glycoside hydrolase [Dictyobacter arantiisoli]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| GH43_Pc3Gal43A-like | cd18821 | Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ... |
56-318 | 1.96e-160 | |||||
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. : Pssm-ID: 350142 [Multi-domain] Cd Length: 262 Bit Score: 454.77 E-value: 1.96e-160
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| beta-trefoil_Ricin_1,3Gal43A | cd23446 | ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ... |
346-484 | 2.59e-65 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. : Pssm-ID: 467324 [Multi-domain] Cd Length: 137 Bit Score: 207.23 E-value: 2.59e-65
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| Name | Accession | Description | Interval | E-value | |||||
| GH43_Pc3Gal43A-like | cd18821 | Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ... |
56-318 | 1.96e-160 | |||||
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350142 [Multi-domain] Cd Length: 262 Bit Score: 454.77 E-value: 1.96e-160
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| beta-trefoil_Ricin_1,3Gal43A | cd23446 | ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ... |
346-484 | 2.59e-65 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467324 [Multi-domain] Cd Length: 137 Bit Score: 207.23 E-value: 2.59e-65
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| XynB2 | COG3507 | Beta-xylosidase [Carbohydrate transport and metabolism]; |
63-262 | 1.02e-26 | |||||
Beta-xylosidase [Carbohydrate transport and metabolism]; Pssm-ID: 442730 [Multi-domain] Cd Length: 351 Bit Score: 110.42 E-value: 1.02e-26
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| RicinB_lectin_2 | pfam14200 | Ricin-type beta-trefoil lectin domain-like; |
381-471 | 3.61e-23 | |||||
Ricin-type beta-trefoil lectin domain-like; Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 93.21 E-value: 3.61e-23
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| Glyco_hydro_43 | pfam04616 | Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ... |
63-263 | 2.05e-19 | |||||
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 398349 [Multi-domain] Cd Length: 281 Bit Score: 88.15 E-value: 2.05e-19
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| lectin_2 | NF035930 | lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ... |
354-481 | 2.48e-11 | |||||
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 63.65 E-value: 2.48e-11
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| RICIN | smart00458 | Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. |
351-484 | 2.03e-09 | |||||
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 55.21 E-value: 2.03e-09
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| lectin_2 | NF035930 | lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ... |
353-433 | 3.74e-08 | |||||
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 54.02 E-value: 3.74e-08
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| lectin_2 | NF035930 | lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ... |
399-482 | 1.06e-04 | |||||
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 43.62 E-value: 1.06e-04
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| Name | Accession | Description | Interval | E-value | |||||
| GH43_Pc3Gal43A-like | cd18821 | Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1, ... |
56-318 | 1.96e-160 | |||||
Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350142 [Multi-domain] Cd Length: 262 Bit Score: 454.77 E-value: 1.96e-160
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| GH43_CtGH43-like | cd18822 | Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ... |
56-318 | 3.81e-106 | |||||
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350143 Cd Length: 266 Bit Score: 316.87 E-value: 3.81e-106
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| GH43_CtGH43-like | cd08985 | Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase ... |
56-318 | 1.07e-104 | |||||
Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350099 [Multi-domain] Cd Length: 273 Bit Score: 313.50 E-value: 1.07e-104
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| GH43_CtGH43-like | cd18825 | Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ... |
56-318 | 1.81e-101 | |||||
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350146 [Multi-domain] Cd Length: 285 Bit Score: 305.68 E-value: 1.81e-101
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| GH43_CtGH43-like | cd18826 | Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ... |
56-318 | 3.96e-68 | |||||
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350147 [Multi-domain] Cd Length: 269 Bit Score: 219.04 E-value: 3.96e-68
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| beta-trefoil_Ricin_1,3Gal43A | cd23446 | ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ... |
346-484 | 2.59e-65 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467324 [Multi-domain] Cd Length: 137 Bit Score: 207.23 E-value: 2.59e-65
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| GH43_RcAra43A-like | cd18823 | Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This ... |
56-318 | 1.03e-61 | |||||
Glycosyl hydrolase family 43 such as Ruminococcus champanellensis arabinanase Ara43A; This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis arabinanase Ara43A and Fibrobacter succinogenes subsp. succinogenes S85 Fisuc_1994 / FSU_2517. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350144 [Multi-domain] Cd Length: 289 Bit Score: 203.35 E-value: 1.03e-61
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| beta-trefoil_Ricin-like | cd00161 | ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ... |
346-481 | 3.27e-49 | |||||
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats. Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 164.85 E-value: 3.27e-49
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| beta-trefoil_Ricin_AgaB34-like | cd23458 | ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ... |
347-481 | 8.53e-40 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 140.15 E-value: 8.53e-40
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| GH43_CtGH43-like | cd18824 | Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1, ... |
56-318 | 6.68e-37 | |||||
Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A; This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350145 [Multi-domain] Cd Length: 282 Bit Score: 137.16 E-value: 6.68e-37
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| beta-trefoil_Ricin-like | cd00161 | ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ... |
398-484 | 5.02e-29 | |||||
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats. Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 110.92 E-value: 5.02e-29
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| beta-trefoil_Ricin-like | cd00161 | ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ... |
339-433 | 2.28e-28 | |||||
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats. Pssm-ID: 467293 [Multi-domain] Cd Length: 134 Bit Score: 109.38 E-value: 2.28e-28
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| XynB2 | COG3507 | Beta-xylosidase [Carbohydrate transport and metabolism]; |
63-262 | 1.02e-26 | |||||
Beta-xylosidase [Carbohydrate transport and metabolism]; Pssm-ID: 442730 [Multi-domain] Cd Length: 351 Bit Score: 110.42 E-value: 1.02e-26
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| beta-trefoil_Ricin_AgaB34-like | cd23458 | ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ... |
395-484 | 4.42e-26 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 102.79 E-value: 4.42e-26
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| beta-trefoil_Ricin_SaAF-like | cd23457 | ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca ... |
350-473 | 1.22e-23 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467335 [Multi-domain] Cd Length: 139 Bit Score: 96.33 E-value: 1.22e-23
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| RicinB_lectin_2 | pfam14200 | Ricin-type beta-trefoil lectin domain-like; |
381-471 | 3.61e-23 | |||||
Ricin-type beta-trefoil lectin domain-like; Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 93.21 E-value: 3.61e-23
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| beta-trefoil_Ricin_AgaB34-like | cd23458 | ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ... |
341-433 | 2.15e-22 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467336 [Multi-domain] Cd Length: 135 Bit Score: 92.77 E-value: 2.15e-22
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| beta-trefoil_Ricin_XLN-like | cd23418 | ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ... |
344-481 | 4.14e-22 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket. Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 91.64 E-value: 4.14e-22
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| beta-trefoil_Ricin_MOA-like | cd23416 | ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and ... |
348-481 | 9.61e-22 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and similar proteins; The family includes Marasmius oreades agglutinin (MOA) and Polyporus squamosus Ricin B-related lectin (PSL). MOA is a lectin isolated from fruiting bodies of the mushroom M. oreades. It specifically binds non-reducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Polyporus squamosus Ricin B-related lectin (PSL) is a lectin specific for glycans terminating with the sequence Neu5Acalpha2-6Galbeta. Like MOA, PSL is a calcium-dependent cysteine protease. Both MOA and PSL contain an N-terminal ricin B-type lectin domain and a C-terminal agglutinin domain. The ricin B-type lectin domain is a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467295 [Multi-domain] Cd Length: 145 Bit Score: 91.25 E-value: 9.61e-22
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| GH_F | cd08978 | Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F ... |
59-288 | 5.00e-21 | |||||
Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F; This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350092 [Multi-domain] Cd Length: 251 Bit Score: 92.11 E-value: 5.00e-21
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| RicinB_lectin_2 | pfam14200 | Ricin-type beta-trefoil lectin domain-like; |
344-423 | 1.32e-20 | |||||
Ricin-type beta-trefoil lectin domain-like; Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 86.28 E-value: 1.32e-20
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| beta-trefoil_Ricin_laminarinase | cd23451 | ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ... |
350-482 | 2.65e-20 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 86.62 E-value: 2.65e-20
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| Glyco_hydro_43 | pfam04616 | Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ... |
63-263 | 2.05e-19 | |||||
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 398349 [Multi-domain] Cd Length: 281 Bit Score: 88.15 E-value: 2.05e-19
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| Ricin_B_lectin | pfam00652 | Ricin-type beta-trefoil lectin domain; |
346-481 | 4.19e-19 | |||||
Ricin-type beta-trefoil lectin domain; Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 82.96 E-value: 4.19e-19
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| GH43_ABN-like | cd08999 | Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase ... |
62-262 | 4.07e-18 | |||||
Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350113 [Multi-domain] Cd Length: 284 Bit Score: 84.50 E-value: 4.07e-18
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| beta-trefoil_Ricin_RPI | cd23452 | ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ... |
342-482 | 1.62e-15 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467330 [Multi-domain] Cd Length: 125 Bit Score: 72.93 E-value: 1.62e-15
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| RicinB_lectin_2 | pfam14200 | Ricin-type beta-trefoil lectin domain-like; |
429-484 | 3.97e-15 | |||||
Ricin-type beta-trefoil lectin domain-like; Pssm-ID: 464102 [Multi-domain] Cd Length: 89 Bit Score: 70.49 E-value: 3.97e-15
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| beta-trefoil_Ricin_laminarinase | cd23451 | ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ... |
339-434 | 4.01e-15 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 71.59 E-value: 4.01e-15
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| GH43_bXyl-like | cd09004 | Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ... |
92-264 | 1.12e-14 | |||||
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350118 [Multi-domain] Cd Length: 266 Bit Score: 73.80 E-value: 1.12e-14
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| GH43_ABN-like | cd18616 | Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl ... |
69-261 | 4.03e-14 | |||||
Glycosyl hydrolase family 43 such as arabinan endo-1 5-alpha-L-arabinosidase; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activity. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350128 [Multi-domain] Cd Length: 291 Bit Score: 72.61 E-value: 4.03e-14
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| beta-trefoil_Ricin_EW29-like | cd23449 | ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ... |
347-481 | 1.28e-13 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin. Pssm-ID: 467327 [Multi-domain] Cd Length: 128 Bit Score: 67.70 E-value: 1.28e-13
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| beta-trefoil_Ricin_SCDase | cd23456 | ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ... |
347-481 | 7.93e-13 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467334 [Multi-domain] Cd Length: 122 Bit Score: 65.07 E-value: 7.93e-13
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| GH43_AXH_like | cd08990 | Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ... |
92-262 | 1.77e-12 | |||||
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase; This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350104 [Multi-domain] Cd Length: 269 Bit Score: 67.62 E-value: 1.77e-12
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| GH43_XYL-like | cd08989 | Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl ... |
63-316 | 4.52e-12 | |||||
Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350103 [Multi-domain] Cd Length: 272 Bit Score: 66.23 E-value: 4.52e-12
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| GH43_HoAraf43-like | cd08991 | Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ... |
69-262 | 6.43e-12 | |||||
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580); This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350105 [Multi-domain] Cd Length: 283 Bit Score: 66.04 E-value: 6.43e-12
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| GH43_ABN | cd08988 | Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes ... |
59-240 | 8.44e-12 | |||||
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350102 [Multi-domain] Cd Length: 277 Bit Score: 65.62 E-value: 8.44e-12
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| lectin_2 | NF035930 | lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ... |
354-481 | 2.48e-11 | |||||
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 63.65 E-value: 2.48e-11
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| beta-trefoil_Ricin_RSA | cd23455 | ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) ... |
348-483 | 4.08e-11 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Rhizoctonia solani agglutinin (RSA) and similar proteins; RSA is a 15.5-kDa lectin accumulated in the mycelium and sclerotia of the soil born plant pathogenic fungus R. solani. It may act as a storage protein implicated in fungal insecticidal activity. It displays high selectivity towards terminal non-reducing N-acetylgalactosamine residues. RSA reveals a domain-swapping dimeric assembly. Each monomer contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467333 [Multi-domain] Cd Length: 131 Bit Score: 60.42 E-value: 4.08e-11
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| beta-trefoil_Ricin_MPL_CNL | cd23422 | ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like ... |
348-481 | 4.58e-11 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like lectin (MPL), Clitocybe nebularis lectin (CNL), and similar proteins; MPL and CNL are a homodimeric ricin B-like lectins with a beta-trefoil fold that is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Their alpha subunit may harbor a sugar-binding pocket. MPL has the highest specificity for terminal N-acetyllactosamine and other beta-galactosides. CNL induces maturation and activation of dendritic cells via the toll-like receptor 4 pathway. It is specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). It is also specific for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end. Pssm-ID: 467300 [Multi-domain] Cd Length: 135 Bit Score: 60.41 E-value: 4.58e-11
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| beta-trefoil_Ricin_MOA-like | cd23416 | ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and ... |
315-437 | 5.32e-11 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and similar proteins; The family includes Marasmius oreades agglutinin (MOA) and Polyporus squamosus Ricin B-related lectin (PSL). MOA is a lectin isolated from fruiting bodies of the mushroom M. oreades. It specifically binds non-reducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Polyporus squamosus Ricin B-related lectin (PSL) is a lectin specific for glycans terminating with the sequence Neu5Acalpha2-6Galbeta. Like MOA, PSL is a calcium-dependent cysteine protease. Both MOA and PSL contain an N-terminal ricin B-type lectin domain and a C-terminal agglutinin domain. The ricin B-type lectin domain is a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467295 [Multi-domain] Cd Length: 145 Bit Score: 60.44 E-value: 5.32e-11
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| beta-trefoil_Ricin_GllA-1 | cd23454 | GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ... |
352-483 | 6.35e-11 | |||||
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain. Pssm-ID: 467332 [Multi-domain] Cd Length: 136 Bit Score: 60.02 E-value: 6.35e-11
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| beta-trefoil_Ricin_HA17-like | cd23445 | ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating ... |
354-483 | 1.36e-10 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating proteins, HA17 and HA33, and similar proteins; The subfamily includes Clostridium botulinum hemagglutinating proteins HA17 and HA33, Lysinibacillus sphaericus mosquitocidal toxin (MTX) and Pieris brassicae pierisin. The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin. It may increase internalization of the neurotoxin into the bloodstream of the host. The hemagglutinin complex, composed of HA-70 (also known as HA3), HA-33 (also known as HA1) and HA-17 (also known as HA2), agglutinates erythrocytes, whereas the individual components do not. HA-33 is involved in recognition of cell-surface carbohydrates. HA-17 and HA-70 are involved in paracellular barrier disruption by E-cadherin binding. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this subfamily contain at least one ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467323 [Multi-domain] Cd Length: 133 Bit Score: 58.87 E-value: 1.36e-10
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| GH43_FsAxh1-like | cd09001 | Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 ... |
63-262 | 3.24e-10 | |||||
Glycosyl hydrolase family 43 such as Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase; This glycosyl hydrolase family 43 (GH43) includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase; xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. This subfamily includes the characterized Clostridium stercorarium F-9 beta-xylosidase Xyl43B. It also includes Humicola insolens AXHd3 (HiAXHd3), a GH43 arabinofuranosidase (EC 3.2.1.55) that hydrolyzes O3-linked arabinose of doubly substituted xylans, a feature of the polysaccharide that is recalcitrant to degradation. It possesses an additional C-terminal beta-sandwich domain such that the interface between the domains comprises a xylan binding cleft that houses the active site pocket. The HiAXHd3 active site is tuned to hydrolyze arabinofuranosyl or xylosyl linkages, and the topology of the distal regions of the substrate binding surface confers specificity. It also includes Fibrobacter succinogenes subsp. succinogenes S85 arabinoxylan alpha-L-arabinofuranosidase (Axh1;Fisuc_1769;FSU_2269), Paenibacillus sp. E18 alpha-L-arabinofuranosidase (Abf43A), Bifidobacterium adolescentis ATCC 15703 double substituted xylan alpha-1,3-L-specific arabinofuranosidase d3 (AXHd3;AXH-d3;BaAXH-d3;BAD_0301;E-AFAM2), and Chrysosporium lucknowense C1 arabinoxylan hydrolase / double substituted xylan alpha-1,3-L-arabinofuranosidase (Abn7;AXHd). A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350115 [Multi-domain] Cd Length: 270 Bit Score: 60.61 E-value: 3.24e-10
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| beta-trefoil_Ricin_MOA-like | cd23416 | ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and ... |
403-484 | 7.31e-10 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Marasmius oreades agglutinin (MOA) and similar proteins; The family includes Marasmius oreades agglutinin (MOA) and Polyporus squamosus Ricin B-related lectin (PSL). MOA is a lectin isolated from fruiting bodies of the mushroom M. oreades. It specifically binds non-reducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Polyporus squamosus Ricin B-related lectin (PSL) is a lectin specific for glycans terminating with the sequence Neu5Acalpha2-6Galbeta. Like MOA, PSL is a calcium-dependent cysteine protease. Both MOA and PSL contain an N-terminal ricin B-type lectin domain and a C-terminal agglutinin domain. The ricin B-type lectin domain is a beta-trefoil domain, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467295 [Multi-domain] Cd Length: 145 Bit Score: 57.36 E-value: 7.31e-10
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| beta-trefoil_Ricin_MTX-like_rpt1-3 | cd23497 | first, second and third ricin B-type lectin domains, beta-trefoil fold, found in ... |
354-484 | 8.19e-10 | |||||
first, second and third ricin B-type lectin domains, beta-trefoil fold, found in Lysinibacillus sphaericus mosquitocidal toxin (MTX) and similar proteins; This subfamily includes Lysinibacillus sphaericus MTX and Pieris brassicae pierisin. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this family contain four ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the first, second and third ricin B-type lectin domains. Each subdomain bears a potential sugar binding site. Pssm-ID: 467375 [Multi-domain] Cd Length: 139 Bit Score: 56.98 E-value: 8.19e-10
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| beta-trefoil_Ricin_RPI | cd23452 | ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ... |
399-483 | 1.36e-09 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467330 [Multi-domain] Cd Length: 125 Bit Score: 55.98 E-value: 1.36e-09
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| RICIN | smart00458 | Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. |
351-484 | 2.03e-09 | |||||
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 55.21 E-value: 2.03e-09
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| beta-trefoil_Ricin_SSA | cd23426 | ricin B-type lectin domain, beta-trefoil fold, found in Sclerotinia sclerotiorum agglutinin ... |
348-483 | 7.78e-09 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Sclerotinia sclerotiorum agglutinin (SSA) and similar proteins; SSA acts as a lectin that primarily recognizes glycans with a non-reducing terminal N-acetylgalactosamine (GalNAc), with a preference for the alpha-over the beta-anomer. It can also bind non-reducing terminal galactose (Gal) residues but with a lower affinity. SSA strongly interacts with glycolipid type glycans with terminal non-reducing Gal or GalNAc but fails to bind sialylated or fucosylated forms of the same glycans. It also strongly interacts with galactosylated N-glycans, displaying highest affinity for alpha-1-3 branched mono-antennary N-glycans but also binding to multi-antennary glycans. SSA is a homodimeric protein. The monomer contains a ricin B-type lectin domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a putative sugar-binding pocket. Pssm-ID: 467304 [Multi-domain] Cd Length: 147 Bit Score: 54.28 E-value: 7.78e-09
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| beta-trefoil_Ricin_AH | cd23415 | ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ... |
346-482 | 8.32e-09 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket. Pssm-ID: 467294 [Multi-domain] Cd Length: 120 Bit Score: 53.59 E-value: 8.32e-09
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| GH43_SXA-like | cd09000 | Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This ... |
63-246 | 1.23e-08 | |||||
Glycosyl hydrolase family 43, such as Selenomonas ruminantium beta-D-xylosidase SXA; This glycosyl hydrolase family 43 (GH43) includes enzymes that have been characterized to mainly have beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium (Xsa;Sxa;SXA), Bifidobacterium adolescentis ATCC 15703 (XylC;XynB;BAD_0428) and Bacillus sp. KK-1 XylB. They are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. These enzymes possess an additional C-terminal beta-sandwich domain that restricts access for substrates to a portion of the active site to form a pocket. The active-site pockets comprise of two subsites, with binding capacity for two monosaccharide moieties and a single route of access for small molecules such as substrate. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350114 [Multi-domain] Cd Length: 292 Bit Score: 56.02 E-value: 1.23e-08
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| GH43_Arb43a-like | cd08998 | Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 ... |
63-241 | 1.34e-08 | |||||
Glycosyl hydrolase family 43 protein such as Bacillus subtilis subsp. subtilis str. 168 endo-alpha-1,5-L-arabinanase Arb43A; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes such as the Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350112 [Multi-domain] Cd Length: 278 Bit Score: 56.02 E-value: 1.34e-08
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| GH43_F5-8_typeC-like | cd18608 | Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 ... |
63-267 | 1.49e-08 | |||||
Glycosyl hydrolase family 43 protein most having a F5/8 type C domain C-terminal to the GH43 domain; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), xylanase (EC 3.2.1.8), and beta-galactosidase (EC 3.2.1.145) activities, and some as F5/8 type C domain (also known as the discoidin (DS) domain)-containing proteins. Most contain a F5/8 type C domain C-terminal to the GH43 domain. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350120 [Multi-domain] Cd Length: 276 Bit Score: 55.75 E-value: 1.49e-08
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| GH43_XynD-like | cd09003 | Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan ... |
71-256 | 1.93e-08 | |||||
Glycosyl hydrolase family 43 protein such as Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized Bacillus subtilis arabinoxylan arabinofuranohydrolase (AXH), Caldicellulosiruptor sp. Tok7B.1 beta-1,4-xylanase (EC 3.2.1.8) / alpha-L-arabinosidase (EC 3.2.1.55) XynA, Caldicellulosiruptor sp. Rt69B.1 xylanase C (EC 3.2.1.8) XynC, and Caldicellulosiruptor saccharolyticus beta-xylosidase (EC 3.2.1.37)/ alpha-L-arabinofuranosidase (EC 3.2.1.55) XynF. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. It belongs to the GH43_AXH-like subgroup which includes enzymes that have been annotated as having beta-xylosidase, alpha-L-arabinofuranosidase and arabinoxylan alpha-L-1,3-arabinofuranohydrolase, xylanase (endo-alpha-L-arabinanase) as well as AXH activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Bacillus subtilis AXH (BsAXH-m2,3) has been shown to cleave arabinose units from O-2- or O-3-mono-substituted xylose residues and superposition of its structure with known structures of the GH43 exo-acting enzymes, beta-xylosidase and alpha-L-arabinanase, each in complex with their substrate, reveals a different orientation of the sugar backbone. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350117 [Multi-domain] Cd Length: 315 Bit Score: 55.73 E-value: 1.93e-08
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| lectin_2 | NF035930 | lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ... |
353-433 | 3.74e-08 | |||||
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 54.02 E-value: 3.74e-08
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| beta-trefoil_Ricin_SCDase_rpt2 | cd23500 | second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ... |
355-481 | 3.81e-08 | |||||
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. The model corresponds to the second lectin domain. Pssm-ID: 467378 [Multi-domain] Cd Length: 128 Bit Score: 52.08 E-value: 3.81e-08
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| beta-trefoil_Ricin_SCDase_rpt1 | cd23499 | first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ... |
347-483 | 5.13e-08 | |||||
first ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. The model corresponds to the first lectin domain. Pssm-ID: 467377 [Multi-domain] Cd Length: 131 Bit Score: 51.68 E-value: 5.13e-08
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| beta-trefoil_Ricin_GllA-1 | cd23454 | GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ... |
350-435 | 6.44e-08 | |||||
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain. Pssm-ID: 467332 [Multi-domain] Cd Length: 136 Bit Score: 51.55 E-value: 6.44e-08
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| GH43_XlnD-like | cd18827 | Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); ... |
92-261 | 8.08e-08 | |||||
Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); includes mostly xylanases; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have mostly been annotated as xylanases (endo-alpha-L-arabinanase, EC 3.2.1.8). It belongs to the GH43_bXyl-like subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl-like subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidases (EC 3.2.1.37) and xylanases, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350148 [Multi-domain] Cd Length: 277 Bit Score: 53.44 E-value: 8.08e-08
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| Ricin_B_lectin | pfam00652 | Ricin-type beta-trefoil lectin domain; |
398-483 | 1.65e-07 | |||||
Ricin-type beta-trefoil lectin domain; Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 49.84 E-value: 1.65e-07
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| GH43_XynB-like | cd18617 | Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, ... |
63-239 | 2.83e-07 | |||||
Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB); This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350129 [Multi-domain] Cd Length: 285 Bit Score: 52.12 E-value: 2.83e-07
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| beta-trefoil_Ricin_GllA-1 | cd23454 | GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ... |
394-483 | 4.26e-07 | |||||
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain. Pssm-ID: 467332 [Multi-domain] Cd Length: 136 Bit Score: 49.24 E-value: 4.26e-07
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| beta-trefoil_Ricin_HA17-like | cd23445 | ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating ... |
321-387 | 5.04e-07 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating proteins, HA17 and HA33, and similar proteins; The subfamily includes Clostridium botulinum hemagglutinating proteins HA17 and HA33, Lysinibacillus sphaericus mosquitocidal toxin (MTX) and Pieris brassicae pierisin. The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin. It may increase internalization of the neurotoxin into the bloodstream of the host. The hemagglutinin complex, composed of HA-70 (also known as HA3), HA-33 (also known as HA1) and HA-17 (also known as HA2), agglutinates erythrocytes, whereas the individual components do not. HA-33 is involved in recognition of cell-surface carbohydrates. HA-17 and HA-70 are involved in paracellular barrier disruption by E-cadherin binding. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this subfamily contain at least one ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467323 [Multi-domain] Cd Length: 133 Bit Score: 48.85 E-value: 5.04e-07
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| GH43_BT3675-like | cd18828 | Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ... |
63-262 | 1.56e-06 | |||||
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675); This glycosyl hydrolase family 43 (GH43) subgroup includes the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the GH43_bXyl subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl subgroup also includes enzymes annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350149 [Multi-domain] Cd Length: 283 Bit Score: 49.58 E-value: 1.56e-06
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| beta-trefoil_Ricin_SaAF-like | cd23457 | ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca ... |
446-483 | 1.78e-06 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Stigmatella aurantiaca alpha-L-arabinofuranosidase (SaAF) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called non-reducing end alpha-L-arabinofuranosidase, or arabinosidase, catalyzes the hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. It acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Members of this subfamily contain a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467335 [Multi-domain] Cd Length: 139 Bit Score: 47.41 E-value: 1.78e-06
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| GH43_XylA-like | cd18620 | Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium ... |
92-262 | 2.03e-06 | |||||
Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium alpha-L-arabinofuranosidase XylA; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. The GH43_XylA-like subgroup includes Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), endo-alpha-L-arabinanase (EC 3.2.1.-) as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Pssm-ID: 350132 [Multi-domain] Cd Length: 274 Bit Score: 49.13 E-value: 2.03e-06
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| beta-trefoil_Ricin_CELIII-like_rpt2 | cd23420 | second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2 ... |
346-480 | 3.87e-06 | |||||
second ricin B-type lectin domain, beta-trefoil fold, found in Cucumaria echinata Ca2+-dependent hemolytic lectin CEL-III and similar proteins; CEL-III is a Ca2+-dependent and galactose-specific lectin that exhibits hemolytic and hemagglutinating activities. It functions as an oligomer that forms an ion-permeable pore in the cell membrane. CEL-III consists of three domains: two N-terminal ricin B-type lectin domains, and a C-terminal pore-forming domain. The ricin B-type lectin domains show a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. The model corresponds to the second ricin B-type lectin domain. Pssm-ID: 467299 [Multi-domain] Cd Length: 133 Bit Score: 46.39 E-value: 3.87e-06
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| GH43_AnAbnA-like | cd18831 | Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA); ... |
101-250 | 5.32e-06 | |||||
Glycosyl hydrolase family 43 protein such as Aspergillus niger endo-alpha-L-arabinanase (AbnA); This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities such as Aspergillus niger AbnA, Aspergillus niveus AbnA, and Chrysosporium lucknowense Abn1. It belongs to the GH43_Arb43a subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_Arb43a subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. The GH43_Arb43a subgroup includes many enzymes such as Bacillus subtilis arabinanase Abn2, that hydrolyzes sugar beet arabinan (branched), linear alpha-1,5-L-arabinan and pectin, and are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350152 [Multi-domain] Cd Length: 286 Bit Score: 47.97 E-value: 5.32e-06
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| beta-trefoil_Ricin_HA33_rpt2 | cd23496 | second ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum ... |
369-483 | 2.00e-05 | |||||
second ricin B-type lectin domain, beta-trefoil fold, found in Clostridium botulinum hemagglutinating protein HA33 and similar proteins; HA33, also called HA1, is a hemagglutinin (HA) 33 kDa subcomponent, which is associated with the large botulinum neurotoxin secreted complexes and plays a critical role in toxin protection, internalization, and possibly activation. HA33 is involved with internalization of the toxin into the bloodstream by binding to oligosaccharides lining the intestine. HA33 contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a potential sugar binding site. The model corresponds to the second ricin B-type lectin domain. Pssm-ID: 467374 [Multi-domain] Cd Length: 136 Bit Score: 44.45 E-value: 2.00e-05
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| beta-trefoil_Ricin_SCDase | cd23456 | ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ... |
398-484 | 3.67e-05 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467334 [Multi-domain] Cd Length: 122 Bit Score: 43.11 E-value: 3.67e-05
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| GH43_GsAbnA-like | cd18832 | Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1, ... |
63-170 | 5.58e-05 | |||||
Glycosyl hydrolase family 43 protein such as Geobacillus stearothermophilus endo-alpha-1,5-L-arabinanase AbnA; This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. It includes Geobacillus stearothermophilus T-6 NCIMB 40222 AbnA, Bacillus subtilis subsp. subtilis str. 168 (Abn2;YxiA;J3A;BSU39330) (Arb43B), and Thermotoga petrophila RKU-1 (AbnA;TpABN;Tpet_0637). These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. Many of these enzymes are different from other arabinases; they are organized into two different domains with a divalent metal cluster close to the catalytic residues to guarantee the correct protonation state of the catalytic residues and consequently the enzyme activity. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350153 [Multi-domain] Cd Length: 332 Bit Score: 45.32 E-value: 5.58e-05
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| beta-trefoil_Ricin_LNBase | cd23386 | ricin B-type lectin domain, beta-trefoil fold, found in Bifidobacterium bifidum ... |
336-423 | 5.71e-05 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Bifidobacterium bifidum lacto-N-biosidase (LNBase) and similar proteins; LNBase (EC2.3.1.140) belongs to the glycoside hydrolase 20 (GH20) family. It is a membrane-anchored extracellular enzyme that liberates lacto-N-biose I (LNB) from the non-reducing end of oligosaccharides and plays a key role in the metabolic pathway of these compounds. B. bifidum LNBase contains a signal peptide, a glycoside hydrolase family 20 (GH20) domain, a carbohydrate-binding module family 32 (CBM32) domain, a bacterial Ig-like domain, and a membrane anchor. The C-terminal region of the GH20 domain of LNBase has a unique ricin B-type lectin domain with a beta-trefoil-like fold. The typical beta-trefoil fold is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. In contrast, the second and third strands (alpha subdomain) and the last beta strand (part of gamma subdomain) are missing in the beta-trefoil fold of LNBase. Pssm-ID: 467873 Cd Length: 109 Bit Score: 42.31 E-value: 5.71e-05
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| beta-trefoil_Ricin_SCDase_rpt2 | cd23500 | second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ... |
331-433 | 7.03e-05 | |||||
second ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. The model corresponds to the second lectin domain. Pssm-ID: 467378 [Multi-domain] Cd Length: 128 Bit Score: 42.45 E-value: 7.03e-05
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| beta-trefoil_Ricin_Cry35Ab1 | cd23448 | ricin B-type lectin domain, beta-trefoil fold, found in Bacillus thuringiensis Cry35Ab1 and ... |
348-483 | 7.03e-05 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Bacillus thuringiensis Cry35Ab1 and similar proteins; Cry35Ab1 is an insecticidal protein belonging to the toxin_10 family (Pfam05431) that includes other insecticidal proteins such as the binary toxin BinA/BinB. It acts together with Cry34Ab1 to control corn rootworms. Cry35Ab1 contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467326 Cd Length: 133 Bit Score: 42.71 E-value: 7.03e-05
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| lectin_2 | NF035930 | lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ... |
399-482 | 1.06e-04 | |||||
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. Pssm-ID: 468267 [Multi-domain] Cd Length: 238 Bit Score: 43.62 E-value: 1.06e-04
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| beta-trefoil_Ricin_EW29-like | cd23449 | ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ... |
349-386 | 1.47e-04 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin. Pssm-ID: 467327 [Multi-domain] Cd Length: 128 Bit Score: 41.51 E-value: 1.47e-04
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| GH43_Bt3655-like | cd08983 | Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ... |
65-290 | 2.64e-04 | |||||
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655; This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350097 Cd Length: 262 Bit Score: 42.61 E-value: 2.64e-04
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| beta-trefoil_Ricin_MTX-like_rpt1-3 | cd23497 | first, second and third ricin B-type lectin domains, beta-trefoil fold, found in ... |
344-388 | 3.88e-04 | |||||
first, second and third ricin B-type lectin domains, beta-trefoil fold, found in Lysinibacillus sphaericus mosquitocidal toxin (MTX) and similar proteins; This subfamily includes Lysinibacillus sphaericus MTX and Pieris brassicae pierisin. MTX acts as an ADP-ribosyl transferase. Pierisin, also called NAD--DNA ADP-ribosyltransferase, pierisin-2, or pierisin-B, catalyzes the ADP ribosylation of double-stranded DNA by targeting the N2 amino group of dG residues. It induces apoptosis in a range of human cell lines. Members of this family contain four ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The model corresponds to the first, second and third ricin B-type lectin domains. Each subdomain bears a potential sugar binding site. Pssm-ID: 467375 [Multi-domain] Cd Length: 139 Bit Score: 40.42 E-value: 3.88e-04
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| beta-trefoil_Ricin_vlAKAP | cd23463 | ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ... |
343-435 | 3.99e-04 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467341 Cd Length: 136 Bit Score: 40.50 E-value: 3.99e-04
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| beta-trefoil_Ricin_EndoBetaGal-like | cd23432 | ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1, ... |
347-484 | 5.16e-04 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium perfringens GlcNac-alpha-1,4-Gal-releasing endo-beta-galactosidase (Endo-beta-Gal(GnGa)) and similar proteins; Endo-beta-Gal(GnGa) can release disaccharide GlcNAc-alpha-1,4Gal from O-glycans expressed in the gastric gland mucous cell-type mucin. It contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467310 Cd Length: 127 Bit Score: 40.02 E-value: 5.16e-04
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| beta-trefoil_Ricin_XLN-like | cd23418 | ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ... |
348-386 | 9.25e-04 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket. Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 39.26 E-value: 9.25e-04
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| beta-trefoil_Ricin_CRYBG | cd23430 | ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin ... |
359-435 | 1.08e-03 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin domain-containing protein (CRYBG) family; The CRYBG family includes three members: CRYBG1, CRYBG2, and CRYBG3/vlAKAP. CRYBG1, also called absent in melanoma 1 protein (AIM1), may function as a suppressor of malignant melanoma. It may exert its effects through interactions with the cytoskeleton. CRYBG2 is also called absent in melanoma 1-like protein (AIM1L). CRYBG3/vlAKAP, also called very large A-kinase anchor protein, is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). CRYBG proteins belong to the beta/gamma-crystallin family. They all contain a ricin B-type lectin domain with a beta-trefoil fold at the C-terminus. The beta-trefoil fold is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467308 [Multi-domain] Cd Length: 133 Bit Score: 39.11 E-value: 1.08e-03
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| RICIN | smart00458 | Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. |
350-436 | 1.09e-03 | |||||
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication. Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 39.03 E-value: 1.09e-03
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| GH43_Xsa43E-like | cd18618 | Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase ... |
92-263 | 1.73e-03 | |||||
Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350130 [Multi-domain] Cd Length: 275 Bit Score: 40.28 E-value: 1.73e-03
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| beta-trefoil_Ricin_AtEULS3-like | cd23431 | ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like ... |
330-437 | 1.74e-03 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Arabidopsis thaliana Ricin B-like lectin EULS3 (AtEULS3) and similar proteins; AtEULS3, also called euonymus lectin S3, is a Ricin B-like lectin that binds carbohydrates in vitro. It interacts through its lectin domain with glycan structures containing one or more Lewis X, Lewis Y or lactosamine motifs. It has been implicated in abiotic stress responses, abscisic acid-induced stomatal closure, as well as disease resistance against Pseudomonas syringae through its involvement in stomatal movement. All subfamily members contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. Pssm-ID: 467309 Cd Length: 152 Bit Score: 38.88 E-value: 1.74e-03
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| beta-trefoil_Ricin_Cry35Ab1 | cd23448 | ricin B-type lectin domain, beta-trefoil fold, found in Bacillus thuringiensis Cry35Ab1 and ... |
399-484 | 2.10e-03 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Bacillus thuringiensis Cry35Ab1 and similar proteins; Cry35Ab1 is an insecticidal protein belonging to the toxin_10 family (Pfam05431) that includes other insecticidal proteins such as the binary toxin BinA/BinB. It acts together with Cry34Ab1 to control corn rootworms. Cry35Ab1 contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Pssm-ID: 467326 Cd Length: 133 Bit Score: 38.47 E-value: 2.10e-03
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| beta-trefoil_Ricin_XLN-like | cd23418 | ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ... |
444-482 | 2.79e-03 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket. Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 38.10 E-value: 2.79e-03
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| GH43-like | cd08986 | Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43) ... |
90-263 | 3.01e-03 | |||||
Glycosyl hydrolase family 43 protein; uncharacterized; This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350100 [Multi-domain] Cd Length: 257 Bit Score: 39.52 E-value: 3.01e-03
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| beta-trefoil_Ricin_MPL_CNL | cd23422 | ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like ... |
444-484 | 3.47e-03 | |||||
ricin B-type lectin domain, beta-trefoil fold, found in Macrolepiota procera ricin B-like lectin (MPL), Clitocybe nebularis lectin (CNL), and similar proteins; MPL and CNL are a homodimeric ricin B-like lectins with a beta-trefoil fold that is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Their alpha subunit may harbor a sugar-binding pocket. MPL has the highest specificity for terminal N-acetyllactosamine and other beta-galactosides. CNL induces maturation and activation of dendritic cells via the toll-like receptor 4 pathway. It is specific for terminal, non-reducing N-acetylgalactosamine (Gal-NAc)-containing carbohydrates including N,N'-diacetyllactosediamine/LDN (GalNAcbeta1-4GlcNAc, LacdiNAc). It is also specific for carbohydrates containing N-acetylglucosamine (-GlcNAc) or N-acetyllactosamine (-Galbeta1-4GlcNAc) at the reducing end. Pssm-ID: 467300 [Multi-domain] Cd Length: 135 Bit Score: 37.68 E-value: 3.47e-03
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| GH43_Bt1873-like | cd08981 | Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873; This ... |
69-262 | 4.98e-03 | |||||
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873; This glycosyl hydrolase family 43 (GH43) subfamily includes Bacteroides thetaiotaomicron VPI-5482 endo-arabinase (Bt1873;BT_1873), as well as uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the GH43 enzymes in this family may display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Pssm-ID: 350095 [Multi-domain] Cd Length: 289 Bit Score: 39.04 E-value: 4.98e-03
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