKHCrHFKAMSLCKQ 645
Cdd:pfam00059   88 GKWNDENC-NSKNPFVCEK 105
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
384-502 2.86e-05

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: 48.93  E-value: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   384 PYNRNCYKLQKEEKTWHEALRSCQA-DNSALIDITSLAEVEFLVTLLGDENASETWIGLSS-NKIPVS-FEWSNDSSV-I 459
Cdd:TIGR00864  326 EENGHCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFSDvNGAEKGpAHQGEAFEAeE 405
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 767917241   460 FTNWHTLEPHifPNRSQLCVSAEQSeGHWKVKNCEERLFYICK 502
Cdd:TIGR00864  406 CEEGLAGEPH--PARAEHCVRLDPR-GQCNSDLCNAPHAYVCE 445
PHA02642 PHA02642
C-type lectin-like protein; Provisional
221-312 1.55e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 44.72  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  221 DPTSAEVGCDTIWEKdlNSHICYQFNLlSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKtvEVWMGLNQLDEH 300
Cdd:PHA02642   80 EPTIKYVTCPKGWIG--FGYKCFYFSE-DSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSS--DHWIGLNRESSN 154
                          90
                  ....*....|..
gi 767917241  301 AGWQWSDGTPLN 312
Cdd:PHA02642  155 HPWKWADNSNYN 166
PHA03097 PHA03097
C-type lectin-like protein; Provisional
378-458 6.22e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 39.08  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENaseTWIGLSSNKipvsfEWSNDSS 457
Cdd:PHA03097   46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQD---LWIGIEKKK-----GDDDDRE 117

                  .
gi 767917241  458 V 458
Cdd:PHA03097  118 V 118
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_PLA2R1 cd23410
ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor ...
38-156 2.18e-62

ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor (PLA2R1) and similar proteins; PLA2R1, also called PLA2-R, PLA2R, 180 kDa secretory phospholipase A2 receptor, C-type lectin domain family 13 member C (CLEC13C), or M-type receptor, is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine production during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. PLA2R1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467788  Cd Length: 118  Bit Score: 208.06  E-value: 2.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   38 KGIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRC 117
Cdd:cd23410     1 KGMFILESESLKKCISADKSGLFLENCDQPSDSMLWKWVSRHRLFNLGSSMCLGLNLSYPQQPLGLFECDSTLRTLWWRC 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767917241  118 NRKMITGPLQYSVQVAHDnTVVASRKYIHKWISYGSGGG 156
Cdd:cd23410    81 NGKMLIGADQYKLTAVGS-KVVASRQSSHKWKPYGSQDE 118
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
378-502 2.77e-29

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: 113.85  E-value: 2.77e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASET-WIGLSSNKIPVSFEWSNDS 456
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYyWIGLSDPDSNGSWQWSDGS 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 767917241    457 S-VIFTNWHTLEPhifPNRSQLCVSAEQSEGHWKVKNCEERLFYICK 502
Cdd:smart00034   81 GpVSYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
beta-trefoil_Ricin_LY75 cd23411
ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and ...
39-141 4.52e-28

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. Ly-75 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467789  Cd Length: 116  Bit Score: 109.83  E-value: 4.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   39 GIFVIQSESLKKCIQAGKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRCN 118
Cdd:cd23411     3 DIFTIQHENSGKCLKVENSQISAVDCKQSSESLQWKWVSEHRLFNLGSKQCLGLDITKPSNTLKMFECDSKSVMLWWRCE 82
                          90       100
                  ....*....|....*....|...
gi 767917241  119 RKMITGPLQYSVQVAhDNTVVAS 141
Cdd:cd23411    83 GGSLYGASQYRLAVK-NGSVTAS 104
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
40-148 9.28e-26

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 103.45  E-value: 9.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   40 IFVIQSESLKKCIQA--GKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRC 117
Cdd:cd23385     2 SFLIYNEDLGKCLAArsSSSKVSLSTCNPNSPNQQWKWTSGHRLFNVGTGKCLGVSSSSPSSPLRLFECDSEDELQKWKC 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767917241  118 NRKMITGPLQYSVQVAHDNT-----VVASRKYIHKW 148
Cdd:cd23385    82 SKDGLLLLKGLGLLLLYDKSgknvvVSKGSGLSSRW 117
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
242-356 2.00e-25

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: 102.31  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  242 CYQFNLlSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMS-SKTVEVWMGLNQLDEHAGWQWSDGTP-LNYLNWSPE 319
Cdd:cd00037     2 CYKFST-EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKkSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767917241  320 vNFEPFVEDHCGTFSSFMPSAWRSRDCESTLPYICKK 356
Cdd:cd00037    81 -EPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
229-355 1.81e-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: 99.98  E-value: 1.81e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    229 CDTIWEKDLNShiCYQFNLlSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTV--EVWMGLNQLDEHAGWQWS 306
Cdd:smart00034    1 CPSGWISYGGK--CYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdYYWIGLSDPDSNGSWQWS 77
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 767917241    307 DGTPL-NYLNWSPevNFEPFVEDHCGTFSSfMPSAWRSRDCESTLPYICK 355
Cdd:smart00034   78 DGSGPvSYSNWAP--GEPNNSSGDCVVLST-SGGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
388-503 4.43e-24

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: 98.46  E-value: 4.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  388 NCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASETWIGLSSNKIPVSFEWSNDSS-VIFTNWHTL 466
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767917241  467 EPhiFPNRSQLCVSAEQS-EGHWKVKNCEERLFYICKK 503
Cdd:cd00037    81 EP--NPGGSEDCVVLSSSsDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
816-938 1.21e-23

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: 97.67  E-value: 1.21e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    816 WLFYQDAEYLFHTFASEWLNFEFVCSWLHSDLLTIHSAHEQEFIHSKIKALSKYGaSWWIGLQEERANDEFRWRDGTP-V 894
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGSWQWSDGSGpV 83
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 767917241    895 IYQNWDTGRErtvNNQSQRCGFISSITGLWGSEECSVSMPSICK 938
Cdd:smart00034   84 SYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1254-1378 4.36e-23

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: 96.13  E-value: 4.36e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   1254 WIKFKSNCYSFSTvlDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLeELFAFGSSVQMVWLNAQFDGNNETIKWFDGTP 1333
Cdd:smart00034    5 WISYGGKCYKFST--EKKTWEDAQAFCQSLGGHLASIHSEAENDFVA-SLLKNSGSSDYYWIGLSDPDSNGSWQWSDGSG 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 767917241   1334 TDQ-SNWgirKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFICK 1378
Cdd:smart00034   82 PVSySNW---APGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
171-219 2.74e-22

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 91.21  E-value: 2.74e-22
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 767917241    171 GNTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWGFC 219
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
958-1097 1.12e-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: 89.20  E-value: 1.12e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    958 CPKGWLYFNYKCLLLNipkdpSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFIT--MNLFGQTTSVWIGLQNDDYET--- 1032
Cdd:smart00034    1 CPSGWISYGGKCYKFS-----TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGswq 75
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767917241   1033 WLNGKPVV-YSNWSPfdiinipshntTEVQKHIPLCALLSSNpnfhfTGKWYFEDCGKEgYGFVCE 1097
Cdd:smart00034   76 WSDGSGPVsYSNWAP-----------GEPNNSSGDCVVLSTS-----GGKWNDVSCTSK-LPFVCE 124
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
172-219 1.82e-20

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 85.82  E-value: 1.82e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 767917241  172 NTHGMPCMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWGFC 219
Cdd:cd00062     1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1260-1379 1.73e-19

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: 85.36  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1260 NCYSFSTvlDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEelFAFGSSVQMVWLNAQFDGNNETIKWFDGTPTDQ-SN 1338
Cdd:cd00037     1 SCYKFST--EKLTWEEAQEYCRSLGGHLASIHSEEENDFLAS--LLKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDyTN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767917241 1339 WGIRKPDTDyfKPHHCVALRI-PEGLWQLSPCQEKKGFICKM 1379
Cdd:cd00037    77 WAPGEPNPG--GSEDCVVLSSsSDGKWNDVSCSSKLPFICEK 116
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
824-939 2.38e-19

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: 84.98  E-value: 2.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  824 YLFHTFASEWLNFEFVCSWLHSDLLTIHSAHEQEFIHSKIKALSKYgaSWWIGLQEERANDEFRWRDGTP-VIYQNWDTG 902
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSS--DVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767917241  903 RERtvNNQSQRCGFIS-SITGLWGSEECSVSMPSICKR 939
Cdd:cd00037    81 EPN--PGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
664-797 4.48e-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: 84.57  E-value: 4.48e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    664 CYLDWESEPGlaSCFKVFHSEKvlmkrTWREAEAFCEEFGAHLASFAHIEEENFVNELLHskfNWTEERQFWIGFNKRNp 743
Cdd:smart00034    1 CPSGWISYGG--KCYKFSTEKK-----TWEDAQAFCQSLGGHLASIHSEAENDFVASLLK---NSGSSDYYWIGLSDPD- 69
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 767917241    744 lNAGSWEWSDRTPVVS-SFLDNTYFGEDARNCAVYKANKTLL-PLHCGSKREWICK 797
Cdd:smart00034   70 -SNGSWQWSDGSGPVSySNWAPGEPNNSSGDCVVLSTSGGKWnDVSCTSKLPFVCE 124
fn2 pfam00040
Fibronectin type II domain;
178-219 3.70e-18

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.15  E-value: 3.70e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 767917241   178 CMFPFQYNHQWHHECTREGREDDLLWCATTSRYERDEKWGFC 219
Cdd:pfam00040    1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
515-644 3.79e-18

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: 81.88  E-value: 3.79e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241    515 CQEGWERHGGFCYKIDTVLRSFDQASSgyYC---PPALVTITNRFEQAFITSLISSVVkmKDSYFWIALQDQNDTGEYTW 591
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQA--FCqslGGHLASIHSEAENDFVASLLKNSG--SSDYYWIGLSDPDSNGSWQW 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767917241    592 KpvgQKPEPVQYTHWNTHQPRYSGG-CVAMRGRhpLGRWEVKHCRHfKAMSLCK 644
Cdd:smart00034   77 S---DGSGPVSYSNWAPGEPNNSSGdCVVLSTS--GGKWNDVSCTS-KLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1116-1232 4.13e-18

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: 81.88  E-value: 4.13e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   1116 PNTLEYGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYA--HWIGLFTTDNGLNFDWSDGTKS 1193
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGSGP 82
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 767917241   1194 -SFTFW-KDEESSLLGDCVFAD-SNGRWHSTACESFLqGAIC 1232
Cdd:smart00034   83 vSYSNWaPGEPNNSSGDCVVLStSGGKWNDVSCTSKL-PFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
676-798 1.23e-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: 79.97  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  676 SCFKVFHSekvlmKRTWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKfnwtEERQFWIGFNKRNplNAGSWEWSDRT 755
Cdd:cd00037     1 SCYKFSTE-----KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKS----SSSDVWIGLNDLS--SEGTWKWSDGS 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767917241  756 PVV--SSFLDNTYFGEDARNCAVYKANKTLL--PLHCGSKREWICKI 798
Cdd:cd00037    70 PLVdyTNWAPGEPNPGGSEDCVVLSSSSDGKwnDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
397-503 3.25e-17

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 78.67  E-value: 3.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   397 KTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASeTWIGLSSNKIPVSFEWSNDSSVIFTNWHTLEPHifPNRSQ 476
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY-FWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNN--NGENE 78
                           90       100
                   ....*....|....*....|....*..
gi 767917241   477 LCVSAEQSEGHWKVKNCEERLFYICKK 503
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
250-356 1.76e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 76.36  E-value: 1.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   250 SLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPFVEDh 329
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENED- 79
                           90       100
                   ....*....|....*....|....*..
gi 767917241   330 CGTFSSFMPSaWRSRDCESTLPYICKK 356
Cdd:pfam00059   80 CVELSSSSGK-WNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1126-1232 2.03e-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: 76.50  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1126 YKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAH-WIGLFTTDNGLNFDWSDGTK-SSFTFWKDEE- 1202
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvWIGLNDLSSEGTWKWSDGSPlVDYTNWAPGEp 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767917241 1203 -SSLLGDCVF--ADSNGRWHSTACESfLQGAIC 1232
Cdd:cd00037    83 nPGGSEDCVVlsSSSDGKWNDVSCSS-KLPFIC 114
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1133-1233 2.04e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 76.36  E-value: 2.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  1133 MTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFTTDNGLNFDWSDGTKSSFTFWKDEES--SLLGDCV 1210
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNnnGENEDCV 81
                           90       100
                   ....*....|....*....|....
gi 767917241  1211 -FADSNGRWHSTACESfLQGAICH 1233
Cdd:pfam00059   82 eLSSSSGKWNDENCNS-KNPFVCE 104
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
979-1098 2.97e-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: 76.12  E-value: 2.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  979 SSWKNWTHAQHFCAEEGGTLVAIESEVEQAFITMNL-FGQTTSVWIGLQNDDYE---TWLNGKPVV-YSNWSPfdiiNIP 1053
Cdd:cd00037     7 TEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkKSSSSDVWIGLNDLSSEgtwKWSDGSPLVdYTNWAP----GEP 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767917241 1054 SHNTTEvqkhipLCALLSSNPNfhftGKWYFEDCGKEgYGFVCEK 1098
Cdd:cd00037    83 NPGGSE------DCVVLSSSSD----GKWNDVSCSSK-LPFICEK 116
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
242-355 4.59e-16

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: 76.26  E-value: 4.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  242 CYQFnLLSSLSWSEAHSSCQM--QGGTLLSITDETEENFIREHMSS---KTVEVWMGLNQLDEHAGWQWSDGTPLNYLNW 316
Cdd:cd03594    12 CYGY-FRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSyqkAYQPVWIGLHDPQQSRGWEWSDGSKLDYRSW 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767917241  317 SPEVNFEPfvEDHCGTFSS---FMpsAWRSRDCESTLPYICK 355
Cdd:cd03594    91 DRNPPYAR--GGYCAELSRstgFL--KWNDANCEERNPFICK 128
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
378-503 8.61e-16

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: 74.68  E-value: 8.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGdenASETWIGLSSNKIPVSFEWSNDSs 457
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIG---SSSYWIGLSREKSEKPWKWIDGS- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767917241  458 vIFTNWHTLephIFPNRSQLCVSAEQSEGHwkVKNCEERLFYICKK 503
Cdd:cd03593    77 -PLNNLFNI---RGSTKSGNCAYLSSTGIY--SEDCSTKKRWICEK 116
beta-trefoil_Ricin_MRC2 cd23408
ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) ...
39-118 9.95e-16

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) and similar proteins; MRC2, also called C-type mannose receptor 2, C-type lectin domain family 13 member E (CLEC13E), endocytic receptor 180 (Endo180), urokinase-type plasminogen activator receptor-associated protein (UPARAP), UPAR-associated protein, urokinase receptor-associated protein, or CD280, may play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). MRC2 contains an atypical ricin B-type lectin domain at the N-terminus. The typical ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. In contrast, the ninth, tenth and eleventh beta strands, comprising the gamma subdomain, are missing in the ricin B-type lectin domain of MRC2.


Pssm-ID: 467786  Cd Length: 124  Bit Score: 74.83  E-value: 9.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   39 GIFVIQSESLKKCIQAGKSVLTLEN-CKQANKHMLWKWVSNHGLFNIGGSGCLGL---NFSAPEQPLSLYECDSTLVSLR 114
Cdd:cd23408     1 DVFLIYSDGAQGCLEVRDSVVRLSPaCNTSSPAQQWKWVSRNRLFNLGSMQCLGVsgpNGSGTSATLGTYECDRESVNMR 80

                  ....
gi 767917241  115 WRCN 118
Cdd:cd23408    81 WHCR 84
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
43-151 3.59e-15

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 73.31  E-value: 3.59e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241     43 IQSESLKKCIQA--GKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAPeQPLSLYECDSTLVSLRWRCNR- 119
Cdd:smart00458    1 IISGNTGKCLDVngNKNPVGLFDCHGTGGNQLWKLTSDGAIRIKDTDLCLTANGNTG-STVTLYSCDGTNDNQYWEVNKd 79
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 767917241    120 KMITGP-LQYSVQVAHDNT--VVASRKYIH----KWISY 151
Cdd:smart00458   80 GTIRNPdSGKCLDVKDGNTgtKVILWTCSGnpnqKWIFE 118
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
982-1098 4.45e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.51  E-value: 4.45e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   982 KNWTHAQHFCAEEGGTLVAIESEVEQAFITMNLFGQTTSVWIGL---QNDDYETWLNGKPVVYSNWSPFDIINIPShntt 1058
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdrKNEGTWKWVDGSPVNYTNWAPEPNNNGEN---- 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 767917241  1059 evqkhiPLCALLSSNPnfhftGKWYFEDCGKEgYGFVCEK 1098
Cdd:pfam00059   78 ------EDCVELSSSS-----GKWNDENCNSK-NPFVCEK 105
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
378-502 4.52e-15

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: 73.17  E-value: 4.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQA--DNSALIDITSLAEVEFLVTLLGDENASE--TWIGLSSNKIPVSFEWS 453
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQKAYqpVWIGLHDPQQSRGWEWS 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767917241  454 NDSSVIFTNWHTLEPHifpNRSQLCVSAEQSEGH--WKVKNCEERLFYICK 502
Cdd:cd03594    81 DGSKLDYRSWDRNPPY---ARGGYCAELSRSTGFlkWNDANCEERNPFICK 128
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
242-356 1.26e-14

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 71.59  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  242 CYQFNLlSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTveVWMGLNQLDEHAGWQWSDGTPLNylNWSPEVN 321
Cdd:cd03593    12 CYYFSM-EKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS--YWIGLSREKSEKPWKWIDGSPLN--NLFNIRG 86
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767917241  322 FEPfvEDHCGTFSSFMPSawrSRDCESTLPYICKK 356
Cdd:cd03593    87 STK--SGNCAYLSSTGIY---SEDCSTKKRWICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
833-939 2.15e-14

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 70.58  E-value: 2.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   833 WLNFEFVCSWLHSDLLTIHSAHEQEFIHSKIKalsKYGASWWIGLQEERANDEFRWRDGTPVIYQNWdtGRERTVNNQSQ 912
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTLK---KSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNW--APEPNNNGENE 78
                           90       100
                   ....*....|....*....|....*..
gi 767917241   913 RCGFISSITGLWGSEECSVSMPSICKR 939
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1270-1379 3.11e-14

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 70.20  E-value: 3.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  1270 SMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSvqmVWLNAQFDGNNETIKWFDGTPTDQSNWGiRKPDTDYF 1349
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY---FWIGLTDRKNEGTWKWVDGSPVNYTNWA-PEPNNNGE 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 767917241  1350 KPhHCVALRIPEGLWQLSPCQEKKGFICKM 1379
Cdd:pfam00059   77 NE-DCVELSSSSGKWNDENCNSKNPFVCEK 105
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
378-503 3.19e-14

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: 70.80  E-value: 3.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENAseTWIGLSSNKIPVSFEWSNDSS 457
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS--YWIGLSDEETEGEWKWVDGTP 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767917241  458 VI--FTNWHTLEPHIFPNRSQLCVSAEQSEGHWKVKNCEERLFYICKK 503
Cdd:cd03590    79 LNssKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
1254-1379 9.62e-14

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: 69.26  E-value: 9.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1254 WIKFKSNCYSFSTvlDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLleelFAFGSSVQMVWLNAqFDGNNE-TIKWFDGT 1332
Cdd:cd03590     5 WKSFQSSCYFFST--EKKSWEESRQFCEDMGAHLVIINSQEEQEFI----SKILSGNRSYWIGL-SDEETEgEWKWVDGT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767917241 1333 P--TDQSNWGIRKPDTDYFKPHHCVALRIPEGLWQLSPCQEKKGFICKM 1379
Cdd:cd03590    78 PlnSSKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
1124-1227 4.64e-13

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: 66.63  E-value: 4.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1124 RTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAHWIGLFttDNGLNFDWSDGTKSSFTFWKDEES 1203
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLY--RDVDSWRWSDGSESSFRNWNTFQP 78
                          90       100
                  ....*....|....*....|....
gi 767917241 1204 SLLGDCVFADSNGRWHSTACESFL 1227
Cdd:cd03602    79 FGQGDCATMYSSGRWYAALCSALK 102
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
525-645 5.85e-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: 66.87  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  525 FCYKIDTVLRSFDQASSgyYC---PPALVTITNRFEQAFITSLISsvvKMKDSYFWIALQDQNDTGEYTWkpvGQKPEPV 601
Cdd:cd00037     1 SCYKFSTEKLTWEEAQE--YCrslGGHLASIHSEEENDFLASLLK---KSSSSDVWIGLNDLSSEGTWKW---SDGSPLV 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767917241  602 QYTHWNTHQPRYSGG--CVAMRgRHPLGRWEVKHCRHfKAMSLCKQ 645
Cdd:cd00037    73 DYTNWAPGEPNPGGSedCVVLS-SSSDGKWNDVSCSS-KLPFICEK 116
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
378-503 1.48e-12

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 66.06  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENasetWIGLSSNKIPVSFEWSNDSS 457
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ----WIGLNDRTIEGDFRWSDGHP 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767917241  458 VIFTNWHTLEPHIFPNRSQLC-VSAEQSEGHWKVKNCEERLFYICKK 503
Cdd:cd03588    77 LQFENWRPNQPDNFFATGEDCvVMIWHEEGEWNDVPCNYHLPFTCKK 123
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
1254-1378 5.23e-12

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: 64.32  E-value: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1254 WIKFKSNCYSFstVLDSMSFEAAHEFCKK--EGSNLLTIKDEAENAFLLEELFAFGSSVQMVWLNAQFDGNNETIKWFDG 1331
Cdd:cd03594     5 WLPYKGNCYGY--FRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRGWEWSDG 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767917241 1332 TPTDQSNWgirKPDTDYFKPHHCVALRIPEG--LWQLSPCQEKKGFICK 1378
Cdd:cd03594    83 SKLDYRSW---DRNPPYARGGYCAELSRSTGflKWNDANCEERNPFICK 128
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
378-502 8.31e-12

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: 64.30  E-value: 8.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSA-----LIDITSLAEVEFLVTLL----GDENASETWIGLSSNKIPV 448
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFVYDLFessrGPDTPYGLWIGLHDRTSEG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767917241  449 SFEWSNDSSVIFTNWHTLEPHIFPNRSQlCV---SAEQSEGHWKVKNCEERLFYICK 502
Cdd:cd03589    81 PFEWTDGSPVDFTKWAGGQPDNYGGNED-CVqmwRRGDAGQSWNDMPCDAVFPYICK 136
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
816-939 2.32e-11

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: 62.71  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  816 WLFYQDAEYLFHTFASEWLNFEFVCSWLHSDLLTIHSAHEQEFIhskiKALSKYGASWWIGLQEERANDEFRWRDGTPVI 895
Cdd:cd03590     5 WKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFI----SKILSGNRSYWIGLSDEETEGEWKWVDGTPLN 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767917241  896 --YQNWDTGRERTVNNQSQRCGFISSITGLWGSEECSVSMPSICKR 939
Cdd:cd03590    81 ssKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
229-355 3.83e-11

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: 62.38  E-value: 3.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  229 CDTIWEKdLNSHiCYQ-FNLlsSLSWSEAHSSCQMQG-----GTLLSITDETEENFIREHMSSKTV-----EVWMGLNQL 297
Cdd:cd03589     1 CPTFWTA-FGGY-CYRfFGD--RLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGpdtpyGLWIGLHDR 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767917241  298 DEHAGWQWSDGTPLNYLNWSP-EVNFEPFVEDhCGTFSSFMPS--AWRSRDCESTLPYICK 355
Cdd:cd03589    77 TSEGPFEWTDGSPVDFTKWAGgQPDNYGGNED-CVQMWRRGDAgqSWNDMPCDAVFPYICK 136
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
689-797 4.50e-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: 60.95  E-value: 4.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   689 KRTWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKfnwteERQFWIGFNKRNplNAGSWEWSDRTPVVSSFLDNtYFG 768
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKS-----NKYFWIGLTDRK--NEGTWKWVDGSPVNYTNWAP-EPN 72
                           90       100       110
                   ....*....|....*....|....*....|..
gi 767917241   769 EDARN--CAVY-KANKTLLPLHCGSKREWICK 797
Cdd:pfam00059   73 NNGENedCVELsSSSGKWNDENCNSKNPFVCE 104
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
816-938 6.83e-11

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: 61.60  E-value: 6.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  816 WLFYQDAEYLFHTFASEWLNFEFVC-----SWLHSDLLTIHSAHEQEFIHSKIKALSK----YGAswWIGLQEERANDEF 886
Cdd:cd03589     5 WTAFGGYCYRFFGDRLTWEEAELRCrsfsiPGLIAHLVSIHSQEENDFVYDLFESSRGpdtpYGL--WIGLHDRTSEGPF 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767917241  887 RWRDGTPVIYQNWDTGrERTVNNQSQRCGFI---SSITGLWGSEECSVSMPSICK 938
Cdd:cd03589    83 EWTDGSPVDFTKWAGG-QPDNYGGNEDCVQMwrrGDAGQSWNDMPCDAVFPYICK 136
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
242-356 7.43e-11

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: 61.17  E-value: 7.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  242 CYQFNLlSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTvEVWMGLNQLDEHAGWQWSDGTPLN--YLNWSPe 319
Cdd:cd03590    12 CYFFST-EKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNR-SYWIGLSDEETEGEWKWVDGTPLNssKTFWHP- 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767917241  320 vnFEP----FVEDHCGTFSSfMPSAWRSRDCESTLPYICKK 356
Cdd:cd03590    89 --GEPnnwgGGGEDCAELVY-DSGGWNDVPCNLEYRWICEK 126
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
249-325 9.50e-11

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: 60.52  E-value: 9.50e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767917241  249 SSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTvEVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEPF 325
Cdd:cd03603     8 GGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG-ASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNNG 83
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
676-797 1.29e-10

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: 60.04  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  676 SCFKVFHSEKvlmkrTWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKFnwteerqFWIGFNKRNPlnAGSWEWSDRT 755
Cdd:cd03593    11 KCYYFSMEKK-----TWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS-------YWIGLSREKS--EKPWKWIDGS 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767917241  756 PVVSSFLDNTYFGEDarNCAVYKANKtLLPLHCGSKREWICK 797
Cdd:cd03593    77 PLNNLFNIRGSTKSG--NCAYLSSTG-IYSEDCSTKKRWICE 115
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
250-354 1.60e-10

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: 59.69  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  250 SLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTVEVWMGLnqLDEHAGWQWSDGTPLNYLNWSPevnFEPFVEDH 329
Cdd:cd03602     9 SKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWNT---FQPFGQGD 83
                          90       100
                  ....*....|....*....|....*
gi 767917241  330 CGTFSSFmpSAWRSRDCESTLPYIC 354
Cdd:cd03602    84 CATMYSS--GRWYAALCSALKPFIC 106
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
664-797 5.72e-10

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: 58.54  E-value: 5.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  664 CYLDWESEPGlaSCFKVFHSEKvlmkrTWREAEAFCEEF--GAHLASFAHIEEENFVNELLhSKFNWTEERqFWIGFNkr 741
Cdd:cd03594     1 CPKGWLPYKG--NCYGYFRQPL-----SWSDAELFCQKYgpGAHLASIHSPAEAAAIASLI-SSYQKAYQP-VWIGLH-- 69
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  742 NPLNAGSWEWSDRT-PVVSSFLDNTYFGeDARNCAVYKANKTLLPLH---CGSKREWICK 797
Cdd:cd03594    70 DPQQSRGWEWSDGSkLDYRSWDRNPPYA-RGGYCAELSRSTGFLKWNdanCEERNPFICK 128
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
958-1098 9.31e-10

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: 58.08  E-value: 9.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  958 CPKGWLYFNYKCLLLNipkdpSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFITMNLFGQtTSVWIGLQNDDYE---TWL 1034
Cdd:cd03590     1 CPTNWKSFQSSCYFFS-----TEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGN-RSYWIGLSDEETEgewKWV 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767917241 1035 NGKPVV--YSNWSPFDiiniPSHNTTEVQKhiplCALLSSNpnfhfTGKWYFEDCGKEgYGFVCEK 1098
Cdd:cd03590    75 DGTPLNssKTFWHPGE----PNNWGGGGED----CAELVYD-----SGGWNDVPCNLE-YRWICEK 126
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
664-797 9.49e-10

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: 58.08  E-value: 9.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  664 CYLDWESEpgLASCFkvFHSEKvlmKRTWREAEAFCEEFGAHLASFAHIEEENFVNELLHSKFNwteerqFWIGFNKRNp 743
Cdd:cd03590     1 CPTNWKSF--QSSCY--FFSTE---KKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS------YWIGLSDEE- 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767917241  744 lNAGSWEWSDRTPVVSSFL--------DNTYFGEDarnCAVYKANK-TLLPLHCGSKREWICK 797
Cdd:cd03590    67 -TEGEWKWVDGTPLNSSKTfwhpgepnNWGGGGED---CAELVYDSgGWNDVPCNLEYRWICE 125
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
664-757 1.06e-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: 58.14  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  664 CYLDWESEPGlaSCFKVFHSEKvlmkrTWREAEAFCEEFG-----AHLASFAHIEEENFVNELLHSKFNWTEERQFWIGF 738
Cdd:cd03589     1 CPTFWTAFGG--YCYRFFGDRL-----TWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPDTPYGLWIGL 73
                          90
                  ....*....|....*....
gi 767917241  739 NKRNplNAGSWEWSDRTPV 757
Cdd:cd03589    74 HDRT--SEGPFEWTDGSPV 90
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
1254-1379 1.34e-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: 57.75  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1254 WIKFKSNCYSFSTvlDSMSFEAAHEFCKKEGSN-----LLTIKDEAENAFLleelFAFGSSVQM------VWLNAQFDGN 1322
Cdd:cd03589     5 WTAFGGYCYRFFG--DRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFV----YDLFESSRGpdtpygLWIGLHDRTS 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1323 NETIKWFDGTPTDQSNWGIRKPDtDYFKPHHCVALR---IPEGLWQLSPCQEKKGFICKM 1379
Cdd:cd03589    79 EGPFEWTDGSPVDFTKWAGGQPD-NYGGNEDCVQMWrrgDAGQSWNDMPCDAVFPYICKM 137
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
515-644 2.52e-09

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: 56.54  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  515 CQEGWERHGGFCYKIDTVLRSFDQASSgyYCPPA---LVTITNRFEQAFITSLISSvvkmkDSYFWIALQDQNDTGEytW 591
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQ--FCEDMgahLVIINSQEEQEFISKILSG-----NRSYWIGLSDEETEGE--W 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767917241  592 KPVGQKPEPVQYTHWNTHQPRYSGG----CVAMrgRHPLGRWEVKHCrHFKAMSLCK 644
Cdd:cd03590    72 KWVDGTPLNSSKTFWHPGEPNNWGGggedCAEL--VYDSGGWNDVPC-NLEYRWICE 125
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
958-1098 3.59e-09

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: 55.80  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  958 CPKGWLYFNYKCLLLNipkdpSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFITMNLFGQttSVWIGLQNDDYE---TWL 1034
Cdd:cd03593     1 CPKDWICYGNKCYYFS-----MEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS--SYWIGLSREKSEkpwKWI 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917241 1035 NGKPvvYSNWSpFDIINIPSHNttevqkhiplCALLSSNpnfhftgKWYFEDCGKEgYGFVCEK 1098
Cdd:cd03593    74 DGSP--LNNLF-NIRGSTKSGN----------CAYLSST-------GIYSEDCSTK-KRWICEK 116
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
390-501 8.80e-09

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: 54.69  E-value: 8.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  390 YKLQKEEKTWHEALRSCQADNSALIDITSLAEVEfLVTLLGDENASETWIGLSSNKIPVSfeWSNDSSVIFTNWHTLEPH 469
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNA-LLSNLSRVSNSAAWIGLYRDVDSWR--WSDGSESSFRNWNTFQPF 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767917241  470 IfpnrSQLCVSAEQSeGHWKVKNCEERLFYIC 501
Cdd:cd03602    80 G----QGDCATMYSS-GRWYAALCSALKPFIC 106
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
255-354 1.08e-08

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 55.09  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  255 EAHSSCQMQGGTLLSITDETEENFIREHMSsKTV----EVWMGLNQLDEHAGWQWSDGTPLNYLNWSPEVNFEP--FVED 328
Cdd:cd03596    23 EASEDCIARGGTLATPRDSDENDALRDYVK-ASVpgnwEVWLGINDMVAEGKWVDVNGSPISYFNWEREITAQPdgGKRE 101
                          90       100
                  ....*....|....*....|....*.
gi 767917241  329 HCGTFSSFMPSAWRSRDCESTLPYIC 354
Cdd:cd03596   102 NCVALSSSAQGKWFDEDCRREKPYVC 127
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
1124-1204 2.54e-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: 53.58  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1124 RTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYAhWIGLFTTDNGLNFDWSDGTKSSFTFWKDEES 1203
Cdd:cd03603     1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAS-WIGASDAATEGTWKWSDGEESTYTNWGSGEP 79

                  .
gi 767917241 1204 S 1204
Cdd:cd03603    80 H 80
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
229-356 2.94e-08

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 53.74  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  229 CDTIWEKdLNSHiCYQFnLLSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKTvevWMGLNQLDEHAGWQWSDG 308
Cdd:cd03588     1 CEEGWDK-FQGH-CYRH-FPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSDG 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767917241  309 TPLNYLNWSPEV--NFEPFVEDhCGTFSSFMPSAWRSRDCESTLPYICKK 356
Cdd:cd03588    75 HPLQFENWRPNQpdNFFATGED-CVVMIWHEEGEWNDVPCNYHLPFTCKK 123
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
816-939 3.32e-08

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: 53.10  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  816 WLFYQDAEYLFHTFASEWLNFEFVCSWLHSDLLTIHSAHEQEFIHSKIKAlskygASWWIGLQEERANDEFRWRDGTPvi 895
Cdd:cd03593     5 WICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS-----SSYWIGLSREKSEKPWKWIDGSP-- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767917241  896 yqnWDTGRERTVNNQSQRCGFISSiTGLWgSEECSVSMPSICKR 939
Cdd:cd03593    78 ---LNNLFNIRGSTKSGNCAYLSS-TGIY-SEDCSTKKRWICEK 116
PHA02642 PHA02642
C-type lectin-like protein; Provisional
944-1028 3.83e-08

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 55.51  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  944 LIEKKKDTPK---QHGTCPKGWLYFNYKCLLLNipkdpSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFitMNLFGQTTS 1020
Cdd:PHA02642   71 LMAFKSDTQEptiKYVTCPKGWIGFGYKCFYFS-----EDSKNWTFGNTFCTSLGATLVKVETEEELNF--LKRYKDSSD 143

                  ....*...
gi 767917241 1021 VWIGLQND 1028
Cdd:PHA02642  144 HWIGLNRE 151
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
958-1097 5.04e-08

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: 53.14  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  958 CPKGWLYFNYKCL-LLNIPkdpsswKNWTHAQHFCAE--EGGTLVAIESEVEQAFIT---MNLFGQTTSVWIGL----QN 1027
Cdd:cd03594     1 CPKGWLPYKGNCYgYFRQP------LSWSDAELFCQKygPGAHLASIHSPAEAAAIAsliSSYQKAYQPVWIGLhdpqQS 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1028 DDYEtWLNGKPVVYSNWSPFDIINIPSHnttevqkhiplCALLSSNPNFHftgKWYFEDCGKEgYGFVCE 1097
Cdd:cd03594    75 RGWE-WSDGSKLDYRSWDRNPPYARGGY-----------CAELSRSTGFL---KWNDANCEER-NPFICK 128
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
1254-1378 5.99e-08

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: 52.33  E-value: 5.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1254 WIKFKSNCYSFSTvlDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSsvqmvWLNAQFDGNNETIKWFDGTP 1333
Cdd:cd03593     5 WICYGNKCYYFSM--EKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY-----WIGLSREKSEKPWKWIDGSP 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767917241 1334 TdqSNWGIRKPDTDYfkpHHCVALripeGLWQLSP--CQEKKGFICK 1378
Cdd:cd03593    78 L--NNLFNIRGSTKS---GNCAYL----SSTGIYSedCSTKKRWICE 115
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
1254-1379 7.96e-08

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 52.19  E-value: 7.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1254 WIKFKSNCYSFSTvlDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEElfafGSSVQMVWLNAQ-FDGNnetIKWFDGT 1332
Cdd:cd03588     5 WDKFQGHCYRHFP--DRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN----AQDYQWIGLNDRtIEGD---FRWSDGH 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767917241 1333 PTDQSNWGIRKPDTDYFKPHHCVALRIPE-GLWQLSPCQEKKGFICKM 1379
Cdd:cd03588    76 PLQFENWRPNQPDNFFATGEDCVVMIWHEeGEWNDVPCNYHLPFTCKK 123
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
840-937 1.01e-07

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: 51.61  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  840 CSWLHSDLLTIHSAHEQEFIHSKIKALSKYGaswWIGLQeeRANDEFRWRDGTPVIYQNWDTGRErtvnNQSQRCGFISS 919
Cdd:cd03602    19 CRENYTDLATVQNQEDNALLSNLSRVSNSAA---WIGLY--RDVDSWRWSDGSESSFRNWNTFQP----FGQGDCATMYS 89
                          90
                  ....*....|....*...
gi 767917241  920 iTGLWGSEECSVSMPSIC 937
Cdd:cd03602    90 -SGRWYAALCSALKPFIC 106
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
1126-1224 1.48e-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: 51.54  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1126 YKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRlGYAHWIGLFTTDNGLNFDWSDGTK--SSFTFWKDEES 1203
Cdd:cd03590    13 YFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSG-NRSYWIGLSDEETEGEWKWVDGTPlnSSKTFWHPGEP 91
                          90       100
                  ....*....|....*....|....*.
gi 767917241 1204 SLLG----DCV-FADSNGRWHSTACE 1224
Cdd:cd03590    92 NNWGgggeDCAeLVYDSGGWNDVPCN 117
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
1120-1223 2.77e-07

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: 51.20  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1120 EYGNRTYKIINANMTWYAAIKTCLM-----HKAQLVSITDQYHQSFL-----TVVLNRLGYAHWIGLFTTDNGLNFDWSD 1189
Cdd:cd03589     7 AFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVydlfeSSRGPDTPYGLWIGLHDRTSEGPFEWTD 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767917241 1190 GTKSSFTFWKDEESSLLG---DCVF----ADSNGRWHSTAC 1223
Cdd:cd03589    87 GSPVDFTKWAGGQPDNYGgneDCVQmwrrGDAGQSWNDMPC 127
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
983-1046 3.55e-07

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: 50.50  E-value: 3.55e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767917241  983 NWTHAQHFCAEEGGTLVAIESEVEQAFITmNLFGQTTSVWIGLQNDDYE---TWLNGKPVVYSNWSP 1046
Cdd:cd03603    11 TWEAAQTLAESLGGHLVTINSAEENDWLL-SNFGGYGASWIGASDAATEgtwKWSDGEESTYTNWGS 76
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
1269-1340 4.39e-07

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: 50.12  E-value: 4.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767917241 1269 DSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSvqmvWLNAQfDGNNE-TIKWFDGTPTDQSNWG 1340
Cdd:cd03603     8 GGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAS----WIGAS-DAATEgTWKWSDGEESTYTNWG 75
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
816-939 6.95e-07

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 49.50  E-value: 6.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  816 WLFYQDAEYLFHTFASEWLNFEFVCSWLHSDLLTIHSAHEQEFIHSKikalskYGASWWIGLQEERANDEFRWRDGTPVI 895
Cdd:cd03588     5 WDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN------AQDYQWIGLNDRTIEGDFRWSDGHPLQ 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767917241  896 YQNWDTGRERTVNNQSQRC-GFISSITGLWGSEECSVSMPSICKR 939
Cdd:cd03588    79 FENWRPNQPDNFFATGEDCvVMIWHEEGEWNDVPCNYHLPFTCKK 123
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
390-469 7.70e-07

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: 49.35  E-value: 7.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  390 YKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGdeNASETWIGLSSNKIPVSFEWSNDSSVIFTNWHTLEPH 469
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFG--GYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
549-616 8.82e-07

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: 49.35  E-value: 8.82e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767917241  549 LVTITNRFEQAFITSLISSvvkmkDSYFWIALQDQNDTGEYTWKpvgqKPEPVQYTHWNTHQPRYSGG 616
Cdd:cd03603    26 LVTINSAEENDWLLSNFGG-----YGASWIGASDAATEGTWKWS----DGEESTYTNWGSGEPHNNGG 84
beta-trefoil_Ricin_MRC1 cd23407
ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) ...
39-117 9.09e-07

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) and similar proteins; MRC1, also called MMR, C-type lectin domain family 13 member D (CLEC13D), C-type lectin domain family 13 member D-like (CLEC13DL), macrophage mannose receptor 1-like protein 1 (MRC1L1), or CD206, mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains. MRC1 acts as phagocytic receptor for bacteria, fungi and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467785  Cd Length: 123  Bit Score: 49.29  E-value: 9.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   39 GIFVIQSESLKKCIQA-GKSVLTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGLNFSAPEQPLSLYECDSTLVSLRWRC 117
Cdd:cd23407     1 RSFLIYNEDHNRCVQArSSSSVTTATCNPNAESQKFRWVSGSQILSVAFKLCLGVPSKKDWVTVTLFPCNEKSELQKWEC 80
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
816-938 1.11e-06

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: 49.29  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  816 WLFYQDAEYLFHTFASEWLNFEFVCSWLHS--DLLTIHSAHEQEFIHSKIKALSKYGASWWIGLQEERANDEFRWRDGTP 893
Cdd:cd03594     5 WLPYKGNCYGYFRQPLSWSDAELFCQKYGPgaHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRGWEWSDGSK 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767917241  894 VIYQNWDTGRERtvnNQSQRCGFISSITG--LWGSEECSVSMPSICK 938
Cdd:cd03594    85 LDYRSWDRNPPY---ARGGYCAELSRSTGflKWNDANCEERNPFICK 128
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
1264-1377 1.36e-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: 48.45  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1264 FSTVLDSMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVqmvwlnaqFDGNNETIK-----WFDGTPTDQSN 1338
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYA--------FIGITDLETegqfvYLDGGPLTYTN 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767917241 1339 WGIRKPDtDYFKPHHCVALrIPEGLWQLSPCQEKKGFIC 1377
Cdd:cd03591    76 WKPGEPN-NAGGGEDCVEM-YTSGKWNDVACNLTRLFVC 112
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
549-645 2.68e-06

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 47.47  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   549 LVTITNRFEQAFItsliSSVVKMKDSYFWIALQDQNDTGEYTWkPVGqkpEPVQYTHWNTHQPRYSGG--CVAMrgRHPL 626
Cdd:pfam00059   18 LVSINSAEELDFL----SSTLKKSNKYFWIGLTDRKNEGTWKW-VDG---SPVNYTNWAPEPNNNGENedCVEL--SSSS 87
                           90
                   ....*....|....*....
gi 767917241   627 GRWEVKHCrHFKAMSLCKQ 645
Cdd:pfam00059   88 GKWNDENC-NSKNPFVCEK 105
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
389-501 2.90e-06

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: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  389 CYKLQKEEKTWHEALRSCQADNSA-LIDITSLAEVEFLVTLLGDENASETWIG--LSSNKIPVSFEWSNDSSVIFTNWHT 465
Cdd:cd03598     3 CYRFVKSPRTFRDAQVICRRCYRGnLASIHSFAFNYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYWAP 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767917241  466 LEPHifpNRSQLCVSAEQSEGHWKVKNCEERLFYIC 501
Cdd:cd03598    83 GQPG---NRRGHCVELCTRGGHWRRAHCKLRRPFIC 115
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
845-902 2.96e-06

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: 47.80  E-value: 2.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767917241  845 SDLLTIHSAHEQEFIHSKikaLSKYGASWwIGLQEERANDEFRWRDGTPVIYQNWDTG 902
Cdd:cd03603    24 GHLVTINSAEENDWLLSN---FGGYGASW-IGASDAATEGTWKWSDGEESTYTNWGSG 77
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
664-757 3.36e-06

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 47.57  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  664 CYLDWESEPGlaSCFKVFHSekvlmKRTWREAEAFCEEFGAHLASFAHIEEENFVNELLHSkfnwteerQFWIGFNKRnp 743
Cdd:cd03588     1 CEEGWDKFQG--HCYRHFPD-----RETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQD--------YQWIGLNDR-- 63
                          90
                  ....*....|....
gi 767917241  744 LNAGSWEWSDRTPV 757
Cdd:cd03588    64 TIEGDFRWSDGHPL 77
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
390-501 3.54e-06

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: 47.37  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  390 YKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASETWIGLssNKIPVSFEW--SNDSSVIFTNWHTLE 467
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDG--NDINNEGTWvdTDKKELEYKNWAPGE 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767917241  468 PHifPNRSQLCV-SAEQSEGHWKVKNCEERLFYIC 501
Cdd:cd03592    81 PN--NGRNENCLeIYIKDNGKWNDEPCSKKKSAIC 113
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
1262-1377 3.57e-06

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: 47.37  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1262 YSFSTVLdsMSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSvqMVWLNAqfDGNNETIKWFD--GTPTDQSNW 1339
Cdd:cd03592     3 YHYSTEK--MTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLG--YYWIDG--NDINNEGTWVDtdKKELEYKNW 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767917241 1340 GIRKPDTDyfKPHHCVALRI-PEGLWQLSPCQEKKGFIC 1377
Cdd:cd03592    77 APGEPNNG--RNENCLEIYIkDNGKWNDEPCSKKKSAIC 113
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
254-354 3.58e-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: 47.29  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  254 SEAHSSCQMQGGTLLSITDETEENFIREHMSSKTVEVWMGLNQLDEHAGWQWSDGTPLNYLNWSP-EVNFEPFVEDhCGT 332
Cdd:cd03591    14 DDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPgEPNNAGGGED-CVE 92
                          90       100
                  ....*....|....*....|...
gi 767917241  333 -FSSfmpSAWRSRDCESTLPYIC 354
Cdd:cd03591    93 mYTS---GKWNDVACNLTRLFVC 112
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
387-502 7.34e-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: 47.58  E-value: 7.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  387 RNCYKLQKEEKT-----WHEALRSCQADNSALIDITSLAEVEFLVTLLGDENASET--WIGL--------SSNKIPVSFE 451
Cdd:cd03595    10 KPCYKIAYFQDSrrrlnFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGdfWIGLrrssqynvTSSACSSLYY 89
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767917241  452 WSNDSSVIFTNWHTLEPHIfpnRSQLCV------SAEQSEG-----HWKVKNCEERLFYICK 502
Cdd:cd03595    90 WLDGSISTFRNWYVDEPSC---GSEVCVvmyhqpSAPAGQGgpylfQWNDDNCNMKNNFICK 148
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
390-501 9.09e-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: 9.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  390 YKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENaSETWIGLSSNKIPVSFEWSNDSSVIFTNWHTLEPH 469
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGN-TYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPN 82
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767917241  470 iFPNRSQLCVSAEQSeGHWKVKNCEERLFYIC 501
Cdd:cd03591    83 -NAGGGEDCVEMYTS-GKWNDVACNLTRLFVC 112
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
241-355 9.14e-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: 47.19  E-value: 9.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  241 ICYQFNLLSSLSWSEAHSSCQMQGGTLLSITDETE----ENFIREHMSSKTvEVWMGL--------NQLDEHAGWQWSDG 308
Cdd:cd03595    15 IAYFQDSRRRLNFEEARQACREDGGELLSIESENEqkliERFIQTLRASDG-DFWIGLrrssqynvTSSACSSLYYWLDG 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767917241  309 TPLNYLNWSpevnfepFVEDHCGTFSS----FMPSA-----------WRSRDCESTLPYICK 355
Cdd:cd03595    94 SISTFRNWY-------VDEPSCGSEVCvvmyHQPSApagqggpylfqWNDDNCNMKNNFICK 148
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
958-1097 1.03e-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: 46.61  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  958 CPKGwLYFNYKCLLLNipkdpSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFIT---MNLFGQTTSVWIGLQNDDYE-TW 1033
Cdd:cd03596     1 CLKG-TKIHKKCYLVS-----EETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWEVWLGINDMVAEgKW 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767917241 1034 L--NGKPVVYSNWSPfDIINIPSHNTTEVqkhiplCALLSSNPNfhftGKWYFEDCGKEGYgFVCE 1097
Cdd:cd03596    75 VdvNGSPISYFNWER-EITAQPDGGKREN------CVALSSSAQ----GKWFDEDCRREKP-YVCE 128
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
982-1097 1.17e-05

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: 45.75  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  982 KNWTHAQHFCAEEGGTLVAIESEVEQAFITMNLFGQTTSVWIGLQNDDYE---TWLNGKPVVYSNWSPfdiiNIPS-HNT 1057
Cdd:cd03591    11 KNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEgqfVYLDGGPLTYTNWKP----GEPNnAGG 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767917241 1058 TEVqkhiplCALLSSNpnfhftGKWYFEDCGKEGYgFVCE 1097
Cdd:cd03591    87 GED------CVEMYTS------GKWNDVACNLTRL-FVCE 113
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
1261-1377 1.20e-05

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: 45.90  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1261 CYSFstVLDSMSFEAAHEFCKK-EGSNLLTIKDEAENAFLLEelFAFGSSVQMVWLNAQ--FDGNNETIKWFDGTPTDQS 1337
Cdd:cd03598     3 CYRF--VKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQR--LVSTLNQAQVWIGGIitGKGRCRRFSWVDGSVWNYA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767917241 1338 NWGIRKPDTDYfkpHHCVALRIPEGLWQLSPCQEKKGFIC 1377
Cdd:cd03598    79 YWAPGQPGNRR---GHCVELCTRGGHWRRAHCKLRRPFIC 115
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
384-502 2.86e-05

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: 48.93  E-value: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   384 PYNRNCYKLQKEEKTWHEALRSCQA-DNSALIDITSLAEVEFLVTLLGDENASETWIGLSS-NKIPVS-FEWSNDSSV-I 459
Cdd:TIGR00864  326 EENGHCFQIVPEEAAWLDAQEQCLArAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFSDvNGAEKGpAHQGEAFEAeE 405
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 767917241   460 FTNWHTLEPHifPNRSQLCVSAEQSeGHWKVKNCEERLFYICK 502
Cdd:TIGR00864  406 CEEGLAGEPH--PARAEHCVRLDPR-GQCNSDLCNAPHAYVCE 445
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
982-1047 2.95e-05

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: 44.67  E-value: 2.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767917241  982 KNWTHAQHFCAEEGGTLVAIESEVEQAFITMNLFGQTTSVWIGLQNDDYE-TWLNGKPVVYSNWSPF 1047
Cdd:cd03602    10 KTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSwRWSDGSESSFRNWNTF 76
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
387-501 3.36e-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: 45.07  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  387 RNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDE--NASETWIGLSSNKIPVSFEWSNDSSVIFTNWH 464
Cdd:cd03596     9 KKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASvpGNWEVWLGINDMVAEGKWVDVNGSPISYFNWE 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767917241  465 TLEPHIfPN--RSQLCVS-AEQSEGHWKVKNCEERLFYIC 501
Cdd:cd03596    89 REITAQ-PDggKRENCVAlSSSAQGKWFDEDCRREKPYVC 127
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
1257-1378 5.72e-05

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: 44.88  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1257 FKSNCYSFSTVLDS---MSFEAAHEFCKKEGSNLLTIKDEAENAFLLEELFAFGSSVQMVW--LNAQFDGNNETIK---- 1327
Cdd:cd03595     8 TEKPCYKIAYFQDSrrrLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWigLRRSSQYNVTSSAcssl 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917241 1328 --WFDGTPTDQSNWGIRKPDTDYfkpHHCVAL----RIPEGL-------WQLSPCQEKKGFICK 1378
Cdd:cd03595    88 yyWLDGSISTFRNWYVDEPSCGS---EVCVVMyhqpSAPAGQggpylfqWNDDNCNMKNNFICK 148
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
847-937 1.00e-04

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: 43.21  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  847 LLTIHSAHeqefIHSKIKALSKYG--ASWWIGLQEERA--NDEFRWRDGTPVIYQNWDTGRERtvnNQSQRCGFISSITG 922
Cdd:cd03598    28 LASIHSFA----FNYRVQRLVSTLnqAQVWIGGIITGKgrCRRFSWVDGSVWNYAYWAPGQPG---NRRGHCVELCTRGG 100
                          90
                  ....*....|....*
gi 767917241  923 LWGSEECSVSMPSIC 937
Cdd:cd03598   101 HWRRAHCKLRRPFIC 115
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
840-939 1.23e-04

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: 43.13  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  840 CSWLHSDLLTIHSAHEQEFIHSKIKALSKygASWWIGLQEerANDEFRW--RDGTPVIYQNWDTGRERtvNNQSQRCGFI 917
Cdd:cd03592    19 CKSRGTDLVAIQNAEENALLNGFALKYNL--GYYWIDGND--INNEGTWvdTDKKELEYKNWAPGEPN--NGRNENCLEI 92
                          90       100
                  ....*....|....*....|...
gi 767917241  918 S-SITGLWGSEECSVSMPSICKR 939
Cdd:cd03592    93 YiKDNGKWNDEPCSKKKSAICYT 115
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
847-937 1.37e-04

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: 43.15  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  847 LLTIHSAHEQEFIHSKIKALSKYGASWWIGLQEERANDEFRWRDGTPVIYQNWDTGRERTVN-NQSQRCGFISSIT-GLW 924
Cdd:cd03596    35 LATPRDSDENDALRDYVKASVPGNWEVWLGINDMVAEGKWVDVNGSPISYFNWEREITAQPDgGKRENCVALSSSAqGKW 114
                          90
                  ....*....|...
gi 767917241  925 GSEECSVSMPSIC 937
Cdd:cd03596   115 FDEDCRREKPYVC 127
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
515-629 1.45e-04

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 42.95  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  515 CQEGWERHGGFCYKIDTVLRSFDQASSgyYCPPA---LVTITNRFEQAFITSLissvvkmKDSYFWIALQDQNDTGEYTW 591
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAER--RCREQqghLSSIVTPEEQEFVNNN-------AQDYQWIGLNDRTIEGDFRW 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767917241  592 kpvgQKPEPVQYTHWNTHQPR--YSGG--CVAMRGrHPLGRW 629
Cdd:cd03588    72 ----SDGHPLQFENWRPNQPDnfFATGedCVVMIW-HEEGEW 108
PHA02642 PHA02642
C-type lectin-like protein; Provisional
221-312 1.55e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 44.72  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  221 DPTSAEVGCDTIWEKdlNSHICYQFNLlSSLSWSEAHSSCQMQGGTLLSITDETEENFIREHMSSKtvEVWMGLNQLDEH 300
Cdd:PHA02642   80 EPTIKYVTCPKGWIG--FGYKCFYFSE-DSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSS--DHWIGLNRESSN 154
                          90
                  ....*....|..
gi 767917241  301 AGWQWSDGTPLN 312
Cdd:PHA02642  155 HPWKWADNSNYN 166
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
515-629 1.70e-04

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: 43.12  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  515 CQEGWERHGGFCYKIDTVLRSFDQASS---GYYCPPA---LVTITNRFEQAFITSLISSVVKMKDSY-FWIALQDQNDTG 587
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELrcrSFSIPGLiahLVSIHSQEENDFVYDLFESSRGPDTPYgLWIGLHDRTSEG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767917241  588 EYTWkpvgQKPEPVQYTHWNTHQPRYSGG---CVAMRGR-HPLGRW 629
Cdd:cd03589    81 PFEW----TDGSPVDFTKWAGGQPDNYGGnedCVQMWRRgDAGQSW 122
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
389-502 2.95e-04

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 42.42  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  389 CYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLG------DENASETWIGL-------SSNKIPV-SFEW-S 453
Cdd:cd03600     6 CYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAagpgrhGRGSLRLWIGLqreprqcSDPSLPLrGFSWvT 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767917241  454 NDSSVIFTNWHTlEPHIfPNRSQLCVSAEQSEGH-----WKVKNCEERL-FYICK 502
Cdd:cd03600    86 GDQDTDFSNWLQ-EPAG-TCTSPRCVALSAAGSTpdnlkWKDGPCSARAdGYLCK 138
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
676-753 4.67e-04

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 42.03  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  676 SCFKVFHSekvlmKRTWREAEAFCEEFGAHLASFAHIEEENFVNELLHS--KFNWTEERQFWIGFNKR--------NPLN 745
Cdd:cd03600     5 ACYTLHPQ-----KLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAgpGRHGRGSLRLWIGLQREprqcsdpsLPLR 79

                  ....*...
gi 767917241  746 AGSWEWSD 753
Cdd:cd03600    80 GFSWVTGD 87
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
958-1046 5.08e-04

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 41.41  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  958 CPKGWLYFNYKCLllnipKDPSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFITMNlfGQTTSvWIGLQNDDYET---WL 1034
Cdd:cd03588     1 CEEGWDKFQGHCY-----RHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN--AQDYQ-WIGLNDRTIEGdfrWS 72
                          90
                  ....*....|..
gi 767917241 1035 NGKPVVYSNWSP 1046
Cdd:cd03588    73 DGHPLQFENWRP 84
beta-trefoil_Ricin_PTPRB-like cd23409
ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein ...
41-151 5.95e-04

ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e and similar proteins; PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, R-PTP-beta, vascular endothelial protein tyrosine phosphatase, or VE-PTP, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells, which requires the presence of plakoglobin. The subfamily corresponds to PTPRB isoform e, which contains an extra ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467787  Cd Length: 117  Bit Score: 40.88  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   41 FVIQSESLKKCIQAGKSVlTLENCKQANKHMLWKWVSNHGLFNIGGSGCLGL--NFSAPEQPLSLYECDStlvSLRWRCN 118
Cdd:cd23409     4 FLILHVQKQQCLFGNKTV-SVGKCNATSPNQQWQWTEDGKLLHVKSGQCLGIsnSSAFHSRRAILLDCSQ---APRWTCH 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767917241  119 RKMitGPLQ------YSVQVAHDNTVVASRKYIHKWISY 151
Cdd:cd23409    80 ENE--GLLEvansslFLTKQGQRVVVKQGKKYLHNWMKY 116
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
976-1044 6.30e-04

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: 41.80  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  976 KDPSSWKNWTHAQHFCAEEGGTLVAIESEVEQAFITMNLFGQTTS---VWIGLQND-----------DYETWLNGKPVVY 1041
Cdd:cd03595    19 QDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASdgdFWIGLRRSsqynvtssacsSLYYWLDGSISTF 98

                  ...
gi 767917241 1042 SNW 1044
Cdd:cd03595    99 RNW 101
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
242-354 6.43e-04

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: 40.90  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  242 CYQFNLlSSLSWSEAHSSCQ-MQGGTLLSITDETEENFIReHMSSKT--VEVWMGLNQLDEHAGWQ--WSDGTPLNYLNW 316
Cdd:cd03598     3 CYRFVK-SPRTFRDAQVICRrCYRGNLASIHSFAFNYRVQ-RLVSTLnqAQVWIGGIITGKGRCRRfsWVDGSVWNYAYW 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767917241  317 SPEvnfEPFVED-HCGTFSSfMPSAWRSRDCESTLPYIC 354
Cdd:cd03598    81 APG---QPGNRRgHCVELCT-RGGHWRRAHCKLRRPFIC 115
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
852-937 7.33e-04

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: 40.74  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  852 SAHEQEFIHSKIKALSKYGaswWIGLQEERANDEFRWRDGTPVIYQNWDTGRErtvNNQ--SQRCGFISSiTGLWGSEEC 929
Cdd:cd03591    32 NAAENAAIASYVKKGNTYA---FIGITDLETEGQFVYLDGGPLTYTNWKPGEP---NNAggGEDCVEMYT-SGKWNDVAC 104

                  ....*...
gi 767917241  930 SVSMPSIC 937
Cdd:cd03591   105 NLTRLFVC 112
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
1121-1225 1.10e-03

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: 40.39  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1121 YGNRTYKIINANMTWYAAIKTCLMHKAQLVSITDQYHQSFLTVVLNRLGYahWIGLFTTDNGLNFDWSDGTKSSFTFwKD 1200
Cdd:cd03593     8 YGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWKWIDGSPLNNLF-NI 84
                          90       100
                  ....*....|....*....|....*
gi 767917241 1201 EESSLLGDCVFAdSNGRWHSTACES 1225
Cdd:cd03593    85 RGSTKSGNCAYL-SSTGIYSEDCST 108
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
1123-1232 1.84e-03

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: 39.74  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1123 NRTYKIINANMTWYAAIKTCL-MHKAQLVSITDQYHQSFLTVVLNRLGYAH-WIGLFTTDNGLN--FDWSDGTKSSFTFW 1198
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRrCYRGNLASIHSFAFNYRVQRLVSTLNQAQvWIGGIITGKGRCrrFSWVDGSVWNYAYW 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767917241 1199 -KDEESSLLGDCV-FADSNGRWHSTACeSFLQGAIC 1232
Cdd:cd03598    81 aPGQPGNRRGHCVeLCTRGGHWRRAHC-KLRRPFIC 115
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
527-635 2.49e-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: 39.28  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  527 YKIDTVLRSFDQASSgyYC---PPALVTITNRFEQAFITSLIssvVKMKDSYFWIALQDQNDTGeyTWkpVGQKPEPVQY 603
Cdd:cd03592     3 YHYSTEKMTFNEAVK--YCksrGTDLVAIQNAEENALLNGFA---LKYNLGYYWIDGNDINNEG--TW--VDTDKKELEY 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767917241  604 THWNTHQPRYSGG--CVAMRgRHPLGRWEVKHCR 635
Cdd:cd03592    74 KNWAPGEPNNGRNenCLEIY-IKDNGKWNDEPCS 106
beta-trefoil_Ricin_unchar cd23412
ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose ...
41-120 2.86e-03

ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose receptor (MRC)-like proteins; The subfamily corresponds to a group of uncharacterized ricin B-type lectin beta-trefoil domain-containing proteins from Gnathostomata. They show high sequence similarity with macrophage mannose receptor (MRC) family proteins.


Pssm-ID: 467790  Cd Length: 127  Bit Score: 39.31  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241   41 FVIQSESLKKCIQA---GKSVLTLENCKQANKHMLWKW-VSNHGLFNIGGSGCLGLnFSAPEQP-LSLYECDSTlVSLRW 115
Cdd:cd23412     5 FMIRNVQLEKCIQVdhgESERVSLAECKPHSEHQQWSWdPETRALSSLHTGECLTV-LKIQEFGsVRLEPCGSR-EPQAW 82

                  ....*
gi 767917241  116 RCNRK 120
Cdd:cd23412    83 SCSKK 87
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
1119-1225 3.01e-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: 39.28  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241 1119 LEYGNRTYKIINANMTWYAAIKTCLMHK--AQLVSITDQYHQSFLTVVLNRLGYAH---WIGLFTTDNGLNFDWSDGTKS 1193
Cdd:cd03594     6 LPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSYQKAYqpvWIGLHDPQQSRGWEWSDGSKL 85
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767917241 1194 SFTFWKDEESSLLGD-CV-FADSNG--RWHSTACES 1225
Cdd:cd03594    86 DYRSWDRNPPYARGGyCAeLSRSTGflKWNDANCEE 121
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
549-638 3.03e-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: 38.89  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  549 LVTITNRFEQAfitsLISSVVKMKDSYFWIALQDQNDTgeytWKPVGQkpEPVQYTHWNTHQPRYSGGCVAMRgrhPLGR 628
Cdd:cd03602    26 LATVQNQEDNA----LLSNLSRVSNSAAWIGLYRDVDS----WRWSDG--SESSFRNWNTFQPFGQGDCATMY---SSGR 92
                          90
                  ....*....|
gi 767917241  629 WEVKHCRHFK 638
Cdd:cd03602    93 WYAALCSALK 102
PHA03097 PHA03097
C-type lectin-like protein; Provisional
378-458 6.22e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 39.08  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLLGDENaseTWIGLSSNKipvsfEWSNDSS 457
Cdd:PHA03097   46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQD---LWIGIEKKK-----GDDDDRE 117

                  .
gi 767917241  458 V 458
Cdd:PHA03097  118 V 118
PHA02642 PHA02642
C-type lectin-like protein; Provisional
378-457 6.93e-03

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 39.71  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  378 CEPGWNPYNRNCYKLQKEEKTWHEALRSCQADNSALIDITSLAEVEFLVTLlgdENASETWIGLSSNKIPVSFEWSNDSS 457
Cdd:PHA02642   88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRY---KDSSDHWIGLNRESSNHPWKWADNSN 164
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
251-354 8.50e-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: 37.74  E-value: 8.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917241  251 LSWSEAHSSCQMQGGTLLSITDETEENFI---REHMSSKTVevWMGLNQLDEHAGWQWSDGTPLNYLNWSPEvnfEP--F 325
Cdd:cd03592    10 MTFNEAVKYCKSRGTDLVAIQNAEENALLngfALKYNLGYY--WIDGNDINNEGTWVDTDKKELEYKNWAPG---EPnnG 84
                          90       100
                  ....*....|....*....|....*....
gi 767917241  326 VEDHCGTFSSFMPSAWRSRDCESTLPYIC 354
Cdd:cd03592    85 RNENCLEIYIKDNGKWNDEPCSKKKSAIC 113
 
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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