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Conserved domains on  [gi|18396479|ref|NP_566197|]
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expansin A13 [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
 40-263 1.07e-86

expansin A; Provisional


The actual alignment was detected with superfamily member PLN00050:

Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 258.42  E-value: 1.07e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479   40 WRPARATYYAATNPRDAVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDLRWCIPGtSIILTATNFCA 119
Cdd:PLN00050  25 WTGAHATFYGGGDASGTMGGACGYGNLYSQGYGTNTAALSTALFNNGLSCGACFEIKCVNDNIWCLPG-SIIITATNFCP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  120 PNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINCRKEGSMRFTVDGGGIFISVLITNVAGSGDIAAV 199
Cdd:PLN00050 104 PNLALPNNDGGWCNPPQQHFDLSQPVFQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGDIVAV 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18396479  200 KIKGSRTGWLPMGRNWGQNWHINADLRNQALSFEVTSSDRSTVTSYNVSPKNWNYGQTFEGKQF 263
Cdd:PLN00050 184 SIKGSKSNWQAMSRNWGQNWQSNSYLNGQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTGMQF 247
 
Name Accession Description Interval E-value
PLN00050 PLN00050
expansin A; Provisional
 40-263 1.07e-86

expansin A; Provisional


Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 258.42  E-value: 1.07e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479   40 WRPARATYYAATNPRDAVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDLRWCIPGtSIILTATNFCA 119
Cdd:PLN00050  25 WTGAHATFYGGGDASGTMGGACGYGNLYSQGYGTNTAALSTALFNNGLSCGACFEIKCVNDNIWCLPG-SIIITATNFCP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  120 PNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINCRKEGSMRFTVDGGGIFISVLITNVAGSGDIAAV 199
Cdd:PLN00050 104 PNLALPNNDGGWCNPPQQHFDLSQPVFQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGDIVAV 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18396479  200 KIKGSRTGWLPMGRNWGQNWHINADLRNQALSFEVTSSDRSTVTSYNVSPKNWNYGQTFEGKQF 263
Cdd:PLN00050 184 SIKGSKSNWQAMSRNWGQNWQSNSYLNGQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTGMQF 247
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 39-166 2.93e-71

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: 214.77  E-value: 2.93e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  39 EWRPARATYYAATNPRDAVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDLR-WCIPGTSIILTATNF 117
Cdd:cd22274   1 GWRSAHATFYGGSDASGTMGGACGYGNLYSQGYGTNTAALSTALFNDGASCGACYEIRCVDDPSpCCPGGPSITVTATNF 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 18396479 118 CAPNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINC 166
Cdd:cd22274  81 CPPNYALPSDNGGWCNPPREHFDLSQPAFLKIAQYKAGIVPVQYRRVPC 129
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 75-161 2.17e-38

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: 129.49  E-value: 2.17e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479     75 TVGLSETLFERGQICGACFELRCVDDLRWCIPGTSIILTATNFCAPNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKA 154
Cdd:smart00837   1 TAALSTALFNNGASCGACYEIMCVDSPKWCKPGGSITVTATNFCPPNYALSNDNGGWCNPPRKHFDLSQPAFEKIAQYKA 80


                   ....*..
gi 18396479    155 GNMPVQY 161
Cdd:smart00837  81 GIVPVKY 87
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 173-245 8.65e-28

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: 101.88  E-value: 8.65e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18396479   173 RFTVDGGG-IFISVLITNVAGSGDIAAVKIKGSRTGWLPMGRNWGQNWHINADLRNQALSFEVTS-SDRSTVTSY 245
Cdd:pfam01357   1 RFTVDGGSyPYLAVLVENVGGAGDISAVEVKQAGSGWIPMSRNWGANWQLNSSLPGQPLSFRVTSgSDGKTLVAD 75
 
Name Accession Description Interval E-value
PLN00050 PLN00050
expansin A; Provisional
 40-263 1.07e-86

expansin A; Provisional


Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 258.42  E-value: 1.07e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479   40 WRPARATYYAATNPRDAVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDLRWCIPGtSIILTATNFCA 119
Cdd:PLN00050  25 WTGAHATFYGGGDASGTMGGACGYGNLYSQGYGTNTAALSTALFNNGLSCGACFEIKCVNDNIWCLPG-SIIITATNFCP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  120 PNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINCRKEGSMRFTVDGGGIFISVLITNVAGSGDIAAV 199
Cdd:PLN00050 104 PNLALPNNDGGWCNPPQQHFDLSQPVFQKIAQYKAGIVPVQYRRVACRKSGGIRFTINGHSYFNLVLITNVGGAGDIVAV 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18396479  200 KIKGSRTGWLPMGRNWGQNWHINADLRNQALSFEVTSSDRSTVTSYNVSPKNWNYGQTFEGKQF 263
Cdd:PLN00050 184 SIKGSKSNWQAMSRNWGQNWQSNSYLNGQALSFKVTTSDGRTVISNNAAPSNWAFGQTYTGMQF 247
PLN00193 PLN00193
expansin-A; Provisional
 40-262 1.56e-82

expansin-A; Provisional


Pssm-ID: 215097 [Multi-domain]  Cd Length: 256  Bit Score: 248.29  E-value: 1.56e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479   40 WRPARATYYAATNPRDAVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRC--VDDLRWCIPGTSIILTATNF 117
Cdd:PLN00193  30 WTKAHATFYGGSDASGTMGGACGYGNLYSTGYGTRTAALSTALFNDGASCGQCYRIMCdyQADSRWCIKGASVTITATNF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  118 CAPNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINCRKEGSMRFTVDGGGIFISVLITNVAGSGDIA 197
Cdd:PLN00193 110 CPPNYALPNNNGGWCNPPLQHFDMAQPAWEKIGIYRGGIVPVLFQRVPCKKHGGVRFTINGRDYFELVLISNVGGAGSIQ 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18396479  198 AVKIKGSRTGWLPMGRNWGQNWHINADLRNQALSFEVTSSDRSTVTSYNVSPKNWNYGQTFEGKQ 262
Cdd:PLN00193 190 SVSIKGSKTGWMAMSRNWGANWQSNAYLDGQSLSFKVTTTDGQTRFFLNVVPANWGFGQTFSSSV 254
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 39-166 2.93e-71

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: 214.77  E-value: 2.93e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  39 EWRPARATYYAATNPRDAVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDLR-WCIPGTSIILTATNF 117
Cdd:cd22274   1 GWRSAHATFYGGSDASGTMGGACGYGNLYSQGYGTNTAALSTALFNDGASCGACYEIRCVDDPSpCCPGGPSITVTATNF 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 18396479 118 CAPNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINC 166
Cdd:cd22274  81 CPPNYALPSDNGGWCNPPREHFDLSQPAFLKIAQYKAGIVPVQYRRVPC 129
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 75-161 2.17e-38

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: 129.49  E-value: 2.17e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479     75 TVGLSETLFERGQICGACFELRCVDDLRWCIPGTSIILTATNFCAPNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKA 154
Cdd:smart00837   1 TAALSTALFNNGASCGACYEIMCVDSPKWCKPGGSITVTATNFCPPNYALSNDNGGWCNPPRKHFDLSQPAFEKIAQYKA 80


                   ....*..
gi 18396479    155 GNMPVQY 161
Cdd:smart00837  81 GIVPVKY 87
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 173-245 8.65e-28

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: 101.88  E-value: 8.65e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18396479   173 RFTVDGGG-IFISVLITNVAGSGDIAAVKIKGSRTGWLPMGRNWGQNWHINADLRNQALSFEVTS-SDRSTVTSY 245
Cdd:pfam01357   1 RFTVDGGSyPYLAVLVENVGGAGDISAVEVKQAGSGWIPMSRNWGANWQLNSSLPGQPLSFRVTSgSDGKTLVAD 75
DPBB_EXP_N-like cd22271
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ...
 43-166 6.66e-26

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: 97.83  E-value: 6.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  43 ARATYYAATnprDAVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDlrWCIPGTSIILTATNFCapny 122
Cdd:cd22271   3 GRATFYGGP---DLSGGACGYGPLPPPPGGGFVAALNPALYDNGAGCGACYEVTCPGS--PCCSGGSVVVMVTDSC---- 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18396479 123 gfdpdgggHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINC 166
Cdd:cd22271  74 --------PECGDAGHFDLSPDAFAALADPSGGIVPVTWRRVPC 109
DPBB_EXPB_N cd22275
N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins ...
 40-166 2.96e-17

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: 75.35  E-value: 2.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  40 WRPARATYYAATNPRDAVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDlRWCiPGTSIILTATNFCA 119
Cdd:cd22275   1 WLPARATWYGDPNGAGSNGGACGYKNVVQPPFSGMVSAGNPPIFKDGKGCGSCYEVKCTGP-PAC-SGKPVTVVITDECP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18396479 120 pnygfdpdggGHCNPPNkHFVLPIEAFEKIAI-------WKAGNMPVQYRRINC 166
Cdd:cd22275  79 ----------GGPIAPY-HFDLSGTAFGAMAKpgqedqlRNAGILDVQYRRVPC 121
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 76-161 6.34e-16

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: 70.70  E-value: 6.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479    76 VGLSETLFERGQICGACFELRCV------DDLRW-CIP--GTSIILTATNFCAPnygfdpdggghcnPPNKHFVLPIEAF 146
Cdd:pfam03330   1 AAGSASLYNNGTACGECYDVRCLtaahptLPFGTyCRVlsGRSVIVRITDRGPF-------------PPGRHFDLSGAAF 67

                          90
                  ....*....|....*
gi 18396479   147 EKIAIWKAGNMPVQY 161
Cdd:pfam03330  68 EKLAMPRAGIVPVQY 82
PLN03023 PLN03023
Expansin-like B1; Provisional
 43-259 9.38e-14

Expansin-like B1; Provisional


Pssm-ID: 215542 [Multi-domain]  Cd Length: 247  Bit Score: 69.07  E-value: 9.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479   43 ARATYYAATNPRDAVGGACGYGDLVKSGYGMATVGLSEtLFERGQICGACFELRCvddlrwcipgtsiilTATNFCAPNy 122
Cdd:PLN03023  28 SRATYYGSPDCLGTPTGACGFGEYGRTVNGGNVAGVSR-LYRNGTGCGACYQVRC---------------KAPNLCSDD- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  123 GFDPDGGGHCNPPNKHFVLPIEAFEKIA-------IWKAGNMPVQYRRINCRKEGS-MRFTVDGGGIF---ISVLITNVA 191
Cdd:PLN03023  91 GVNVVVTDYGEGDKTDFILSPRAYARLArpnmaaeLFAYGVVDVEYRRIPCRYAGYnLFFKVHEHSRFpdyLAIVMLYQA 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18396479  192 GSGDIAAVKI-KGSRTGWLPMGRNWGQNWhinaDLRNQ-----ALSFEVTSSDRST-VTSYNVSPKNWNYGQTFE 259
Cdd:PLN03023 171 GQNDILAVEIwQEDCKEWRGMRKAYGAVW----DMPNPpkgpiTLRFQVSGSAGQTwVQAKNVIPSDWKAGVAYD 241
DPBB_EXLB_N cd22277
N-terminal double-psi beta-barrel fold domain of the expansin-like B subfamily; Expansin-like ...
 44-166 1.41e-07

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: 48.97  E-value: 1.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  44 RATYYAATNPRDAVGGACGYGDLVKSGYGmATVGLSETLFERGQICGACFELRCVdDLRWCIP-GTSIILTatnfcapny 122
Cdd:cd22277   4 RATYYGNPDGKGTPTGACGYGSFGRTNNG-GDVSASSKLYRNGVGCGACYQVRCT-NPVYCSEkGVTIVIT--------- 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18396479 123 gfdpDGGGhcnPPNKHFVLPIEAFEKIA--------IWKAGNMPVQYRRINC 166
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 ...
 41-166 1.85e-07

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: 48.95  E-value: 1.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  41 RPARATYYAATNPrdAVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDLRWCIPGTSIILtaTNFCAP 120
Cdd:cd22276  11 RRSKAAYFSSASA--LSSGACGYGSMATSFNGGHLAAASPSLYRDGVGCGACFQVRCKDPKLCSKAGVRVVV--TDLNRS 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18396479 121 NygfdpdggghcnppNKHFVLPIEAFEKIA-------IWKAGNMPVQYRRINC 166
Cdd:cd22276  87 N--------------QTDFVLSSPAFAAMAkpgmaaqLLKRGAVDVEYKRVPC 125
DPBB_EXLX1-like cd22272
N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus ...
 40-162 3.68e-06

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: 44.48  E-value: 3.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  40 WRPARATYYAATNPrdavGGACGYGDlvkSGYGMATVGLSETLFERGQICGACFELRCVDDlrwcipgtSIILTATNFCa 119
Cdd:cd22272   1 THTGEATFYGAGAG----GGNCSLDP---PPADRMIAALNTADYNGSAACGACLEVTGPKG--------TVVVQVVDRC- 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18396479 120 pnygfdPDGGGHcnppnkHFVLPIEAFEKIAIWKAGNMPVQYR 162
Cdd:cd22272  65 ------PECAPG------DLDLSEEAFAKIADPSAGRVPITWR 95
DPBB_EG45-like cd22269
double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains ...
 42-162 3.81e-05

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: 41.84  E-value: 3.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396479  42 PARATYYAatnpRDAVGGACGYGDLVKSGYGMATVGlsETLFERGQICGACFELRCVDDLRW---CIPGTSIILTATNFC 118
Cdd:cd22269   2 VGTATFYT----PPYTPSACYGNDPSPSGNLFAAAG--DALWDNGAACGRRYRVRCIGGTNPgprPCTGGSVVVKIVDYC 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18396479 119 ApnygfdpdggGHCNPPnkhFVLPIEAFEKIAIWKAGNMPVQYR 162
Cdd:cd22269  76 P----------GCCGAT---FDLSQEAFAKIADPDAGRINIEYV 106
 
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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