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Conserved domains on  [gi|1622826441|ref|XP_014977258|]
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LOW QUALITY PROTEIN: putative C-type lectin domain family 20 member A [Macaca mulatta]

Protein Classification

C-type lectin-like domain-containing protein( domain architecture ID 96)

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

PubMed:  16336259|10508765

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT super family cl02432
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 91-200 5.57e-33

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 cd03602:

Pssm-ID: 470576  Cd Length: 108  Bit Score: 115.16  E-value: 5.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441  91 RDLVLVKEALSWYDAQQHCRLHYTDLADLQPSDLLNLYSLMT---STQAWIGLFFDasTSGLRWSSGSTYTALEWVPtLP 167
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSrvsNSAAWIGLYRD--VDSWRWSDGSESSFRNWNT-FQ 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622826441 168 EFGVGICATLYTrlkFPSIGANSCTAQNPFFCY 200
Cdd:cd03602    78 PFGQGDCATMYS---SGRWYAALCSALKPFICY 107
 
Name Accession Description Interval E-value
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 91-200 5.57e-33

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: 115.16  E-value: 5.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441  91 RDLVLVKEALSWYDAQQHCRLHYTDLADLQPSDLLNLYSLMT---STQAWIGLFFDasTSGLRWSSGSTYTALEWVPtLP 167
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSrvsNSAAWIGLYRD--VDSWRWSDGSESSFRNWNT-FQ 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622826441 168 EFGVGICATLYTrlkFPSIGANSCTAQNPFFCY 200
Cdd:cd03602    78 PFGQGDCATMYS---SGRWYAALCSALKPFICY 107
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 95-199 9.81e-12

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: 60.31  E-value: 9.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441   95 LVKEALSWYDAQQHCRLHYTDLADLQPSD----LLNLYSLMT-STQAWIGLFFDASTSGLRWSSGSTYTALE-WVPTLPE 168
Cdd:smart00034  15 FSTEKKTWEDAQAFCQSLGGHLASIHSEAendfVASLLKNSGsSDYYWIGLSDPDSNGSWQWSDGSGPVSYSnWAPGEPN 94

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1622826441  169 FGVGICATLYTRLKFpsIGANSCTAQNPFFC 199
Cdd:smart00034  95 NSSGDCVVLSTSGGK--WNDVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 99-201 2.21e-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: 53.25  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441  99 ALSWYDAQQHCRLHYTDLADLQPS---DLLNLYSLMTSTQAWIGLFFDASTSGLRWSSGSTYTALEWVPTLPEFGV-GIC 174
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAeelDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGEnEDC 80

                          90       100
                  ....*....|....*....|....*..
gi 1622826441 175 ATLYtrLKFPSIGANSCTAQNPFFCYY 201
Cdd:pfam00059  81 VELS--SSSGKWNDENCNSKNPFVCEK 105
 
Name Accession Description Interval E-value
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 91-200 5.57e-33

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: 115.16  E-value: 5.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441  91 RDLVLVKEALSWYDAQQHCRLHYTDLADLQPSDLLNLYSLMT---STQAWIGLFFDasTSGLRWSSGSTYTALEWVPtLP 167
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSrvsNSAAWIGLYRD--VDSWRWSDGSESSFRNWNT-FQ 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622826441 168 EFGVGICATLYTrlkFPSIGANSCTAQNPFFCY 200
Cdd:cd03602    78 PFGQGDCATMYS---SGRWYAALCSALKPFICY 107
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 95-201 2.28e-12

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: 61.87  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441  95 LVKEALSWYDAQQHCRLHYTDLADLQPSD----LLNLYSLMTSTQAWIGLFFDASTSGLRWSSGSTYTALE-WVPTLPEF 169
Cdd:cd00037     5 FSTEKLTWEEAQEYCRSLGGHLASIHSEEendfLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPLVDYTnWAPGEPNP 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622826441 170 -GVGICATLYTRLKFpSIGANSCTAQNPFFCYY 201
Cdd:cd00037    85 gGSEDCVVLSSSSDG-KWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 95-199 9.81e-12

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: 60.31  E-value: 9.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441   95 LVKEALSWYDAQQHCRLHYTDLADLQPSD----LLNLYSLMT-STQAWIGLFFDASTSGLRWSSGSTYTALE-WVPTLPE 168
Cdd:smart00034  15 FSTEKKTWEDAQAFCQSLGGHLASIHSEAendfVASLLKNSGsSDYYWIGLSDPDSNGSWQWSDGSGPVSYSnWAPGEPN 94

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1622826441  169 FGVGICATLYTRLKFpsIGANSCTAQNPFFC 199
Cdd:smart00034  95 NSSGDCVVLSTSGGK--WNDVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 99-201 2.21e-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: 53.25  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441  99 ALSWYDAQQHCRLHYTDLADLQPS---DLLNLYSLMTSTQAWIGLFFDASTSGLRWSSGSTYTALEWVPTLPEFGV-GIC 174
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAeelDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGEnEDC 80

                          90       100
                  ....*....|....*....|....*..
gi 1622826441 175 ATLYtrLKFPSIGANSCTAQNPFFCYY 201
Cdd:pfam00059  81 VELS--SSSGKWNDENCNSKNPFVCEK 105
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 100-201 7.20e-07

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: 46.98  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441 100 LSWYDAQQHCRLHY--TDLAD-LQPSDLLNLYSLMTSTQA-----WIGLFFDASTSGLRWSSGSTYTALEWVPTLPEFGV 171
Cdd:cd03594    20 LSWSDAELFCQKYGpgAHLASiHSPAEAAAIASLISSYQKayqpvWIGLHDPQQSRGWEWSDGSKLDYRSWDRNPPYARG 99

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622826441 172 GICATLYTRLKFPSIGANSCTAQNPFFCYY 201
Cdd:cd03594   100 GYCAELSRSTGFLKWNDANCEERNPFICKY 129
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 97-199 4.52e-03

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: 35.77  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441  97 KEALSWYDAQQHCRLHYTDLADLQPSDLLN-LYSLMTSTQAWIGLFFDASTSGLRWSSGSTYTAleWVPTLPEFGVGICA 175
Cdd:cd03593    17 MEKKTWNESKEACSSKNSSLLKIDDEEELEfLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLNN--LFNIRGSTKSGNCA 94

                          90       100
                  ....*....|....*....|....*
gi 1622826441 176 TLY-TRLKfpsigANSCTAQNPFFC 199
Cdd:cd03593    95 YLSsTGIY-----SEDCSTKKRWIC 114
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 100-199 7.09e-03

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: 35.80  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826441 100 LSWYDAQQHCR--------LHYTDLADLQPSDLLnlYSLMTS-------TQAWIGLFFDASTSGLRWSSGSTYTALEWVP 164
Cdd:cd03589    20 LTWEEAELRCRsfsipgliAHLVSIHSQEENDFV--YDLFESsrgpdtpYGLWIGLHDRTSEGPFEWTDGSPVDFTKWAG 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1622826441 165 TLPEFGVGI--CATLYTRlkfPSIGA----NSCTAQNPFFC 199
Cdd:cd03589    98 GQPDNYGGNedCVQMWRR---GDAGQswndMPCDAVFPYIC 135
 
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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