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Conserved domains on  [gi|2319235287|gb|KAI9398757|]
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hypothetical protein POPTR_003G223501v4, partial [Populus trichocarpa]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00050 super family cl31535
expansin A; Provisional
 6-120 1.32e-68

expansin A; Provisional


The actual alignment was detected with superfamily member PLN00050:

Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 206.42  E-value: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319235287   6 FQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVVITNVGGAGDVVAVSIKGSKSNWQAMSRNWGQNWQSNTYL 85
Cdd:PLN00050  130 FQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGDIVAVSIKGSKSNWQAMSRNWGQNWQSNSYL 209

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2319235287  86 NNQALSFKVTTSDGHTMVSNNVAPSNWAFGRTYTG 120
Cdd:PLN00050  210 NGQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTG 244
 
Name Accession Description Interval E-value
PLN00050 PLN00050
expansin A; Provisional
 6-120 1.32e-68

expansin A; Provisional


Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 206.42  E-value: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319235287   6 FQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVVITNVGGAGDVVAVSIKGSKSNWQAMSRNWGQNWQSNTYL 85
Cdd:PLN00050  130 FQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGDIVAVSIKGSKSNWQAMSRNWGQNWQSNSYL 209

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2319235287  86 NNQALSFKVTTSDGHTMVSNNVAPSNWAFGRTYTG 120
Cdd:PLN00050  210 NGQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTG 244
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 33-105 6.16e-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: 104.96  E-value: 6.16e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2319235287  33 RFTINGHSY-FNLVVITNVGGAGDVVAVSIKGSKSNWQAMSRNWGQNWQSNTYLNNQALSFKVTT-SDGHTMVSN 105
Cdd:pfam01357   1 RFTVDGGSYpYLAVLVENVGGAGDISAVEVKQAGSGWIPMSRNWGANWQLNSSLPGQPLSFRVTSgSDGKTLVAD 75
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 6-26 3.40e-09

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: 51.06  E-value: 3.40e-09
                          10        20
                  ....*....|....*....|.
gi 2319235287   6 FQKIAQYKAGIVPVQYRRVAC 26
Cdd:cd22274   109 FLKIAQYKAGIVPVQYRRVPC 129
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 6-21 8.50e-04

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: 35.88  E-value: 8.50e-04
                           10
                   ....*....|....*.
gi 2319235287    6 FQKIAQYKAGIVPVQY 21
Cdd:smart00837  72 FEKIAQYKAGIVPVKY 87
 
Name Accession Description Interval E-value
PLN00050 PLN00050
expansin A; Provisional
 6-120 1.32e-68

expansin A; Provisional


Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 206.42  E-value: 1.32e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319235287   6 FQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVVITNVGGAGDVVAVSIKGSKSNWQAMSRNWGQNWQSNTYL 85
Cdd:PLN00050  130 FQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGDIVAVSIKGSKSNWQAMSRNWGQNWQSNSYL 209

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2319235287  86 NNQALSFKVTTSDGHTMVSNNVAPSNWAFGRTYTG 120
Cdd:PLN00050  210 NGQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTG 244
PLN00193 PLN00193
expansin-A; Provisional
 6-119 1.21e-51

expansin-A; Provisional


Pssm-ID: 215097 [Multi-domain]  Cd Length: 256  Bit Score: 163.54  E-value: 1.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319235287   6 FQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVVITNVGGAGDVVAVSIKGSKSNWQAMSRNWGQNWQSNTYL 85
Cdd:PLN00193  138 WEKIGIYRGGIVPVLFQRVPCKKHGGVRFTINGRDYFELVLISNVGGAGSIQSVSIKGSKTGWMAMSRNWGANWQSNAYL 217

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2319235287  86 NNQALSFKVTTSDGHTMVSNNVAPSNWAFGRTYT 119
Cdd:PLN00193  218 DGQSLSFKVTTTDGQTRFFLNVVPANWGFGQTFS 251
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 33-105 6.16e-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: 104.96  E-value: 6.16e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2319235287  33 RFTINGHSY-FNLVVITNVGGAGDVVAVSIKGSKSNWQAMSRNWGQNWQSNTYLNNQALSFKVTT-SDGHTMVSN 105
Cdd:pfam01357   1 RFTVDGGSYpYLAVLVENVGGAGDISAVEVKQAGSGWIPMSRNWGANWQLNSSLPGQPLSFRVTSgSDGKTLVAD 75
PLN03023 PLN03023
Expansin-like B1; Provisional
 12-118 8.19e-12

Expansin-like B1; Provisional


Pssm-ID: 215542 [Multi-domain]  Cd Length: 247  Bit Score: 59.83  E-value: 8.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2319235287  12 YKAGIVPVQYRRVACRKSG-GIRFTINGHSYFN---LVVITNVGGAGDVVAVSIKGSKSN-WQAMSRNWGQNWQ-SNTYL 85
Cdd:PLN03023  127 FAYGVVDVEYRRIPCRYAGyNLFFKVHEHSRFPdylAIVMLYQAGQNDILAVEIWQEDCKeWRGMRKAYGAVWDmPNPPK 206

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2319235287  86 NNQALSFKVTTSDGHTMV-SNNVAPSNWAFGRTY 118
Cdd:PLN03023  207 GPITLRFQVSGSAGQTWVqAKNVIPSDWKAGVAY 240
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 6-26 3.40e-09

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: 51.06  E-value: 3.40e-09
                          10        20
                  ....*....|....*....|.
gi 2319235287   6 FQKIAQYKAGIVPVQYRRVAC 26
Cdd:cd22274   109 FLKIAQYKAGIVPVQYRRVPC 129
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 6-21 8.50e-04

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: 35.88  E-value: 8.50e-04
                           10
                   ....*....|....*.
gi 2319235287    6 FQKIAQYKAGIVPVQY 21
Cdd:smart00837  72 FEKIAQYKAGIVPVKY 87
DPBB_EXP_N-like cd22271
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ...
 6-26 4.82e-03

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: 34.27  E-value: 4.82e-03
                          10        20
                  ....*....|....*....|.
gi 2319235287   6 FQKIAQYKAGIVPVQYRRVAC 26
Cdd:cd22271    89 FAALADPSGGIVPVTWRRVPC 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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