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Conserved domains on  [gi|919047189|ref|XP_013406786|]
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low affinity immunoglobulin epsilon Fc receptor [Lingula anatina]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10034483)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 252-375 6.75e-31

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: 113.87  E-value: 6.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 252 SCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYrkynAEKWSSSFFWSGGNDLHNEGTWTWVGTGKPLTF 331
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLG--GHLASIHSEEENDFLASL----LKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 919047189 332 TFWLPGEPNSfHQHQDCMYFTGDGEHRWDDWNCHSlKINYVCEI 375
Cdd:cd00037   75 TNWAPGEPNP-GGSEDCVVLSSSSDGKWNDVSCSS-KLPFICEK 116
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 76-229 2.33e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189    76 KKKTAKLQKTVDKMANEMKQLREIVDQLRS--GKMNIGGRSQAD--SGYLYDQSPTSVRGGQDTSQIMRIVHEMTDHSRN 151
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAelTLLNEEAANLRErlESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189   152 MTHAMLSRTEH--KYRVLERKMDNLQEISRQEANRFRSKEAEIRKMREENHKKARELVKQQDTIVDMEKRIHWLESTANR 229
Cdd:TIGR02168  861 IEELEELIEELesELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
 
Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 252-375 6.75e-31

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: 113.87  E-value: 6.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 252 SCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYrkynAEKWSSSFFWSGGNDLHNEGTWTWVGTGKPLTF 331
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLG--GHLASIHSEEENDFLASL----LKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 919047189 332 TFWLPGEPNSfHQHQDCMYFTGDGEHRWDDWNCHSlKINYVCEI 375
Cdd:cd00037   75 TNWAPGEPNP-GGSEDCVVLSSSSDGKWNDVSCSS-KLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 242-374 8.04e-31

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: 8.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189   242 CPEGFLRYARSCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYRKYNaekWSSSFFWSGGNDLHNEGTWT 321
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLG--GHLASIHSEAENDFVASLLKNS---GSSDYYWIGLSDPDSNGSWQ 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 919047189   322 WVGTGKPLTFTFWLPGEPNSfhQHQDCMYFTGDGeHRWDDWNCHSlKINYVCE 374
Cdd:smart00034  76 WSDGSGPVSYSNWAPGEPNN--SSGDCVVLSTSG-GKWNDVSCTS-KLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 260-374 1.99e-18

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 79.83  E-value: 1.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189  260 TVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYRKYnaekwSSSFFWSGGNDLHNEGTWTWVgTGKPLTFTFWLPgEP 339
Cdd:pfam00059   1 SKTWDEAREACRKLG--GHLVSINSAEELDFLSSTLKK-----SNKYFWIGLTDRKNEGTWKWV-DGSPVNYTNWAP-EP 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 919047189  340 NSFHQHQDCMYFTGDGeHRWDDWNCHSLKiNYVCE 374
Cdd:pfam00059  72 NNNGENEDCVELSSSS-GKWNDENCNSKN-PFVCE 104
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 242-322 3.48e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 44.72  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 242 CPEGFLRYARSCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYRkynaekwSSSFFWSGGNDLHNEGTWT 321
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLG--ATLVKVETEEELNFLKRYK-------DSSDHWIGLNRESSNHPWK 158


                 .
gi 919047189 322 W 322
Cdd:PHA02642 159 W 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 76-229 2.33e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189    76 KKKTAKLQKTVDKMANEMKQLREIVDQLRS--GKMNIGGRSQAD--SGYLYDQSPTSVRGGQDTSQIMRIVHEMTDHSRN 151
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAelTLLNEEAANLRErlESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189   152 MTHAMLSRTEH--KYRVLERKMDNLQEISRQEANRFRSKEAEIRKMREENHKKARELVKQQDTIVDMEKRIHWLESTANR 229
Cdd:TIGR02168  861 IEELEELIEELesELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
 
Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 252-375 6.75e-31

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: 113.87  E-value: 6.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 252 SCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYrkynAEKWSSSFFWSGGNDLHNEGTWTWVGTGKPLTF 331
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLG--GHLASIHSEEENDFLASL----LKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 919047189 332 TFWLPGEPNSfHQHQDCMYFTGDGEHRWDDWNCHSlKINYVCEI 375
Cdd:cd00037   75 TNWAPGEPNP-GGSEDCVVLSSSSDGKWNDVSCSS-KLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 242-374 8.04e-31

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: 8.04e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189   242 CPEGFLRYARSCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYRKYNaekWSSSFFWSGGNDLHNEGTWT 321
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLG--GHLASIHSEAENDFVASLLKNS---GSSDYYWIGLSDPDSNGSWQ 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 919047189   322 WVGTGKPLTFTFWLPGEPNSfhQHQDCMYFTGDGeHRWDDWNCHSlKINYVCE 374
Cdd:smart00034  76 WSDGSGPVSYSNWAPGEPNN--SSGDCVVLSTSG-GKWNDVSCTS-KLPFVCE 124
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 242-375 1.20e-27

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: 105.90  E-value: 1.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 242 CPEGFLRYARSCYRFGNTTVTWLKAEETCQSLD---PRAHLVGVESKEENDFLIAYRKYNAEKWSSSFFWSGGNDLHNEG 318
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSipgLIAHLVSIHSQEENDFVYDLFESSRGPDTPYGLWIGLHDRTSEG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 919047189 319 TWTWVgTGKPLTFTFWLPGEPNSFHQHQDC--MYFTGDGEHRWDDWNChSLKINYVCEI 375
Cdd:cd03589   81 PFEWT-DGSPVDFTKWAGGQPDNYGGNEDCvqMWRRGDAGQSWNDMPC-DAVFPYICKM 137
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 242-374 3.29e-23

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: 93.52  E-value: 3.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 242 CPEGFLRYARSCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLiayrkyNAEKWSSSFFWSGGNDLHNEGTWT 321
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMG--AHLVIINSQEEQEFI------SKILSGNRSYWIGLSDEETEGEWK 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 919047189 322 WV-GTGKPLTFTFWLPGEPNSFHQH-QDCMYFTGDGEhRWDDWNCHsLKINYVCE 374
Cdd:cd03590   73 WVdGTPLNSSKTFWHPGEPNNWGGGgEDCAELVYDSG-GWNDVPCN-LEYRWICE 125
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 260-374 1.99e-18

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 79.83  E-value: 1.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189  260 TVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYRKYnaekwSSSFFWSGGNDLHNEGTWTWVgTGKPLTFTFWLPgEP 339
Cdd:pfam00059   1 SKTWDEAREACRKLG--GHLVSINSAEELDFLSSTLKK-----SNKYFWIGLTDRKNEGTWKWV-DGSPVNYTNWAP-EP 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 919047189  340 NSFHQHQDCMYFTGDGeHRWDDWNCHSLKiNYVCE 374
Cdd:pfam00059  72 NNNGENEDCVELSSSS-GKWNDENCNSKN-PFVCE 104
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 254-368 2.19e-17

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: 77.42  E-value: 2.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 254 YRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYRKynaeKWSSSFFWSGGNDLHNEgtWTWVGT-GKPLTFT 332
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRG--TDLVAIQNAEENALLNGFAL----KYNLGYYWIDGNDINNE--GTWVDTdKKELEYK 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 919047189 333 FWLPGEPNSfHQHQDC--MYFTGDGehRWDDWNCHSLK 368
Cdd:cd03592   75 NWAPGEPNN-GRNENCleIYIKDNG--KWNDEPCSKKK 109
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 254-375 2.19e-16

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: 74.77  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 254 YRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAyrkyNAEKWSssFFWSGGNDLHNEGTWTWVgTGKPLTFTF 333
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLG--GHLVTINSAEENDWLLS----NFGGYG--ASWIGASDAATEGTWKWS-DGEESTYTN 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 919047189 334 WLPGEP-NSFHQHQDCMYFTGDGE--HRWDDWNCHSLKINYVCEI 375
Cdd:cd03603   74 WGSGEPhNNGGGNEDYAAINHFPGisGKWNDLANSYNTLGYVIEW 118
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 265-375 2.55e-13

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: 65.78  E-value: 2.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 265 KAEETCQSLdpRAHLVGVESKEENDFLIAYrkynAEKWSSSFFWsGGNDLHNEGTWTWVgTGKPLTFTFWLPGEPNSFHQ 344
Cdd:cd03591   15 DAQKLCSEA--GGTLAMPRNAAENAAIASY----VKKGNTYAFI-GITDLETEGQFVYL-DGGPLTYTNWKPGEPNNAGG 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 919047189 345 HQDC--MYFTGdgehRWDDWNCHSlKINYVCEI 375
Cdd:cd03591   87 GEDCveMYTSG----KWNDVACNL-TRLFVCEF 114
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 242-374 2.96e-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: 63.16  E-value: 2.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 242 CPEGFLRYARSCYRFGNTTVTWLKAEETCQSLDPRAHLVGVESKEENDFLIAYRKYNAEKwsSSFFWSGGNDLHNEGTWT 321
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGPGAHLASIHSPAEAAAIASLISSYQKA--YQPVWIGLHDPQQSRGWE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 919047189 322 WVGTGKPLTFTfWLPGEPNSFHQHqdCMYFTG-DGEHRWDDWNCHSLKiNYVCE 374
Cdd:cd03594   79 WSDGSKLDYRS-WDRNPPYARGGY--CAELSRsTGFLKWNDANCEERN-PFICK 128
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 242-374 3.69e-11

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: 59.65  E-value: 3.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 242 CPEGFLRYARSCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYRKynaekwsSSFFWSGgndLHNEGT-- 319
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKN--SSLLKIDDEEELEFLQSQIG-------SSSYWIG---LSREKSek 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 919047189 320 -WTWVGTGkplTFTFWLpgEPNSFHQHQDCMYFTGDGEHrwdDWNCHSLKiNYVCE 374
Cdd:cd03593   69 pWKWIDGS---PLNNLF--NIRGSTKSGNCAYLSSTGIY---SEDCSTKK-RWICE 115
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 242-374 4.44e-11

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: 60.09  E-value: 4.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 242 CPEGFlRYARSCYRFGNTTVTWLKAEETCQSLDPRahLVGVESKEENDFLIAYRK----YNAEkwsssfFWSGGNDLHNE 317
Cdd:cd03596    1 CLKGT-KIHKKCYLVSEETKHYHEASEDCIARGGT--LATPRDSDENDALRDYVKasvpGNWE------VWLGINDMVAE 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 318 GTWTWVgTGKPLTFTFW---LPGEPNSFHQHqDCMYFTGDGEHRWDDWNCHSLKiNYVCE 374
Cdd:cd03596   72 GKWVDV-NGSPISYFNWereITAQPDGGKRE-NCVALSSSAQGKWFDEDCRREK-PYVCE 128
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 242-365 5.49e-11

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: 59.51  E-value: 5.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 242 CPEGFLRYARSCYRFGNTTVTWLKAEETCQslDPRAHLVGVESKEENDFLiaYRKYNaekwssSFFWSGGNDLHNEGTWT 321
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCR--EQQGHLSSIVTPEEQEFV--NNNAQ------DYQWIGLNDRTIEGDFR 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 919047189 322 WvGTGKPLTFTFWLPGEPNS-FHQHQDCMYFTGDGEHRWDDWNCH 365
Cdd:cd03588   71 W-SDGHPLQFENWRPNQPDNfFATGEDCVVMIWHEEGEWNDVPCN 114
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 242-322 3.48e-05

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 44.72  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 242 CPEGFLRYARSCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYRkynaekwSSSFFWSGGNDLHNEGTWT 321
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLG--ATLVKVETEEELNFLKRYK-------DSSDHWIGLNRESSNHPWK 158


                 .
gi 919047189 322 W 322
Cdd:PHA02642 159 W 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 76-229 2.33e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189    76 KKKTAKLQKTVDKMANEMKQLREIVDQLRS--GKMNIGGRSQAD--SGYLYDQSPTSVRGGQDTSQIMRIVHEMTDHSRN 151
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDELRAelTLLNEEAANLRErlESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189   152 MTHAMLSRTEH--KYRVLERKMDNLQEISRQEANRFRSKEAEIRKMREENHKKARELVKQQDTIVDMEKRIHWLESTANR 229
Cdd:TIGR02168  861 IEELEELIEELesELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 252-373 3.52e-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: 37.05  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 252 SCYRFGNTTVTWLKAEETCQSLdPRAHLVGVESkeendFLIAYRkynAEKWSSSF----FWSGGNDLHNEGTWT--WVgT 325
Cdd:cd03598    2 RCYRFVKSPRTFRDAQVICRRC-YRGNLASIHS-----FAFNYR---VQRLVSTLnqaqVWIGGIITGKGRCRRfsWV-D 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 919047189 326 GKPLTFTFWLPGEPNSFHQHqdCM-YFTGDGehRWDDWNChSLKINYVC 373
Cdd:cd03598   72 GSVWNYAYWAPGQPGNRRGH--CVeLCTRGG--HWRRAHC-KLRRPFIC 115
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 256-375 6.13e-03

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 36.36  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919047189 256 FGNTTVTWLKAEETCQSLDPRAHLVGVESKEENDFLIAYR--KYNAekwsssfFWSGGNDLHN-EGTWTWV-GTGKPLTF 331
Cdd:cd03601    5 CSDETMNYAKAGAFCRSRGMRLASLAMRDSEMRDAILAFTlvKGHG-------YWVGADNLQDgEYDFLWNdGVSLPTDS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 919047189 332 TFWLPGEPNSFHQHQDC--MYFTgdgEHRWDDWNCHSLKiNYVCEI 375
Cdd:cd03601   78 DLWAPNEPSNPQSRQLCvqLWSK---YNLLDDEYCGRAK-RVICEK 119
PHA02867 PHA02867
C-type lectin protein; Provisional
 239-296 9.64e-03

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 36.58  E-value: 9.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 919047189 239 DSACPEGFLRYARSCYRFGNTTVTWLKAEETCQSLDprAHLVGVESKEENDFLIAYRK 296
Cdd:PHA02867  46 SKVCPDEWIGYNSKCYYFTINETNWNDSKKLCDVMD--SSLIRFDNIETLNFVSRYGK 101
 
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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