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Conserved domains on  [gi|15233283|ref|NP_191109|]
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expansin A16 [Arabidopsis thaliana]

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
 31-258 1.69e-124

expansin A; Provisional


The actual alignment was detected with superfamily member PLN00050:

Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 353.95  E-value: 1.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283   31 GGSWQTAHATFYGGNDASGTMGGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKCVNDPKWCHPGnpSVFVTAT 110
Cdd:PLN00050  22 GSGWTGAHATFYGGGDASGTMGGACGYGNLYSQGYGTNTAALSTALFNNGLSCGACFEIKCVNDNIWCLPG--SIIITAT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  111 NFCPPNLAQPSDNGGWCNPPRSHFDLAMPVFLKIAEYRAGIVPISYRRVACRKSGGIRFTINGHRYFNLVLITNVAGAGD 190
Cdd:PLN00050 100 NFCPPNLALPNNDGGWCNPPQQHFDLSQPVFQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGD 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233283  191 IARTSVKGSKTGWMSLTRNWGQNWQSNAVLVGQSLSFRVTSSDRRTSTSWNIAPSNWQFGQTFVGKNF 258
Cdd:PLN00050 180 IVAVSIKGSKSNWQAMSRNWGQNWQSNSYLNGQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTGMQF 247
 
Name Accession Description Interval E-value
PLN00050 PLN00050
expansin A; Provisional
 31-258 1.69e-124

expansin A; Provisional


Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 353.95  E-value: 1.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283   31 GGSWQTAHATFYGGNDASGTMGGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKCVNDPKWCHPGnpSVFVTAT 110
Cdd:PLN00050  22 GSGWTGAHATFYGGGDASGTMGGACGYGNLYSQGYGTNTAALSTALFNNGLSCGACFEIKCVNDNIWCLPG--SIIITAT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  111 NFCPPNLAQPSDNGGWCNPPRSHFDLAMPVFLKIAEYRAGIVPISYRRVACRKSGGIRFTINGHRYFNLVLITNVAGAGD 190
Cdd:PLN00050 100 NFCPPNLALPNNDGGWCNPPQQHFDLSQPVFQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGD 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233283  191 IARTSVKGSKTGWMSLTRNWGQNWQSNAVLVGQSLSFRVTSSDRRTSTSWNIAPSNWQFGQTFVGKNF 258
Cdd:PLN00050 180 IVAVSIKGSKSNWQAMSRNWGQNWQSNSYLNGQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTGMQF 247
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 34-161 3.17e-96

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: 277.95  E-value: 3.17e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  34 WQTAHATFYGGNDASGTMGGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKCVNDPKWCHPGNPSVFVTATNFC 113
Cdd:cd22274   2 WRSAHATFYGGSDASGTMGGACGYGNLYSQGYGTNTAALSTALFNDGASCGACYEIRCVDDPSPCCPGGPSITVTATNFC 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15233283 114 PPNLAQPSDNGGWCNPPRSHFDLAMPVFLKIAEYRAGIVPISYRRVAC 161
Cdd:cd22274  82 PPNYALPSDNGGWCNPPREHFDLSQPAFLKIAQYKAGIVPVQYRRVPC 129
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 69-156 1.00e-53

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: 168.39  E-value: 1.00e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283     69 TAALSTSLFNSGQSCGACFEIKCVNDPKWCHPGNpSVFVTATNFCPPNLAQPSDNGGWCNPPRSHFDLAMPVFLKIAEYR 148
Cdd:smart00837   1 TAALSTALFNNGASCGACYEIMCVDSPKWCKPGG-SITVTATNFCPPNYALSNDNGGWCNPPRKHFDLSQPAFEKIAQYK 79


                   ....*...
gi 15233283    149 AGIVPISY 156
Cdd:smart00837  80 AGIVPVKY 87
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 168-240 1.55e-27

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: 101.11  E-value: 1.55e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233283   168 RFTINGHRY-FNLVLITNVAGAGDIARTSVKGSKTGWMSLTRNWGQNWQSNAVLVGQSLSFRVTS-SDRRTSTSW 240
Cdd:pfam01357   1 RFTVDGGSYpYLAVLVENVGGAGDISAVEVKQAGSGWIPMSRNWGANWQLNSSLPGQPLSFRVTSgSDGKTLVAD 75
 
Name Accession Description Interval E-value
PLN00050 PLN00050
expansin A; Provisional
 31-258 1.69e-124

expansin A; Provisional


Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 353.95  E-value: 1.69e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283   31 GGSWQTAHATFYGGNDASGTMGGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKCVNDPKWCHPGnpSVFVTAT 110
Cdd:PLN00050  22 GSGWTGAHATFYGGGDASGTMGGACGYGNLYSQGYGTNTAALSTALFNNGLSCGACFEIKCVNDNIWCLPG--SIIITAT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  111 NFCPPNLAQPSDNGGWCNPPRSHFDLAMPVFLKIAEYRAGIVPISYRRVACRKSGGIRFTINGHRYFNLVLITNVAGAGD 190
Cdd:PLN00050 100 NFCPPNLALPNNDGGWCNPPQQHFDLSQPVFQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGD 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233283  191 IARTSVKGSKTGWMSLTRNWGQNWQSNAVLVGQSLSFRVTSSDRRTSTSWNIAPSNWQFGQTFVGKNF 258
Cdd:PLN00050 180 IVAVSIKGSKSNWQAMSRNWGQNWQSNSYLNGQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTGMQF 247
PLN00193 PLN00193
expansin-A; Provisional
 29-253 2.91e-116

expansin-A; Provisional


Pssm-ID: 215097 [Multi-domain]  Cd Length: 256  Bit Score: 333.41  E-value: 2.91e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283   29 FSGGSWQTAHATFYGGNDASGTMGGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKC--VNDPKWCHPGNpSVF 106
Cdd:PLN00193  25 FTPSGWTKAHATFYGGSDASGTMGGACGYGNLYSTGYGTRTAALSTALFNDGASCGQCYRIMCdyQADSRWCIKGA-SVT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  107 VTATNFCPPNLAQPSDNGGWCNPPRSHFDLAMPVFLKIAEYRAGIVPISYRRVACRKSGGIRFTINGHRYFNLVLITNVA 186
Cdd:PLN00193 104 ITATNFCPPNYALPNNNGGWCNPPLQHFDMAQPAWEKIGIYRGGIVPVLFQRVPCKKHGGVRFTINGRDYFELVLISNVG 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233283  187 GAGDIARTSVKGSKTGWMSLTRNWGQNWQSNAVLVGQSLSFRVTSSDRRTSTSWNIAPSNWQFGQTF 253
Cdd:PLN00193 184 GAGSIQSVSIKGSKTGWMAMSRNWGANWQSNAYLDGQSLSFKVTTTDGQTRFFLNVVPANWGFGQTF 250
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 34-161 3.17e-96

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: 277.95  E-value: 3.17e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  34 WQTAHATFYGGNDASGTMGGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKCVNDPKWCHPGNPSVFVTATNFC 113
Cdd:cd22274   2 WRSAHATFYGGSDASGTMGGACGYGNLYSQGYGTNTAALSTALFNDGASCGACYEIRCVDDPSPCCPGGPSITVTATNFC 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15233283 114 PPNLAQPSDNGGWCNPPRSHFDLAMPVFLKIAEYRAGIVPISYRRVAC 161
Cdd:cd22274  82 PPNYALPSDNGGWCNPPREHFDLSQPAFLKIAQYKAGIVPVQYRRVPC 129
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 69-156 1.00e-53

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: 168.39  E-value: 1.00e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283     69 TAALSTSLFNSGQSCGACFEIKCVNDPKWCHPGNpSVFVTATNFCPPNLAQPSDNGGWCNPPRSHFDLAMPVFLKIAEYR 148
Cdd:smart00837   1 TAALSTALFNNGASCGACYEIMCVDSPKWCKPGG-SITVTATNFCPPNYALSNDNGGWCNPPRKHFDLSQPAFEKIAQYK 79


                   ....*...
gi 15233283    149 AGIVPISY 156
Cdd:smart00837  80 AGIVPVKY 87
DPBB_EXP_N-like cd22271
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ...
 35-161 1.84e-35

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: 122.48  E-value: 1.84e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  35 QTAHATFYGGNDASGtmgGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKCVNDPkwcHPGNPSVFVTATNFCP 114
Cdd:cd22271   1 STGRATFYGGPDLSG---GACGYGPLPPPPGGGFVAALNPALYDNGAGCGACYEVTCPGSP---CCSGGSVVVMVTDSCP 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15233283 115 pnlaqpsdnggwCNPPRSHFDLAMPVFLKIAEYRAGIVPISYRRVAC 161
Cdd:cd22271  75 ------------ECGDAGHFDLSPDAFAALADPSGGIVPVTWRRVPC 109
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 168-240 1.55e-27

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: 101.11  E-value: 1.55e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233283   168 RFTINGHRY-FNLVLITNVAGAGDIARTSVKGSKTGWMSLTRNWGQNWQSNAVLVGQSLSFRVTS-SDRRTSTSW 240
Cdd:pfam01357   1 RFTVDGGSYpYLAVLVENVGGAGDISAVEVKQAGSGWIPMSRNWGANWQLNSSLPGQPLSFRVTSgSDGKTLVAD 75
DPBB_EXPB_N cd22275
N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins ...
 34-161 9.30e-27

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: 100.39  E-value: 9.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  34 WQTAHATFYGGNDASGTMGGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKCvNDPKWCHpGNPsVFVTATNFC 113
Cdd:cd22275   1 WLPARATWYGDPNGAGSNGGACGYKNVVQPPFSGMVSAGNPPIFKDGKGCGSCYEVKC-TGPPACS-GKP-VTVVITDEC 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15233283 114 PpnlaqpsdnGGWCNPPrsHFDLAMPVFLKIAEY-------RAGIVPISYRRVAC 161
Cdd:cd22275  78 P---------GGPIAPY--HFDLSGTAFGAMAKPgqedqlrNAGILDVQYRRVPC 121
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 70-156 5.20e-22

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: 86.88  E-value: 5.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283    70 AALSTSLFNSGQSCGACFEIKCVND-------PKWCHPGN-PSVFVTATNFCPPnlaqpsdnggwcnPPRSHFDLAMPVF 141
Cdd:pfam03330   1 AAGSASLYNNGTACGECYDVRCLTAahptlpfGTYCRVLSgRSVIVRITDRGPF-------------PPGRHFDLSGAAF 67

                          90
                  ....*....|....*
gi 15233283   142 LKIAEYRAGIVPISY 156
Cdd:pfam03330  68 EKLAMPRAGIVPVQY 82
PLN03023 PLN03023
Expansin-like B1; Provisional
 39-253 1.21e-16

Expansin-like B1; Provisional


Pssm-ID: 215542 [Multi-domain]  Cd Length: 247  Bit Score: 76.78  E-value: 1.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283   39 ATFYGGNDASGTMGGACGYGNLYSQGYGTNTAALStSLFNSGQSCGACFEIKCvNDPKWChpGNPSVFVTATNFcppnla 118
Cdd:PLN03023  30 ATYYGSPDCLGTPTGACGFGEYGRTVNGGNVAGVS-RLYRNGTGCGACYQVRC-KAPNLC--SDDGVNVVVTDY------ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  119 QPSDNGGWCNPPRSHFDLAMPVflKIAE-YRAGIVPISYRRVACRKSG-GIRFTINGHRYFN---LVLITNVAGAGDIAR 193
Cdd:PLN03023 100 GEGDKTDFILSPRAYARLARPN--MAAElFAYGVVDVEYRRIPCRYAGyNLFFKVHEHSRFPdylAIVMLYQAGQNDILA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233283  194 TSV-KGSKTGWMSLTRNWGQNWQ-SNAVLVGQSLSFRVTSSDRRT-STSWNIAPSNWQFGQTF 253
Cdd:PLN03023 178 VEIwQEDCKEWRGMRKAYGAVWDmPNPPKGPITLRFQVSGSAGQTwVQAKNVIPSDWKAGVAY 240
DPBB_EXLX1-like cd22272
N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus ...
 34-157 1.00e-14

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: 67.98  E-value: 1.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  34 WQTAHATFYGGNDAsgtmGGACGYGNLysqGYGTNTAALSTSLFNSGQSCGACFEIKcvndpkwcHPgNPSVFVTATNFC 113
Cdd:cd22272   1 THTGEATFYGAGAG----GGNCSLDPP---PADRMIAALNTADYNGSAACGACLEVT--------GP-KGTVVVQVVDRC 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15233283 114 PPnlaqpsdnggwCNPprSHFDLAMPVFLKIAEYRAGIVPISYR 157
Cdd:cd22272  65 PE-----------CAP--GDLDLSEEAFAKIADPSAGRVPITWR 95
DPBB_EXLB_N cd22277
N-terminal double-psi beta-barrel fold domain of the expansin-like B subfamily; Expansin-like ...
 39-161 4.37e-13

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: 63.99  E-value: 4.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  39 ATFYGGNDASGTMGGACGYGNLYSQGYGTNTAAlSTSLFNSGQSCGACFEIKCVNdPKWCHPGNPSVFVTatnfcppnla 118
Cdd:cd22277   5 ATYYGNPDGKGTPTGACGYGSFGRTNNGGDVSA-SSKLYRNGVGCGACYQVRCTN-PVYCSEKGVTIVIT---------- 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15233283 119 qpsDNGGwcnPPRSHFDLAMPVFLKIAE--------YRAGIVPISYRRVAC 161
Cdd:cd22277  73 ---DQGS---GDRTDFILSKHAFNRLAQpgdaseslLKLGVVDIQYRRVPC 117
DPBB_EXLA_N cd22276
N-terminal double-psi beta-barrel fold domain of the expansin-like A subfamily; Expansin-like ...
 47-161 5.88e-13

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: 63.97  E-value: 5.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  47 ASGTMGGACGYGNLYSQGYGTNTAALSTSLFNSGQSCGACFEIKCvNDPKWCHPGNPSVFVTATNfcppnlaqpSDNggw 126
Cdd:cd22276  21 ASALSSGACGYGSMATSFNGGHLAAASPSLYRDGVGCGACFQVRC-KDPKLCSKAGVRVVVTDLN---------RSN--- 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15233283 127 cnppRSHFDLAMPVFLKIAE-------YRAGIVPISYRRVAC 161
Cdd:cd22276  88 ----QTDFVLSSPAFAAMAKpgmaaqlLKRGAVDVEYKRVPC 125
DPBB_EG45-like cd22269
double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains ...
 54-157 3.33e-08

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: 50.32  E-value: 3.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  54 ACgYGNLYSQGyGTNTAALSTSLFNSGQSCGACFEIKCVNDP-KWCHP-GNPSVFVTATNFCPpnlaqpsdngGWCNPPr 131
Cdd:cd22269  16 AC-YGNDPSPS-GNLFAAAGDALWDNGAACGRRYRVRCIGGTnPGPRPcTGGSVVVKIVDYCP----------GCCGAT- 82

                        90       100
                ....*....|....*....|....*.
gi 15233283 132 shFDLAMPVFLKIAEYRAGIVPISYR 157
Cdd:cd22269  83 --FDLSQEAFAKIADPDAGRINIEYV 106
DPBB_RlpA_EXP_N-like cd22191
double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The ...
 39-156 5.89e-08

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: 49.19  E-value: 5.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  39 ATFYGGNDASGtmggACGYGNLYSQgygtNTAALSTSLFNSGQSCGACFEIKCvndpkwchPGNPSVFVTATNFCPPnla 118
Cdd:cd22191   3 ATYYDPSGGLG----ACGTTNSDSD----LVVALSAALFDSGPLCGKCIRITY--------NDGKTVTATVVDECPG--- 63

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15233283 119 qpsdnggwCNPprSHFDLAMPVFLKIAE-YRAGIVPISY 156
Cdd:cd22191  64 --------CGP--GDLDLSPAAFQALAGdLDGGVIPVTW 92
PLN03024 PLN03024
Putative EG45-like domain containing protein 1; Provisional
 1-156 4.18e-07

Putative EG45-like domain containing protein 1; Provisional


Pssm-ID: 178595  Cd Length: 125  Bit Score: 47.72  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283    1 MAINPLILLTIFPLFLLLSFTDAGIprvfsggswqtahATFYGGNDASgtmggACgYGNlysQGYGTNTAALSTSLFNSG 80
Cdd:PLN03024   1 MSKRILIFSTVLVFLFSVSYATPGI-------------ATFYTSYTPS-----AC-YRG---TSFGVMIAAASDSLWNNG 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283   81 QSCGACFEIKCVNdpkwchPGNP--------SVFVTATNFCPPNLAqpsdnggwcnpprSHFDLAMPVFLKIAEYRAGIV 152
Cdd:PLN03024  59 RVCGKMFTVKCKG------PRNAvphpctgkSVTVKIVDHCPSGCA-------------STLDLSREAFAQIANPVAGII 119


                 ....
gi 15233283  153 PISY 156
Cdd:PLN03024 120 NIDY 123
DPBB_GH45_endoglucanase cd22278
double-psi beta-barrel fold of glycoside hydrolase family 45 endoglucanase EG27II and similar ...
 53-161 1.54e-05

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: 43.62  E-value: 1.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233283  53 GACGYGNL-----YSQGYGTNTAALSTSLFNS------GQSCGACFEIKCVNDPKWCH---PGNPSVFVTATNFCPPNLA 118
Cdd:cd22278  14 GACGCGGKsgdtqFGWNLGYYTAAINQAAFDSgsglwcGQACGRCYQLTPTGGPYPGGgppPAGQSIVVMVTNLCPDGGN 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15233283 119 QPSDNGGWCNPPRS-----HFDLAMPV--FLKIAEYRAGIVPISYRRVAC 161
Cdd:cd22278  94 NEWCGQTGTNPTNQhgyefHFDLAIPGgqVTAFFFLGWDNPEVTFEEVSC 143
 
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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