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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10314021  18 WLDAKATFYGsDPRGAapDDHGGACGYKDVDKAPFDGMTGCGNEPIFKDGLACGSCYEIKCKEPAECSGEPVLIKITDKN 97
Cdd:cd22275   1 WLPARATWYG-DPNGA--GSNGGACGYKNVVQPPFSGMVSAGNPPIFKDGKGCGSCYEVKCTGPPACSGKPVTVVITDEC 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 10314021  98 YEH-IAAYHFDLSGKAFGAMAKKGEEDKLRKAGELMLQFRRVKC 140
Cdd:cd22275  78 PGGpIAPYHFDLSGTAFGAMAKPGQEDQLRNAGILDVQYRRVPC 121

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10314021  18 WLDAKATFYGsDPRGAapDDHGGACGYKDVDKAPFDGMTGCGNEPIFKDGLACGSCYEIKCKEPAECSGEPVLIKITDKN 97
Cdd:cd22275   1 WLPARATWYG-DPNGA--GSNGGACGYKNVVQPPFSGMVSAGNPPIFKDGKGCGSCYEVKCTGPPACSGKPVTVVITDEC 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 10314021  98 YEH-IAAYHFDLSGKAFGAMAKKGEEDKLRKAGELMLQFRRVKC 140
Cdd:cd22275  78 PGGpIAPYHFDLSGTAFGAMAKPGQEDQLRNAGILDVQYRRVPC 121

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10314021   149 AFHVEKGSSPnYLALLVKYAAGDGNIVGVDIKPKGSDeFLPMKQSWGAIWRMDPPkPLKGPFTIRLTSESGGHV 222
Cdd:pfam01357   1 RFTVDGGSYP-YLAVLVENVGGAGDISAVEVKQAGSG-WIPMSRNWGANWQLNSS-LPGQPLSFRVTSGSDGKT 71

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10314021    58 CGNEPIFKDGLACGSCYEIKCKEPA--------EC---SGEPVLIKITDKNYEHiAAYHFDLSGKAFGAMAKKG 120
Cdd:pfam03330   2 AGSASLYNNGTACGECYDVRCLTAAhptlpfgtYCrvlSGRSVIVRITDRGPFP-PGRHFDLSGAAFEKLAMPR 74

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10314021  18 WLDAKATFYGsDPRGAapDDHGGACGYKDVDKAPFDGMTGCGNEPIFKDGLACGSCYEIKCKEPAECSGEPVLIKITDKN 97
Cdd:cd22275   1 WLPARATWYG-DPNGA--GSNGGACGYKNVVQPPFSGMVSAGNPPIFKDGKGCGSCYEVKCTGPPACSGKPVTVVITDEC 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 10314021  98 YEH-IAAYHFDLSGKAFGAMAKKGEEDKLRKAGELMLQFRRVKC 140
Cdd:cd22275  78 PGGpIAPYHFDLSGTAFGAMAKPGQEDQLRNAGILDVQYRRVPC 121

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10314021  20 DAKATFYGsdprgaAPDDHGGACGYKDVDKAPFDGMTGCGNEPIFKDGLACGSCYEIKCKEPAECSGEPVLIKITDKNYE 99
Cdd:cd22271   2 TGRATFYG------GPDLSGGACGYGPLPPPPGGGFVAALNPALYDNGAGCGACYEVTCPGSPCCSGGSVVVMVTDSCPE 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 10314021 100 HIAAYHFDLSGKAFGAMAkkgeedkLRKAGELMLQFRRVKC 140
Cdd:cd22271  76 CGDAGHFDLSPDAFAALA-------DPSGGIVPVTWRRVPC 109

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10314021  18 WLDAKATFYGSDPrgaAPDDHGGACGYKDVDKAPFDGMTGCGNEPIFKDGLACGSCYEIKC---KEPAECSGEPVLIKIT 94
Cdd:cd22274   2 WRSAHATFYGGSD---ASGTMGGACGYGNLYSQGYGTNTAALSTALFNDGASCGACYEIRCvddPSPCCPGGPSITVTAT 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 10314021  95 D---KNYEHIAAY---------HFDLSGKAFGAMAKkgeedklRKAGELMLQFRRVKC 140
Cdd:cd22274  79 NfcpPNYALPSDNggwcnppreHFDLSQPAFLKIAQ-------YKAGIVPVQYRRVPC 129

pollen allergen group 3; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10314021  146 TKIAFHVEKGSSPNYLALLVKYAagdgnIVGVDIKPKGSDEFLP-MKQSWGAIWRMDPPKPLKGPFTIRLTSESGGHVEQ 224
Cdd:PLN00115  24 TEVTFKVGKGSSSTSLELVTNVA-----ISEVEIKEKGAKDWVDdLKESSTNTWTLKSKAPLKGPFSVRFLVKGGGYRVV 98

                         90       100
                 ....*....|....*....|
gi 10314021  225 DDVIPEDWKPDTVYKSKIQF 244
Cdd:PLN00115  99 DDVIPESFKAGSVYKTGIQV 118

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10314021  20 DAKATFYGSDPRGAAPDdhgGACGYKDVDKAPFDGMTGCGNEpIFKDGLACGSCYEIKCKEPAECSGEPVLIKITDknYE 99
Cdd:cd22277   2 DSRATYYGNPDGKGTPT---GACGYGSFGRTNNGGDVSASSK-LYRNGVGCGACYQVRCTNPVYCSEKGVTIVITD--QG 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 10314021 100 HIAAYHFDLSGKAFGAMAKKGEE-DKLRKAGELMLQFRRVKC 140
Cdd:cd22277  76 SGDRTDFILSKHAFNRLAQPGDAsESLLKLGVVDIQYRRVPC 117

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 10314021    58 CGNEPIFKDGLACGSCYEIKCKEPA--------EC---SGEPVLIKITDKNYEHiAAYHFDLSGKAFGAMAKKG 120
Cdd:pfam03330   2 AGSASLYNNGTACGECYDVRCLTAAhptlpfgtYCrvlSGRSVIVRITDRGPFP-PGRHFDLSGAAFEKLAMPR 74

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10314021  21 AKATFYGsdprgaaPDDHGGACGYKDVDkapfDGMTGCGNEPIFKDGLACGSCYEIKCKepaecSGEPVLIKITDKnYEH 100
Cdd:cd22191   1 GRATYYD-------PSGGLGACGTTNSD----SDLVVALSAALFDSGPLCGKCIRITYN-----DGKTVTATVVDE-CPG 63

                        90
                ....*....|....*..
gi 10314021 101 IAAYHFDLSGKAFGAMA 117
Cdd:cd22191  64 CGPGDLDLSPAAFQALA 80

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10314021     62 PIFKDGLACGSCYEIKC-KEPAEC-SGEPVLIKITD---KNYEHIAAY---------HFDLSGKAFGAMAK 118
Cdd:smart00837   7 ALFNNGASCGACYEIMCvDSPKWCkPGGSITVTATNfcpPNYALSNDNggwcnpprkHFDLSQPAFEKIAQ 77