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Conserved domains on  [gi|71987589|ref|NP_501229|]
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C-type lectin domain-containing protein 180 [Caenorhabditis elegans]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 59-184 1.04e-17

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: 79.95  E-value: 1.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589     59 YQFRAGDQNWLTAREHCLSLNADLAAIRNVEQLDWILSHyapLSSRFAQRLVQIGLYAPEgQTHEWKWLNGNEINKTLLW 138
Cdd:smart00034  13 YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASL---LKNSGSSDYYWIGLSDPD-SNGSWQWSDGSGPVSYSNW 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 71987589    139 SSGEPYDhsmeGRERCGLLNVEKRVLDDVDCESTspdhhaQRYICQ 184
Cdd:smart00034  89 APGEPNN----SSGDCVVLSTSGGKWNDVSCTSK------LPFVCE 124
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 743-852 4.34e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.14  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   743 TVETKQETAVTPAPTTSEKTSTTAAPSTKPAEETTTTTEAPSTTTKPVTVAVKKVSPeemeklvkkesTEKVTllPPLPT 822
Cdd:pfam05109 467 TVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSP-----------TPAVT--TPTPN 533

                          90       100       110
                  ....*....|....*....|....*....|...
gi 71987589   823 FTFPTL---APFTFPTLPTLATTKPSPAPKVPT 852
Cdd:pfam05109 534 ATSPTLgktSPTSAVTTPTPNATSPTPAVTTPT 566
PTZ00121 super family cl31754
MAEBL; Provisional
 230-597 4.95e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   230 DEVLKNETSATVKSTVKFSDSEEETSSEEEESVSKTLAALPKIEGSGESTALKELQEPEGSGQIVEKKAIET---TGDLV 306
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkADELK 1411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   307 SGVDEEKLDKMINKMEEMIKSIDDLTvpPAVLERTTVSTVVLKKEEIVKQEKTDEKKVEDKK-ETLANELNDNKISESIE 385
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKaDEAKKKAEEAKKADEAK 1489

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   386 GDFDQAQSK--DMPKADIEPPKEEDCDEEGSGSGSGEEDEKDESSEKIELAPEKEDKIKEFLGVLRLFLDRAEHGDLRKL 463
Cdd:PTZ00121 1490 KKAEEAKKKadEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA 1569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   464 LDDQSGKTLLERMKNAVREANRREFEMLEKLENSKKSEEEKEELAKKDQMSTEEQ-----------KDLYKKISSAVMKA 532
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaeeekkkvEQLKKKEAEEKKKA 1649

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71987589   533 AKIHKIEEADKVQDEQAMEKFNIAKVKAD----SEEAESEGTVEVLKSAKEGKA--EIKEKNREKKDAKEE 597
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEE 1720
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 59-184 1.04e-17

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: 79.95  E-value: 1.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589     59 YQFRAGDQNWLTAREHCLSLNADLAAIRNVEQLDWILSHyapLSSRFAQRLVQIGLYAPEgQTHEWKWLNGNEINKTLLW 138
Cdd:smart00034  13 YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASL---LKNSGSSDYYWIGLSDPD-SNGSWQWSDGSGPVSYSNW 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 71987589    139 SSGEPYDhsmeGRERCGLLNVEKRVLDDVDCESTspdhhaQRYICQ 184
Cdd:smart00034  89 APGEPNN----SSGDCVVLSTSGGKWNDVSCTSK------LPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 59-185 4.48e-17

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 78.05  E-value: 4.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589  59 YQFRAGDQNWLTAREHCLSLNADLAAIRNVEQLDWILSHYAPLSSRFaqrlVQIGLYApEGQTHEWKWLNGNEINKTLLW 138
Cdd:cd00037   3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD----VWIGLND-LSSEGTWKWSDGSPLVDYTNW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71987589 139 SSGEPYDHsmeGRERCGLLNVEKR-VLDDVDCESTSPdhhaqrYICQR 185
Cdd:cd00037  78 APGEPNPG---GSEDCVVLSSSSDgKWNDVSCSSKLP------FICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 67-185 3.76e-09

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 54.79  E-value: 3.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589    67 NWLTAREHCLSLNADLAAIRNVEQLDWILSHYAPLSSRFaqrlvQIGLyAPEGQTHEWKWLNGNeinkTLLWSSGEPYDH 146
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYF-----WIGL-TDRKNEGTWKWVDGS----PVNYTNWAPEPN 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 71987589   147 SMEGRERCGLLNVEKRVLDDVDCESTSPdhhaqrYICQR 185
Cdd:pfam00059  73 NNGENEDCVELSSSSGKWNDENCNSKNP------FVCEK 105
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 743-852 4.34e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.14  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   743 TVETKQETAVTPAPTTSEKTSTTAAPSTKPAEETTTTTEAPSTTTKPVTVAVKKVSPeemeklvkkesTEKVTllPPLPT 822
Cdd:pfam05109 467 TVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSP-----------TPAVT--TPTPN 533

                          90       100       110
                  ....*....|....*....|....*....|...
gi 71987589   823 FTFPTL---APFTFPTLPTLATTKPSPAPKVPT 852
Cdd:pfam05109 534 ATSPTLgktSPTSAVTTPTPNATSPTPAVTTPT 566
PTZ00121 PTZ00121
MAEBL; Provisional
 230-597 4.95e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   230 DEVLKNETSATVKSTVKFSDSEEETSSEEEESVSKTLAALPKIEGSGESTALKELQEPEGSGQIVEKKAIET---TGDLV 306
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkADELK 1411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   307 SGVDEEKLDKMINKMEEMIKSIDDLTvpPAVLERTTVSTVVLKKEEIVKQEKTDEKKVEDKK-ETLANELNDNKISESIE 385
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKaDEAKKKAEEAKKADEAK 1489

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   386 GDFDQAQSK--DMPKADIEPPKEEDCDEEGSGSGSGEEDEKDESSEKIELAPEKEDKIKEFLGVLRLFLDRAEHGDLRKL 463
Cdd:PTZ00121 1490 KKAEEAKKKadEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA 1569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   464 LDDQSGKTLLERMKNAVREANRREFEMLEKLENSKKSEEEKEELAKKDQMSTEEQ-----------KDLYKKISSAVMKA 532
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaeeekkkvEQLKKKEAEEKKKA 1649

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71987589   533 AKIHKIEEADKVQDEQAMEKFNIAKVKAD----SEEAESEGTVEVLKSAKEGKA--EIKEKNREKKDAKEE 597
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEE 1720
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 59-184 1.04e-17

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: 79.95  E-value: 1.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589     59 YQFRAGDQNWLTAREHCLSLNADLAAIRNVEQLDWILSHyapLSSRFAQRLVQIGLYAPEgQTHEWKWLNGNEINKTLLW 138
Cdd:smart00034  13 YKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASL---LKNSGSSDYYWIGLSDPD-SNGSWQWSDGSGPVSYSNW 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 71987589    139 SSGEPYDhsmeGRERCGLLNVEKRVLDDVDCESTspdhhaQRYICQ 184
Cdd:smart00034  89 APGEPNN----SSGDCVVLSTSGGKWNDVSCTSK------LPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 59-185 4.48e-17

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 78.05  E-value: 4.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589  59 YQFRAGDQNWLTAREHCLSLNADLAAIRNVEQLDWILSHYAPLSSRFaqrlVQIGLYApEGQTHEWKWLNGNEINKTLLW 138
Cdd:cd00037   3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD----VWIGLND-LSSEGTWKWSDGSPLVDYTNW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71987589 139 SSGEPYDHsmeGRERCGLLNVEKR-VLDDVDCESTSPdhhaqrYICQR 185
Cdd:cd00037  78 APGEPNPG---GSEDCVVLSSSSDgKWNDVSCSSKLP------FICEK 116
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 59-185 3.62e-12

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: 63.89  E-value: 3.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589  59 YQFRAGDQNWLTAREHCLSLNADLAAIRNVEQLDWILShYAPLSSRFaqrlvqIGLYaPEGQTHEWKWLNGNEINKTLLw 138
Cdd:cd03593  13 YYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQS-QIGSSSYW------IGLS-REKSEKPWKWIDGSPLNNLFN- 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71987589 139 ssgepyDHSMEGRERCGLLNVEKrvLDDVDCESTspdhhaQRYICQR 185
Cdd:cd03593  84 ------IRGSTKSGNCAYLSSTG--IYSEDCSTK------KRWICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 67-185 3.76e-09

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 54.79  E-value: 3.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589    67 NWLTAREHCLSLNADLAAIRNVEQLDWILSHYAPLSSRFaqrlvQIGLyAPEGQTHEWKWLNGNeinkTLLWSSGEPYDH 146
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYF-----WIGL-TDRKNEGTWKWVDGS----PVNYTNWAPEPN 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 71987589   147 SMEGRERCGLLNVEKRVLDDVDCESTSPdhhaqrYICQR 185
Cdd:pfam00059  73 NNGENEDCVELSSSSGKWNDENCNSKNP------FVCEK 105
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 67-185 6.30e-09

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 55.00  E-value: 6.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589  67 NWLTAREHCLSLNADLAAIRNVEQLDWILSHyapLSSRFAqrlVQIGLYAPEGQThEWKWLNGNEINKTL-LWSSGEPyD 145
Cdd:cd03590  21 SWEESRQFCEDMGAHLVIINSQEEQEFISKI---LSGNRS---YWIGLSDEETEG-EWKWVDGTPLNSSKtFWHPGEP-N 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71987589 146 HSMEGRERCGLLNVEKRVLDDVDCEStspdhhAQRYICQR 185
Cdd:cd03590  93 NWGGGGEDCAELVYDSGGWNDVPCNL------EYRWICEK 126
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 59-150 1.13e-05

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: 45.49  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589  59 YQFRAGDQNWLTAREHCLSLNADLAAIRNVEQLDWILShyapLSSRFAQrlVQIGLY--APEGqthEWKWLNGNEINKTl 136
Cdd:cd03603   3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLS----NFGGYGA--SWIGASdaATEG---TWKWSDGEESTYT- 72

                        90
                ....*....|....
gi 71987589 137 LWSSGEPYDHSMEG 150
Cdd:cd03603  73 NWGSGEPHNNGGGN 86
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 743-852 4.34e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.14  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   743 TVETKQETAVTPAPTTSEKTSTTAAPSTKPAEETTTTTEAPSTTTKPVTVAVKKVSPeemeklvkkesTEKVTllPPLPT 822
Cdd:pfam05109 467 TVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSP-----------TPAVT--TPTPN 533

                          90       100       110
                  ....*....|....*....|....*....|...
gi 71987589   823 FTFPTL---APFTFPTLPTLATTKPSPAPKVPT 852
Cdd:pfam05109 534 ATSPTLgktSPTSAVTTPTPNATSPTPAVTTPT 566
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 67-174 1.67e-03

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 38.89  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589  67 NWLTAREHCLSLNADLAAIRNVEqlDWI-LSHYAPLSSRFAqrlvQIGLYapeGQTHEWKWLNGNEInkTLL-WSSGEPY 144
Cdd:cd03602  11 TWSEAQQYCRENYTDLATVQNQE--DNAlLSNLSRVSNSAA----WIGLY---RDVDSWRWSDGSES--SFRnWNTFQPF 79

                        90       100       110
                ....*....|....*....|....*....|
gi 71987589 145 dhsmeGRERCGLLNVEKRvLDDVDCESTSP 174
Cdd:cd03602  80 -----GQGDCATMYSSGR-WYAALCSALKP 103
PTZ00121 PTZ00121
MAEBL; Provisional
 230-597 4.95e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 4.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   230 DEVLKNETSATVKSTVKFSDSEEETSSEEEESVSKTLAALPKIEGSGESTALKELQEPEGSGQIVEKKAIET---TGDLV 306
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkADELK 1411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   307 SGVDEEKLDKMINKMEEMIKSIDDLTvpPAVLERTTVSTVVLKKEEIVKQEKTDEKKVEDKK-ETLANELNDNKISESIE 385
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKaDEAKKKAEEAKKADEAK 1489

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   386 GDFDQAQSK--DMPKADIEPPKEEDCDEEGSGSGSGEEDEKDESSEKIELAPEKEDKIKEFLGVLRLFLDRAEHGDLRKL 463
Cdd:PTZ00121 1490 KKAEEAKKKadEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA 1569

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71987589   464 LDDQSGKTLLERMKNAVREANRREFEMLEKLENSKKSEEEKEELAKKDQMSTEEQ-----------KDLYKKISSAVMKA 532
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaeeekkkvEQLKKKEAEEKKKA 1649

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71987589   533 AKIHKIEEADKVQDEQAMEKFNIAKVKAD----SEEAESEGTVEVLKSAKEGKA--EIKEKNREKKDAKEE 597
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEeakkAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEE 1720
 
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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