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Conserved domains on  [gi|193207690|ref|NP_507665|]
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CW domain-containing protein [Caenorhabditis elegans]

Protein Classification

CW and CLECT domain-containing protein( domain architecture ID 10652030)

CW and CLECT domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CW smart00605
CW domain;
23-111 1.51e-17

CW domain;


:

Pssm-ID: 214742  Cd Length: 94  Bit Score: 75.93  E-value: 1.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207690    23 VKMVLFYGTIVTGIATNVTSSKSVGDCRNGCFEDEHCFLMYFRV-EKCYFHSYlntGQLISVVEVHKSQWAYVAFKTDIS 101
Cdd:smart00605   1 VKMVLIYGKPTTSSSSVTAATLSWDECIQKCYEDSNCVLAYGNSsETCYLFSY---GTVLTVKKLSSSSGKKVAFKVSTD 77

                           90
                   ....*....|
gi 193207690   102 nipNNTCPES 111
Cdd:smart00605  78 ---QPSCPAM 84
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 157-282 1.52e-09

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: 54.55  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207690 157 CMKVFPciSIEPQSAAITRCVEQNVTLTGIASLDEAKWVQEYKISNKTYPAWIGGARDCPEDSpctiFKWTDGyTNLYDA 236
Cdd:cd00037    2 CYKFST--EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGT----WKWSDG-SPLVDY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 193207690 237 LNNNAQLTERTGFDNCLAIlppRNNTDAIIFSQPCgYSGFNYVCGY 282
Cdd:cd00037   75 TNWAPGEPNPGGSEDCVVL---SSSSDGKWNDVSC-SSKLPFICEK 116
 
Name Accession Description Interval E-value
CW smart00605
CW domain;
23-111 1.51e-17

CW domain;


Pssm-ID: 214742  Cd Length: 94  Bit Score: 75.93  E-value: 1.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207690    23 VKMVLFYGTIVTGIATNVTSSKSVGDCRNGCFEDEHCFLMYFRV-EKCYFHSYlntGQLISVVEVHKSQWAYVAFKTDIS 101
Cdd:smart00605   1 VKMVLIYGKPTTSSSSVTAATLSWDECIQKCYEDSNCVLAYGNSsETCYLFSY---GTVLTVKKLSSSSGKKVAFKVSTD 77

                           90
                   ....*....|
gi 193207690   102 nipNNTCPES 111
Cdd:smart00605  78 ---QPSCPAM 84
PAN_3 pfam08277
PAN-like domain;
25-95 2.75e-16

PAN-like domain;


Pssm-ID: 429894  Cd Length: 71  Bit Score: 71.61  E-value: 2.75e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193207690   25 MVLFYGTIVTGIATNVTSSKSVGDCRNGCFEDEHCFLMYFRVEKCYFHSYLNTGQLISVVEVHKSQWAYVA 95
Cdd:pfam08277   1 MVLIYGEPEDYYSTSSTTSESWDDCVTKCYEDSTCVLAYFNSENCYLFSIGNVSTVKKIESSSGSKVAFKI 71
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 157-282 1.52e-09

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: 54.55  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207690 157 CMKVFPciSIEPQSAAITRCVEQNVTLTGIASLDEAKWVQEYKISNKTYPAWIGGARDCPEDSpctiFKWTDGyTNLYDA 236
Cdd:cd00037    2 CYKFST--EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGT----WKWSDG-SPLVDY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 193207690 237 LNNNAQLTERTGFDNCLAIlppRNNTDAIIFSQPCgYSGFNYVCGY 282
Cdd:cd00037   75 TNWAPGEPNPGGSEDCVVL---SSSSDGKWNDVSC-SSKLPFICEK 116
 
Name Accession Description Interval E-value
CW smart00605
CW domain;
23-111 1.51e-17

CW domain;


Pssm-ID: 214742  Cd Length: 94  Bit Score: 75.93  E-value: 1.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207690    23 VKMVLFYGTIVTGIATNVTSSKSVGDCRNGCFEDEHCFLMYFRV-EKCYFHSYlntGQLISVVEVHKSQWAYVAFKTDIS 101
Cdd:smart00605   1 VKMVLIYGKPTTSSSSVTAATLSWDECIQKCYEDSNCVLAYGNSsETCYLFSY---GTVLTVKKLSSSSGKKVAFKVSTD 77

                           90
                   ....*....|
gi 193207690   102 nipNNTCPES 111
Cdd:smart00605  78 ---QPSCPAM 84
PAN_3 pfam08277
PAN-like domain;
25-95 2.75e-16

PAN-like domain;


Pssm-ID: 429894  Cd Length: 71  Bit Score: 71.61  E-value: 2.75e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193207690   25 MVLFYGTIVTGIATNVTSSKSVGDCRNGCFEDEHCFLMYFRVEKCYFHSYLNTGQLISVVEVHKSQWAYVA 95
Cdd:pfam08277   1 MVLIYGEPEDYYSTSSTTSESWDDCVTKCYEDSTCVLAYFNSENCYLFSIGNVSTVKKIESSSGSKVAFKI 71
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 157-282 1.52e-09

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: 54.55  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207690 157 CMKVFPciSIEPQSAAITRCVEQNVTLTGIASLDEAKWVQEYKISNKTYPAWIGGARDCPEDSpctiFKWTDGyTNLYDA 236
Cdd:cd00037    2 CYKFST--EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGT----WKWSDG-SPLVDY 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 193207690 237 LNNNAQLTERTGFDNCLAIlppRNNTDAIIFSQPCgYSGFNYVCGY 282
Cdd:cd00037   75 TNWAPGEPNPGGSEDCVVL---SSSSDGKWNDVSC-SSKLPFICEK 116
 
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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