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Conserved domains on  [gi|71998057|ref|NP_496687|]
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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 ...
 303-413 5.88e-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: 101.33  E-value: 5.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057 303 CNSSMI-MAPGTISSPAYPGYYDNNMYCSYLLSTTGAYNILLKFTDF----STNLNLDYVTVYDGETTSSPMLGSFSGfN 377
Cdd:cd00041   1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFdlesSPNCSYDYLEIYDGPSTSSPLLGRFCG-S 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71998057 378 ETPINLVSTGNTMLVTFRSgnseDSNIRY-GFSATFS 413
Cdd:cd00041  80 TLPPPIISSGNSLTVRFRS----DSSVTGrGFKATYS 112
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 23-152 4.25e-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: 85.34  E-value: 4.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057     23 CSNGYTLvNNNKCLRLFKTPETHKTAELTCLKNGGaTLANIKSSIDNRAITIFVGGASNS--IWIGLFCTKSSaKECFWD 100
Cdd:smart00034   1 CPSGWIS-YGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSN-GSWQWS 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 71998057    101 DDSGSaDQFQNFKSGFPLVEKGRCVYSSQvafDRGQWSSGDCEKESRaFVCE 152
Cdd:smart00034  78 DGSGP-VSYSNWAPGEPNNSSGDCVVLST---SGGKWNDVSCTSKLP-FVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 165-279 8.28e-13

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: 64.93  E-value: 8.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057    165 YNGYCY-FDFAPLPFVSAQKICKENCGIIASILSPMENRYIN---ANFYTYSALLIGATWSY-NSSYTWFDGSSW-SYHN 238
Cdd:smart00034   8 YGGKCYkFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAsllKNSGSSDYYWIGLSDPDsNGSWQWSDGSGPvSYSN 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 71998057    239 ID--HTARRGGVCLAMSTGtgsmvpTGSWYPVDCKASNSFLCK 279
Cdd:smart00034  88 WApgEPNNSSGDCVVLSTS------GGKWNDVSCTSKLPFVCE 124
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 303-413 5.88e-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: 101.33  E-value: 5.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057 303 CNSSMI-MAPGTISSPAYPGYYDNNMYCSYLLSTTGAYNILLKFTDF----STNLNLDYVTVYDGETTSSPMLGSFSGfN 377
Cdd:cd00041   1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFdlesSPNCSYDYLEIYDGPSTSSPLLGRFCG-S 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71998057 378 ETPINLVSTGNTMLVTFRSgnseDSNIRY-GFSATFS 413
Cdd:cd00041  80 TLPPPIISSGNSLTVRFRS----DSSVTGrGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 312-412 8.11e-25

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: 97.85  E-value: 8.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057    312 GTISSPAYPGYYDNNMYCSYLLSTTGAYNILLKFTDF----STNLNLDYVTVYDGETTSSPMLGSFSGFNETPINLVSTG 387
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFdlesSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|....*
gi 71998057    388 NTMLVTFRSGNSEDSNiryGFSATF 412
Cdd:smart00042  81 NSLTLTFVSDSSVQKR---GFSARY 102
CUB pfam00431
CUB domain;
310-412 2.16e-20

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 85.81  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057   310 APGTISSPAYPGYYDNNMYCSYLLSTTGAYNILLKFTDF----STNLNLDYVTVYDGETTSSPMLGSFSGFnETPINLVS 385
Cdd:pfam00431   8 SSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFeledHDECGYDYVEIRDGPSASSPLLGRFCGS-GIPEDIVS 86

                          90       100
                  ....*....|....*....|....*...
gi 71998057   386 TGNTMLVTFRSgnseDSNIRY-GFSATF 412
Cdd:pfam00431  87 SSNQMTIKFVS----DASVQKrGFKATY 110
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 23-152 4.25e-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: 85.34  E-value: 4.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057     23 CSNGYTLvNNNKCLRLFKTPETHKTAELTCLKNGGaTLANIKSSIDNRAITIFVGGASNS--IWIGLFCTKSSaKECFWD 100
Cdd:smart00034   1 CPSGWIS-YGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSN-GSWQWS 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 71998057    101 DDSGSaDQFQNFKSGFPLVEKGRCVYSSQvafDRGQWSSGDCEKESRaFVCE 152
Cdd:smart00034  78 DGSGP-VSYSNWAPGEPNNSSGDCVVLST---SGGKWNDVSCTSKLP-FVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 165-279 8.28e-13

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: 64.93  E-value: 8.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057    165 YNGYCY-FDFAPLPFVSAQKICKENCGIIASILSPMENRYIN---ANFYTYSALLIGATWSY-NSSYTWFDGSSW-SYHN 238
Cdd:smart00034   8 YGGKCYkFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAsllKNSGSSDYYWIGLSDPDsNGSWQWSDGSGPvSYSN 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 71998057    239 ID--HTARRGGVCLAMSTGtgsmvpTGSWYPVDCKASNSFLCK 279
Cdd:smart00034  88 WApgEPNNSSGDCVVLSTS------GGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 168-280 1.69e-10

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: 58.01  E-value: 1.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057 168 YCY-FDFAPLPFVSAQKICKENCGIIASILSPMENRYINANF--YTYSALLIGATWSY-NSSYTWFDGSS-WSYHN---I 239
Cdd:cd00037   1 SCYkFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkkSSSSDVWIGLNDLSsEGTWKWSDGSPlVDYTNwapG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71998057 240 DHTARRGGVCLAMSTGtgsmvPTGSWYPVDCKASNSFLCKR 280
Cdd:cd00037  81 EPNPGGSEDCVVLSSS-----SDGKWNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 42-152 1.91e-08

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 51.71  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057    42 PETHKTAELTCLKNGGaTLANIKSSIDNRAITIFVGGASNSIWIGLFCTKSSAKECfWDDDSGSaDQFQNFKSGFPLVEK 121
Cdd:pfam00059   1 SKTWDEAREACRKLGG-HLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWK-WVDGSPV-NYTNWAPEPNNNGEN 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 71998057   122 GRCVYssqVAFDRGQWSSGDCEKeSRAFVCE 152
Cdd:pfam00059  78 EDCVE---LSSSSGKWNDENCNS-KNPFVCE 104
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 23-152 7.85e-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: 50.83  E-value: 7.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057  23 CSNGYTLVNNNkCLRLFKTPETHKTAELTCLKNG-GATLANIKSSIDNRAITIFV---GGASNSIWIGLFCTKSSAKecf 98
Cdd:cd03594   1 CPKGWLPYKGN-CYGYFRQPLSWSDAELFCQKYGpGAHLASIHSPAEAAAIASLIssyQKAYQPVWIGLHDPQQSRG--- 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71998057  99 WDDDSGSADQFQNFKSGFPLVEKGRCV-YSSQVAFDRgqWSSGDCEKEsRAFVCE 152
Cdd:cd03594  77 WEWSDGSKLDYRSWDRNPPYARGGYCAeLSRSTGFLK--WNDANCEER-NPFICK 128
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 21-153 2.61e-04

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 43.53  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057     21 PVC-SNGYTLVNNNKCLRLFKTPETHKTAELTCLKNGGATLANIKS-SIDNRAITIFVGGASNSIWIGLFCTKSSAKECF 98
Cdd:TIGR00864  316 PHCpKDGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNdALQNFLARKVTHSLDRGVWIGFSDVNGAEKGPA 395

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 71998057     99 WDDDSGSADQFQNFKSGFPLVEKGR-CVYSSQvafdRGQWSSGDCEKEsRAFVCEL 153
Cdd:TIGR00864  396 HQGEAFEAEECEEGLAGEPHPARAEhCVRLDP----RGQCNSDLCNAP-HAYVCEL 446
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 303-413 5.88e-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: 101.33  E-value: 5.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057 303 CNSSMI-MAPGTISSPAYPGYYDNNMYCSYLLSTTGAYNILLKFTDF----STNLNLDYVTVYDGETTSSPMLGSFSGfN 377
Cdd:cd00041   1 CGGTLTaSTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFdlesSPNCSYDYLEIYDGPSTSSPLLGRFCG-S 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71998057 378 ETPINLVSTGNTMLVTFRSgnseDSNIRY-GFSATFS 413
Cdd:cd00041  80 TLPPPIISSGNSLTVRFRS----DSSVTGrGFKATYS 112
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 312-412 8.11e-25

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: 97.85  E-value: 8.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057    312 GTISSPAYPGYYDNNMYCSYLLSTTGAYNILLKFTDF----STNLNLDYVTVYDGETTSSPMLGSFSGFNETPINLVSTG 387
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFdlesSDNCEYDYVEIYDGPSASSPLLGRFCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|....*
gi 71998057    388 NTMLVTFRSGNSEDSNiryGFSATF 412
Cdd:smart00042  81 NSLTLTFVSDSSVQKR---GFSARY 102
CUB pfam00431
CUB domain;
310-412 2.16e-20

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 85.81  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057   310 APGTISSPAYPGYYDNNMYCSYLLSTTGAYNILLKFTDF----STNLNLDYVTVYDGETTSSPMLGSFSGFnETPINLVS 385
Cdd:pfam00431   8 SSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFeledHDECGYDYVEIRDGPSASSPLLGRFCGS-GIPEDIVS 86

                          90       100
                  ....*....|....*....|....*...
gi 71998057   386 TGNTMLVTFRSgnseDSNIRY-GFSATF 412
Cdd:pfam00431  87 SSNQMTIKFVS----DASVQKrGFKATY 110
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 23-152 4.25e-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: 85.34  E-value: 4.25e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057     23 CSNGYTLvNNNKCLRLFKTPETHKTAELTCLKNGGaTLANIKSSIDNRAITIFVGGASNS--IWIGLFCTKSSaKECFWD 100
Cdd:smart00034   1 CPSGWIS-YGGKCYKFSTEKKTWEDAQAFCQSLGG-HLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSN-GSWQWS 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 71998057    101 DDSGSaDQFQNFKSGFPLVEKGRCVYSSQvafDRGQWSSGDCEKESRaFVCE 152
Cdd:smart00034  78 DGSGP-VSYSNWAPGEPNNSSGDCVVLST---SGGKWNDVSCTSKLP-FVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 165-279 8.28e-13

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: 64.93  E-value: 8.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057    165 YNGYCY-FDFAPLPFVSAQKICKENCGIIASILSPMENRYIN---ANFYTYSALLIGATWSY-NSSYTWFDGSSW-SYHN 238
Cdd:smart00034   8 YGGKCYkFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAsllKNSGSSDYYWIGLSDPDsNGSWQWSDGSGPvSYSN 87

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 71998057    239 ID--HTARRGGVCLAMSTGtgsmvpTGSWYPVDCKASNSFLCK 279
Cdd:smart00034  88 WApgEPNNSSGDCVVLSTS------GGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 168-280 1.69e-10

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: 58.01  E-value: 1.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057 168 YCY-FDFAPLPFVSAQKICKENCGIIASILSPMENRYINANF--YTYSALLIGATWSY-NSSYTWFDGSS-WSYHN---I 239
Cdd:cd00037   1 SCYkFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkkSSSSDVWIGLNDLSsEGTWKWSDGSPlVDYTNwapG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71998057 240 DHTARRGGVCLAMSTGtgsmvPTGSWYPVDCKASNSFLCKR 280
Cdd:cd00037  81 EPNPGGSEDCVVLSSS-----SDGKWNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 42-152 1.91e-08

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 51.71  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057    42 PETHKTAELTCLKNGGaTLANIKSSIDNRAITIFVGGASNSIWIGLFCTKSSAKECfWDDDSGSaDQFQNFKSGFPLVEK 121
Cdd:pfam00059   1 SKTWDEAREACRKLGG-HLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWK-WVDGSPV-NYTNWAPEPNNNGEN 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 71998057   122 GRCVYssqVAFDRGQWSSGDCEKeSRAFVCE 152
Cdd:pfam00059  78 EDCVE---LSSSSGKWNDENCNS-KNPFVCE 104
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 23-152 7.85e-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: 50.83  E-value: 7.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057  23 CSNGYTLVNNNkCLRLFKTPETHKTAELTCLKNG-GATLANIKSSIDNRAITIFV---GGASNSIWIGLFCTKSSAKecf 98
Cdd:cd03594   1 CPKGWLPYKGN-CYGYFRQPLSWSDAELFCQKYGpGAHLASIHSPAEAAAIASLIssyQKAYQPVWIGLHDPQQSRG--- 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71998057  99 WDDDSGSADQFQNFKSGFPLVEKGRCV-YSSQVAFDRgqWSSGDCEKEsRAFVCE 152
Cdd:cd03594  77 WEWSDGSKLDYRSWDRNPPYARGGYCAeLSRSTGFLK--WNDANCEER-NPFICK 128
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 33-151 7.90e-08

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: 50.53  E-value: 7.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057  33 NKCLRLFKTPETHKTAELTCLKNGGATLANIKS-SIDNRAITIFVGGASNSIWIGLFCTKSSAKECF-WDDdsGSADQFQ 110
Cdd:cd03598   1 GRCYRFVKSPRTFRDAQVICRRCYRGNLASIHSfAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFsWVD--GSVWNYA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71998057 111 NFKSGFPLVEKGRCVyssQVAFDRGQWSSGDCeKESRAFVC 151
Cdd:cd03598  79 YWAPGQPGNRRGHCV---ELCTRGGHWRRAHC-KLRRPFIC 115
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 165-279 1.30e-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: 47.37  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057 165 YNGYCYFDFA-PLPFVSAQKICKE--NCGIIASILSPMEN----RYINANFYTYSALLIGA-TWSYNSSYTWFDGSSWSY 236
Cdd:cd03594   8 YKGNCYGYFRqPLSWSDAELFCQKygPGAHLASIHSPAEAaaiaSLISSYQKAYQPVWIGLhDPQQSRGWEWSDGSKLDY 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71998057 237 HNIDHT--ARRGGVCLAMSTGTGSMvptgSWYPVDCKASNSFLCK 279
Cdd:cd03594  88 RSWDRNppYARGGYCAELSRSTGFL----KWNDANCEERNPFICK 128
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 167-278 4.64e-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: 42.44  E-value: 4.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057 167 GYCYFDF-APLPFVSAQKICKEnC--GIIASILSPMENRYIN--ANFYTYSALLIGA---TWSYNSSYTWFDGSSWSYHN 238
Cdd:cd03598   1 GRCYRFVkSPRTFRDAQVICRR-CyrGNLASIHSFAFNYRVQrlVSTLNQAQVWIGGiitGKGRCRRFSWVDGSVWNYAY 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71998057 239 --IDHTARRGGVCLAMSTgtgsmvPTGSWYPVDCKASNSFLC 278
Cdd:cd03598  80 waPGQPGNRRGHCVELCT------RGGHWRRAHCKLRRPFIC 115
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 21-153 2.61e-04

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 43.53  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057     21 PVC-SNGYTLVNNNKCLRLFKTPETHKTAELTCLKNGGATLANIKS-SIDNRAITIFVGGASNSIWIGLFCTKSSAKECF 98
Cdd:TIGR00864  316 PHCpKDGEIFEENGHCFQIVPEEAAWLDAQEQCLARAGAALAIVDNdALQNFLARKVTHSLDRGVWIGFSDVNGAEKGPA 395

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 71998057     99 WDDDSGSADQFQNFKSGFPLVEKGR-CVYSSQvafdRGQWSSGDCEKEsRAFVCEL 153
Cdd:TIGR00864  396 HQGEAFEAEECEEGLAGEPHPARAEhCVRLDP----RGQCNSDLCNAP-HAYVCEL 446
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 165-280 7.39e-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: 39.10  E-value: 7.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057 165 YNGYCYFDF-APLPFVSAQKICKENCGIIASILSPMENRYINANFYTYSalLIGAT-WSYNSSYTWFDGSS-----WSYH 237
Cdd:cd03588   8 FQGHCYRHFpDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ--WIGLNdRTIEGDFRWSDGHPlqfenWRPN 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 71998057 238 NIDHTARRGGVCLAMSTGTgsmvpTGSWYPVDCKASNSFLCKR 280
Cdd:cd03588  86 QPDNFFATGEDCVVMIWHE-----EGEWNDVPCNYHLPFTCKK 123
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 43-153 7.77e-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: 38.82  E-value: 7.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057  43 ETHKTAELTCLKNGGaTLANIKSSIDNRAITIFVGGASNSIWIGLfctKSSAKECFWDDDSGSADQFQNFKSGFPLVEKG 122
Cdd:cd03591  11 KNFDDAQKLCSEAGG-TLAMPRNAAENAAIASYVKKGNTYAFIGI---TDLETEGQFVYLDGGPLTYTNWKPGEPNNAGG 86

                        90       100       110
                ....*....|....*....|....*....|...
gi 71998057 123 R--CVyssqVAFDRGQWSSGDCEkESRAFVCEL 153
Cdd:cd03591  87 GedCV----EMYTSGKWNDVACN-LTRLFVCEF 114
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 60-151 2.18e-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: 37.35  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998057  60 LANIKSSIDNRAITIFVGGASNSIWIGLFCTKSSAKecfWDDDSGSA----DQFQNFKSgfplvekGRCVYSSQvafdRG 135
Cdd:cd03602  26 LATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSWR---WSDGSESSfrnwNTFQPFGQ-------GDCATMYS----SG 91

                        90
                ....*....|....*.
gi 71998057 136 QWSSGDCEkESRAFVC 151
Cdd:cd03602  92 RWYAALCS-ALKPFIC 106
 
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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