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Conserved domains on  [gi|2515484675|gb|WIM33583|]
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hypothetical protein [Vernicia fordii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPBB_barwin-like cd22777
double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi ...
 72-190 2.70e-88

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.


:

Pssm-ID: 439259  Cd Length: 119  Bit Score: 255.14  E-value: 2.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515484675  72 SASNVRATYHLYNPQQHGWDLNAVSAYCSTWDANKPYSWRSKYGWTAFCGPVGPRGQASCGKCLRVTNTRTGAQTTVRIV 151
Cdd:cd22777     1 SATNVRATYHLYNPQQIGWDLRAVSAYCATWDADKPLSWRSKYGWTAFCGPAGPRGQASCGKCLRVTNTGTGAQTTVRIV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2515484675 152 DQCSNGGLDLDVNVFRKLDTDGKGYQQGHLTVNYQFVNC 190
Cdd:cd22777    81 DQCSNGGLDLDVNVFNKIDTNGIGYQQGHLIVNYQFVDC 119
Chitin_bind_1 pfam00187
Chitin recognition protein;
23-62 6.37e-15

Chitin recognition protein;


:

Pssm-ID: 459705  Cd Length: 38  Bit Score: 65.65  E-value: 6.37e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2515484675  23 QCGRQAGGKLCPNNLCCSQFGWCGSSDDYCspSKNCQSNC 62
Cdd:pfam00187   1 RCGKQAGGATCPNNLCCSQYGYCGTTSDYC--GDGCQSGC 38
 
Name Accession Description Interval E-value
DPBB_barwin-like cd22777
double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi ...
 72-190 2.70e-88

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.


Pssm-ID: 439259  Cd Length: 119  Bit Score: 255.14  E-value: 2.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515484675  72 SASNVRATYHLYNPQQHGWDLNAVSAYCSTWDANKPYSWRSKYGWTAFCGPVGPRGQASCGKCLRVTNTRTGAQTTVRIV 151
Cdd:cd22777     1 SATNVRATYHLYNPQQIGWDLRAVSAYCATWDADKPLSWRSKYGWTAFCGPAGPRGQASCGKCLRVTNTGTGAQTTVRIV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2515484675 152 DQCSNGGLDLDVNVFRKLDTDGKGYQQGHLTVNYQFVNC 190
Cdd:cd22777    81 DQCSNGGLDLDVNVFNKIDTNGIGYQQGHLIVNYQFVDC 119
Barwin pfam00967
Barwin family;
75-190 8.53e-69

Barwin family;


Pssm-ID: 395772  Cd Length: 116  Bit Score: 205.57  E-value: 8.53e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515484675  75 NVRATYHLYNPQQHGWDLNAVSAYCSTWDANKPYSWRSKYGWTAFCGPVGPRGQASCGKCLRVTNTRTGAQTTVRIVDQC 154
Cdd:pfam00967   1 NVRATYHYYNPAQNNWDLRAVSAYCATWDADKPLAWRSKYGWTAFCGPAGPRGQASCGKCLRVTNTATNAQVTVRIVDQC 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2515484675 155 SNGGLDLDVNVFRKLDTDGKGYQQGHLTVNYQFVNC 190
Cdd:pfam00967  81 SNGGLDLDVCVFNALDTNGAGYQQGHLNVDYQFVDC 116
Chitin_bind_1 pfam00187
Chitin recognition protein;
23-62 6.37e-15

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 65.65  E-value: 6.37e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2515484675  23 QCGRQAGGKLCPNNLCCSQFGWCGSSDDYCspSKNCQSNC 62
Cdd:pfam00187   1 RCGKQAGGATCPNNLCCSQYGYCGTTSDYC--GDGCQSGC 38
ChtBD1_GH19_hevein cd06921
Hevein or Type 1 chitin binding domain subfamily co-occuring with family 19 glycosyl ...
 22-62 3.97e-14

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.


Pssm-ID: 211312  Cd Length: 40  Bit Score: 63.66  E-value: 3.97e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2515484675  22 EQCGRQAGGKLCPNNLCCSQFGWCGSSDDYCSPskNCQSNC 62
Cdd:cd06921     1 EQCGRQAGGALCPGGLCCSQWGWCGSTDDYCGD--GCQSQC 39
ChtBD1 smart00270
Chitin binding domain;
23-62 8.70e-12

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 57.38  E-value: 8.70e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2515484675   23 QCGRQAGGKLCPNNLCCSQFGWCGSSDDYCspSKNCQSNC 62
Cdd:smart00270   1 RCGSQAGGKVCPNNLCCSQFGYCGSGDEYC--GRGCQSQC 38
YoaJ COG4305
Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];
127-193 1.74e-07

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


Pssm-ID: 443446 [Multi-domain]  Cd Length: 226  Bit Score: 49.60  E-value: 1.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515484675 127 GQASCGKCLRVTNTRTgaQTTVRIVDQ---CSNGGLDLDVNVFRKLdtdGKGyQQGHLTVNYQFVNCGDS 193
Cdd:COG4305    70 NSAACGACLEVTGPKG--SVTVRVVDRcpeCAPGDLDLSPEAFAKI---ADL-EAGRVPITWRLVSCPVS 133
 
Name Accession Description Interval E-value
DPBB_barwin-like cd22777
double-psi beta-barrel fold of the barwin family; This family represents a group of double-psi ...
 72-190 2.70e-88

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.


Pssm-ID: 439259  Cd Length: 119  Bit Score: 255.14  E-value: 2.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515484675  72 SASNVRATYHLYNPQQHGWDLNAVSAYCSTWDANKPYSWRSKYGWTAFCGPVGPRGQASCGKCLRVTNTRTGAQTTVRIV 151
Cdd:cd22777     1 SATNVRATYHLYNPQQIGWDLRAVSAYCATWDADKPLSWRSKYGWTAFCGPAGPRGQASCGKCLRVTNTGTGAQTTVRIV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2515484675 152 DQCSNGGLDLDVNVFRKLDTDGKGYQQGHLTVNYQFVNC 190
Cdd:cd22777    81 DQCSNGGLDLDVNVFNKIDTNGIGYQQGHLIVNYQFVDC 119
Barwin pfam00967
Barwin family;
75-190 8.53e-69

Barwin family;


Pssm-ID: 395772  Cd Length: 116  Bit Score: 205.57  E-value: 8.53e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515484675  75 NVRATYHLYNPQQHGWDLNAVSAYCSTWDANKPYSWRSKYGWTAFCGPVGPRGQASCGKCLRVTNTRTGAQTTVRIVDQC 154
Cdd:pfam00967   1 NVRATYHYYNPAQNNWDLRAVSAYCATWDADKPLAWRSKYGWTAFCGPAGPRGQASCGKCLRVTNTATNAQVTVRIVDQC 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2515484675 155 SNGGLDLDVNVFRKLDTDGKGYQQGHLTVNYQFVNC 190
Cdd:pfam00967  81 SNGGLDLDVCVFNALDTNGAGYQQGHLNVDYQFVDC 116
Chitin_bind_1 pfam00187
Chitin recognition protein;
23-62 6.37e-15

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 65.65  E-value: 6.37e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2515484675  23 QCGRQAGGKLCPNNLCCSQFGWCGSSDDYCspSKNCQSNC 62
Cdd:pfam00187   1 RCGKQAGGATCPNNLCCSQYGYCGTTSDYC--GDGCQSGC 38
ChtBD1_GH19_hevein cd06921
Hevein or Type 1 chitin binding domain subfamily co-occuring with family 19 glycosyl ...
 22-62 3.97e-14

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.


Pssm-ID: 211312  Cd Length: 40  Bit Score: 63.66  E-value: 3.97e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2515484675  22 EQCGRQAGGKLCPNNLCCSQFGWCGSSDDYCSPskNCQSNC 62
Cdd:cd06921     1 EQCGRQAGGALCPGGLCCSQWGWCGSTDDYCGD--GCQSQC 39
ChtBD1 cd00035
Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a ...
 23-62 2.88e-12

Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, 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.


Pssm-ID: 211311  Cd Length: 39  Bit Score: 58.94  E-value: 2.88e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2515484675  23 QCGRQAGGKLCPNNLCCSQFGWCGSSDDYCspSKNCQSNC 62
Cdd:cd00035     1 RCGSQAGGPPCPNNLCCSQYGYCGTGDDYC--GEGCQSQC 38
ChtBD1 smart00270
Chitin binding domain;
23-62 8.70e-12

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 57.38  E-value: 8.70e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2515484675   23 QCGRQAGGKLCPNNLCCSQFGWCGSSDDYCspSKNCQSNC 62
Cdd:smart00270   1 RCGSQAGGKVCPNNLCCSQFGYCGSGDEYC--GRGCQSQC 38
YoaJ COG4305
Peptidoglycan-binding domain, expansin YoaJ [Cell wall/membrane/envelope biogenesis];
127-193 1.74e-07

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


Pssm-ID: 443446 [Multi-domain]  Cd Length: 226  Bit Score: 49.60  E-value: 1.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515484675 127 GQASCGKCLRVTNTRTgaQTTVRIVDQ---CSNGGLDLDVNVFRKLdtdGKGyQQGHLTVNYQFVNCGDS 193
Cdd:COG4305    70 NSAACGACLEVTGPKG--SVTVRVVDRcpeCAPGDLDLSPEAFAKI---ADL-EAGRVPITWRLVSCPVS 133
DPBB_EXP_N-like cd22271
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ...
 121-190 1.45e-06

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: 45.44  E-value: 1.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2515484675 121 GPVGPRGQASCGKCLRVTNT----RTGAQTTVRIVDQC----SNGGLDLDVNVFRKLDTDGkgyqQGHLTVNYQFVNC 190
Cdd:cd22271    36 NPALYDNGAGCGACYEVTCPgspcCSGGSVVVMVTDSCpecgDAGHFDLSPDAFAALADPS----GGIVPVTWRRVPC 109
DPBB_RlpA_EXP_N-like cd22191
double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The ...
 129-185 5.52e-06

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: 43.41  E-value: 5.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2515484675 129 ASCGKCLRVTNTrTGAQTTVRIVDQC---SNGGLDLDVNVFRKLdtdGKGYQQGHLTVNY 185
Cdd:cd22191    37 PLCGKCIRITYN-DGKTVTATVVDECpgcGPGDLDLSPAAFQAL---AGDLDGGVIPVTW 92
DPBB_CEPL-like cd22778
double-psi beta-barrel fold of the cerato-platanin family; This family represents a group of ...
 129-190 1.40e-05

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.


Pssm-ID: 439260  Cd Length: 117  Bit Score: 42.75  E-value: 1.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2515484675 129 ASCGKCLRVTNTRTGAQTTVRIVDQCSNgGLDLDVNVFRKLdTDGKGYQQGHLTVNYQFV---NC 190
Cdd:cd22778    55 PSCGSCWKLTYAGNGNTIYVTAVDSAGE-GFVLSTEAFDDL-TGGQAVELGTVDVTATEVdasNC 117
DPBB_EXLX1-like cd22272
N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus ...
 129-169 3.41e-05

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: 41.02  E-value: 3.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2515484675 129 ASCGKCLRVTNTRtgAQTTVRIVDQC---SNGGLDLDVNVFRKL 169
Cdd:cd22272    41 AACGACLEVTGPK--GTVVVQVVDRCpecAPGDLDLSEEAFAKI 82
DPBB_RlpA-like cd22268
double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar ...
 131-175 1.50e-04

double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar proteins; Endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A, RlpA) is a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. It adopts a double-psi beta-barrel (DPBB) fold and is one of four SPOR-domain containing proteins in Escherichia coli (including FtsN, DedA and DamX) that bind peptidoglycan (PG) and are targeted to the septum during division. It directly interacts with the divisome protein FtsK in vitro, and deletion of the rlpA gene partially bypasses the requirement for functional FtsK, a large, multi-spanning membrane protein that facilitates double-stranded DNA translocation during division and sporulation in E. coli and Bacillus subtilis, respectively. In Pseudomonas aeruginosa, RlpA contributes to rod shape maintenance and daughter cell separation. The separation of daughter cells requires extensive PG remodeling. It has been suggested that amidases and RlpA work in tandem to degrade PG in the division septum and lateral wall to facilitate daughter cell separation.


Pssm-ID: 439248 [Multi-domain]  Cd Length: 92  Bit Score: 39.35  E-value: 1.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2515484675 131 CGKCLRVTNTRTGAQTTVRIVDQCS-NGGLDLDVN--VFRKLDTDGKG 175
Cdd:cd22268    37 FGTKVRVTNLENGKSVVVRVNDRGPfVKGRIIDLSyaAAKKLGMLGAG 84
 
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.
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