expansin A14 [Arabidopsis thaliana]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PLN00050 super family | cl31535 | expansin A; Provisional |
1-251 | 8.06e-139 | |||||
expansin A; Provisional The actual alignment was detected with superfamily member PLN00050: Pssm-ID: 165628 [Multi-domain] Cd Length: 247 Bit Score: 390.16 E-value: 8.06e-139
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| Name | Accession | Description | Interval | E-value | |||||
| PLN00050 | PLN00050 | expansin A; Provisional |
1-251 | 8.06e-139 | |||||
expansin A; Provisional Pssm-ID: 165628 [Multi-domain] Cd Length: 247 Bit Score: 390.16 E-value: 8.06e-139
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| DPBB_EXPA_N | cd22274 | N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ... |
28-154 | 1.65e-91 | |||||
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins (EXPA, expansin-A) have cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. They also affect environmental stress responses. Arabidopsis thaliana EXPA1 is a cell wall modifying enzyme that controls the divisions marking lateral root initiation. Nicotiana tabacum EXPA4 positively regulates abiotic stress tolerance, and negatively regulates pathogen resistance. Wheat TaEXPA2 is involved in conferring cadmium tolerance. Alpha-expansins belong to the expansin family of proteins that contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This model represents the N-terminal domain of alpha-expansins, which adopts a double-psi beta-barrel (DPBB) fold. Pssm-ID: 439254 Cd Length: 129 Bit Score: 265.62 E-value: 1.65e-91
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| DPBB_1 | smart00837 | Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ... |
64-149 | 3.46e-54 | |||||
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Pssm-ID: 129070 [Multi-domain] Cd Length: 87 Bit Score: 169.55 E-value: 3.46e-54
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| Expansin_C | pfam01357 | Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ... |
161-233 | 9.09e-31 | |||||
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell wall proteins involved in the non-enzymatic rearrangement of cell walls during cell growth. It contains the allergens lol PI, PII and PIII from Lolium perenne. Pssm-ID: 460173 [Multi-domain] Cd Length: 75 Bit Score: 109.20 E-value: 9.09e-31
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| Name | Accession | Description | Interval | E-value | |||||
| PLN00050 | PLN00050 | expansin A; Provisional |
1-251 | 8.06e-139 | |||||
expansin A; Provisional Pssm-ID: 165628 [Multi-domain] Cd Length: 247 Bit Score: 390.16 E-value: 8.06e-139
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| PLN00193 | PLN00193 | expansin-A; Provisional |
5-250 | 1.48e-116 | |||||
expansin-A; Provisional Pssm-ID: 215097 [Multi-domain] Cd Length: 256 Bit Score: 333.80 E-value: 1.48e-116
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| DPBB_EXPA_N | cd22274 | N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ... |
28-154 | 1.65e-91 | |||||
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins (EXPA, expansin-A) have cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. They also affect environmental stress responses. Arabidopsis thaliana EXPA1 is a cell wall modifying enzyme that controls the divisions marking lateral root initiation. Nicotiana tabacum EXPA4 positively regulates abiotic stress tolerance, and negatively regulates pathogen resistance. Wheat TaEXPA2 is involved in conferring cadmium tolerance. Alpha-expansins belong to the expansin family of proteins that contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This model represents the N-terminal domain of alpha-expansins, which adopts a double-psi beta-barrel (DPBB) fold. Pssm-ID: 439254 Cd Length: 129 Bit Score: 265.62 E-value: 1.65e-91
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| DPBB_1 | smart00837 | Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ... |
64-149 | 3.46e-54 | |||||
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Pssm-ID: 129070 [Multi-domain] Cd Length: 87 Bit Score: 169.55 E-value: 3.46e-54
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| DPBB_EXP_N-like | cd22271 | N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ... |
30-154 | 3.03e-37 | |||||
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The plant expansin family consists of four subfamilies, alpha-expansin (EXPA), beta-expansin (EXPB), expansin-like A (EXLA), and expansin-like B (EXLB). EXPA and EXPB display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. EXPA proteins function more efficiently on dicotyledonous cell walls, whereas EXPB proteins exhibit specificity for the cell walls of monocotyledons. Expansins also affect environmental stress responses. Expansin family proteins contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This family also includes GH45 endoglucanases from mollusks. This model represents the N-terminal domain of expansins and similar proteins, which adopts a double-psi beta-barrel (DPBB) fold. Pssm-ID: 439251 [Multi-domain] Cd Length: 109 Bit Score: 127.11 E-value: 3.03e-37
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| Expansin_C | pfam01357 | Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ... |
161-233 | 9.09e-31 | |||||
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell wall proteins involved in the non-enzymatic rearrangement of cell walls during cell growth. It contains the allergens lol PI, PII and PIII from Lolium perenne. Pssm-ID: 460173 [Multi-domain] Cd Length: 75 Bit Score: 109.20 E-value: 9.09e-31
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| DPBB_EXPB_N | cd22275 | N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins ... |
29-154 | 1.68e-30 | |||||
N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins (EXPB, expansin-B) have cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. They also affect environmental stress responses. The EXPB subfamily is known in the allergen literature as group-1 grass pollen allergens. EXPB of Bermuda, Johnson, and Para grass pollens, is a major cross-reactive allergen for allergic rhinitis patients in subtropical climate. EXPB1 induces extension and stress relaxation of grass cell walls. Wheat TaEXPB7-B is a beta-expansin gene involved in low-temperature stress and abscisic acid responses. Beta-expansins belong to the expansin family of proteins that contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This model represents the N-terminal domain of beta-expansins, which adopts a double-psi beta-barrel (DPBB) fold. Pssm-ID: 439255 Cd Length: 121 Bit Score: 110.02 E-value: 1.68e-30
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| PLN03023 | PLN03023 | Expansin-like B1; Provisional |
25-246 | 1.68e-25 | |||||
Expansin-like B1; Provisional Pssm-ID: 215542 [Multi-domain] Cd Length: 247 Bit Score: 100.66 E-value: 1.68e-25
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| DPBB_1 | pfam03330 | Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ... |
65-149 | 2.13e-21 | |||||
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity. Pssm-ID: 427248 [Multi-domain] Cd Length: 82 Bit Score: 84.95 E-value: 2.13e-21
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| DPBB_EXLX1-like | cd22272 | N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus ... |
33-150 | 1.02e-15 | |||||
N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus subtilis EXLX1; This subfamily is composed of bacterial expansins including Bacillus subtilis EXLX1, also called expansin-YoaJ. Similar to plant expansins, EXLX1 contains an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. It strongly binds to crystalline cellulose via D2, and weakly binds soluble cellooligosaccharides. Bacterial expansins, which are present in some plant pathogens, have the ability to loosen plant cell walls, but with weaker activity compared to plant expansins. They may have a role in plant-bacterial interactions. This model represents the N-terminal domain of EXLX1 and similar bacterial expansins, which adopts a double-psi beta-barrel (DPBB) fold. Pssm-ID: 439252 [Multi-domain] Cd Length: 95 Bit Score: 70.29 E-value: 1.02e-15
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| DPBB_EXLA_N | cd22276 | N-terminal double-psi beta-barrel fold domain of the expansin-like A subfamily; Expansin-like ... |
31-154 | 3.67e-15 | |||||
N-terminal double-psi beta-barrel fold domain of the expansin-like A subfamily; Expansin-like A (EXLA) belongs to the plant expansin family that also includes alpha-expansin (EXPA), beta-expansin (EXPB), and expansin-like B (EXLB). Unlike EXPA and EXPB, EXLA proteins have not been shown to display cell wall loosening activity. EXLA2 is one of the three EXLA members in Arabidopsis. It lacks expansin activity, but contains a presumed cellulose-interacting domain. EXLA2 may function as a positive regulator of cell elongation in the dark-grown hypocotyl of Arabidopsis, possibly by interference with cellulose metabolism, deposition, or its organization. EXLA belongs to the expansin family of proteins that contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This model represents the N-terminal domain of EXLA proteins, which adopts a double-psi beta-barrel (DPBB) fold. Pssm-ID: 439256 Cd Length: 127 Bit Score: 69.75 E-value: 3.67e-15
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| DPBB_EXLB_N | cd22277 | N-terminal double-psi beta-barrel fold domain of the expansin-like B subfamily; Expansin-like ... |
30-154 | 5.55e-15 | |||||
N-terminal double-psi beta-barrel fold domain of the expansin-like B subfamily; Expansin-like B (EXLB) belongs to the plant expansin family that also includes alpha-expansin (EXPA), beta-expansin (EXPB), and expansin-like A (EXLA). Unlike EXPA and EXPB, EXLA proteins have not been shown to display cell wall loosening activity. Solanum tuberosum StEXLB6 showed differential expression under the treatments of abscisic acid (ABA), indoleacetic acid (IAA), and gibberellin acid 3 (GA3), as well as under drought and heat stresses, indicating that it is likely involved in potato stress resistance. Soybean GmEXLB1 improves phosphorus acquisition by regulating root elongation and architecture in Arabidopsis. EXLB belongs to the expansin family of proteins that contain an N-terminal domain (D1) homologous to the catalytic domain of glycoside hydrolase family 45 (GH45) proteins but with no hydrolytic activity, and a C-terminal domain (D2) homologous to group-2 grass pollen allergens. This model represents the N-terminal domain of EXLB proteins, which adopts a double-psi beta-barrel (DPBB) fold. Pssm-ID: 439257 Cd Length: 117 Bit Score: 69.00 E-value: 5.55e-15
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| DPBB_EG45-like | cd22269 | double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains ... |
49-150 | 3.61e-10 | |||||
double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains plant EG45-like domain-containing proteins which show sequence similarity to expansins, and similar proteins. Citrus jambhiri EG45-like domain-containing protein was identified as a protein associated with citrus blight (CB), and is also called blight-associated protein p12 (CjBAp12) or plant natriuretic peptide (PNP). CjBAp12 does not display cell wall loosening activity of expansins. Arabidopsis thaliana EG45-like domain-containing protein 2, also called plant natriuretic peptide A (AtPNP-A), is a systemically mobile natriuretic peptide immunoanalog, recognized by antibodies against vertebrate atrial natriuretic peptides (ANPs), that functions in cell volume regulation. Thus, it has an important and systemic role in plant growth and homeostasis. Due to their similarity to the N-terminal domain of expansin and to endolytic peptidoglycan transglycosylase RlpA, EG45-like domain-containing proteins may adopt a double-psi beta-barrel fold. Pssm-ID: 439249 [Multi-domain] Cd Length: 106 Bit Score: 55.71 E-value: 3.61e-10
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| DPBB_RlpA_EXP_N-like | cd22191 | double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The ... |
32-149 | 9.00e-09 | |||||
double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The double-psi beta-barrel (DPBB) fold is found in a divergent group of proteins, including endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), EG45-like domain containing proteins, kiwellins, Streptomyces papain inhibitor (SPI), the N-terminal domain of plant and bacterial expansins, GH45 family of endoglucanases, barwins, cerato-platanins, membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins. RlpA may work in tandem with amidases to degrade peptidoglycan (PG) in the division septum and lateral wall to facilitate daughter cell separation. An EG45-like domain containing protein from Arabidopsis thaliana, called plant natriuretic peptide A (AtPNP-A), functions in cell volume regulation. Kiwellin proteins comprise a widespread family of plant-defense proteins that target pathogenic bacterial/fungal effectors that down-regulate plant defense responses. SPI is a stress protein produced under hyperthermal stress conditions that serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes. Some expansin family proteins display cell wall loosening activity and are involved in cell expansion and other developmental events during which cell wall modification occurs. Endoglucanases (EC 3.2.1.4) catalyze the endohydrolysis of (1-4)-beta-D-glucosidic linkages in cellulose, lichenin, and cereal beta-D-glucans. Animal cellulases, such as endoglucanase EG27II, have great potential for industrial applications such as bioethanol production. Barwin is a basic protein from barley seed. It is a probable plant lectin that may be involved in a defense mechanism. Cerato-platanin is a phytotoxin which causes production of phytoalexin in platanus acerifolia, platanus occidentalis, and platanus orientalis. It also induces cell necrosis. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. YuiC is a Firmicute stationary phase survival (Sps) protein. Pssm-ID: 439247 [Multi-domain] Cd Length: 92 Bit Score: 51.50 E-value: 9.00e-09
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| PLN03024 | PLN03024 | Putative EG45-like domain containing protein 1; Provisional |
34-149 | 2.59e-07 | |||||
Putative EG45-like domain containing protein 1; Provisional Pssm-ID: 178595 Cd Length: 125 Bit Score: 48.49 E-value: 2.59e-07
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| DPBB_GH45_endoglucanase | cd22278 | double-psi beta-barrel fold of glycoside hydrolase family 45 endoglucanase EG27II and similar ... |
48-154 | 2.71e-06 | |||||
double-psi beta-barrel fold of glycoside hydrolase family 45 endoglucanase EG27II and similar proteins; This group is made up of endoglucanases from mollusks similar to Ampullaria crossean endoglucanase EG27II, a glycoside hydrolase family 45 (GH45) subfamily B protein. Endoglucanases (EC 3.2.1.4) catalyze the endohydrolysis of (1-4)-beta-D-glucosidic linkages in cellulose, lichenin, and cereal beta-D-glucans. Animal cellulases, such as endoglucanase EG27II, have great potential for industrial applications such as bioethanol production. GH45 endoglucanases from mollusks adopt a double-psi beta-barrel (DPBB) fold. Pssm-ID: 439258 Cd Length: 143 Bit Score: 45.93 E-value: 2.71e-06
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