double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi beta-barrel (DPBB) fold proteins similar to Barwin, including Wheatwin-1/-2, pathogenesis-related protein P2, and the C-terminal domains of Pro-hevein, Wound-induced proteins WIN1/WIN2, and hevein-like preproprotein. Barwin is a basic protein from barley seed. It is a probable plant lectin that may be involved in a defense mechanism. Barwin binds weakly to a chitin analog. Pro-hevein, also called major hevein, is a rubber tree N-acetyl-D-glucosamine/N-acetyl-D-neuraminic acid binding lectin that can inhibit fungal growth. WIN1 and WIN2 from potato are cysteine-rich proteins which show striking homology to several chitin-binding proteins. Wheatwin-1 and Wheatwin-2 from bread wheat are also called pathogenesis-related protein 4a and 4b, respectively. They show antifungal activity towards B. cinerea and towards the wheat-specific pathogenic fungi F. culmorum and F. graminearum (groups 1 and 2). Wheatwin-1 has ribonuclease activity. Pathogenesis-related protein P2 (also called PR protein P2) from tomato is homologous to WINs and pro-hevein, but lack the N-terminal, chitin-binding "hevein" domain. Hevein-like preproprotein (also called HEL protein) from Arabidopsis is a fungal growth inhibitor. Neither its N-terminal hevein-like domain (CB-HEL) nor the C-terminal domain (CD-HEL) have chitinase activity, but both have antimicrobial activities. CD-HEL has RNase, but no DNase activity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229342  73 SASNVRATYHFYNPAQNNWDLRAVSAYCSTWDADKPYAWRSKYGWTAFCGPAGPRGQASCGKCLRVKNTRTNAAVTVRIV 152
Cdd:cd22777   1 SATNVRATYHLYNPQQIGWDLRAVSAYCATWDADKPLSWRSKYGWTAFCGPAGPRGQASCGKCLRVTNTGTGAQTTVRIV 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15229342 153 DQCSNGGLDLDVAMFNQIDTDGFGYQQGHLIVDYQFVDC 191
Cdd:cd22777  81 DQCSNGGLDLDVNVFNKIDTNGIGYQQGHLIVNYQFVDC 119

double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi beta-barrel (DPBB) fold proteins similar to Barwin, including Wheatwin-1/-2, pathogenesis-related protein P2, and the C-terminal domains of Pro-hevein, Wound-induced proteins WIN1/WIN2, and hevein-like preproprotein. Barwin is a basic protein from barley seed. It is a probable plant lectin that may be involved in a defense mechanism. Barwin binds weakly to a chitin analog. Pro-hevein, also called major hevein, is a rubber tree N-acetyl-D-glucosamine/N-acetyl-D-neuraminic acid binding lectin that can inhibit fungal growth. WIN1 and WIN2 from potato are cysteine-rich proteins which show striking homology to several chitin-binding proteins. Wheatwin-1 and Wheatwin-2 from bread wheat are also called pathogenesis-related protein 4a and 4b, respectively. They show antifungal activity towards B. cinerea and towards the wheat-specific pathogenic fungi F. culmorum and F. graminearum (groups 1 and 2). Wheatwin-1 has ribonuclease activity. Pathogenesis-related protein P2 (also called PR protein P2) from tomato is homologous to WINs and pro-hevein, but lack the N-terminal, chitin-binding "hevein" domain. Hevein-like preproprotein (also called HEL protein) from Arabidopsis is a fungal growth inhibitor. Neither its N-terminal hevein-like domain (CB-HEL) nor the C-terminal domain (CD-HEL) have chitinase activity, but both have antimicrobial activities. CD-HEL has RNase, but no DNase activity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229342  73 SASNVRATYHFYNPAQNNWDLRAVSAYCSTWDADKPYAWRSKYGWTAFCGPAGPRGQASCGKCLRVKNTRTNAAVTVRIV 152
Cdd:cd22777   1 SATNVRATYHLYNPQQIGWDLRAVSAYCATWDADKPLSWRSKYGWTAFCGPAGPRGQASCGKCLRVTNTGTGAQTTVRIV 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15229342 153 DQCSNGGLDLDVAMFNQIDTDGFGYQQGHLIVDYQFVDC 191
Cdd:cd22777  81 DQCSNGGLDLDVNVFNKIDTNGIGYQQGHLIVNYQFVDC 119

Chitin recognition protein;

                          10        20        30
                  ....*....|....*....|....*....|.
gi 15229342    32 TCPGNICCSQYGYCGTTADYCSptNNCQSNC 62
Cdd:pfam00187  10 TCPNNLCCSQYGYCGTTSDYCG--DGCQSGC 38

Chitin binding domain;

                           10        20        30
                   ....*....|....*....|....*....|.
gi 15229342     32 TCPGNICCSQYGYCGTTADYCSPtnNCQSNC 62
Cdd:smart00270  10 VCPNNLCCSQFGYCGSGDEYCGR--GCQSQC 38

double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi beta-barrel (DPBB) fold proteins similar to Barwin, including Wheatwin-1/-2, pathogenesis-related protein P2, and the C-terminal domains of Pro-hevein, Wound-induced proteins WIN1/WIN2, and hevein-like preproprotein. Barwin is a basic protein from barley seed. It is a probable plant lectin that may be involved in a defense mechanism. Barwin binds weakly to a chitin analog. Pro-hevein, also called major hevein, is a rubber tree N-acetyl-D-glucosamine/N-acetyl-D-neuraminic acid binding lectin that can inhibit fungal growth. WIN1 and WIN2 from potato are cysteine-rich proteins which show striking homology to several chitin-binding proteins. Wheatwin-1 and Wheatwin-2 from bread wheat are also called pathogenesis-related protein 4a and 4b, respectively. They show antifungal activity towards B. cinerea and towards the wheat-specific pathogenic fungi F. culmorum and F. graminearum (groups 1 and 2). Wheatwin-1 has ribonuclease activity. Pathogenesis-related protein P2 (also called PR protein P2) from tomato is homologous to WINs and pro-hevein, but lack the N-terminal, chitin-binding "hevein" domain. Hevein-like preproprotein (also called HEL protein) from Arabidopsis is a fungal growth inhibitor. Neither its N-terminal hevein-like domain (CB-HEL) nor the C-terminal domain (CD-HEL) have chitinase activity, but both have antimicrobial activities. CD-HEL has RNase, but no DNase activity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229342  73 SASNVRATYHFYNPAQNNWDLRAVSAYCSTWDADKPYAWRSKYGWTAFCGPAGPRGQASCGKCLRVKNTRTNAAVTVRIV 152
Cdd:cd22777   1 SATNVRATYHLYNPQQIGWDLRAVSAYCATWDADKPLSWRSKYGWTAFCGPAGPRGQASCGKCLRVTNTGTGAQTTVRIV 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15229342 153 DQCSNGGLDLDVAMFNQIDTDGFGYQQGHLIVDYQFVDC 191
Cdd:cd22777  81 DQCSNGGLDLDVNVFNKIDTNGIGYQQGHLIVNYQFVDC 119

Chitin recognition protein;

                          10        20        30
                  ....*....|....*....|....*....|.
gi 15229342    32 TCPGNICCSQYGYCGTTADYCSptNNCQSNC 62
Cdd:pfam00187  10 TCPNNLCCSQYGYCGTTSDYCG--DGCQSGC 38

Hevein or Type 1 chitin binding domain subfamily co-occuring with family 19 glycosyl hydrolases or with barwin domains; This subfamily includes Hevein, a major IgE-binding allergen in natural rubber latex. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.

                        10        20        30
                ....*....|....*....|....*....|.
gi 15229342  32 TCPGNICCSQYGYCGTTADYCSPtnNCQSNC 62
Cdd:cd06921  11 LCPGGLCCSQWGWCGSTDDYCGD--GCQSQC 39

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229342 122 GPAGPRGQASCGKCLRVKNT----RTNAAVTVRIVDQC----SNGGLDLDVAMFNQIDTDGfgyqQGHLIVDYQFVDC 191
Cdd:cd22271  36 NPALYDNGAGCGACYEVTCPgspcCSGGSVVVMVTDSCpecgDAGHFDLSPDAFAALADPS----GGIVPVTWRRVPC 109

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
                ....*....|....*....|....*....|....*....|....*..
gi 15229342 130 ASCGKCLRVKNTrTNAAVTVRIVDQC---SNGGLDLDVAMFNQIDTD 173
Cdd:cd22191  37 PLCGKCIRITYN-DGKTVTATVVDECpgcGPGDLDLSPAAFQALAGD 82

double-psi beta-barrel fold of the cerato-platanin family; This family represents a group of double-psi beta-barrel (DPBB) fold proteins similar to cerato-platanin, including protein SnodProt1, heat-stable 19 kDa antigen, allergen Asp f 15/Asp f 13, and Epl1 protein. They are involved in plant pathogenesis and elicitation of plant defense responses. Cerato-platanin is a phytotoxin which causes production of phytoalexin in Platanus acerifolia, P. occidentalis, and P. orientalis. It also induces cell necrosis. Cerato-platanin behaves as a fungal toxin. Protein SnodProt1 is also a phytotoxic protein. Heat-stable 19 kDa antigen is a Coccidioides-specific antigen (CS antigen) with serine proteinase activity. Epl1 protein is an elicitor of plant defence responses from Trichoderma virens.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229342 130 ASCGKCLRVKNTRTNAAVTVRIVDQCSNgGLDLDVAMFNQIdTDGFGYQQGHLIVDYQFVD 190
Cdd:cd22778  55 PSCGSCWKLTYAGNGNTIYVTAVDSAGE-GFVLSTEAFDDL-TGGQAVELGTVDVTATEVD 113