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Conserved domains on  [gi|17559568|ref|NP_507659|]
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PAN-3 domain-containing protein [Caenorhabditis elegans]

Protein Classification

CW domain-containing protein( domain architecture ID 10652033)

CW domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CW smart00605
CW domain;
22-107 3.73e-14

CW domain;


:

Pssm-ID: 214742  Cd Length: 94  Bit Score: 65.91  E-value: 3.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559568     22 LKMIKIFGY---TDILQLQNFENVQSCIDGCFEQPNCLAVHFKS--VCSHYFVNNySVTVVESDRSEEHYVAIKTELPEA 96
Cdd:smart00605   1 VKMVLIYGKpttSSSSVTAATLSWDECIQKCYEDSNCVLAYGNSseTCYLFSYGT-VLTVKKLSSSSGKKVAFKVSTDQP 79

                           90
                   ....*....|....*
gi 17559568     97 TCPAS----YKDIKY 107
Cdd:smart00605  80 SCPAMqlllFNEYTT 94
CLECT super family cl02432
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 131-198 3.07e-04

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.


The actual alignment was detected with superfamily member smart00034:

Pssm-ID: 470576 [Multi-domain]  Cd Length: 124  Bit Score: 39.51  E-value: 3.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559568    131 CNFGWKRFQKTdtlvmCVKVMVDQVTQQVAKEKCIERGAVLARIETPEECKWKQDIVANKYFEKGIWI 198
Cdd:smart00034   1 CPSGWISYGGK-----CYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWI 63
 
Name Accession Description Interval E-value
CW smart00605
CW domain;
22-107 3.73e-14

CW domain;


Pssm-ID: 214742  Cd Length: 94  Bit Score: 65.91  E-value: 3.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559568     22 LKMIKIFGY---TDILQLQNFENVQSCIDGCFEQPNCLAVHFKS--VCSHYFVNNySVTVVESDRSEEHYVAIKTELPEA 96
Cdd:smart00605   1 VKMVLIYGKpttSSSSVTAATLSWDECIQKCYEDSNCVLAYGNSseTCYLFSYGT-VLTVKKLSSSSGKKVAFKVSTDQP 79

                           90
                   ....*....|....*
gi 17559568     97 TCPAS----YKDIKY 107
Cdd:smart00605  80 SCPAMqlllFNEYTT 94
PAN_3 pfam08277
PAN-like domain;
24-91 2.33e-06

PAN-like domain;


Pssm-ID: 429894  Cd Length: 71  Bit Score: 44.27  E-value: 2.33e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559568    24 MIKIFGY---TDILQLQNFENVQSCIDGCFEQPNCLAVHFKS-VCSHYFVNNYSvTVVESDRSEEHYVAIKT 91
Cdd:pfam08277   1 MVLIYGEpedYYSTSSTTSESWDDCVTKCYEDSTCVLAYFNSeNCYLFSIGNVS-TVKKIESSSGSKVAFKI 71
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 131-198 3.07e-04

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: 39.51  E-value: 3.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559568    131 CNFGWKRFQKTdtlvmCVKVMVDQVTQQVAKEKCIERGAVLARIETPEECKWKQDIVANKYFEKGIWI 198
Cdd:smart00034   1 CPSGWISYGGK-----CYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWI 63
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 147-201 5.24e-04

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: 38.75  E-value: 5.24e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17559568 147 CVKVMVDQVTQQVAKEKCIERGAVLARIETPEECKWKQDIVANKYFEKgIWIDGR 201
Cdd:cd00037   2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD-VWIGLN 55
 
Name Accession Description Interval E-value
CW smart00605
CW domain;
22-107 3.73e-14

CW domain;


Pssm-ID: 214742  Cd Length: 94  Bit Score: 65.91  E-value: 3.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17559568     22 LKMIKIFGY---TDILQLQNFENVQSCIDGCFEQPNCLAVHFKS--VCSHYFVNNySVTVVESDRSEEHYVAIKTELPEA 96
Cdd:smart00605   1 VKMVLIYGKpttSSSSVTAATLSWDECIQKCYEDSNCVLAYGNSseTCYLFSYGT-VLTVKKLSSSSGKKVAFKVSTDQP 79

                           90
                   ....*....|....*
gi 17559568     97 TCPAS----YKDIKY 107
Cdd:smart00605  80 SCPAMqlllFNEYTT 94
PAN_3 pfam08277
PAN-like domain;
24-91 2.33e-06

PAN-like domain;


Pssm-ID: 429894  Cd Length: 71  Bit Score: 44.27  E-value: 2.33e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17559568    24 MIKIFGY---TDILQLQNFENVQSCIDGCFEQPNCLAVHFKS-VCSHYFVNNYSvTVVESDRSEEHYVAIKT 91
Cdd:pfam08277   1 MVLIYGEpedYYSTSSTTSESWDDCVTKCYEDSTCVLAYFNSeNCYLFSIGNVS-TVKKIESSSGSKVAFKI 71
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 131-198 3.07e-04

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: 39.51  E-value: 3.07e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17559568    131 CNFGWKRFQKTdtlvmCVKVMVDQVTQQVAKEKCIERGAVLARIETPEECKWKQDIVANKYFEKGIWI 198
Cdd:smart00034   1 CPSGWISYGGK-----CYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWI 63
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 147-201 5.24e-04

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: 38.75  E-value: 5.24e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17559568 147 CVKVMVDQVTQQVAKEKCIERGAVLARIETPEECKWKQDIVANKYFEKgIWIDGR 201
Cdd:cd00037   2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD-VWIGLN 55
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 131-191 9.83e-03

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: 35.25  E-value: 9.83e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17559568 131 CNFGWKRFQKtdtlvMCVKVMVDQVTQQVAKEKCIERGAVLARIETPEEckwkQDIVANKY 191
Cdd:cd03588   1 CEEGWDKFQG-----HCYRHFPDRETWEDAERRCREQQGHLSSIVTPEE----QEFVNNNA 52
 
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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