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Conserved domains on  [gi|145334147|ref|NP_001078454|]
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expansin B3 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPBB_EXPB_N cd22275
N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins ...
 36-154 9.06e-71

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: 212.87  E-value: 9.06e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  36 WLPAVATWYGSPNGDGSDGGACGYGTLVdVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPG 115
Cdd:cd22275    1 WLPARATWYGDPNGAGSNGGACGYKNVV-QPPFSGMVSAGNPPIFKDGKGCGSCYEVKCTGPPACSGKPVTVVITDECPG 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 145334147 116 CSKTSTHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRR 154
Cdd:cd22275   80 GPIAPYHFDLSGTAFGAMAKPGQEDQLRNAGILDVQYRR 118
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 159-235 5.54e-26

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: 96.87  E-value: 5.54e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334147  159 AFHVNEGSTDfWLSLLVEFEDGEGDIGSMHIRQAGArEWLEMKHVWGANWCIIGGPLKGPFSIKLTTLSAGKTLSAT 235
Cdd:pfam01357   1 RFTVDGGSYP-YLAVLVENVGGAGDISAVEVKQAGS-GWIPMSRNWGANWQLNSSLPGQPLSFRVTSGSDGKTLVAD 75
 
Name Accession Description Interval E-value
DPBB_EXPB_N cd22275
N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins ...
 36-154 9.06e-71

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: 212.87  E-value: 9.06e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  36 WLPAVATWYGSPNGDGSDGGACGYGTLVdVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPG 115
Cdd:cd22275    1 WLPARATWYGDPNGAGSNGGACGYKNVV-QPPFSGMVSAGNPPIFKDGKGCGSCYEVKCTGPPACSGKPVTVVITDECPG 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 145334147 116 CSKTSTHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRR 154
Cdd:cd22275   80 GPIAPYHFDLSGTAFGAMAKPGQEDQLRNAGILDVQYRR 118
PLN03023 PLN03023
Expansin-like B1; Provisional
 41-255 2.04e-37

Expansin-like B1; Provisional


Pssm-ID: 215542 [Multi-domain]  Cd Length: 247  Bit Score: 131.86  E-value: 2.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  41 ATWYGSPNGDGSDGGACGYGTL-VDVKplHARVGAVNPiLFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPGcskT 119
Cdd:PLN03023  30 ATYYGSPDCLGTPTGACGFGEYgRTVN--GGNVAGVSR-LYRNGTGCGACYQVRCKAPNLCSDDGVNVVVTDYGEG---D 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 120 STHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRR------GKNIAFHVNEGSTD-FWLSLLVEFEDGEGDIGSMHIRQA 192
Cdd:PLN03023 104 KTDFILSPRAYARLARPNMAAELFAYGVVDVEYRRipcryaGYNLFFKVHEHSRFpDYLAIVMLYQAGQNDILAVEIWQE 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334147 193 GAREWLEMKHVWGANWcIIGGPLKGPFSIK-LTTLSAGKT-LSATDVVPRNWAPKATYSSRLNFS 255
Cdd:PLN03023 184 DCKEWRGMRKAYGAVW-DMPNPPKGPITLRfQVSGSAGQTwVQAKNVIPSDWKAGVAYDSNIQLD 247
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 159-235 5.54e-26

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: 96.87  E-value: 5.54e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334147  159 AFHVNEGSTDfWLSLLVEFEDGEGDIGSMHIRQAGArEWLEMKHVWGANWCIIGGPLKGPFSIKLTTLSAGKTLSAT 235
Cdd:pfam01357   1 RFTVDGGSYP-YLAVLVENVGGAGDISAVEVKQAGS-GWIPMSRNWGANWQLNSSLPGQPLSFRVTSGSDGKTLVAD 75
expansin_EXLX1 NF041144
expansin EXLX1-like domain; This HMM represents nearly the full length of EXLX1 (YoaJ) of ...
 40-237 7.44e-19

expansin EXLX1-like domain; This HMM represents nearly the full length of EXLX1 (YoaJ) of Bacillus subtilis, a cellulose-binding bacterial expansin, and similar domains in related bacteirial proteins. Expansins, which are small and non-catalytic, have the ability to loosen plant cell wall material and improve enzyme access, but an expansin domain can occur as an auxiliary domain in cellulases such as CelA of Clavibacter michiganensis, a bacterial pathogen of tomato plants. Pfam model PF01357 (expansin C-terminal domain), somewhat less than half the size, is related but is oriented toward plant expansin and hits relatively few members of this family above cutoffs (as of version PF01357.23).


Pssm-ID: 469065 [Multi-domain]  Cd Length: 192  Bit Score: 81.49  E-value: 7.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  40 VATWYGSpnGDGsdGGACGYgtlvDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSicsrraVTVIITDECPGCSkt 119
Cdd:NF041144   2 EATFYGA--GYG--GGACSL----DPIPADMMIAALNPADYNGAAACGAYLEVTGPKGT------VTVRVTDRCPECA-- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 120 STHFDLSGAVFGRlaIAGESgplrnRGLIPVIYR------RGKNIAFHVNEGSTDFWLSLLVefeDGEGD-IGSMHIRQA 192
Cdd:NF041144  66 PGHLDLSPQAFAK--IADPV-----AGIVPITWRlvsapsGPGPVSYRIKEGSSQYWAAIQV---RNHRNpVAKLEYRKG 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 145334147 193 GAreWLEMKHVWGANWCIIGGPLKGPFSIKLTTLSaGKTLSATDV 237
Cdd:NF041144 136 GT--WVALPRTDYNYFVSESGMGTGPLTIRVTDIY-GQVLTDTGI 177
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 74-152 1.28e-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: 72.62  E-value: 1.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147   74 AVNPILFKNGEGCGACYKVRCLD--------KSIC---SRRAVTVIITDECPGCSKtsTHFDLSGAVFGRLAIagesgpl 142
Cdd:pfam03330   2 AGSASLYNNGTACGECYDVRCLTaahptlpfGTYCrvlSGRSVIVRITDRGPFPPG--RHFDLSGAAFEKLAM------- 72

                          90
                  ....*....|
gi 145334147  143 RNRGLIPVIY 152
Cdd:pfam03330  73 PRAGIVPVQY 82
YoaJ COG4305
Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];
40-224 8.49e-16

Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443446 [Multi-domain]  Cd Length: 226  Bit Score: 73.86  E-value: 8.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  40 VATWYGSpngDGsdGGACGYgtlvDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSicsrraVTVIITDECPGCskT 119
Cdd:COG4305   37 EATYYDA---DG--GGNCSF----DPIPADLLVAALNPTDYANSAACGACLEVTGPKGS------VTVRVVDRCPEC--A 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 120 STHFDLSGAVFGRLAiAGEsgplrnRGLIPVIYR-----RGKNIAFHVNEGSTDFWLSllVEFEDGEGDIGSMHIRQAGA 194
Cdd:COG4305  100 PGDLDLSPEAFAKIA-DLE------AGRVPITWRlvscpVSGNVSYRFKEGSSQWWTA--VQVRNHRNPIAKLEVRSGGQ 170

                        170       180       190
                 ....*....|....*....|....*....|
gi 145334147 195 reWLEMKHVWGANWCIIGGPLKGPFSIKLT 224
Cdd:COG4305  171 --WVALPREDYNYFVAESGMGPGPFTIRVT 198
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 74-152 6.39e-09

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: 51.68  E-value: 6.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147    74 AVNPILFKNGEGCGACYKVRCLDKS-IC-SRRAVTVIITDECPG-----------CSKTSTHFDLSGAVFgrLAIAGESG 140
Cdd:smart00837   3 ALSTALFNNGASCGACYEIMCVDSPkWCkPGGSITVTATNFCPPnyalsndnggwCNPPRKHFDLSQPAF--EKIAQYKA 80

                           90
                   ....*....|..
gi 145334147   141 plrnrGLIPVIY 152
Cdd:smart00837  81 -----GIVPVKY 87
PLN00115 PLN00115
pollen allergen group 3; Provisional
 148-254 1.17e-05

pollen allergen group 3; Provisional


Pssm-ID: 177729  Cd Length: 118  Bit Score: 43.62  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 148 IPVIYRRGKNIAFHVNEGSTDFWLSLLVEFedgegDIGSMHIRQAGAREWLE-MKHVWGANWCI-IGGPLKGPFSIKLTT 225
Cdd:PLN00115  16 LFAVGSCATEVTFKVGKGSSSTSLELVTNV-----AISEVEIKEKGAKDWVDdLKESSTNTWTLkSKAPLKGPFSVRFLV 90

                         90       100
                 ....*....|....*....|....*....
gi 145334147 226 LSAGKTLsATDVVPRNWAPKATYSSRLNF 254
Cdd:PLN00115  91 KGGGYRV-VDDVIPESFKAGSVYKTGIQV 118
 
Name Accession Description Interval E-value
DPBB_EXPB_N cd22275
N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins ...
 36-154 9.06e-71

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: 212.87  E-value: 9.06e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  36 WLPAVATWYGSPNGDGSDGGACGYGTLVdVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPG 115
Cdd:cd22275    1 WLPARATWYGDPNGAGSNGGACGYKNVV-QPPFSGMVSAGNPPIFKDGKGCGSCYEVKCTGPPACSGKPVTVVITDECPG 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 145334147 116 CSKTSTHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRR 154
Cdd:cd22275   80 GPIAPYHFDLSGTAFGAMAKPGQEDQLRNAGILDVQYRR 118
PLN03023 PLN03023
Expansin-like B1; Provisional
 41-255 2.04e-37

Expansin-like B1; Provisional


Pssm-ID: 215542 [Multi-domain]  Cd Length: 247  Bit Score: 131.86  E-value: 2.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  41 ATWYGSPNGDGSDGGACGYGTL-VDVKplHARVGAVNPiLFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPGcskT 119
Cdd:PLN03023  30 ATYYGSPDCLGTPTGACGFGEYgRTVN--GGNVAGVSR-LYRNGTGCGACYQVRCKAPNLCSDDGVNVVVTDYGEG---D 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 120 STHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRR------GKNIAFHVNEGSTD-FWLSLLVEFEDGEGDIGSMHIRQA 192
Cdd:PLN03023 104 KTDFILSPRAYARLARPNMAAELFAYGVVDVEYRRipcryaGYNLFFKVHEHSRFpDYLAIVMLYQAGQNDILAVEIWQE 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334147 193 GAREWLEMKHVWGANWcIIGGPLKGPFSIK-LTTLSAGKT-LSATDVVPRNWAPKATYSSRLNFS 255
Cdd:PLN03023 184 DCKEWRGMRKAYGAVW-DMPNPPKGPITLRfQVSGSAGQTwVQAKNVIPSDWKAGVAYDSNIQLD 247
DPBB_EXP_N-like cd22271
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ...
 39-154 3.82e-29

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: 106.31  E-value: 3.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  39 AVATWYGspnGDGSDGGACGYGTLvDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPGCsK 118
Cdd:cd22271    3 GRATFYG---GPDLSGGACGYGPL-PPPPGGGFVAALNPALYDNGAGCGACYEVTCPGSPCCSGGSVVVMVTDSCPEC-G 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145334147 119 TSTHFDLSGAVFGRLAiagesgpLRNRGLIPVIYRR 154
Cdd:cd22271   78 DAGHFDLSPDAFAALA-------DPSGGIVPVTWRR 106
PLN00050 PLN00050
expansin A; Provisional
 34-251 4.69e-28

expansin A; Provisional


Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 107.43  E-value: 4.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  34 SHWLPAVATWYGSPNGDGSDGGACGYGTLVDvKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSI-CSRRAVTVIITDE 112
Cdd:PLN00050  23 SGWTGAHATFYGGGDASGTMGGACGYGNLYS-QGYGTNTAALSTALFNNGLSCGACFEIKCVNDNIwCLPGSIIITATNF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 113 CPG-----------CSKTSTHFDLSGAVFGRLAiagesgpLRNRGLIPVIYRR-----GKNIAFHVNeGSTDFWLSLLVE 176
Cdd:PLN00050 102 CPPnlalpnndggwCNPPQQHFDLSQPVFQKIA-------QYKAGIVPVQYRRvacrkSGGIRFTIN-GHSYFNLVLITN 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334147 177 FeDGEGDIGSMHIRQAGArEWLEMKHVWGANWCIIGGPLKGPFSIKLTTlSAGKTLSATDVVPRNWAPKATYSSR 251
Cdd:PLN00050 174 V-GGAGDIVAVSIKGSKS-NWQAMSRNWGQNWQSNSYLNGQALSFKVTT-SDGRTVISNNAAPSNWAFGQTYTGM 245
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 159-235 5.54e-26

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: 96.87  E-value: 5.54e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145334147  159 AFHVNEGSTDfWLSLLVEFEDGEGDIGSMHIRQAGArEWLEMKHVWGANWCIIGGPLKGPFSIKLTTLSAGKTLSAT 235
Cdd:pfam01357   1 RFTVDGGSYP-YLAVLVENVGGAGDISAVEVKQAGS-GWIPMSRNWGANWQLNSSLPGQPLSFRVTSGSDGKTLVAD 75
PLN00193 PLN00193
expansin-A; Provisional
 8-254 1.29e-24

expansin-A; Provisional


Pssm-ID: 215097 [Multi-domain]  Cd Length: 256  Bit Score: 98.44  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147   8 LATLCIVLQLLigsSALATTNRHVSNSHWLPAVATWYGSPNGDGSDGGACGYGTLVDVKpLHARVGAVNPILFKNGEGCG 87
Cdd:PLN00193   5 LLGLAILLQFC---CYLFINVNAFTPSGWTKAHATFYGGSDASGTMGGACGYGNLYSTG-YGTRTAALSTALFNDGASCG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  88 ACYKVRC---LDKSICSR-RAVTVIITDECPG-----------CSKTSTHFDLSGAVFGRLAIagesgplRNRGLIPVIY 152
Cdd:PLN00193  81 QCYRIMCdyqADSRWCIKgASVTITATNFCPPnyalpnnnggwCNPPLQHFDMAQPAWEKIGI-------YRGGIVPVLF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 153 RR-----GKNIAFHVNegSTDFWLSLLVEFEDGEGDIGSMHIRqaGARE-WLEMKHVWGANWcIIGGPLKG-PFSIKLTT 225
Cdd:PLN00193 154 QRvpckkHGGVRFTIN--GRDYFELVLISNVGGAGSIQSVSIK--GSKTgWMAMSRNWGANW-QSNAYLDGqSLSFKVTT 228

                        250       260
                 ....*....|....*....|....*....
gi 145334147 226 lSAGKTLSATDVVPRNWAPKATYSSRLNF 254
Cdd:PLN00193 229 -TDGQTRFFLNVVPANWGFGQTFSSSVQF 256
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 36-154 1.27e-23

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: 92.28  E-value: 1.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  36 WLPAVATWYGSPNGDGSDGGACGYGTLVDvkplhARVG----AVNPILFKNGEGCGACYKVRC---LDKSICSRRAVTVI 108
Cdd:cd22274    2 WRSAHATFYGGSDASGTMGGACGYGNLYS-----QGYGtntaALSTALFNDGASCGACYEIRCvddPSPCCPGGPSITVT 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145334147 109 ITDECP-----------GCSKTSTHFDLSGAVFGRLAIagesgplRNRGLIPVIYRR 154
Cdd:cd22274   77 ATNFCPpnyalpsdnggWCNPPREHFDLSQPAFLKIAQ-------YKAGIVPVQYRR 126
DPBB_EXLB_N cd22277
N-terminal double-psi beta-barrel fold domain of the expansin-like B subfamily; Expansin-like ...
 41-154 1.16e-22

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: 89.41  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  41 ATWYGSPNGDGSDGGACGYGTLVDVkpLHARVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDECPGcskTS 120
Cdd:cd22277    5 ATYYGNPDGKGTPTGACGYGSFGRT--NNGGDVSASSKLYRNGVGCGACYQVRCTNPVYCSEKGVTIVITDQGSG---DR 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145334147 121 THFDLSGAVFGRLAIAG-ESGPLRNRGLIPVIYRR 154
Cdd:cd22277   80 TDFILSKHAFNRLAQPGdASESLLKLGVVDIQYRR 114
DPBB_EXLA_N cd22276
N-terminal double-psi beta-barrel fold domain of the expansin-like A subfamily; Expansin-like ...
 41-154 3.70e-19

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: 80.54  E-value: 3.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  41 ATWYGSPNGDGSdgGACGYGTL-VDVKPLHarVGAVNPILFKNGEGCGACYKVRCLDKSICSRRAVTVIITDEcpgCSKT 119
Cdd:cd22276   15 AAYFSSASALSS--GACGYGSMaTSFNGGH--LAAASPSLYRDGVGCGACFQVRCKDPKLCSKAGVRVVVTDL---NRSN 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 145334147 120 STHFDLSGAVFGRLAIAGESGPLRNRGLIPVIYRR 154
Cdd:cd22276   88 QTDFVLSSPAFAAMAKPGMAAQLLKRGAVDVEYKR 122
expansin_EXLX1 NF041144
expansin EXLX1-like domain; This HMM represents nearly the full length of EXLX1 (YoaJ) of ...
 40-237 7.44e-19

expansin EXLX1-like domain; This HMM represents nearly the full length of EXLX1 (YoaJ) of Bacillus subtilis, a cellulose-binding bacterial expansin, and similar domains in related bacteirial proteins. Expansins, which are small and non-catalytic, have the ability to loosen plant cell wall material and improve enzyme access, but an expansin domain can occur as an auxiliary domain in cellulases such as CelA of Clavibacter michiganensis, a bacterial pathogen of tomato plants. Pfam model PF01357 (expansin C-terminal domain), somewhat less than half the size, is related but is oriented toward plant expansin and hits relatively few members of this family above cutoffs (as of version PF01357.23).


Pssm-ID: 469065 [Multi-domain]  Cd Length: 192  Bit Score: 81.49  E-value: 7.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  40 VATWYGSpnGDGsdGGACGYgtlvDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSicsrraVTVIITDECPGCSkt 119
Cdd:NF041144   2 EATFYGA--GYG--GGACSL----DPIPADMMIAALNPADYNGAAACGAYLEVTGPKGT------VTVRVTDRCPECA-- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 120 STHFDLSGAVFGRlaIAGESgplrnRGLIPVIYR------RGKNIAFHVNEGSTDFWLSLLVefeDGEGD-IGSMHIRQA 192
Cdd:NF041144  66 PGHLDLSPQAFAK--IADPV-----AGIVPITWRlvsapsGPGPVSYRIKEGSSQYWAAIQV---RNHRNpVAKLEYRKG 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 145334147 193 GAreWLEMKHVWGANWCIIGGPLKGPFSIKLTTLSaGKTLSATDV 237
Cdd:NF041144 136 GT--WVALPRTDYNYFVSESGMGTGPLTIRVTDIY-GQVLTDTGI 177
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 74-152 1.28e-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: 72.62  E-value: 1.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147   74 AVNPILFKNGEGCGACYKVRCLD--------KSIC---SRRAVTVIITDECPGCSKtsTHFDLSGAVFGRLAIagesgpl 142
Cdd:pfam03330   2 AGSASLYNNGTACGECYDVRCLTaahptlpfGTYCrvlSGRSVIVRITDRGPFPPG--RHFDLSGAAFEKLAM------- 72

                          90
                  ....*....|
gi 145334147  143 RNRGLIPVIY 152
Cdd:pfam03330  73 PRAGIVPVQY 82
YoaJ COG4305
Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];
40-224 8.49e-16

Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443446 [Multi-domain]  Cd Length: 226  Bit Score: 73.86  E-value: 8.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  40 VATWYGSpngDGsdGGACGYgtlvDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSicsrraVTVIITDECPGCskT 119
Cdd:COG4305   37 EATYYDA---DG--GGNCSF----DPIPADLLVAALNPTDYANSAACGACLEVTGPKGS------VTVRVVDRCPEC--A 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 120 STHFDLSGAVFGRLAiAGEsgplrnRGLIPVIYR-----RGKNIAFHVNEGSTDFWLSllVEFEDGEGDIGSMHIRQAGA 194
Cdd:COG4305  100 PGDLDLSPEAFAKIA-DLE------AGRVPITWRlvscpVSGNVSYRFKEGSSQWWTA--VQVRNHRNPIAKLEVRSGGQ 170

                        170       180       190
                 ....*....|....*....|....*....|
gi 145334147 195 reWLEMKHVWGANWCIIGGPLKGPFSIKLT 224
Cdd:COG4305  171 --WVALPREDYNYFVAESGMGPGPFTIRVT 198
DPBB_EXLX1-like cd22272
N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus ...
 41-153 7.98e-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: 67.98  E-value: 7.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  41 ATWYGSPNGdgsdGGACGYgtlvDVKPLHARVGAVNPILFKNGEGCGACYKVRCLDKSicsrraVTVIITDECPGCSKts 120
Cdd:cd22272    6 ATFYGAGAG----GGNCSL----DPPPADRMIAALNTADYNGSAACGACLEVTGPKGT------VVVQVVDRCPECAP-- 69

                         90       100       110
                 ....*....|....*....|....*....|...
gi 145334147 121 THFDLSGAVFGRLAiagesgPLrNRGLIPVIYR 153
Cdd:cd22272   70 GDLDLSEEAFAKIA------DP-SAGRVPITWR 95
DPBB_RlpA_EXP_N-like cd22191
double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The ...
 41-140 2.49e-13

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: 63.83  E-value: 2.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  41 ATWYGSPNGdgsdGGACGYgTLVDvkplHARVGAVNPILFKNGEGCGACYKVRCLDKsicsrRAVTVIITDECPGCSktS 120
Cdd:cd22191    3 ATYYDPSGG----LGACGT-TNSD----SDLVVALSAALFDSGPLCGKCIRITYNDG-----KTVTATVVDECPGCG--P 66

                         90       100
                 ....*....|....*....|
gi 145334147 121 THFDLSGAVFGRLAIAGESG 140
Cdd:cd22191   67 GDLDLSPAAFQALAGDLDGG 86
DPBB_EG45-like cd22269
double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains ...
 38-134 2.87e-12

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: 61.49  E-value: 2.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  38 PAVATWYGS---PNgdgsdggACgYGTlvDVKPLHARVGAVNPILFKNGEGCGACYKVRCLD-----KSICSRRAVTVII 109
Cdd:cd22269    2 VGTATFYTPpytPS-------AC-YGN--DPSPSGNLFAAAGDALWDNGAACGRRYRVRCIGgtnpgPRPCTGGSVVVKI 71

                         90       100
                 ....*....|....*....|....*
gi 145334147 110 TDECPGCSKTSthFDLSGAVFGRLA 134
Cdd:cd22269   72 VDYCPGCCGAT--FDLSQEAFAKIA 94
DPBB_SPI-like cd22273
double-psi beta-barrel fold of Streptomyces papain inhibitor and similar proteins; ...
 40-152 1.85e-09

double-psi beta-barrel fold of Streptomyces papain inhibitor and similar proteins; Streptomyces papain inhibitor (SPI) adopts a rigid, thermo-resistant double-psi-beta-barrel (DPBB) fold that is stabilized by two cysteine bridges. SPI serves as a glutamine and lysine donor substrate for microbial transglutaminase (MTG, EC 2.3.2.13) from Streptomycetes, that is used to covalently and specifically link functional amines to glutamine donor sites of therapeutic proteins. SPI is a stress protein produced under hyperthermal stress conditions, and is able to inhibit the cysteine proteases, papain and bromelain, as well as the bovine serine protease trypsin.


Pssm-ID: 439253  Cd Length: 101  Bit Score: 53.89  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  40 VATWYgspNGDGSdgGACGygtlvdvKPLHARVG---AVNPILFKNGEG------CGACYKVRCLDKSIcsrravTVIIT 110
Cdd:cd22273    4 DFTYY---NDAGY--GACG-------TPINAATEmlvAVSPAYWTTPNPnndppcCNVCVKVTYNGKTI------TVPVK 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 145334147 111 DECPGCSKtsTHFDLSGAVFGRLAiagesgPLRNRGLIPVIY 152
Cdd:cd22273   66 DKCPSCGK--NHIDLSQPAFKQLA------PLLVGGIIGATW 99
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 74-152 6.39e-09

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: 51.68  E-value: 6.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147    74 AVNPILFKNGEGCGACYKVRCLDKS-IC-SRRAVTVIITDECPG-----------CSKTSTHFDLSGAVFgrLAIAGESG 140
Cdd:smart00837   3 ALSTALFNNGASCGACYEIMCVDSPkWCkPGGSITVTATNFCPPnyalsndnggwCNPPRKHFDLSQPAF--EKIAQYKA 80

                           90
                   ....*....|..
gi 145334147   141 plrnrGLIPVIY 152
Cdd:smart00837  81 -----GIVPVKY 87
PLN03024 PLN03024
Putative EG45-like domain containing protein 1; Provisional
 16-137 1.31e-06

Putative EG45-like domain containing protein 1; Provisional


Pssm-ID: 178595  Cd Length: 125  Bit Score: 46.56  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147  16 QLLIGSSALATTnrhVSNSHWLPAVATWYGS--PNgdgsdggACGYGTLVDVKplharVGAVNPILFKNGEGCGACYKVR 93
Cdd:PLN03024   4 RILIFSTVLVFL---FSVSYATPGIATFYTSytPS-------ACYRGTSFGVM-----IAAASDSLWNNGRVCGKMFTVK 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145334147  94 CLDKS-----ICSRRAVTVIITDECP-GCSKTsthFDLSGAVFGRLA--IAG 137
Cdd:PLN03024  69 CKGPRnavphPCTGKSVTVKIVDHCPsGCAST---LDLSREAFAQIAnpVAG 117
PLN00115 PLN00115
pollen allergen group 3; Provisional
 148-254 1.17e-05

pollen allergen group 3; Provisional


Pssm-ID: 177729  Cd Length: 118  Bit Score: 43.62  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334147 148 IPVIYRRGKNIAFHVNEGSTDFWLSLLVEFedgegDIGSMHIRQAGAREWLE-MKHVWGANWCI-IGGPLKGPFSIKLTT 225
Cdd:PLN00115  16 LFAVGSCATEVTFKVGKGSSSTSLELVTNV-----AISEVEIKEKGAKDWVDdLKESSTNTWTLkSKAPLKGPFSVRFLV 90

                         90       100
                 ....*....|....*....|....*....
gi 145334147 226 LSAGKTLsATDVVPRNWAPKATYSSRLNF 254
Cdd:PLN00115  91 KGGGYRV-VDDVIPESFKAGSVYKTGIQV 118
 
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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