polycystin-1 isoform X20 [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||||||||||||||||||||||||||||
| PCC super family | cl28216 | polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
97-2725 | 0e+00 | ||||||||||||||||||||||||||||||||||||
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half. The actual alignment was detected with superfamily member TIGR00864: Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 3837.75 E-value: 0e+00
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| Polycystin_dom | pfam20519 | Polycystin domain; This domain represents the polycystin domain from group II of Transient ... |
3667-3845 | 6.11e-66 | ||||||||||||||||||||||||||||||||||||
Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other. : Pssm-ID: 466668 Cd Length: 199 Bit Score: 223.07 E-value: 6.11e-66
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| PKD_channel | pfam08016 | Polycystin cation channel; This family contains the cation channel region from group II of ... |
3846-4067 | 2.64e-59 | ||||||||||||||||||||||||||||||||||||
Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins. : Pssm-ID: 462341 [Multi-domain] Cd Length: 225 Bit Score: 205.20 E-value: 2.64e-59
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| PLAT_polycystin | cd01752 | PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
3112-3231 | 6.86e-57 | ||||||||||||||||||||||||||||||||||||
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins. : Pssm-ID: 238850 Cd Length: 120 Bit Score: 193.65 E-value: 6.86e-57
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| LRR_8 | pfam13855 | Leucine rich repeat; |
61-127 | 2.26e-13 | ||||||||||||||||||||||||||||||||||||
Leucine rich repeat; : Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 67.55 E-value: 2.26e-13
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| GPS super family | cl02559 | GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for ... |
3005-3054 | 9.61e-10 | ||||||||||||||||||||||||||||||||||||
GPCR proteolysis site, GPS, motif; The GPS motif is found in GPCRs, and is the site for auto-proteolysis, so is thus named, GPS. The GPS motif is a conserved sequence of ~40 amino acids containing canonical cysteine and tryptophan residues, and is the most highly conserved part of the domain. In most, if not all, cell-adhesion GPCRs these undergo autoproteolysis in the GPS between a conserved aliphatic residue (usually a leucine) and a threonine, serine, or cysteine residue. In higher eukaryotes this motif is found embedded in the C-terminal beta-stranded part of a GAIN domain - GPCR-Autoproteolysis INducing (GAIN). The GAIN-GPS domain adopts a fold in which the GPS motif, at the C-terminus, forms five beta-strands that are tightly integrated into the overall GAIN domain. The GPS motif, evolutionarily conserved from tetrahymena to mammals, is the only extracellular domain shared by all human cell-adhesion GPCRs and PKD proteins, and is the locus of multiple human disease mutations. The GAIN-GPS domain is both necessary and sufficient functionally for autoproteolysis, suggesting an autoproteolytic mechanism whereby the overall GAIN domain fine-tunes the chemical environment in the GPS to catalyze peptide bond hydrolysis. In the cell-adhesion GPCRs and PKD proteins, the GPS motif is always located at the end of their long N-terminal extracellular regions, immediately before the first transmembrane helix of the respective protein. The actual alignment was detected with superfamily member smart00303: Pssm-ID: 470616 Cd Length: 49 Bit Score: 56.63 E-value: 9.61e-10
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| LRRNT | smart00013 | Leucine rich repeat N-terminal domain; |
32-71 | 4.61e-05 | ||||||||||||||||||||||||||||||||||||
Leucine rich repeat N-terminal domain; : Pssm-ID: 214470 [Multi-domain] Cd Length: 33 Bit Score: 43.08 E-value: 4.61e-05
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| Name | Accession | Description | Interval | E-value | ||||||||||||||||||||||||||||||||||||
| PCC | TIGR00864 | polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
97-2725 | 0e+00 | ||||||||||||||||||||||||||||||||||||
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half. Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 3837.75 E-value: 0e+00
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| REJ | pfam02010 | REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ... |
2169-2612 | 1.39e-116 | ||||||||||||||||||||||||||||||||||||
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains. Pssm-ID: 366875 [Multi-domain] Cd Length: 448 Bit Score: 378.77 E-value: 1.39e-116
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| Polycystin_dom | pfam20519 | Polycystin domain; This domain represents the polycystin domain from group II of Transient ... |
3667-3845 | 6.11e-66 | ||||||||||||||||||||||||||||||||||||
Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other. Pssm-ID: 466668 Cd Length: 199 Bit Score: 223.07 E-value: 6.11e-66
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| PKD_channel | pfam08016 | Polycystin cation channel; This family contains the cation channel region from group II of ... |
3846-4067 | 2.64e-59 | ||||||||||||||||||||||||||||||||||||
Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins. Pssm-ID: 462341 [Multi-domain] Cd Length: 225 Bit Score: 205.20 E-value: 2.64e-59
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| PLAT_polycystin | cd01752 | PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
3112-3231 | 6.86e-57 | ||||||||||||||||||||||||||||||||||||
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins. Pssm-ID: 238850 Cd Length: 120 Bit Score: 193.65 E-value: 6.86e-57
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| PLAT | pfam01477 | PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
3114-3217 | 1.84e-22 | ||||||||||||||||||||||||||||||||||||
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich. Pssm-ID: 396180 Cd Length: 115 Bit Score: 95.19 E-value: 1.84e-22
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| WSC | smart00321 | present in yeast cell wall integrity and stress response component proteins; Domain present in ... |
177-271 | 3.54e-19 | ||||||||||||||||||||||||||||||||||||
present in yeast cell wall integrity and stress response component proteins; Domain present in WSC proteins, polycystin and fungal exoglucanase Pssm-ID: 214616 [Multi-domain] Cd Length: 95 Bit Score: 85.21 E-value: 3.54e-19
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| LH2 | smart00308 | Lipoxygenase homology 2 (beta barrel) domain; |
3112-3214 | 5.47e-19 | ||||||||||||||||||||||||||||||||||||
Lipoxygenase homology 2 (beta barrel) domain; Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 85.00 E-value: 5.47e-19
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| CLECT | cd00037 | C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ... |
418-530 | 1.26e-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: 81.51 E-value: 1.26e-17
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| LRR_8 | pfam13855 | Leucine rich repeat; |
61-127 | 2.26e-13 | ||||||||||||||||||||||||||||||||||||
Leucine rich repeat; Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 67.55 E-value: 2.26e-13
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| COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1483-1770 | 6.28e-11 | ||||||||||||||||||||||||||||||||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 67.39 E-value: 6.28e-11
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| PPP1R42 | cd21340 | protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
56-127 | 1.19e-10 | ||||||||||||||||||||||||||||||||||||
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation. Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 64.42 E-value: 1.19e-10
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| GPS | smart00303 | G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ... |
3005-3054 | 9.61e-10 | ||||||||||||||||||||||||||||||||||||
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin. Pssm-ID: 197639 Cd Length: 49 Bit Score: 56.63 E-value: 9.61e-10
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
48-128 | 5.76e-09 | ||||||||||||||||||||||||||||||||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 61.87 E-value: 5.76e-09
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| LRRNT | smart00013 | Leucine rich repeat N-terminal domain; |
32-71 | 4.61e-05 | ||||||||||||||||||||||||||||||||||||
Leucine rich repeat N-terminal domain; Pssm-ID: 214470 [Multi-domain] Cd Length: 33 Bit Score: 43.08 E-value: 4.61e-05
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
1553-1881 | 2.96e-04 | ||||||||||||||||||||||||||||||||||||
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes. Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 47.34 E-value: 2.96e-04
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| Name | Accession | Description | Interval | E-value | ||||||||||||||||||||||||||||||||||||
| PCC | TIGR00864 | polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ... |
97-2725 | 0e+00 | ||||||||||||||||||||||||||||||||||||
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half. Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 3837.75 E-value: 0e+00
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| REJ | pfam02010 | REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ... |
2169-2612 | 1.39e-116 | ||||||||||||||||||||||||||||||||||||
REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains. Pssm-ID: 366875 [Multi-domain] Cd Length: 448 Bit Score: 378.77 E-value: 1.39e-116
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| Polycystin_dom | pfam20519 | Polycystin domain; This domain represents the polycystin domain from group II of Transient ... |
3667-3845 | 6.11e-66 | ||||||||||||||||||||||||||||||||||||
Polycystin domain; This domain represents the polycystin domain from group II of Transient receptor potential (TRP) channels (TRPP) including PKD1, PKD2, PKD2L and mucolipins. The polycystin domain display a sandwich-like shape with five beta-sheets in the tilted middle layer, three alpha-helices on one side and a large loop with two short antiparallel beta-sheets on the other. Pssm-ID: 466668 Cd Length: 199 Bit Score: 223.07 E-value: 6.11e-66
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| PKD_channel | pfam08016 | Polycystin cation channel; This family contains the cation channel region from group II of ... |
3846-4067 | 2.64e-59 | ||||||||||||||||||||||||||||||||||||
Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins. Pssm-ID: 462341 [Multi-domain] Cd Length: 225 Bit Score: 205.20 E-value: 2.64e-59
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| PLAT_polycystin | cd01752 | PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane ... |
3112-3231 | 6.86e-57 | ||||||||||||||||||||||||||||||||||||
PLAT/LH2 domain of polycystin-1 like proteins. Polycystins are a large family of membrane proteins composed of multiple domains, present in fish, invertebrates, mammals, and humans that are widely expressed in various cell types and whose biological functions remain poorly defined. In human, mutations in polycystin-1 (PKD1) and polycystin-2 (PKD2) have been shown to be the cause for autosomal dominant polycystic kidney disease (ADPKD). The generally proposed function of PLAT/LH2 domains is to mediate interaction with lipids or membrane bound proteins. Pssm-ID: 238850 Cd Length: 120 Bit Score: 193.65 E-value: 6.86e-57
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| PLAT_repeat | cd01756 | PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 ... |
3112-3231 | 2.30e-29 | ||||||||||||||||||||||||||||||||||||
PLAT/LH2 domain repeats of family of proteins with unknown function. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins. Pssm-ID: 238854 Cd Length: 120 Bit Score: 114.96 E-value: 2.30e-29
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| PLAT | pfam01477 | PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. ... |
3114-3217 | 1.84e-22 | ||||||||||||||||||||||||||||||||||||
PLAT/LH2 domain; This domain is found in a variety of membrane or lipid associated proteins. It is called the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain. The known structure of pancreatic lipase shows this domain binds to procolipase pfam01114, which mediates membrane association. So it appears possible that this domain mediates membrane attachment via other protein binding partners. The structure of this domain is known for many members of the family and is composed of a beta sandwich. Pssm-ID: 396180 Cd Length: 115 Bit Score: 95.19 E-value: 1.84e-22
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| WSC | smart00321 | present in yeast cell wall integrity and stress response component proteins; Domain present in ... |
177-271 | 3.54e-19 | ||||||||||||||||||||||||||||||||||||
present in yeast cell wall integrity and stress response component proteins; Domain present in WSC proteins, polycystin and fungal exoglucanase Pssm-ID: 214616 [Multi-domain] Cd Length: 95 Bit Score: 85.21 E-value: 3.54e-19
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| PLAT | cd00113 | PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. ... |
3113-3214 | 4.02e-19 | ||||||||||||||||||||||||||||||||||||
PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology 2) domain. It consists of an eight stranded beta-barrel. The domain can be found in various domain architectures, in case of lipoxygenases, alpha toxin, lipases and polycystin, but also as a single domain or as repeats.The putative function of this domain is to facilitate access to sequestered membrane or micelle bound substrates. Pssm-ID: 238061 Cd Length: 116 Bit Score: 85.85 E-value: 4.02e-19
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| LH2 | smart00308 | Lipoxygenase homology 2 (beta barrel) domain; |
3112-3214 | 5.47e-19 | ||||||||||||||||||||||||||||||||||||
Lipoxygenase homology 2 (beta barrel) domain; Pssm-ID: 214608 [Multi-domain] Cd Length: 105 Bit Score: 85.00 E-value: 5.47e-19
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| CLECT | cd00037 | C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ... |
418-530 | 1.26e-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: 81.51 E-value: 1.26e-17
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1722-1791 | 1.43e-17 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 79.74 E-value: 1.43e-17
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1890-1959 | 3.25e-17 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 78.58 E-value: 3.25e-17
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| CLECT | smart00034 | C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ... |
406-530 | 5.32e-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: 5.32e-17
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1381-1452 | 1.67e-16 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 76.66 E-value: 1.67e-16
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1216-1281 | 2.20e-16 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 76.27 E-value: 2.20e-16
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1127-1198 | 3.83e-16 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 75.50 E-value: 3.83e-16
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1549-1618 | 8.35e-16 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 74.73 E-value: 8.35e-16
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
2066-2133 | 4.13e-15 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 72.80 E-value: 4.13e-15
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| CLECT_DC-SIGN_like | cd03590 | C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ... |
406-530 | 1.47e-13 | ||||||||||||||||||||||||||||||||||||
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: 70.03 E-value: 1.47e-13
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1213-1289 | 1.93e-13 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 68.29 E-value: 1.93e-13
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1130-1205 | 2.00e-13 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 68.25 E-value: 2.00e-13
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| LRR_8 | pfam13855 | Leucine rich repeat; |
61-127 | 2.26e-13 | ||||||||||||||||||||||||||||||||||||
Leucine rich repeat; Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 67.55 E-value: 2.26e-13
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1487-1541 | 2.36e-13 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 67.86 E-value: 2.36e-13
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1210-1288 | 2.81e-13 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 67.86 E-value: 2.81e-13
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1638-1707 | 3.50e-13 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 67.03 E-value: 3.50e-13
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1471-1534 | 4.74e-13 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 66.64 E-value: 4.74e-13
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1546-1624 | 2.10e-12 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 65.17 E-value: 2.10e-12
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
277-344 | 3.86e-12 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 64.33 E-value: 3.86e-12
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
2071-2140 | 6.38e-12 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 64.01 E-value: 6.38e-12
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1811-1875 | 1.07e-11 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 62.79 E-value: 1.07e-11
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1131-1204 | 2.77e-11 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 62.13 E-value: 2.77e-11
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| COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1483-1770 | 6.28e-11 | ||||||||||||||||||||||||||||||||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 67.39 E-value: 6.28e-11
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1723-1798 | 6.64e-11 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 60.93 E-value: 6.64e-11
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| PPP1R42 | cd21340 | protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
56-127 | 1.19e-10 | ||||||||||||||||||||||||||||||||||||
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation. Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 64.42 E-value: 1.19e-10
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1020-1118 | 2.21e-10 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 59.39 E-value: 2.21e-10
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1978-2049 | 2.84e-10 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 58.94 E-value: 2.84e-10
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1547-1624 | 6.81e-10 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 58.28 E-value: 6.81e-10
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| GPS | smart00303 | G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin ... |
3005-3054 | 9.61e-10 | ||||||||||||||||||||||||||||||||||||
G-protein-coupled receptor proteolytic site domain; Present in latrophilin/CL-1, sea urchin REJ and polycystin. Pssm-ID: 197639 Cd Length: 49 Bit Score: 56.63 E-value: 9.61e-10
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1020-1112 | 2.17e-09 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 56.24 E-value: 2.17e-09
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
70-128 | 4.59e-09 | ||||||||||||||||||||||||||||||||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 61.87 E-value: 4.59e-09
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1467-1540 | 5.00e-09 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 55.58 E-value: 5.00e-09
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
48-128 | 5.76e-09 | ||||||||||||||||||||||||||||||||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 61.87 E-value: 5.76e-09
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
2071-2141 | 1.37e-08 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 54.42 E-value: 1.37e-08
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
72-128 | 1.73e-08 | ||||||||||||||||||||||||||||||||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 60.33 E-value: 1.73e-08
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
276-352 | 1.81e-08 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 54.04 E-value: 1.81e-08
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| WSC | pfam01822 | WSC domain; This domain is involved in carbohydrate binding. |
180-233 | 2.26e-08 | ||||||||||||||||||||||||||||||||||||
WSC domain; This domain is involved in carbohydrate binding. Pssm-ID: 460348 Cd Length: 82 Bit Score: 54.00 E-value: 2.26e-08
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| PKD_4 | pfam18911 | PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1121-1204 | 3.43e-08 | ||||||||||||||||||||||||||||||||||||
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 53.43 E-value: 3.43e-08
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
286-353 | 3.84e-08 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 53.22 E-value: 3.84e-08
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| PKD_4 | pfam18911 | PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1487-1540 | 4.01e-08 | ||||||||||||||||||||||||||||||||||||
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 53.43 E-value: 4.01e-08
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
70-128 | 6.25e-08 | ||||||||||||||||||||||||||||||||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 58.41 E-value: 6.25e-08
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1382-1459 | 8.55e-08 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 52.07 E-value: 8.55e-08
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1723-1795 | 1.04e-07 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 52.11 E-value: 1.04e-07
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1292-1373 | 1.47e-07 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 51.73 E-value: 1.47e-07
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| CLECT_REG-1_like | cd03594 | C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ... |
406-530 | 1.53e-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: 53.14 E-value: 1.53e-07
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1292-1373 | 1.71e-07 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 51.30 E-value: 1.71e-07
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| CLECT_CEL-1_like | cd03589 | C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ... |
406-531 | 3.41e-07 | ||||||||||||||||||||||||||||||||||||
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: 52.36 E-value: 3.41e-07
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
70-128 | 3.84e-07 | ||||||||||||||||||||||||||||||||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 56.10 E-value: 3.84e-07
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1970-2056 | 3.86e-07 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 50.53 E-value: 3.86e-07
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| PLAT_plant_stress | cd01754 | PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of ... |
3114-3221 | 5.52e-07 | ||||||||||||||||||||||||||||||||||||
PLAT/LH2 domain of plant-specific single domain protein family with unknown function. Many of its members are stress induced. In general, PLAT/LH2 consists of an eight stranded beta-barrel and it's proposed function is to mediate interaction with lipids or membrane bound proteins. Pssm-ID: 238852 Cd Length: 129 Bit Score: 51.39 E-value: 5.52e-07
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| COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1021-1277 | 1.09e-06 | ||||||||||||||||||||||||||||||||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 53.91 E-value: 1.09e-06
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| LRRCT | smart00082 | Leucine rich repeat C-terminal domain; |
125-177 | 1.21e-06 | ||||||||||||||||||||||||||||||||||||
Leucine rich repeat C-terminal domain; Pssm-ID: 214507 [Multi-domain] Cd Length: 51 Bit Score: 48.20 E-value: 1.21e-06
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| CLECT_collectin_like | cd03591 | C-type lectin-like domain (CTLD) of the type found in human collectins including lung ... |
420-531 | 2.27e-06 | ||||||||||||||||||||||||||||||||||||
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: 49.22 E-value: 2.27e-06
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1388-1458 | 6.28e-06 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 47.11 E-value: 6.28e-06
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1818-1882 | 1.02e-05 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 46.29 E-value: 1.02e-05
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| PKD | pfam00801 | PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. ... |
1298-1362 | 1.69e-05 | ||||||||||||||||||||||||||||||||||||
PKD domain; This domain was first identified in the Polycystic kidney disease protein PKD1. This domain has been predicted to contain an Ig-like fold. Pssm-ID: 395646 [Multi-domain] Cd Length: 70 Bit Score: 45.46 E-value: 1.69e-05
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| LRR | COG4886 | Leucine-rich repeat (LRR) protein [Transcription]; |
55-128 | 1.71e-05 | ||||||||||||||||||||||||||||||||||||
Leucine-rich repeat (LRR) protein [Transcription]; Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 50.70 E-value: 1.71e-05
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| PKD | cd00146 | polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an ... |
1020-1118 | 4.28e-05 | ||||||||||||||||||||||||||||||||||||
polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases. Pssm-ID: 238084 [Multi-domain] Cd Length: 81 Bit Score: 44.79 E-value: 4.28e-05
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| LRRNT | smart00013 | Leucine rich repeat N-terminal domain; |
32-71 | 4.61e-05 | ||||||||||||||||||||||||||||||||||||
Leucine rich repeat N-terminal domain; Pssm-ID: 214470 [Multi-domain] Cd Length: 33 Bit Score: 43.08 E-value: 4.61e-05
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| CLECT_NK_receptors_like | cd03593 | C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ... |
417-530 | 1.59e-04 | ||||||||||||||||||||||||||||||||||||
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: 43.86 E-value: 1.59e-04
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| COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1723-1878 | 1.76e-04 | ||||||||||||||||||||||||||||||||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 46.97 E-value: 1.76e-04
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| CLECT_CSPGs | cd03588 | C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ... |
417-530 | 2.11e-04 | ||||||||||||||||||||||||||||||||||||
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: 44.11 E-value: 2.11e-04
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| COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1404-1665 | 2.29e-04 | ||||||||||||||||||||||||||||||||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 46.59 E-value: 2.29e-04
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| PKD_4 | pfam18911 | PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1227-1289 | 2.58e-04 | ||||||||||||||||||||||||||||||||||||
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 42.64 E-value: 2.58e-04
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| PKD_4 | pfam18911 | PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1407-1458 | 2.93e-04 | ||||||||||||||||||||||||||||||||||||
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 42.26 E-value: 2.93e-04
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
1553-1881 | 2.96e-04 | ||||||||||||||||||||||||||||||||||||
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes. Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 47.34 E-value: 2.96e-04
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| CLECT_VCBS | cd03603 | A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ... |
418-501 | 7.53e-04 | ||||||||||||||||||||||||||||||||||||
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: 42.03 E-value: 7.53e-04
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| LRR_4 | pfam12799 | Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
61-108 | 1.45e-03 | ||||||||||||||||||||||||||||||||||||
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains. Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 39.15 E-value: 1.45e-03
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| PKD_4 | pfam18911 | PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
271-344 | 1.49e-03 | ||||||||||||||||||||||||||||||||||||
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 40.33 E-value: 1.49e-03
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| COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
1298-1624 | 1.59e-03 | ||||||||||||||||||||||||||||||||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 43.89 E-value: 1.59e-03
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| CLECT_TC14_like | cd03601 | C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ... |
435-530 | 1.84e-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: 40.98 E-value: 1.84e-03
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| LRR | smart00370 | Leucine-rich repeats, outliers; |
90-113 | 2.02e-03 | ||||||||||||||||||||||||||||||||||||
Leucine-rich repeats, outliers; Pssm-ID: 197688 [Multi-domain] Cd Length: 24 Bit Score: 38.10 E-value: 2.02e-03
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| LRR_TYP | smart00369 | Leucine-rich repeats, typical (most populated) subfamily; |
90-113 | 2.02e-03 | ||||||||||||||||||||||||||||||||||||
Leucine-rich repeats, typical (most populated) subfamily; Pssm-ID: 197687 [Multi-domain] Cd Length: 24 Bit Score: 38.10 E-value: 2.02e-03
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| PKD_4 | pfam18911 | PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
2074-2126 | 2.11e-03 | ||||||||||||||||||||||||||||||||||||
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 39.95 E-value: 2.11e-03
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1892-1965 | 3.22e-03 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 39.36 E-value: 3.22e-03
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| PKD_4 | pfam18911 | PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. |
1024-1118 | 3.92e-03 | ||||||||||||||||||||||||||||||||||||
PKD domain; This entry is composed of PKD domains found in bacterial surface proteins. Pssm-ID: 436824 [Multi-domain] Cd Length: 85 Bit Score: 39.18 E-value: 3.92e-03
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| PKD | smart00089 | Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 ... |
1643-1711 | 4.11e-03 | ||||||||||||||||||||||||||||||||||||
Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases. Pssm-ID: 214510 [Multi-domain] Cd Length: 79 Bit Score: 38.97 E-value: 4.11e-03
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| LRR_4 | pfam12799 | Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ... |
93-126 | 4.20e-03 | ||||||||||||||||||||||||||||||||||||
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains. Pssm-ID: 463713 [Multi-domain] Cd Length: 44 Bit Score: 37.61 E-value: 4.20e-03
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| COG3291 | COG3291 | Uncharacterized conserved protein, PKD repeat domain [Function unknown]; |
2074-2140 | 7.93e-03 | ||||||||||||||||||||||||||||||||||||
Uncharacterized conserved protein, PKD repeat domain [Function unknown]; Pssm-ID: 442520 [Multi-domain] Cd Length: 333 Bit Score: 41.96 E-value: 7.93e-03
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