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Conserved domains on  [gi|40739414|gb|EAA58604|]
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hypothetical protein AN6786.2 [Aspergillus nidulans FGSC A4]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DPBB_GH45_endoglucanase cd22278
double-psi beta-barrel fold of glycoside hydrolase family 45 endoglucanase EG27II and similar ...
 28-165 7.82e-30

double-psi beta-barrel fold of glycoside hydrolase family 45 endoglucanase EG27II and similar proteins; This group is made up of endoglucanases from mollusks similar to Ampullaria crossean endoglucanase EG27II, a glycoside hydrolase family 45 (GH45) subfamily B protein. 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. GH45 endoglucanases from mollusks adopt a double-psi beta-barrel (DPBB) fold.


:

Pssm-ID: 439258  Cd Length: 143  Bit Score: 108.72  E-value: 7.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414  28 ASSSCPGYHNC---ACGCGNKIGTYDWSYGIANkvYTAAANQALFDSGPNDathWCGNGCGKCYRLTSTGVSTCEtcGAG 104
Cdd:cd22278   1 GCASTTRYTDChkgACGCGGKSGDTQFGWNLGY--YTAAINQAAFDSGSGL---WCGQACGRCYQLTPTGGPYPG--GGP 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414 105 GEQGKSIVVMVTNLCPFKGNERWCPNP--GQLNPHGYAYHFDIMGGAGVFG-------DNVVVEFEEVPC 165
Cdd:cd22278  74 PPAGQSIVVMVTNLCPDGGNNEWCGQTgtNPTNQHGYEFHFDLAIPGGQVTaffflgwDNPEVTFEEVSC 143
 
Name Accession Description Interval E-value
DPBB_GH45_endoglucanase cd22278
double-psi beta-barrel fold of glycoside hydrolase family 45 endoglucanase EG27II and similar ...
 28-165 7.82e-30

double-psi beta-barrel fold of glycoside hydrolase family 45 endoglucanase EG27II and similar proteins; This group is made up of endoglucanases from mollusks similar to Ampullaria crossean endoglucanase EG27II, a glycoside hydrolase family 45 (GH45) subfamily B protein. 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. GH45 endoglucanases from mollusks adopt a double-psi beta-barrel (DPBB) fold.


Pssm-ID: 439258  Cd Length: 143  Bit Score: 108.72  E-value: 7.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414  28 ASSSCPGYHNC---ACGCGNKIGTYDWSYGIANkvYTAAANQALFDSGPNDathWCGNGCGKCYRLTSTGVSTCEtcGAG 104
Cdd:cd22278   1 GCASTTRYTDChkgACGCGGKSGDTQFGWNLGY--YTAAINQAAFDSGSGL---WCGQACGRCYQLTPTGGPYPG--GGP 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414 105 GEQGKSIVVMVTNLCPFKGNERWCPNP--GQLNPHGYAYHFDIMGGAGVFG-------DNVVVEFEEVPC 165
Cdd:cd22278  74 PPAGQSIVVMVTNLCPDGGNNEWCGQTgtNPTNQHGYEFHFDLAIPGGQVTaffflgwDNPEVTFEEVSC 143
PLN00193 PLN00193
expansin-A; Provisional
 26-165 6.72e-06

expansin-A; Provisional


Pssm-ID: 215097 [Multi-domain]  Cd Length: 256  Bit Score: 46.06  E-value: 6.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414   26 GGASSScpGYHNCACGCGNkigTYDWSYGiankVYTAAANQALFDSGPNdathwcgngCGKCYRLTSTGVSTCETCgagg 105
Cdd:PLN00193  39 GGSDAS--GTMGGACGYGN---LYSTGYG----TRTAALSTALFNDGAS---------CGQCYRIMCDYQADSRWC---- 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414  106 EQGKSIVVMVTNLCP-----FKGNERWCPNPGQlnphgyayHFDIMGGA----GVF-GDNVVVEFEEVPC 165
Cdd:PLN00193  97 IKGASVTITATNFCPpnyalPNNNGGWCNPPLQ--------HFDMAQPAwekiGIYrGGIVPVLFQRVPC 158
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 61-138 7.10e-04

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: 37.81  E-value: 7.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40739414     61 TAAANQALFDSGpndathwcgNGCGKCYRLtstgvsTCETCGAGGEQGKSIVVMVTNLCPfkgnerwcPNPGQLNPHG 138
Cdd:smart00837   1 TAALSTALFNNG---------ASCGACYEI------MCVDSPKWCKPGGSITVTATNFCP--------PNYALSNDNG 55
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 62-124 5.18e-03

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: 34.87  E-value: 5.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40739414    62 AAANQALFDSGpndathwcgNGCGKCYR---LTSTGVSTCETCGAGGEQGKSIVVMVTNLCPFKGN 124
Cdd:pfam03330   1 AAGSASLYNNG---------TACGECYDvrcLTAAHPTLPFGTYCRVLSGRSVIVRITDRGPFPPG 57
 
Name Accession Description Interval E-value
DPBB_GH45_endoglucanase cd22278
double-psi beta-barrel fold of glycoside hydrolase family 45 endoglucanase EG27II and similar ...
 28-165 7.82e-30

double-psi beta-barrel fold of glycoside hydrolase family 45 endoglucanase EG27II and similar proteins; This group is made up of endoglucanases from mollusks similar to Ampullaria crossean endoglucanase EG27II, a glycoside hydrolase family 45 (GH45) subfamily B protein. 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. GH45 endoglucanases from mollusks adopt a double-psi beta-barrel (DPBB) fold.


Pssm-ID: 439258  Cd Length: 143  Bit Score: 108.72  E-value: 7.82e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414  28 ASSSCPGYHNC---ACGCGNKIGTYDWSYGIANkvYTAAANQALFDSGPNDathWCGNGCGKCYRLTSTGVSTCEtcGAG 104
Cdd:cd22278   1 GCASTTRYTDChkgACGCGGKSGDTQFGWNLGY--YTAAINQAAFDSGSGL---WCGQACGRCYQLTPTGGPYPG--GGP 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414 105 GEQGKSIVVMVTNLCPFKGNERWCPNP--GQLNPHGYAYHFDIMGGAGVFG-------DNVVVEFEEVPC 165
Cdd:cd22278  74 PPAGQSIVVMVTNLCPDGGNNEWCGQTgtNPTNQHGYEFHFDLAIPGGQVTaffflgwDNPEVTFEEVSC 143
DPBB_EXP_N-like cd22271
N-terminal double-psi beta-barrel fold domain of the expansin family and similar domains; The ...
 33-165 4.94e-08

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: 49.68  E-value: 4.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414  33 PGYHNCACGcgnkigtYDWSYGIANKVYTAAANQALFDSGpndathwcgNGCGKCYRLTSTGVSTCetcgaggeQGKSIV 112
Cdd:cd22271  11 PDLSGGACG-------YGPLPPPPGGGFVAALNPALYDNG---------AGCGACYEVTCPGSPCC--------SGGSVV 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 40739414 113 VMVTNLCPFkgnerwCPNPGQLNPHGYAYHFDIMGGAGVFGdnvvVEFEEVPC 165
Cdd:cd22271  67 VMVTDSCPE------CGDAGHFDLSPDAFAALADPSGGIVP----VTWRRVPC 109
DPBB_EXPA_N cd22274
N-terminal double-psi beta-barrel fold domain of the alpha-expansin subfamily; Alpha-expansins ...
 39-138 1.07e-07

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: 49.52  E-value: 1.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414  39 ACGCGNkigTYDWSYGiankVYTAAANQALFDSGpndathwcgNGCGKCYRLTStgVSTCETCGAGGeqgKSIVVMVTNL 118
Cdd:cd22274  22 ACGYGN---LYSQGYG----TNTAALSTALFNDG---------ASCGACYEIRC--VDDPSPCCPGG---PSITVTATNF 80

                        90       100
                ....*....|....*....|
gi 40739414 119 CPfkgnerwcPNPGQLNPHG 138
Cdd:cd22274  81 CP--------PNYALPSDNG 92
PLN00193 PLN00193
expansin-A; Provisional
 26-165 6.72e-06

expansin-A; Provisional


Pssm-ID: 215097 [Multi-domain]  Cd Length: 256  Bit Score: 46.06  E-value: 6.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414   26 GGASSScpGYHNCACGCGNkigTYDWSYGiankVYTAAANQALFDSGPNdathwcgngCGKCYRLTSTGVSTCETCgagg 105
Cdd:PLN00193  39 GGSDAS--GTMGGACGYGN---LYSTGYG----TRTAALSTALFNDGAS---------CGQCYRIMCDYQADSRWC---- 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414  106 EQGKSIVVMVTNLCP-----FKGNERWCPNPGQlnphgyayHFDIMGGA----GVF-GDNVVVEFEEVPC 165
Cdd:PLN00193  97 IKGASVTITATNFCPpnyalPNNNGGWCNPPLQ--------HFDMAQPAwekiGIYrGGIVPVLFQRVPC 158
DPBB_1 smart00837
Rare lipoprotein A (RlpA)-like double-psi beta-barrel; Rare lipoprotein A (RlpA) contains a ...
 61-138 7.10e-04

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: 37.81  E-value: 7.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40739414     61 TAAANQALFDSGpndathwcgNGCGKCYRLtstgvsTCETCGAGGEQGKSIVVMVTNLCPfkgnerwcPNPGQLNPHG 138
Cdd:smart00837   1 TAALSTALFNNG---------ASCGACYEI------MCVDSPKWCKPGGSITVTATNFCP--------PNYALSNDNG 55
DPBB_EXPB_N cd22275
N-terminal double-psi beta-barrel fold domain of the beta-expansin subfamily; Beta-expansins ...
 61-149 3.23e-03

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: 36.45  E-value: 3.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40739414  61 TAAANQALFDSGpndathwcgNGCGKCYRLTSTGVSTCetcgaggeQGKSIVVMVTNLCPFKGNERwcpnpgqlnphgya 140
Cdd:cd22275  36 VSAGNPPIFKDG---------KGCGSCYEVKCTGPPAC--------SGKPVTVVITDECPGGPIAP-------------- 84


                ....*....
gi 40739414 141 YHFDIMGGA 149
Cdd:cd22275  85 YHFDLSGTA 93
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 62-124 5.18e-03

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: 34.87  E-value: 5.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40739414    62 AAANQALFDSGpndathwcgNGCGKCYR---LTSTGVSTCETCGAGGEQGKSIVVMVTNLCPFKGN 124
Cdd:pfam03330   1 AAGSASLYNNG---------TACGECYDvrcLTAAHPTLPFGTYCRVLSGRSVIVRITDRGPFPPG 57
 
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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