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Conserved domains on  [gi|26449323|dbj|BAC41789|]
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unknown protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03023 super family cl33621
Expansin-like B1; Provisional
 12-200 1.54e-58

Expansin-like B1; Provisional


The actual alignment was detected with superfamily member PLN03023:

Pssm-ID: 215542 [Multi-domain]  Cd Length: 247  Bit Score: 184.63  E-value: 1.54e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   12 AAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSNQTDLVLSSRAFRAMAKPVVGVDkyLLKQGIVDVEYQR 91
Cdd:PLN03023  61 AGVSRLYRNGTGCGACYQVRCKAPNLCSDDGVNVVVTDYGEGDKTDFILSPRAYARLARPNMAAE--LFAYGVVDVEYRR 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   92 VPCNYGKRNLNVRVEEASKKPNYLAIKLLYQGGQTEVVGIDIAPVGSSQWSYMSRSHGAVWATDKVPTGALQFKFTVTGG 171
Cdd:PLN03023 139 IPCRYAGYNLFFKVHEHSRFPDYLAIVMLYQAGQNDILAVEIWQEDCKEWRGMRKAYGAVWDMPNPPKGPITLRFQVSGS 218

                        170       180
                 ....*....|....*....|....*....
gi 26449323  172 YDGKTVWSKRVLPANWNSGRIYDAGVQIT 200
Cdd:PLN03023 219 AGQTWVQAKNVIPSDWKAGVAYDSNIQLD 247
 
Name Accession Description Interval E-value
PLN03023 PLN03023
Expansin-like B1; Provisional
 12-200 1.54e-58

Expansin-like B1; Provisional


Pssm-ID: 215542 [Multi-domain]  Cd Length: 247  Bit Score: 184.63  E-value: 1.54e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   12 AAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSNQTDLVLSSRAFRAMAKPVVGVDkyLLKQGIVDVEYQR 91
Cdd:PLN03023  61 AGVSRLYRNGTGCGACYQVRCKAPNLCSDDGVNVVVTDYGEGDKTDFILSPRAYARLARPNMAAE--LFAYGVVDVEYRR 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   92 VPCNYGKRNLNVRVEEASKKPNYLAIKLLYQGGQTEVVGIDIAPVGSSQWSYMSRSHGAVWATDKVPTGALQFKFTVTGG 171
Cdd:PLN03023 139 IPCRYAGYNLFFKVHEHSRFPDYLAIVMLYQAGQNDILAVEIWQEDCKEWRGMRKAYGAVWDMPNPPKGPITLRFQVSGS 218

                        170       180
                 ....*....|....*....|....*....
gi 26449323  172 YDGKTVWSKRVLPANWNSGRIYDAGVQIT 200
Cdd:PLN03023 219 AGQTWVQAKNVIPSDWKAGVAYDSNIQLD 247
DPBB_EXLA_N cd22276
N-terminal double-psi beta-barrel fold domain of the expansin-like A subfamily; Expansin-like ...
 1-96 1.65e-58

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: 180.30  E-value: 1.65e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   1 MATSFFAGHIAAAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSNQTDLVLSSRAFRAMAKPvvGVDKYLL 80
Cdd:cd22276  34 MATSFNGGHLAAASPSLYRDGVGCGACFQVRCKDPKLCSKAGVRVVVTDLNRSNQTDFVLSSPAFAAMAKP--GMAAQLL 111

                        90
                ....*....|....*.
gi 26449323  81 KQGIVDVEYQRVPCNY 96
Cdd:cd22276 112 KRGAVDVEYKRVPCEY 127
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 102-177 1.70e-15

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: 68.36  E-value: 1.70e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26449323   102 NVRVEEASKKpnYLAIKLLYQGGQTEVVGIDIAPVGSSqWSYMSRSHGAVWATDKVPT-GALQFKFTVTGgyDGKTV 177
Cdd:pfam01357   1 RFTVDGGSYP--YLAVLVENVGGAGDISAVEVKQAGSG-WIPMSRNWGANWQLNSSLPgQPLSFRVTSGS--DGKTL 72
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 11-51 7.10e-06

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: 42.82  E-value: 7.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 26449323     11 AAAIPSIYKDGAGCGACFQVRC-KNPKLCNSKGTIVmVTDLN 51
Cdd:smart00837   2 AALSTALFNNGASCGACYEIMCvDSPKWCKPGGSIT-VTATN 42
 
Name Accession Description Interval E-value
PLN03023 PLN03023
Expansin-like B1; Provisional
 12-200 1.54e-58

Expansin-like B1; Provisional


Pssm-ID: 215542 [Multi-domain]  Cd Length: 247  Bit Score: 184.63  E-value: 1.54e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   12 AAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSNQTDLVLSSRAFRAMAKPVVGVDkyLLKQGIVDVEYQR 91
Cdd:PLN03023  61 AGVSRLYRNGTGCGACYQVRCKAPNLCSDDGVNVVVTDYGEGDKTDFILSPRAYARLARPNMAAE--LFAYGVVDVEYRR 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   92 VPCNYGKRNLNVRVEEASKKPNYLAIKLLYQGGQTEVVGIDIAPVGSSQWSYMSRSHGAVWATDKVPTGALQFKFTVTGG 171
Cdd:PLN03023 139 IPCRYAGYNLFFKVHEHSRFPDYLAIVMLYQAGQNDILAVEIWQEDCKEWRGMRKAYGAVWDMPNPPKGPITLRFQVSGS 218

                        170       180
                 ....*....|....*....|....*....
gi 26449323  172 YDGKTVWSKRVLPANWNSGRIYDAGVQIT 200
Cdd:PLN03023 219 AGQTWVQAKNVIPSDWKAGVAYDSNIQLD 247
DPBB_EXLA_N cd22276
N-terminal double-psi beta-barrel fold domain of the expansin-like A subfamily; Expansin-like ...
 1-96 1.65e-58

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: 180.30  E-value: 1.65e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   1 MATSFFAGHIAAAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSNQTDLVLSSRAFRAMAKPvvGVDKYLL 80
Cdd:cd22276  34 MATSFNGGHLAAASPSLYRDGVGCGACFQVRCKDPKLCSKAGVRVVVTDLNRSNQTDFVLSSPAFAAMAKP--GMAAQLL 111

                        90
                ....*....|....*.
gi 26449323  81 KQGIVDVEYQRVPCNY 96
Cdd:cd22276 112 KRGAVDVEYKRVPCEY 127
DPBB_EXLB_N cd22277
N-terminal double-psi beta-barrel fold domain of the expansin-like B subfamily; Expansin-like ...
 8-94 1.48e-27

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: 100.97  E-value: 1.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   8 GHIAAAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSNQTDLVLSSRAFRAMAKPvVGVDKYLLKQGIVDV 87
Cdd:cd22277  32 GGDVSASSKLYRNGVGCGACYQVRCTNPVYCSEKGVTIVITDQGSGDRTDFILSKHAFNRLAQP-GDASESLLKLGVVDI 110


                ....*..
gi 26449323  88 EYQRVPC 94
Cdd:cd22277 111 QYRRVPC 117
DPBB_EXPB_N cd22275
N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins ...
 6-94 2.76e-25

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: 95.38  E-value: 2.76e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   6 FAGHIAAAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSNQTDLV---LSSRAFRAMAKPvvGVDKYLLKQ 82
Cdd:cd22275  32 FSGMVSAGNPPIFKDGKGCGSCYEVKCTGPPACSGKPVTVVITDECPGGPIAPYhfdLSGTAFGAMAKP--GQEDQLRNA 109

                        90
                ....*....|..
gi 26449323  83 GIVDVEYQRVPC 94
Cdd:cd22275 110 GILDVQYRRVPC 121
DPBB_EXP_N-like cd22271
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ...
 3-94 2.81e-20

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: 82.04  E-value: 2.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   3 TSFFAGHIAAAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSN--QTDLVLSSRAFRAMAKPvvgvdkyll 80
Cdd:cd22271  25 PPPGGGFVAALNPALYDNGAGCGACYEVTCPGSPCCSGGSVVVMVTDSCPECgdAGHFDLSPDAFAALADP--------- 95

                        90
                ....*....|....
gi 26449323  81 KQGIVDVEYQRVPC 94
Cdd:cd22271  96 SGGIVPVTWRRVPC 109
Expansin_C pfam01357
Expansin C-terminal domain; This domain is found at the C-terminus of expansins, plant cell ...
 102-177 1.70e-15

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: 68.36  E-value: 1.70e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26449323   102 NVRVEEASKKpnYLAIKLLYQGGQTEVVGIDIAPVGSSqWSYMSRSHGAVWATDKVPT-GALQFKFTVTGgyDGKTV 177
Cdd:pfam01357   1 RFTVDGGSYP--YLAVLVENVGGAGDISAVEVKQAGSG-WIPMSRNWGANWQLNSSLPgQPLSFRVTSGS--DGKTL 72
PLN00050 PLN00050
expansin A; Provisional
 6-193 3.14e-13

expansin A; Provisional


Pssm-ID: 165628 [Multi-domain]  Cd Length: 247  Bit Score: 66.60  E-value: 3.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323    6 FAGHIAAAIPSIYKDGAGCGACFQVRCKNP-KLCNSKGTIVMVTDLNTSN--------------QTDLVLSSRAFRAMAK 70
Cdd:PLN00050  56 YGTNTAALSTALFNNGLSCGACFEIKCVNDnIWCLPGSIIITATNFCPPNlalpnndggwcnppQQHFDLSQPVFQKIAQ 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   71 pvvgvdkylLKQGIVDVEYQRVPCnygKRNLNVRVeeASKKPNYLAIKLLYQ-GGQTEVVGIDIAPVgSSQWSYMSRSHG 149
Cdd:PLN00050 136 ---------YKAGIVPVQYRRVAC---RKSGGIRF--TINGHSYFNLVLITNvGGAGDIVAVSIKGS-KSNWQAMSRNWG 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 26449323  150 AVWATDKVPTG-ALQFKFTVTggyDGKTVWSKRVLPANWNSGRIY 193
Cdd:PLN00050 201 QNWQSNSYLNGqALSFKVTTS---DGRTVISNNAAPSNWAFGQTY 242
PLN00193 PLN00193
expansin-A; Provisional
 11-198 6.95e-13

expansin-A; Provisional


Pssm-ID: 215097 [Multi-domain]  Cd Length: 256  Bit Score: 65.70  E-value: 6.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   11 AAAIPSIYKDGAGCGACFQVRC---KNPKLCnSKGTIVMVTDLN--------TSNQTDLVLSSRAFRAMAKPV---VGVd 76
Cdd:PLN00193  66 AALSTALFNDGASCGQCYRIMCdyqADSRWC-IKGASVTITATNfcppnyalPNNNGGWCNPPLQHFDMAQPAwekIGI- 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   77 kylLKQGIVDVEYQRVPCnygKRNLNVRVEEASKkpNYLAIKLLYQ-GGQTEVVGIDIApvGS-SQWSYMSRSHGAVWAT 154
Cdd:PLN00193 144 ---YRGGIVPVLFQRVPC---KKHGGVRFTINGR--DYFELVLISNvGGAGSIQSVSIK--GSkTGWMAMSRNWGANWQS 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 26449323  155 DKVPTG-ALQFKFTVTggyDGKTVWSKRVLPANWNSGRIYDAGVQ 198
Cdd:PLN00193 214 NAYLDGqSLSFKVTTT---DGQTRFFLNVVPANWGFGQTFSSSVQ 255
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 11-89 3.47e-12

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: 59.91  E-value: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323    11 AAAIPSIYKDGAGCGACFQVRC--------KNPKLC---NSKGTIVMVTDLNTS-NQTDLVLSSRAFRAMAKPvvgvdky 78
Cdd:pfam03330   1 AAGSASLYNNGTACGECYDVRCltaahptlPFGTYCrvlSGRSVIVRITDRGPFpPGRHFDLSGAAFEKLAMP------- 73

                          90
                  ....*....|.
gi 26449323    79 llKQGIVDVEY 89
Cdd:pfam03330  74 --RAGIVPVQY 82
DPBB_EG45-like cd22269
double-psi beta-barrel fold of EG45-like domain-containing proteins; This family contains ...
 10-90 2.27e-11

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: 58.41  E-value: 2.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323  10 IAAAIPSIYKDGAGCGACFQVRC-----KNPKLCNSKGTIVMVTDL-NTSNQTDLVLSSRAFRAMAKPVVGVdkyllkqg 83
Cdd:cd22269  29 FAAAGDALWDNGAACGRRYRVRCiggtnPGPRPCTGGSVVVKIVDYcPGCCGATFDLSQEAFAKIADPDAGR-------- 100


                ....*..
gi 26449323  84 iVDVEYQ 90
Cdd:cd22269 101 -INIEYV 106
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 11-94 2.72e-09

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: 53.37  E-value: 2.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323  11 AAAIPSIYKDGAGCGACFQVRCKN---PKLCNSKGTIVMVTDL---NTSNQTD-----------LVLSSRAFRAMAKPvv 73
Cdd:cd22274  38 AALSTALFNDGASCGACYEIRCVDdpsPCCPGGPSITVTATNFcppNYALPSDnggwcnpprehFDLSQPAFLKIAQY-- 115

                        90       100
                ....*....|....*....|.
gi 26449323  74 gvdkyllKQGIVDVEYQRVPC 94
Cdd:cd22274 116 -------KAGIVPVQYRRVPC 129
PLN03024 PLN03024
Putative EG45-like domain containing protein 1; Provisional
 10-75 6.59e-07

Putative EG45-like domain containing protein 1; Provisional


Pssm-ID: 178595  Cd Length: 125  Bit Score: 46.95  E-value: 6.59e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26449323   10 IAAAIPSIYKDGAGCGACFQVRCKNPK-----LCNSKGTIVMVTD-LNTSNQTDLVLSSRAFRAMAKPVVGV 75
Cdd:PLN03024  47 IAAASDSLWNNGRVCGKMFTVKCKGPRnavphPCTGKSVTVKIVDhCPSGCASTLDLSREAFAQIANPVAGI 118
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 11-51 7.10e-06

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: 42.82  E-value: 7.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 26449323     11 AAAIPSIYKDGAGCGACFQVRC-KNPKLCNSKGTIVmVTDLN 51
Cdd:smart00837   2 AALSTALFNNGASCGACYEIMCvDSPKWCKPGGSIT-VTATN 42
DPBB_EXLX1-like cd22272
N-terminal double-psi beta-barrel fold domain of bacterial expansins similar to Bacillus ...
 8-90 2.02e-04

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: 39.09  E-value: 2.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   8 GHIAAAIPSIYKDGAGCGACFQVRcknpklcNSKGTI-VMVTDL-NTSNQTDLVLSSRAFRAMAKPvvgvdkyllKQGIV 85
Cdd:cd22272  27 RMIAALNTADYNGSAACGACLEVT-------GPKGTVvVQVVDRcPECAPGDLDLSEEAFAKIADP---------SAGRV 90


                ....*
gi 26449323  86 DVEYQ 90
Cdd:cd22272  91 PITWR 95
DPBB_RlpA_EXP_N-like cd22191
double-psi beta-barrel fold of RlpA, N-terminal domain of expansins, and similar domains; The ...
 9-89 2.77e-03

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: 35.71  E-value: 2.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26449323   9 HIAAAIPSIYKDGAGCGACFQVRCKnpklcNSKGTIVMVTDLNTS-NQTDLVLSSRAFRAMAKPvvgvdkylLKQGIVDV 87
Cdd:cd22191  24 LVVALSAALFDSGPLCGKCIRITYN-----DGKTVTATVVDECPGcGPGDLDLSPAAFQALAGD--------LDGGVIPV 90


                ..
gi 26449323  88 EY 89
Cdd:cd22191  91 TW 92
 
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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