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Conserved domains on  [gi|17508937|ref|NP_493196|]
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C-type LECtin [Caenorhabditis elegans]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 309-408 1.79e-26

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


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 102.49  E-value: 1.79e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937 309 VITSPNYPENYFNNANCTYTLSTLGSYKIILVFYDFRLEA----GRDFVTVYDGETTSSPVLaARLSGTIKGGfSYTSTG 384
Cdd:cd00041  12 TISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLL-GRFCGSTLPP-PIISSG 89

                        90       100
                ....*....|....*....|....
gi 17508937 385 NNMLVTFTSDASIVGPGFTARFTS 408
Cdd:cd00041  90 NSLTVRFRSDSSVTGRGFKATYSA 113
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 24-152 6.97e-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: 95.74  E-value: 6.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937     24 CTNGFTLINNKCLKLFSTPVNHTTAEKSCGSFGATLVQAKNNIDNQAIATIAGS-GSSTLIWLGLYCfESDPSQCFWDDE 102
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsGSSDYYWIGLSD-PDSNGSWQWSDG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17508937    103 TGSAhTYNNFSSGFPIVELGQCVYYSTQGvltGKWLSENCESQRiSYICE 152
Cdd:smart00034  80 SGPV-SYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKL-PFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 165-277 2.84e-21

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: 88.81  E-value: 2.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937    165 YNGYCYTFSTADAPFSTAQGICAQSCGNLASIHSSNEARYLTTFAPE----GYYYIGAVWH-HDSSLIWLDRSAW-DYSD 238
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgssDYYWIGLSDPdSNGSWQWSDGSGPvSYSN 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 17508937    239 IDPIFP--RVDYCLKMSAFNGYptgmWYSNNCVDNNKYVCK 277
Cdd:smart00034  88 WAPGEPnnSSGDCVVLSTSGGK----WNDVSCTSKLPFVCE 124
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 309-408 1.79e-26

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


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 102.49  E-value: 1.79e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937 309 VITSPNYPENYFNNANCTYTLSTLGSYKIILVFYDFRLEA----GRDFVTVYDGETTSSPVLaARLSGTIKGGfSYTSTG 384
Cdd:cd00041  12 TISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLL-GRFCGSTLPP-PIISSG 89

                        90       100
                ....*....|....*....|....
gi 17508937 385 NNMLVTFTSDASIVGPGFTARFTS 408
Cdd:cd00041  90 NSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 309-406 6.59e-26

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


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 100.54  E-value: 6.59e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937    309 VITSPNYPENYFNNANCTYTLSTLGSYKIILVFYDFRLEAGR----DFVTVYDGETTSSPVLaARLSGTIKGGFSYTSTG 384
Cdd:smart00042   2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLL-GRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 17508937    385 NNMLVTFTSDASIVGPGFTARF 406
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 24-152 6.97e-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: 95.74  E-value: 6.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937     24 CTNGFTLINNKCLKLFSTPVNHTTAEKSCGSFGATLVQAKNNIDNQAIATIAGS-GSSTLIWLGLYCfESDPSQCFWDDE 102
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsGSSDYYWIGLSD-PDSNGSWQWSDG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17508937    103 TGSAhTYNNFSSGFPIVELGQCVYYSTQGvltGKWLSENCESQRiSYICE 152
Cdd:smart00034  80 SGPV-SYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKL-PFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 165-277 2.84e-21

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: 88.81  E-value: 2.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937    165 YNGYCYTFSTADAPFSTAQGICAQSCGNLASIHSSNEARYLTTFAPE----GYYYIGAVWH-HDSSLIWLDRSAW-DYSD 238
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgssDYYWIGLSDPdSNGSWQWSDGSGPvSYSN 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 17508937    239 IDPIFP--RVDYCLKMSAFNGYptgmWYSNNCVDNNKYVCK 277
Cdd:smart00034  88 WAPGEPnnSSGDCVVLSTSGGK----WNDVSCTSKLPFVCE 124
CUB pfam00431
CUB domain;
307-406 1.34e-18

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 80.80  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937   307 NAVITSPNYPENYFNNANCTYTLSTLGSYKIILVFYDFRLEAGR----DFVTVYDGETTSSPVLaARLSGTIKGGfSYTS 382
Cdd:pfam00431   9 SGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDecgyDYVEIRDGPSASSPLL-GRFCGSGIPE-DIVS 86

                          90       100
                  ....*....|....*....|....
gi 17508937   383 TGNNMLVTFTSDASIVGPGFTARF 406
Cdd:pfam00431  87 SSNQMTIKFVSDASVQKRGFKATY 110
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 34-152 1.42e-15

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 72.65  E-value: 1.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937  34 KCLKLFSTPVNHTTAEKSCGSFGATLVQAKNNIDNQAIATIAGSGSSTLIWLGLYCFESDpSQCFWDDETGSAhTYNNFS 113
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSE-GTWKWSDGSPLV-DYTNWA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17508937 114 SGFP-IVELGQCVYYSTQGvlTGKWLSENCESQRiSYICE 152
Cdd:cd00037  79 PGEPnPGGSEDCVVLSSSS--DGKWNDVSCSSKL-PFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 168-278 9.42e-14

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: 67.26  E-value: 9.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937 168 YCYTFSTADAPFSTAQGICAQSCGNLASIHSSNEARYLTTFAPEG---YYYIGAVWH-HDSSLIWLDRS-AWDYSDIDPI 242
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSsssDVWIGLNDLsSEGTWKWSDGSpLVDYTNWAPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17508937 243 FPRVD---YCLkmsAFNGYPTGMWYSNNCVDNNKYVCKR 278
Cdd:cd00037  81 EPNPGgseDCV---VLSSSSDGKWNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 42-152 3.59e-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: 45.55  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937    42 PVNHTTAEKSCGSFGATLVQAKNNIDNQAIATIAGSgSSTLIWLGLYcFESDPSQCFWDDETGSahTYNNFSSGFPIV-E 120
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKK-SNKYFWIGLT-DRKNEGTWKWVDGSPV--NYTNWAPEPNNNgE 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 17508937   121 LGQCVYYSTQgvlTGKWLSENCESQRiSYICE 152
Cdd:pfam00059  77 NEDCVELSSS---SGKWNDENCNSKN-PFVCE 104
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 178-278 5.70e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 39.00  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937   178 PFSTAQGICAQSCGNLASIHSSNEARYLTTFAPEG--YYYIG-------AVWH-----HDSSLIWLDRSAWDYSDIDpif 243
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSnkYFWIGltdrkneGTWKwvdgsPVNYTNWAPEPNNNGENED--- 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 17508937   244 prvdyCLKMSafngYPTGMWYSNNCVDNNKYVCKR 278
Cdd:pfam00059  80 -----CVELS----SSSGKWNDENCNSKNPFVCEK 105
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 3-151 4.33e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 37.54  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937    3 TISALLIFTVCLASCVTSSPI-CTNGFTLINNKCLKLFSTPVNHTTAEKSCGSFGATLVQAKNNIDNQAIATIAGSGSst 81
Cdd:PHA03097  24 ALIALVIILSCKLSPGDRSGLnCRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQD-- 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17508937   82 lIWLGlycfesdpsqcfwdDETGSAHTYNNFSSG--FPIVELGQCVYYSTQGVltgkwLSENCESQRiSYIC 151
Cdd:PHA03097 102 -LWIG--------------IEKKKGDDDDREVLDkvVKPPKSGKCAYLKDKTI-----ISSNCNATK-GWIC 152
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 309-408 1.79e-26

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


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 102.49  E-value: 1.79e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937 309 VITSPNYPENYFNNANCTYTLSTLGSYKIILVFYDFRLEA----GRDFVTVYDGETTSSPVLaARLSGTIKGGfSYTSTG 384
Cdd:cd00041  12 TISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLL-GRFCGSTLPP-PIISSG 89

                        90       100
                ....*....|....*....|....
gi 17508937 385 NNMLVTFTSDASIVGPGFTARFTS 408
Cdd:cd00041  90 NSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 309-406 6.59e-26

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


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 100.54  E-value: 6.59e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937    309 VITSPNYPENYFNNANCTYTLSTLGSYKIILVFYDFRLEAGR----DFVTVYDGETTSSPVLaARLSGTIKGGFSYTSTG 384
Cdd:smart00042   2 TITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLL-GRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 17508937    385 NNMLVTFTSDASIVGPGFTARF 406
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 24-152 6.97e-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: 95.74  E-value: 6.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937     24 CTNGFTLINNKCLKLFSTPVNHTTAEKSCGSFGATLVQAKNNIDNQAIATIAGS-GSSTLIWLGLYCfESDPSQCFWDDE 102
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsGSSDYYWIGLSD-PDSNGSWQWSDG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17508937    103 TGSAhTYNNFSSGFPIVELGQCVYYSTQGvltGKWLSENCESQRiSYICE 152
Cdd:smart00034  80 SGPV-SYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKL-PFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 165-277 2.84e-21

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: 88.81  E-value: 2.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937    165 YNGYCYTFSTADAPFSTAQGICAQSCGNLASIHSSNEARYLTTFAPE----GYYYIGAVWH-HDSSLIWLDRSAW-DYSD 238
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgssDYYWIGLSDPdSNGSWQWSDGSGPvSYSN 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 17508937    239 IDPIFP--RVDYCLKMSAFNGYptgmWYSNNCVDNNKYVCK 277
Cdd:smart00034  88 WAPGEPnnSSGDCVVLSTSGGK----WNDVSCTSKLPFVCE 124
CUB pfam00431
CUB domain;
307-406 1.34e-18

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 80.80  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937   307 NAVITSPNYPENYFNNANCTYTLSTLGSYKIILVFYDFRLEAGR----DFVTVYDGETTSSPVLaARLSGTIKGGfSYTS 382
Cdd:pfam00431   9 SGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDecgyDYVEIRDGPSASSPLL-GRFCGSGIPE-DIVS 86

                          90       100
                  ....*....|....*....|....
gi 17508937   383 TGNNMLVTFTSDASIVGPGFTARF 406
Cdd:pfam00431  87 SSNQMTIKFVSDASVQKRGFKATY 110
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 34-152 1.42e-15

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 72.65  E-value: 1.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937  34 KCLKLFSTPVNHTTAEKSCGSFGATLVQAKNNIDNQAIATIAGSGSSTLIWLGLYCFESDpSQCFWDDETGSAhTYNNFS 113
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSE-GTWKWSDGSPLV-DYTNWA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17508937 114 SGFP-IVELGQCVYYSTQGvlTGKWLSENCESQRiSYICE 152
Cdd:cd00037  79 PGEPnPGGSEDCVVLSSSS--DGKWNDVSCSSKL-PFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 168-278 9.42e-14

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: 67.26  E-value: 9.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937 168 YCYTFSTADAPFSTAQGICAQSCGNLASIHSSNEARYLTTFAPEG---YYYIGAVWH-HDSSLIWLDRS-AWDYSDIDPI 242
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSsssDVWIGLNDLsSEGTWKWSDGSpLVDYTNWAPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17508937 243 FPRVD---YCLkmsAFNGYPTGMWYSNNCVDNNKYVCKR 278
Cdd:cd00037  81 EPNPGgseDCV---VLSSSSDGKWNDVSCSSKLPFICEK 116
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 165-277 6.66e-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: 62.39  E-value: 6.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937 165 YNGYCYTFSTADAPFSTAQGICAQ--SCGNLASIHSSNEARYLTTF-----APEGYYYIGA-VWHHDSSLIWLDRSAWDY 236
Cdd:cd03594   8 YKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLissyqKAYQPVWIGLhDPQQSRGWEWSDGSKLDY 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 17508937 237 S--DIDPIFPRVDYCLKMSAFNGYPTgmWYSNNCVDNNKYVCK 277
Cdd:cd03594  88 RswDRNPPYARGGYCAELSRSTGFLK--WNDANCEERNPFICK 128
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 167-276 4.08e-07

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 48.60  E-value: 4.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937 167 GYCYTFSTADAPFSTAQGICaQSC--GNLASIHS---SNEARYLTTFAPEGYYYIGAV---WHHDSSLIWLDRSAWDYSD 238
Cdd:cd03598   1 GRCYRFVKSPRTFRDAQVIC-RRCyrGNLASIHSfafNYRVQRLVSTLNQAQVWIGGIitgKGRCRRFSWVDGSVWNYAY 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17508937 239 --IDPIFPRVDYCLKMSAFNGYptgmWYSNNCVDNNKYVC 276
Cdd:cd03598  80 waPGQPGNRRGHCVELCTRGGH----WRRAHCKLRRPFIC 115
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 24-152 1.69e-06

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: 47.00  E-value: 1.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937  24 CTNGfTLINNKCLKLFSTPVNHTTAEKSCGSFGATLVQAKNNIDNQAIATI--AGSGSSTLIWLGLycfeSD-PSQCFWD 100
Cdd:cd03596   1 CLKG-TKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYvkASVPGNWEVWLGI----NDmVAEGKWV 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17508937 101 DETGSAHTYNNFSSGFPIVELG----QCVYYStqGVLTGKWLSENCESQRiSYICE 152
Cdd:cd03596  76 DVNGSPISYFNWEREITAQPDGgkreNCVALS--SSAQGKWFDEDCRREK-PYVCE 128
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 42-152 3.59e-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: 45.55  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937    42 PVNHTTAEKSCGSFGATLVQAKNNIDNQAIATIAGSgSSTLIWLGLYcFESDPSQCFWDDETGSahTYNNFSSGFPIV-E 120
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKK-SNKYFWIGLT-DRKNEGTWKWVDGSPV--NYTNWAPEPNNNgE 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 17508937   121 LGQCVYYSTQgvlTGKWLSENCESQRiSYICE 152
Cdd:pfam00059  77 NEDCVELSSS---SGKWNDENCNSKN-PFVCE 104
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 165-277 6.86e-05

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: 42.35  E-value: 6.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937 165 YNGYCYTFSTADAPFSTAQGICAQ-SC----GNLASIHSSNEARYLTTF-----APEGYY--YIGAvwhHDSS----LIW 228
Cdd:cd03589   8 FGGYCYRFFGDRLTWEEAELRCRSfSIpgliAHLVSIHSQEENDFVYDLfessrGPDTPYglWIGL---HDRTsegpFEW 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 17508937 229 LDRSAWDYSDIDPIFPRVDY----CLKMsAFNGYPTGMWYSNNCVDNNKYVCK 277
Cdd:cd03589  85 TDGSPVDFTKWAGGQPDNYGgnedCVQM-WRRGDAGQSWNDMPCDAVFPYICK 136
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 24-152 1.53e-04

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 41.20  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937  24 CTNGFTLINNKCLKLFSTPVNHTTAEKSCGSF--GATLVQAKNNIDNQAIAT-IAGSGSST-LIWLGLYcfesDPSQCF- 98
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASlISSYQKAYqPVWIGLH----DPQQSRg 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 17508937  99 --WDDetGSAHTYNNFSSGFPIVELGQCVYYS-TQGVLtgKWLSENCESqRISYICE 152
Cdd:cd03594  77 weWSD--GSKLDYRSWDRNPPYARGGYCAELSrSTGFL--KWNDANCEE-RNPFICK 128
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 178-278 5.70e-04

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 39.00  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937   178 PFSTAQGICAQSCGNLASIHSSNEARYLTTFAPEG--YYYIG-------AVWH-----HDSSLIWLDRSAWDYSDIDpif 243
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSnkYFWIGltdrkneGTWKwvdgsPVNYTNWAPEPNNNGENED--- 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 17508937   244 prvdyCLKMSafngYPTGMWYSNNCVDNNKYVCKR 278
Cdd:pfam00059  80 -----CVELS----SSSGKWNDENCNSKNPFVCEK 105
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 3-151 4.33e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 37.54  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508937    3 TISALLIFTVCLASCVTSSPI-CTNGFTLINNKCLKLFSTPVNHTTAEKSCGSFGATLVQAKNNIDNQAIATIAGSGSst 81
Cdd:PHA03097  24 ALIALVIILSCKLSPGDRSGLnCRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQD-- 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17508937   82 lIWLGlycfesdpsqcfwdDETGSAHTYNNFSSG--FPIVELGQCVYYSTQGVltgkwLSENCESQRiSYIC 151
Cdd:PHA03097 102 -LWIG--------------IEKKKGDDDDREVLDkvVKPPKSGKCAYLKDKTI-----ISSNCNATK-GWIC 152
 
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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