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 685278814  35 EWRPARATYYAATNPRDLVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDLR-WCIPGTSIIVTATNF 113
Cdd:cd22274    1 GWRSAHATFYGGSDASGTMGGACGYGNLYSQGYGTNTAALSTALFNDGASCGACYEIRCVDDPSpCCPGGPSITVTATNF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 685278814 114 CAPNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINC 162
Cdd:cd22274   81 CPPNYALPSDNGGWCNPPREHFDLSQPAFLKIAQYKAGIVPVQYRRVPC 129

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 685278814  169 RFTVDGGG-IFISVLITNVAGSGDISAVKIKGSRTGWLPMGRNWGQNWHINADLKNQALSFEVTS-SDKSTVTAY 241
Cdd:pfam01357   1 RFTVDGGSyPYLAVLVENVGGAGDISAVEVKQAGSGWIPMSRNWGANWQLNSSLPGQPLSFRVTSgSDGKTLVAD 75

expansin-A; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685278814  36 WRPARATYYAATNPRDLVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRC--VDDLRWCIPGTSIIVTATNF 113
Cdd:PLN00193  30 WTKAHATFYGGSDASGTMGGACGYGNLYSTGYGTRTAALSTALFNDGASCGQCYRIMCdyQADSRWCIKGASVTITATNF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685278814 114 CAPNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINCRKEGSIRFTVDGGGIFISVLITNVAGSGDIS 193
Cdd:PLN00193 110 CPPNYALPNNNGGWCNPPLQHFDMAQPAWEKIGIYRGGIVPVLFQRVPCKKHGGVRFTINGRDYFELVLISNVGGAGSIQ 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685278814 194 AVKIKGSRTGWLPMGRNWGQNWHINADLKNQALSFEVTSSDKSTVTAYNVAPRNWDYGQTFEGKQ 258
Cdd:PLN00193 190 SVSIKGSKTGWMAMSRNWGANWQSNAYLDGQSLSFKVTTTDGQTRFFLNVVPANWGFGQTFSSSV 254

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        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685278814    71 TVGLSETLFERGQICGACFELRCVDDLRWCIPGTSIIVTATNFCAPNYGFDPDGGGHCNPPNKHFVLPIEAFEKIAIWKA 150
Cdd:smart00837   1 TAALSTALFNNGASCGACYEIMCVDSPKWCKPGGSITVTATNFCPPNYALSNDNGGWCNPPRKHFDLSQPAFEKIAQYKA 80

                   ....*..
gi 685278814   151 GNMPVQY 157
Cdd:smart00837  81 GIVPVKY 87

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 685278814  39 ARATYYAATnprDLVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDlrWCIPGTSIIVTATNFCapny 118
Cdd:cd22271    3 GRATFYGGP---DLSGGACGYGPLPPPPGGGFVAALNPALYDNGAGCGACYEVTCPGS--PCCSGGSVVVMVTDSC---- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 685278814 119 gfdpdgggHCNPPNKHFVLPIEAFEKIAIWKAGNMPVQYRRINC 162
Cdd:cd22271   74 --------PECGDAGHFDLSPDAFAALADPSGGIVPVTWRRVPC 109

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685278814   72 VGLSETLFERGQICGACFELRCV------DDLRW-CIP--GTSIIVTATNFCAPnygfdpdggghcnPPNKHFVLPIEAF 142
Cdd:pfam03330   1 AAGSASLYNNGTACGECYDVRCLtaahptLPFGTyCRVlsGRSVIVRITDRGPF-------------PPGRHFDLSGAAF 67

                          90
                  ....*....|....*
gi 685278814  143 EKIAIWKAGNMPVQY 157
Cdd:pfam03330  68 EKLAMPRAGIVPVQY 82

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685278814  37 RPARATYYAATNPrdLVGGACGYGDLVKSGYGMATVGLSETLFERGQICGACFELRCVDDLRWCIPGTSIIVtaTNFCAP 116
Cdd:cd22276   11 RRSKAAYFSSASA--LSSGACGYGSMATSFNGGHLAAASPSLYRDGVGCGACFQVRCKDPKLCSKAGVRVVV--TDLNRS 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 685278814 117 NygfdpdggghcnppNKHFVLPIEAFEKIA-------IWKAGNMPVQYRRINC 162
Cdd:cd22276   87 N--------------QTDFVLSSPAFAAMAkpgmaaqLLKRGAVDVEYKRVPC 125

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685278814  36 WRPARATYYAATNPrdlvGGACGYGDlvkSGYGMATVGLSETLFERGQICGACFELRCVDDlrwcipgtSIIVTATNFCa 115
Cdd:cd22272    1 THTGEATFYGAGAG----GGNCSLDP---PPADRMIAALNTADYNGSAACGACLEVTGPKG--------TVVVQVVDRC- 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 685278814 116 pnygfdPDGGGHcnppnkHFVLPIEAFEKIAIWKAGNMPVQYR 158
Cdd:cd22272   65 ------PECAPG------DLDLSEEAFAKIADPSAGRVPITWR 95

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685278814  39 ARATYYAAtnprDLVGGACGYgdlvKSGYGMATVGLSETLFERGQICGACFELRCVDdlrwcipGTSIIVTATNFCA 115
Cdd:cd22191    1 GRATYYDP----SGGLGACGT----TNSDSDLVVALSAALFDSGPLCGKCIRITYND-------GKTVTATVVDECP 62