Chain C, Alpha-mannosidase,ZZ-type zinc finger-containing protein P35G2.11c,Maltose/maltodextrin-binding periplasmic protein
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||||
| malE | PRK09474 | maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1218-1584 | 0e+00 | ||||||||||||
maltose/maltodextrin ABC transporter substrate-binding protein MalE; : Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 838.90 E-value: 0e+00
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| MngB | COG0383 | Alpha-mannosidase [Carbohydrate transport and metabolism]; |
282-1075 | 0e+00 | ||||||||||||
Alpha-mannosidase [Carbohydrate transport and metabolism]; : Pssm-ID: 440152 [Multi-domain] Cd Length: 798 Bit Score: 797.52 E-value: 0e+00
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| ZZ_NBR1_like | cd02340 | Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ... |
1172-1215 | 1.99e-19 | ||||||||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain. : Pssm-ID: 239080 Cd Length: 43 Bit Score: 82.69 E-value: 1.99e-19
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1094-1129 | 7.59e-12 | ||||||||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. : Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 61.30 E-value: 7.59e-12
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| Name | Accession | Description | Interval | E-value | |||||||||||||
| malE | PRK09474 | maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1218-1584 | 0e+00 | |||||||||||||
maltose/maltodextrin ABC transporter substrate-binding protein MalE; Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 838.90 E-value: 0e+00
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| MngB | COG0383 | Alpha-mannosidase [Carbohydrate transport and metabolism]; |
282-1075 | 0e+00 | |||||||||||||
Alpha-mannosidase [Carbohydrate transport and metabolism]; Pssm-ID: 440152 [Multi-domain] Cd Length: 798 Bit Score: 797.52 E-value: 0e+00
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| PBP2_MBP | cd13656 | The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
1223-1584 | 0e+00 | |||||||||||||
The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270374 [Multi-domain] Cd Length: 364 Bit Score: 732.86 E-value: 0e+00
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| GH38N_AMII_ScAms1_like | cd10812 | N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; ... |
282-538 | 1.22e-174 | |||||||||||||
N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38); The family is represented by Saccharomyces cerevisiae alpha-mannosidase (Ams1) and its eukaryotic homologs. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 forms an oligomer in the cytoplasm and retains its oligomeric form during the import process. It utilizes both the Cvt (nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Mutants in either pathway are defective in Ams1 import. Members in this family show high sequence similarity with rat ER/cytosolic alpha-mannosidase Man2C1. Pssm-ID: 212123 [Multi-domain] Cd Length: 258 Bit Score: 523.54 E-value: 1.22e-174
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| MalE | COG2182 | Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1216-1584 | 3.37e-148 | |||||||||||||
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 459.42 E-value: 3.37e-148
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| Glyco_hydro_38N | pfam01074 | Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of ... |
282-549 | 1.35e-108 | |||||||||||||
Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Pssm-ID: 426030 [Multi-domain] Cd Length: 271 Bit Score: 345.77 E-value: 1.35e-108
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| SBP_bac_1 | pfam01547 | Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
1235-1507 | 5.28e-40 | |||||||||||||
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF. Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 150.64 E-value: 5.28e-40
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| Alpha-mann_mid | smart00872 | Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ... |
556-634 | 3.39e-33 | |||||||||||||
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase. Pssm-ID: 214875 [Multi-domain] Cd Length: 79 Bit Score: 123.05 E-value: 3.39e-33
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| PRK09819 | PRK09819 | mannosylglycerate hydrolase; |
280-1016 | 2.40e-20 | |||||||||||||
mannosylglycerate hydrolase; Pssm-ID: 182093 [Multi-domain] Cd Length: 875 Bit Score: 98.12 E-value: 2.40e-20
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| ZZ_NBR1_like | cd02340 | Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ... |
1172-1215 | 1.99e-19 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain. Pssm-ID: 239080 Cd Length: 43 Bit Score: 82.69 E-value: 1.99e-19
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1169-1211 | 9.28e-17 | |||||||||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 75.17 E-value: 9.28e-17
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1094-1129 | 7.59e-12 | |||||||||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 61.30 E-value: 7.59e-12
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| ZZ | cd02249 | Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
1098-1135 | 2.45e-08 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins. Pssm-ID: 239069 [Multi-domain] Cd Length: 46 Bit Score: 51.28 E-value: 2.45e-08
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
1170-1208 | 2.82e-06 | |||||||||||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 45.55 E-value: 2.82e-06
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| Name | Accession | Description | Interval | E-value | |||||||||||||
| malE | PRK09474 | maltose/maltodextrin ABC transporter substrate-binding protein MalE; |
1218-1584 | 0e+00 | |||||||||||||
maltose/maltodextrin ABC transporter substrate-binding protein MalE; Pssm-ID: 236533 [Multi-domain] Cd Length: 396 Bit Score: 838.90 E-value: 0e+00
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| MngB | COG0383 | Alpha-mannosidase [Carbohydrate transport and metabolism]; |
282-1075 | 0e+00 | |||||||||||||
Alpha-mannosidase [Carbohydrate transport and metabolism]; Pssm-ID: 440152 [Multi-domain] Cd Length: 798 Bit Score: 797.52 E-value: 0e+00
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| PBP2_MBP | cd13656 | The periplasmic binding component of ABC tansport system specific for maltose; possess the ... |
1223-1584 | 0e+00 | |||||||||||||
The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270374 [Multi-domain] Cd Length: 364 Bit Score: 732.86 E-value: 0e+00
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| GH38N_AMII_ScAms1_like | cd10812 | N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; ... |
282-538 | 1.22e-174 | |||||||||||||
N-terminal catalytic domain of yeast vacuolar alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38); The family is represented by Saccharomyces cerevisiae alpha-mannosidase (Ams1) and its eukaryotic homologs. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 forms an oligomer in the cytoplasm and retains its oligomeric form during the import process. It utilizes both the Cvt (nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Mutants in either pathway are defective in Ams1 import. Members in this family show high sequence similarity with rat ER/cytosolic alpha-mannosidase Man2C1. Pssm-ID: 212123 [Multi-domain] Cd Length: 258 Bit Score: 523.54 E-value: 1.22e-174
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| MalE | COG2182 | Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; |
1216-1584 | 3.37e-148 | |||||||||||||
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism]; Pssm-ID: 441785 [Multi-domain] Cd Length: 410 Bit Score: 459.42 E-value: 3.37e-148
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| PBP2_ABC_oligosaccharides | cd13522 | The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
1224-1584 | 9.96e-145 | |||||||||||||
The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270240 [Multi-domain] Cd Length: 368 Bit Score: 448.40 E-value: 9.96e-145
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| PBP2_Maltose_binding_like | cd13586 | The periplasmic-binding component of ABC transport systems specific for maltose and related ... |
1224-1584 | 6.62e-136 | |||||||||||||
The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270304 [Multi-domain] Cd Length: 367 Bit Score: 424.79 E-value: 6.62e-136
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| GH38N_AMII_ER_cytosolic | cd10789 | N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; ... |
283-538 | 2.12e-117 | |||||||||||||
N-terminal catalytic domain of endoplasmic reticulum(ER)/cytosolic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38); The subfamily is represented by Saccharomyces cerevisiae vacuolar alpha-mannosidase Ams1, rat ER/cytosolic alpha-mannosidase Man2C1, and similar proteins. Members in this family share high sequence similarity. None of them have any classical signal sequence or membrane spanning domains, which are typical of sorting or targeting signals. Ams1 functions as a second resident vacuolar hydrolase in S. cerevisiae. It aids in recycling macromolecular components of the cell through hydrolysis of terminal, non-reducing alpha-d-mannose residues. Ams1 utilizes both the cytoplasm to vacuole targeting (Cvt, nutrient-rich conditions) and autophagic (starvation conditions) pathways for biosynthetic delivery to the vacuole. Man2C1is involved in oligosaccharide catabolism in both the ER and cytosol. It can catalyze the cobalt-dependent cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl-enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. Pssm-ID: 212101 [Multi-domain] Cd Length: 252 Bit Score: 369.53 E-value: 2.12e-117
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| GH38N_AMII_Man2C1 | cd10813 | N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar ... |
283-538 | 1.31e-110 | |||||||||||||
N-terminal catalytic domain of mammalian cytosolic alpha-mannosidase Man2C1 and similar proteins; glycoside hydrolase family 38 (GH38); The subfamily corresponds to cytosolic alpha-mannosidase Man2C1 (also known as ER-mannosidase II or neutral/cytosolic mannosidase), mainly found in various vertebrates, and similar proteins. Man2C1 plays an essential role in the catabolism of cytosolic free oligomannosides derived from dolichol intermediates and the degradation of newly synthesized glycoproteins in ER or cytosol. It can catalyze the cleavage of alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues. Man2C1 is a cobalt-dependent enzyme belonging to alpha-mannosidase class II. It has a neutral pH optimum and is strongly inhitibed by furanose analogs swainsonine (SW) and 1,4-dideoxy-1,4-imino-D-mannitol (DIM), moderately by deoxymannojirimycin (DMM), but not by kifunensine (KIF). DMM and KIF, both pyranose analogs, are normally known to inhibit class I alpha-mannosidase. Pssm-ID: 212124 [Multi-domain] Cd Length: 252 Bit Score: 350.54 E-value: 1.31e-110
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| Glyco_hydro_38N | pfam01074 | Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of ... |
282-549 | 1.35e-108 | |||||||||||||
Glycosyl hydrolases family 38 N-terminal domain; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Pssm-ID: 426030 [Multi-domain] Cd Length: 271 Bit Score: 345.77 E-value: 1.35e-108
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| PBP2_CMBP | cd13658 | The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ... |
1224-1582 | 1.22e-88 | |||||||||||||
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270376 [Multi-domain] Cd Length: 372 Bit Score: 293.62 E-value: 1.22e-88
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| Glyco_hydro_38C | pfam07748 | Glycosyl hydrolases family 38 C-terminal domain; Glycosyl hydrolases are key enzymes of ... |
722-937 | 3.30e-78 | |||||||||||||
Glycosyl hydrolases family 38 C-terminal domain; Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Pssm-ID: 400208 [Multi-domain] Cd Length: 204 Bit Score: 257.19 E-value: 3.30e-78
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| PBP2_Maltodextrin | cd13657 | The periplasmic binding component of ABC transport system specific for maltodextrin; This ... |
1224-1583 | 2.92e-74 | |||||||||||||
The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270375 [Multi-domain] Cd Length: 368 Bit Score: 252.30 E-value: 2.92e-74
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| PBP2_TMBP_like | cd13585 | The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ... |
1224-1583 | 4.54e-62 | |||||||||||||
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270303 [Multi-domain] Cd Length: 383 Bit Score: 217.66 E-value: 4.54e-62
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| PBP2_UgpB | cd14748 | The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ... |
1224-1584 | 1.26e-58 | |||||||||||||
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270451 [Multi-domain] Cd Length: 385 Bit Score: 207.53 E-value: 1.26e-58
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| UgpB | COG1653 | ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ... |
1221-1531 | 1.32e-58 | |||||||||||||
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism]; Pssm-ID: 441259 [Multi-domain] Cd Length: 363 Bit Score: 206.82 E-value: 1.32e-58
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| PBP2_XBP1_like | cd14749 | The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ... |
1224-1584 | 1.24e-43 | |||||||||||||
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270452 [Multi-domain] Cd Length: 388 Bit Score: 164.09 E-value: 1.24e-43
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| PBP2_MalE | cd14747 | Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ... |
1224-1584 | 5.14e-42 | |||||||||||||
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270450 [Multi-domain] Cd Length: 386 Bit Score: 159.40 E-value: 5.14e-42
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| PBP2_TMBP | cd14750 | The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ... |
1233-1583 | 2.19e-41 | |||||||||||||
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270453 [Multi-domain] Cd Length: 385 Bit Score: 157.46 E-value: 2.19e-41
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| Alpha-mann_mid | pfam09261 | Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three ... |
555-652 | 4.98e-40 | |||||||||||||
Alpha mannosidase middle domain; Members of this family adopt a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. They are predominantly found in the enzyme alpha-mannosidase. Pssm-ID: 462728 [Multi-domain] Cd Length: 98 Bit Score: 143.56 E-value: 4.98e-40
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| SBP_bac_1 | pfam01547 | Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
1235-1507 | 5.28e-40 | |||||||||||||
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF. Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 150.64 E-value: 5.28e-40
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| GH38N_AMII_like | cd10786 | N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside ... |
282-456 | 9.30e-40 | |||||||||||||
N-terminal catalytic domain of class II alpha-mannosidases and similar proteins; glycoside hydrolase family 38 (GH38); Alpha-mannosidases (EC 3.2.1.24) are extensively found in eukaryotes and play important roles in the processing of newly formed N-glycans and in degradation of mature glycoproteins. A deficiency of this enzyme causes the lysosomal storage disease alpha-mannosidosis. Many bacterial and archaeal species also possess putative alpha-mannosidases, but their activity and specificity is largely unknown. Based on different functional characteristics and sequence homology, alpha-mannosidases have been organized into two classes (class I, belonging to glycoside hydrolase family 47, and class II, belonging to glycoside hydrolase family 38). Members of this family corresponds to class II alpha-mannosidases (alphaMII), which contain intermediate Golgi alpha-mannosidases II, acidic lysosomal alpha-mannosidases, animal sperm and epididymal alpha -mannosidases, neutral ER/cytosolic alpha-mannosidases, and some putative prokaryotic alpha-mannosidases. AlphaMII possess a-1,3, a-1,6, and a-1,2 hydrolytic activity, and catalyzes the degradation of N-linked oligosaccharides. The N-terminal catalytic domain of alphaMII adopts a structure consisting of parallel 7-stranded beta/alpha barrel. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. Pssm-ID: 212098 [Multi-domain] Cd Length: 251 Bit Score: 148.32 E-value: 9.30e-40
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| SBP_bac_8 | pfam13416 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
1240-1533 | 1.62e-38 | |||||||||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 433189 [Multi-domain] Cd Length: 281 Bit Score: 146.01 E-value: 1.62e-38
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| PBP2_GacH | cd14751 | The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ... |
1245-1584 | 2.03e-33 | |||||||||||||
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270454 [Multi-domain] Cd Length: 376 Bit Score: 134.04 E-value: 2.03e-33
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| Alpha-mann_mid | smart00872 | Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase ... |
556-634 | 3.39e-33 | |||||||||||||
Alpha mannosidase, middle domain; Members of this entry belong to the glycosyl hydrolase family 38, This domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase. Pssm-ID: 214875 [Multi-domain] Cd Length: 79 Bit Score: 123.05 E-value: 3.39e-33
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| PBP2_oligosaccharide_1 | cd13655 | The periplasmic binding component of ABC tansport system specific for an unknown ... |
1238-1558 | 1.68e-27 | |||||||||||||
The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270373 [Multi-domain] Cd Length: 363 Bit Score: 116.29 E-value: 1.68e-27
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| PRK09819 | PRK09819 | mannosylglycerate hydrolase; |
280-1016 | 2.40e-20 | |||||||||||||
mannosylglycerate hydrolase; Pssm-ID: 182093 [Multi-domain] Cd Length: 875 Bit Score: 98.12 E-value: 2.40e-20
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| PotD | COG0687 | Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
1211-1562 | 4.89e-20 | |||||||||||||
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 93.44 E-value: 4.89e-20
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| GH38N_AMII_1 | cd10790 | N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside ... |
283-452 | 7.60e-20 | |||||||||||||
N-terminal catalytic domain of putative prokaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38); This mainly bacterial subfamily corresponds to a group of putative class II alpha-mannosidases, including various proteins assigned as alpha-mannosidases, Streptococcus pyogenes (SpGH38) encoded by ORF spy1604. Escherichia coli MngB encoded by the mngB/ybgG gene, and Thermotoga maritime TMM, and similar proteins. SpGH38 targets alpha-1,3 mannosidic linkages. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. MngB exhibits alpha-mannosidase activity that catalyzes the conversion of 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. TMM is a homodimeric enzyme that hydrolyzes p-nitrophenyl-alpha-D-mannopyranoside, alpha -1,2-mannobiose, alpha -1,3-mannobiose, alpha -1,4-mannobiose, and alpha -1,6-mannobiose. The GH38 family contains retaining glycosyl hydrolases that employ a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. Divalent metal ions, such as zinc or cobalt ions, are suggested to be required for the catalytic activities of typical class II alpha-mannosidases. However, TMM requires the cobalt or cadmium for its activity. The cadmium ion dependency is unique to TMM. Moreover, TMM is inhibited by swainsonine but not 1-deoxymannojirimycin, which is in agreement with the features of cytosolic alpha-mannosidase. Pssm-ID: 212102 [Multi-domain] Cd Length: 273 Bit Score: 91.37 E-value: 7.60e-20
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| ZZ_NBR1_like | cd02340 | Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ... |
1172-1215 | 1.99e-19 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain. Pssm-ID: 239080 Cd Length: 43 Bit Score: 82.69 E-value: 1.99e-19
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| GH38N_AMII_SpGH38_like | cd10814 | N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, ... |
283-452 | 2.89e-17 | |||||||||||||
N-terminal catalytic domain of SPGH38, a putative alpha-mannosidase of Streptococcus pyogenes, and its prokaryotic homologs; glycoside hydrolase family 38 (GH38); The subfamily is represented by SpGH38 of Streptococcus pyogenes, which has been assigned as a putative alpha-mannosidase, and is encoded by ORF spy1604. SpGH38 appears to exist as an elongated dimer and display alpha-1,3 mannosidase activity. It is active on disaccharides and some aryl glycosides. SpGH38 can also effectively deglycosylate human N-glycans in vitro. A divalent metal ion, such as a zinc ion, is required for its activity. SpGH38 is inhibited by swainsonine. The absence of any secretion signal peptide suggests that SpGH38 may be intracellular. Pssm-ID: 212125 [Multi-domain] Cd Length: 271 Bit Score: 83.85 E-value: 2.89e-17
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1169-1211 | 9.28e-17 | |||||||||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 75.17 E-value: 9.28e-17
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| Glyco_hydro38C2 | pfam17677 | Glycosyl hydrolases family 38 C-terminal beta sandwich domain; This domain is found at the ... |
996-1074 | 8.01e-16 | |||||||||||||
Glycosyl hydrolases family 38 C-terminal beta sandwich domain; This domain is found at the C-terminal end of various glycosyl hydrolases belonging to family 38. The domain has a beta sandwich fold. Pssm-ID: 465454 [Multi-domain] Cd Length: 71 Bit Score: 73.43 E-value: 8.01e-16
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| AfuA | COG1840 | ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
1243-1507 | 1.17e-15 | |||||||||||||
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 79.21 E-value: 1.17e-15
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| GH38N_AMII_GMII_SfManIII_like | cd10809 | N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 ... |
280-472 | 3.99e-13 | |||||||||||||
N-terminal catalytic domain of Golgi alpha-mannosidase II, Spodoptera frugiperda Sf9 alpha-mannosidase III, and similar proteins; glycoside hydrolase family 38 (GH38); This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. This subfamily also includes human alpha-mannosidase 2x (MX, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A2). MX is enzymatically and functionally very similar to GMII, and is thought to also function in the N-glycosylation pathway. Also found in this subfamily is class II alpha-mannosidase encoded by Spodoptera frugiperda Sf9 cell. This alpha-mannosidase is an integral membrane glycoprotein localized in the Golgi apparatus. It shows high sequence homology with mammalian Golgi alpha-mannosidase II(GMII). It can hydrolyze p-nitrophenyl alpha-D-mannopyranoside (pNP-alpha-Man), and it is inhibited by swainsonine. However, the Sf9 enzyme is stimulated by cobalt and can hydrolyze (Man)5(GlcNAc)2 to (Man)3(GlcNAc)2, but it cannot hydrolyze GlcNAc(Man)5(GlcNAc)2, which is distinct from that of GMII. Thus, this enzyme has been designated as Sf9 alpha-mannosidase III (SfManIII). It probably functions in an alternate N-glycan processing pathway in Sf9 cells. Pssm-ID: 212120 [Multi-domain] Cd Length: 340 Bit Score: 72.68 E-value: 3.99e-13
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| PBP2_AlgQ_like_1 | cd13580 | Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
1243-1515 | 4.86e-13 | |||||||||||||
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide. Pssm-ID: 270298 [Multi-domain] Cd Length: 471 Bit Score: 73.52 E-value: 4.86e-13
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| PBP2_PotD_PotF_like | cd13590 | The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
1240-1503 | 1.56e-12 | |||||||||||||
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270308 [Multi-domain] Cd Length: 315 Bit Score: 70.34 E-value: 1.56e-12
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| ZZ | cd02249 | Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
1173-1215 | 2.65e-12 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins. Pssm-ID: 239069 [Multi-domain] Cd Length: 46 Bit Score: 62.84 E-value: 2.65e-12
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| PBP2_polyamine_RpCGA009 | cd13589 | The periplasmic-binding component of an uncharacterized ABC transport system from ... |
1239-1518 | 3.86e-12 | |||||||||||||
The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270307 [Multi-domain] Cd Length: 268 Bit Score: 68.41 E-value: 3.86e-12
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| GH38N_AMII_EcMngB_like | cd10815 | N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial ... |
313-455 | 4.91e-12 | |||||||||||||
N-terminal catalytic domain of Escherichia coli alpha-mannosidase MngB and its bacterial homologs; glycoside hydrolase family 38 (GH38); The bacterial subfamily is represented by Escherichia coli alpha-mannosidase MngB, which is encoded by the mngB gene (previously called ybgG). MngB exhibits alpha-mannosidase activity that converts 2-O-(6-phospho-alpha-mannosyl)-D-glycerate to mannose-6-phosphate and glycerate in the pathway which enables use of mannosyl-D-glycerate as a sole carbon source. A divalent metal ion is required for its activity. Pssm-ID: 212126 [Multi-domain] Cd Length: 270 Bit Score: 68.33 E-value: 4.91e-12
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| ZnF_ZZ | smart00291 | Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ... |
1094-1129 | 7.59e-12 | |||||||||||||
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy. Pssm-ID: 197633 [Multi-domain] Cd Length: 44 Bit Score: 61.30 E-value: 7.59e-12
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| GH38N_AMII_euk | cd00451 | N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase ... |
282-428 | 1.89e-11 | |||||||||||||
N-terminal catalytic domain of eukaryotic class II alpha-mannosidases; glycoside hydrolase family 38 (GH38); The family corresponds to a group of eukaryotic class II alpha-mannosidases (AlphaMII), which contain Golgi alpha-mannosidases II (GMII), the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), the noval core-specific lysosomal alpha 1,6-mannosidases (Epman, MAN2B2), and similar proteins. GMII catalyzes the hydrolysis of the terminal both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2 (GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. LAM is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. Different from LAM, Epman can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. Members in this family are retaining glycosyl hydrolases of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex. Two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. Pssm-ID: 212095 [Multi-domain] Cd Length: 258 Bit Score: 66.09 E-value: 1.89e-11
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| ZZ_Mind_bomb | cd02339 | Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ... |
1172-1215 | 1.53e-10 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster. Pssm-ID: 239079 Cd Length: 45 Bit Score: 57.47 E-value: 1.53e-10
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| GH38N_Man2A1 | cd11666 | N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside ... |
283-460 | 1.67e-10 | |||||||||||||
N-terminal catalytic domain of Golgi alpha-mannosidase II and similar proteins; glycoside hydrolase family 38 (GH38); This subfamily is represented by Golgi alpha-mannosidase II (GMII, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A1), a monomeric, membrane-anchored class II alpha-mannosidase existing in the Golgi apparatus of eukaryotes. GMII plays a key role in the N-glycosylation pathway. It catalyzes the hydrolysis of the terminal of both alpha-1,3-linked and alpha-1,6-linked mannoses from the high-mannose oligosaccharide GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine), which is the committed step of complex N-glycan synthesis. GMII is activated by zinc or cobalt ions and is strongly inhibited by swainsonine. Inhibition of GMII provides a route to block cancer-induced changes in cell surface oligosaccharide structures. GMII has a pH optimum of 5.5-6.0, which is intermediate between those of acidic (lysosomal alpha-mannosidase) and neutral (ER/cytosolic alpha-mannosidase) enzymes. GMII is a retaining glycosyl hydrolase of family GH38 that employs a two-step mechanism involving the formation of a covalent glycosyl enzyme complex; two carboxylic acids positioned within the active site act in concert: one as a catalytic nucleophile and the other as a general acid/base catalyst. Pssm-ID: 212131 [Multi-domain] Cd Length: 344 Bit Score: 64.60 E-value: 1.67e-10
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| PBP2_Fe3_thiamine_like | cd13518 | Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
1224-1512 | 2.53e-10 | |||||||||||||
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270236 [Multi-domain] Cd Length: 260 Bit Score: 62.70 E-value: 2.53e-10
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| GH38N_Man2A2 | cd11667 | N-terminal catalytic domain of Golgi alpha-mannosidase IIx, and similar proteins; glycoside ... |
283-472 | 8.90e-10 | |||||||||||||
N-terminal catalytic domain of Golgi alpha-mannosidase IIx, and similar proteins; glycoside hydrolase family 38 (GH38); This subfamily is represented by human alpha-mannosidase 2x (MX, also known as mannosyl-oligosaccharide 1,3- 1,6-alpha mannosidase, EC 3.2.1.114, Man2A2). MX is enzymatically and functionally very similar to GMII (found in another subfamily), and as an isoenzyme of GMII. It is thought to also function in the N-glycosylation pathway. MX specifically hydrolyzes the same oligosaccharide substrate as does MII. It specifically removes two mannosyl residues from GlcNAc(Man)5(GlcNAc)2 to yield GlcNAc(Man)3(GlcNAc)2(GlcNAc, N-acetylglucosmine). Pssm-ID: 212132 [Multi-domain] Cd Length: 344 Bit Score: 62.31 E-value: 8.90e-10
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| PBP2_AlgQ_like | cd13521 | Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
1241-1507 | 7.64e-09 | |||||||||||||
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide. Pssm-ID: 270239 [Multi-domain] Cd Length: 483 Bit Score: 60.16 E-value: 7.64e-09
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| ZZ_HERC2 | cd02344 | Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ... |
1174-1215 | 1.52e-08 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential E3 ubiquitin protein ligase and/or guanine nucleotide exchange factor. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239084 Cd Length: 45 Bit Score: 52.20 E-value: 1.52e-08
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| ZZ | cd02249 | Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ... |
1098-1135 | 2.45e-08 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins. Pssm-ID: 239069 [Multi-domain] Cd Length: 46 Bit Score: 51.28 E-value: 2.45e-08
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| PBP2_polyamine_2 | cd13587 | The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
1239-1343 | 3.66e-08 | |||||||||||||
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This family represents the periplasmic binding domain that functions as the primary polyamine receptor of an uncharacterized ABC-type transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270305 [Multi-domain] Cd Length: 292 Bit Score: 56.67 E-value: 3.66e-08
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| PBP2_polyamine_1 | cd13588 | The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ... |
1233-1360 | 1.04e-07 | |||||||||||||
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270306 [Multi-domain] Cd Length: 279 Bit Score: 55.38 E-value: 1.04e-07
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| GH38N_AMII_LAM_like | cd10810 | N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside ... |
282-420 | 1.25e-07 | |||||||||||||
N-terminal catalytic domain of lysosomal alpha-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38); The subfamily is represented by lysosomal alpha-mannosidase (LAM, Man2B1, EC 3.2.1.114), which is a broad specificity exoglycosidase hydrolyzing all known alpha 1,2-, alpha 1,3-, and alpha 1,6-mannosidic linkages from numerous high mannose type oligosaccharides. LAM is expressed in all tissues and in many species. In mammals, the absence of LAM can cause the autosomal recessive disease alpha-mannosidosis. LAM has an acidic pH optimum at 4.0-4.5. It is stimulated by zinc ion and is inhibited by cobalt ion and plant alkaloids, such as swainsonine (SW). LAM catalyzes hydrolysis by a double displacement mechanism in which a glycosyl-enzyme intermediate is formed and hydrolyzed via oxacarbenium ion-like transition states. A carboxylic acid in the active site acts as the catalytic nucleophile in the formation of the covalent intermediate while a second carboxylic acid acts as a general acid catalyst. The same residue is thought to assist in the hydrolysis (deglycosylation) step, this time acting as a general base. Pssm-ID: 212121 [Multi-domain] Cd Length: 278 Bit Score: 54.91 E-value: 1.25e-07
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| ZZ | pfam00569 | Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ... |
1170-1208 | 2.82e-06 | |||||||||||||
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure. Pssm-ID: 395451 Cd Length: 45 Bit Score: 45.55 E-value: 2.82e-06
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| GH38N_AMII_Epman_like | cd10811 | N-terminal catalytic domain of mammalian core-specific lysosomal alpha 1,6-mannosidase and ... |
282-430 | 3.67e-06 | |||||||||||||
N-terminal catalytic domain of mammalian core-specific lysosomal alpha 1,6-mannosidase and similar proteins; glycoside hydrolase family 38 (GH38); The subfamily is represented by a novel human core-specific lysosomal alpha 1,6-mannosidase (Epman, Man2B2) and similar proteins. Although it was previously named as epididymal alpha-mannosidase, Epman has a broadly distributed transcript expression profile. Different from the major broad specificity lysosomal alpha-mannosidases (LAM, MAN2B1), Epman is not associated with genetic alpha-mannosidosis that is caused by the absence of LAM. Furthermore, Epman has unique substrate specificity. It can efficiently cleave only the alpha 1,6-linked mannose residue from (Man)3GlcNAc, but not (Man)3(GlcNAc)2 or other larger high mannose oligosaccharides, in the core of N-linked glycans. In contrast, the major LAM can cleave all of the alpha-linked mannose residues from high mannose oligosaccharides except the core alpha 1,6-linked mannose residue. Moreover, it is suggested that the catalytic activity of Epman is dependent on prior action by di-N-acetyl-chitobiase (chitobiase), which indicates there is a functional cooperation between these two enzymes for the full and efficient catabolism of mammalian lysosomal N-glycan core structures. Epman has an acidic pH optimum. It is strongly stimulated by cobalt or zinc ions and strongly inhibited by furanose analogues swainsonine (SW) and 1,4-dideoxy-1,4-imino-d-mannitol (DIM). Pssm-ID: 212122 [Multi-domain] Cd Length: 326 Bit Score: 51.04 E-value: 3.67e-06
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| GH57N_TLGT_like | cd10793 | N-terminal catalytic domain of 4-alpha-glucanotransferase; glycoside hydrolase family 57 (GH57) ... |
283-401 | 3.91e-06 | |||||||||||||
N-terminal catalytic domain of 4-alpha-glucanotransferase; glycoside hydrolase family 57 (GH57); 4-alpha-glucanotransferase (TLGT, EC 2.4.1.25) plays a key role in the maltose metabolism. It catalyzes the disproportionation of amylose and the formation of large cyclic alpha-1,4-glucan (cycloamylose) from linear amylose. TLGT functions as a homodimer. Each monomer is composed of two domains, an N-terminal catalytic domain with a (beta/alpha)7 barrel fold and a C-terminal domain with a twisted beta-sandwich fold. Some family members have been designated as alpha-amylases, such as the heat-stable eubacterial amylase from Dictyoglomus thermophilum (DtAmyA) and the extremely thermostable archaeal amylase from Pyrococcus furiosus(PfAmyA). However, both of these proteins are 4-alpha-glucanotransferases. DtAmyA was shown to have transglycosylating activity and PfAmyA exhibits 4-alpha-glucanotransferase activity. Pssm-ID: 212105 [Multi-domain] Cd Length: 279 Bit Score: 50.27 E-value: 3.91e-06
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| ZZ_NBR1_like | cd02340 | Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ... |
1098-1135 | 4.48e-06 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain. Pssm-ID: 239080 Cd Length: 43 Bit Score: 44.94 E-value: 4.48e-06
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| ZZ_ZZZ3 | cd02341 | Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related ... |
1174-1215 | 4.52e-06 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in ZZZ3 (ZZ finger containing 3) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239081 Cd Length: 48 Bit Score: 45.12 E-value: 4.52e-06
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| ZZ_dystrophin | cd02334 | Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ... |
1172-1210 | 7.25e-06 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan. Pssm-ID: 239074 Cd Length: 49 Bit Score: 44.65 E-value: 7.25e-06
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| PLN02701 | PLN02701 | alpha-mannosidase |
275-460 | 9.24e-06 | |||||||||||||
alpha-mannosidase Pssm-ID: 178304 [Multi-domain] Cd Length: 1050 Bit Score: 50.56 E-value: 9.24e-06
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| PBP2_TbpA | cd13545 | Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ... |
1240-1511 | 1.18e-05 | |||||||||||||
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270263 [Multi-domain] Cd Length: 269 Bit Score: 48.83 E-value: 1.18e-05
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| PBP2_AEPn_like | cd13548 | Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member ... |
1245-1506 | 2.36e-05 | |||||||||||||
Substrate binding domain of a putative 2-amnioethylphosphonate-bindinig transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270266 [Multi-domain] Cd Length: 310 Bit Score: 48.33 E-value: 2.36e-05
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| SBP_bac_6 | pfam13343 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
1275-1513 | 3.14e-05 | |||||||||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 47.35 E-value: 3.14e-05
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| PBP2_AlgQ_like_4 | cd13583 | Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ... |
1243-1509 | 3.65e-05 | |||||||||||||
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide. Pssm-ID: 270301 [Multi-domain] Cd Length: 478 Bit Score: 48.12 E-value: 3.65e-05
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| PBP2_polyamines | cd13523 | The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ... |
1244-1503 | 4.18e-05 | |||||||||||||
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270241 [Multi-domain] Cd Length: 268 Bit Score: 47.05 E-value: 4.18e-05
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| ZZ_PCMF_like | cd02338 | Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ... |
1174-1210 | 5.63e-05 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination. Pssm-ID: 239078 Cd Length: 49 Bit Score: 41.95 E-value: 5.63e-05
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| PBP2_PotD_PotF_like_3 | cd13664 | TThe periplasmic substrate-binding component of an uncharacterized active transport system ... |
1240-1300 | 6.44e-05 | |||||||||||||
TThe periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270382 [Multi-domain] Cd Length: 315 Bit Score: 46.97 E-value: 6.44e-05
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| ZZ_ADA2 | cd02335 | Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ... |
1174-1212 | 9.74e-05 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239075 [Multi-domain] Cd Length: 49 Bit Score: 41.51 E-value: 9.74e-05
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| GH57N_PfGalA_like | cd10794 | N-terminal catalytic domain of alpha-galactosidase; glycoside hydrolase family 57 (GH57); ... |
341-487 | 1.42e-04 | |||||||||||||
N-terminal catalytic domain of alpha-galactosidase; glycoside hydrolase family 57 (GH57); Alpha-galactosidases (GalA, EC 3.2.1.22) catalyze the hydrolysis of alpha-1,6-linked galactose residues from oligosaccharides and polymeric galactomannans. Based on sequence similarity, the majority of eukaryotic and bacterial GalAs have been classified into glycoside hydrolase family GH27, GH36, and GH4, respectively. This subfamily is represented by a novel type of GalA from Pyrococcus furiosus (PfGalA), which belongs to the GH57 family. PfGalA is an extremely thermo-active and thermostable GalA that functions as a bacterial-like GalA, however, without the capacity to hydrolyze polysaccharides. It specifically catalyzes the hydrolysis of para-nitrophenyl-alpha-galactopyranoside, and to some extent that of melibiose and raffinose. PfGalA has a pH optimum between 5.0-5.5. Pssm-ID: 212106 Cd Length: 305 Bit Score: 45.82 E-value: 1.42e-04
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| ZZ_CBP | cd02337 | Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ... |
1174-1206 | 2.21e-04 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear. Pssm-ID: 239077 Cd Length: 41 Bit Score: 40.24 E-value: 2.21e-04
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| PRK15046 | PRK15046 | 2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional |
1243-1514 | 2.66e-04 | |||||||||||||
2-aminoethylphosphonate ABC transporter substrate-binding protein; Provisional Pssm-ID: 237887 [Multi-domain] Cd Length: 349 Bit Score: 45.06 E-value: 2.66e-04
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| PBP2_Fbp_like_5 | cd13551 | Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
1289-1499 | 4.52e-04 | |||||||||||||
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270269 [Multi-domain] Cd Length: 267 Bit Score: 43.93 E-value: 4.52e-04
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| PBP2_TpPotD_like | cd13662 | The periplasmic substrate-binding component of an ABC-type polyamine transport system from ... |
1243-1371 | 5.52e-04 | |||||||||||||
The periplasmic substrate-binding component of an ABC-type polyamine transport system from Treponema pallidum and related proteins; contains the type 2 periplasmic binding fold; This group includes the polyamine-binding component of an ABC-type polyamine transport system from Treponema pallidum and closely related proteins, which is homologous to the spermidine-preferring periplasmic substrate-binding protein component (PotD)of ABC transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270380 Cd Length: 312 Bit Score: 44.05 E-value: 5.52e-04
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| ZZ_CBP | cd02337 | Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ... |
1100-1134 | 1.04e-03 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear. Pssm-ID: 239077 Cd Length: 41 Bit Score: 38.31 E-value: 1.04e-03
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| PBP2_Fbp_like_1 | cd13544 | Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
1244-1553 | 1.33e-03 | |||||||||||||
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270262 [Multi-domain] Cd Length: 292 Bit Score: 42.59 E-value: 1.33e-03
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| ZZ_dah | cd02345 | Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ... |
1174-1210 | 1.61e-03 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dah (discontinuous actin hexagon) is a membrane associated protein essential for cortical furrow formation in Drosophila. Pssm-ID: 239085 Cd Length: 49 Bit Score: 37.95 E-value: 1.61e-03
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| TbpA | COG4143 | ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and ... |
1239-1358 | 1.62e-03 | |||||||||||||
ABC-type thiamine transport system, periplasmic component TbpA [Coenzyme transport and metabolism]; Pssm-ID: 443315 [Multi-domain] Cd Length: 343 Bit Score: 42.53 E-value: 1.62e-03
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| GH57N_like | cd01022 | N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57; Glycoside ... |
341-425 | 5.49e-03 | |||||||||||||
N-terminal catalytic domain of heat stable retaining glycoside hydrolase family 57; Glycoside hydrolase family 57(GH57) is a chiefly prokaryotic family with the majority of thermostable enzymes coming from extremophiles (many of these are archaeal hyperthermophiles), which exhibit the enzyme specificities of alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), amylopullulanase (EC 3.2.1.1/41), and alpha-galactosidase (EC 3.2.1.22). This family also includes many hypothetical proteins with uncharacterized activity and specificity. GH57s cleave alpha-glycosidic bonds by employing a retaining mechanism, which involves a glycosyl-enzyme intermediate, allowing transglycosylation. Pssm-ID: 212096 [Multi-domain] Cd Length: 313 Bit Score: 40.88 E-value: 5.49e-03
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| Glyco_hydro_57 | pfam03065 | Glycosyl hydrolase family 57; This family includes alpha-amylase (EC:3.2.1.1), ... |
333-424 | 5.98e-03 | |||||||||||||
Glycosyl hydrolase family 57; This family includes alpha-amylase (EC:3.2.1.1), 4--glucanotransferase (EC:2.4.1.-) and amylopullulanase enzymes. Pssm-ID: 397267 [Multi-domain] Cd Length: 293 Bit Score: 40.43 E-value: 5.98e-03
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| ZZ_UBA_plant | cd02342 | Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ... |
1174-1202 | 7.26e-03 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ motif coordinates a zinc ion and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239082 Cd Length: 43 Bit Score: 36.02 E-value: 7.26e-03
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| ZZ_EF | cd02343 | Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif ... |
1174-1215 | 7.55e-03 | |||||||||||||
Zinc finger, ZZ type. Zinc finger present in proteins with an EF_hand motif. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Pssm-ID: 239083 Cd Length: 48 Bit Score: 36.14 E-value: 7.55e-03
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