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Conserved domains on  [gi|1033842012|gb|ANH82865|]
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hypothetical protein A8C56_19410 [Niabella ginsenosidivorans]

Protein Classification

cadherin repeat domain-containing protein( domain architecture ID 10626330)

cadherin repeat domain-containing protein similar to cadherins, which are calcium-dependent cell adhesion proteins that preferentially interact with themselves in connecting cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBM_SusE-F_like_u1 cd12967
Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily ...
 154-241 1.53e-28

Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily includes starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.


:

Pssm-ID: 240566  Cd Length: 91  Bit Score: 105.84  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 154 YVPGAYQGWEPSTADSLISATGNGIYTGTILFtPGNLEFKITPAKSWDIAYGDAGDGNISTSASA-NLVAPGAGSYQITA 232
Cdd:cd12967     3 YVPGNYQGWNPATAPALYSPNGDGKYEGYVYL-PGNFEFKFTTAPNWDGDYGGDGGGGGLLDGGGgNIKAPEAGYYKVTV 81


                  ....*....
gi 1033842012 233 NFNDNTYSI 241
Cdd:cd12967    82 DLNDLTYSL 90
CBM_SusE-F_like cd12956
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; ...
 246-332 2.15e-15

carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; This group includes five starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins contain an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. CBM-Fa (the CBM unique to SusF), does not bind insoluble starch; CBM-Fb and CBM-Fc both do, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. CBM-Ec has an additional starch-binding loop that may mediate interactions with partially unwound single helical forms of starch or small starch-breakdown products. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.


:

Pssm-ID: 240562  Cd Length: 93  Bit Score: 70.47  E-value: 2.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 246 WSIIGDATAGGWNADTDMKF--NNGDSTWSVVAALTAGGSVKFRYNHDWGVNYGGSAGT---LKLNGDNIPITTTGTYSI 320
Cdd:cd12956     2 WGIVGSATPNGWDGPPDKPFtyDATDGTFVSYATLAGDGEIKFRPNNDWGENYGDDGDDgtfLSSGGDNIAVSAGGTYKI 81

                          90
                  ....*....|..
gi 1033842012 321 KMDLPHLKYTIT 332
Cdd:cd12956    82 TLNLNNNTYTIE 93
SusE pfam14292
SusE outer membrane protein; This family includes the SusE outer membrane protein from ...
 20-129 1.04e-08

SusE outer membrane protein; This family includes the SusE outer membrane protein from Bacteroides thetaiotaomicron. This protein has a role in starch utilization, but is not essential for growth on starch.


:

Pssm-ID: 433843  Cd Length: 106  Bit Score: 52.40  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012  20 KKDETKVIMNSNTPVLSSDLDKpLVLLQDNKDQPALTFTYDDIDLGFKDALSYILQISVAGHDFKSDSLIEldlDRKALK 99
Cdd:pfam14292   1 DDEDKVYLKSEPAPTLTAPADN-VVLDLENASADAVTFTWTAADYGYPAAVTYTVQFDKDGGDFSSPVDLG---GTTSTS 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1033842012 100 KTFTAQELNLLLLKEFLPPGKTGNYEFRIR 129
Cdd:pfam14292  77 LSITVEELNTLLLNLGLEPGETGELYFRVK 106
 
Name Accession Description Interval E-value
CBM_SusE-F_like_u1 cd12967
Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily ...
 154-241 1.53e-28

Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily includes starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.


Pssm-ID: 240566  Cd Length: 91  Bit Score: 105.84  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 154 YVPGAYQGWEPSTADSLISATGNGIYTGTILFtPGNLEFKITPAKSWDIAYGDAGDGNISTSASA-NLVAPGAGSYQITA 232
Cdd:cd12967     3 YVPGNYQGWNPATAPALYSPNGDGKYEGYVYL-PGNFEFKFTTAPNWDGDYGGDGGGGGLLDGGGgNIKAPEAGYYKVTV 81


                  ....*....
gi 1033842012 233 NFNDNTYSI 241
Cdd:cd12967    82 DLNDLTYSL 90
CBM_SusE-F_like cd12956
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; ...
 246-332 2.15e-15

carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; This group includes five starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins contain an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. CBM-Fa (the CBM unique to SusF), does not bind insoluble starch; CBM-Fb and CBM-Fc both do, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. CBM-Ec has an additional starch-binding loop that may mediate interactions with partially unwound single helical forms of starch or small starch-breakdown products. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.


Pssm-ID: 240562  Cd Length: 93  Bit Score: 70.47  E-value: 2.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 246 WSIIGDATAGGWNADTDMKF--NNGDSTWSVVAALTAGGSVKFRYNHDWGVNYGGSAGT---LKLNGDNIPITTTGTYSI 320
Cdd:cd12956     2 WGIVGSATPNGWDGPPDKPFtyDATDGTFVSYATLAGDGEIKFRPNNDWGENYGDDGDDgtfLSSGGDNIAVSAGGTYKI 81

                          90
                  ....*....|..
gi 1033842012 321 KMDLPHLKYTIT 332
Cdd:cd12956    82 TLNLNNNTYTIE 93
SusE pfam14292
SusE outer membrane protein; This family includes the SusE outer membrane protein from ...
 20-129 1.04e-08

SusE outer membrane protein; This family includes the SusE outer membrane protein from Bacteroides thetaiotaomicron. This protein has a role in starch utilization, but is not essential for growth on starch.


Pssm-ID: 433843  Cd Length: 106  Bit Score: 52.40  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012  20 KKDETKVIMNSNTPVLSSDLDKpLVLLQDNKDQPALTFTYDDIDLGFKDALSYILQISVAGHDFKSDSLIEldlDRKALK 99
Cdd:pfam14292   1 DDEDKVYLKSEPAPTLTAPADN-VVLDLENASADAVTFTWTAADYGYPAAVTYTVQFDKDGGDFSSPVDLG---GTTSTS 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1033842012 100 KTFTAQELNLLLLKEFLPPGKTGNYEFRIR 129
Cdd:pfam14292  77 LSITVEELNTLLLNLGLEPGETGELYFRVK 106
 
Name Accession Description Interval E-value
CBM_SusE-F_like_u1 cd12967
Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily ...
 154-241 1.53e-28

Uncharacterized subgroup of the CBM-SusE-F_like superfamily; The CBM SusE-F_like superfamily includes starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.


Pssm-ID: 240566  Cd Length: 91  Bit Score: 105.84  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 154 YVPGAYQGWEPSTADSLISATGNGIYTGTILFtPGNLEFKITPAKSWDIAYGDAGDGNISTSASA-NLVAPGAGSYQITA 232
Cdd:cd12967     3 YVPGNYQGWNPATAPALYSPNGDGKYEGYVYL-PGNFEFKFTTAPNWDGDYGGDGGGGGLLDGGGgNIKAPEAGYYKVTV 81


                  ....*....
gi 1033842012 233 NFNDNTYSI 241
Cdd:cd12967    82 DLNDLTYSL 90
CBM_SusE-F_like cd12956
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; ...
 246-332 2.15e-15

carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; This group includes five starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins contain an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. CBM-Fa (the CBM unique to SusF), does not bind insoluble starch; CBM-Fb and CBM-Fc both do, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. CBM-Ec has an additional starch-binding loop that may mediate interactions with partially unwound single helical forms of starch or small starch-breakdown products. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.


Pssm-ID: 240562  Cd Length: 93  Bit Score: 70.47  E-value: 2.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 246 WSIIGDATAGGWNADTDMKF--NNGDSTWSVVAALTAGGSVKFRYNHDWGVNYGGSAGT---LKLNGDNIPITTTGTYSI 320
Cdd:cd12956     2 WGIVGSATPNGWDGPPDKPFtyDATDGTFVSYATLAGDGEIKFRPNNDWGENYGDDGDDgtfLSSGGDNIAVSAGGTYKI 81

                          90
                  ....*....|..
gi 1033842012 321 KMDLPHLKYTIT 332
Cdd:cd12956    82 TLNLNNNTYTIE 93
SusE pfam14292
SusE outer membrane protein; This family includes the SusE outer membrane protein from ...
 20-129 1.04e-08

SusE outer membrane protein; This family includes the SusE outer membrane protein from Bacteroides thetaiotaomicron. This protein has a role in starch utilization, but is not essential for growth on starch.


Pssm-ID: 433843  Cd Length: 106  Bit Score: 52.40  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012  20 KKDETKVIMNSNTPVLSSDLDKpLVLLQDNKDQPALTFTYDDIDLGFKDALSYILQISVAGHDFKSDSLIEldlDRKALK 99
Cdd:pfam14292   1 DDEDKVYLKSEPAPTLTAPADN-VVLDLENASADAVTFTWTAADYGYPAAVTYTVQFDKDGGDFSSPVDLG---GTTSTS 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1033842012 100 KTFTAQELNLLLLKEFLPPGKTGNYEFRIR 129
Cdd:pfam14292  77 LSITVEELNTLLLNLGLEPGETGELYFRVK 106
CBM_SusE-F_like cd12956
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; ...
 151-241 4.03e-08

carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; This group includes five starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins contain an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. CBM-Fa (the CBM unique to SusF), does not bind insoluble starch; CBM-Fb and CBM-Fc both do, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. CBM-Ec has an additional starch-binding loop that may mediate interactions with partially unwound single helical forms of starch or small starch-breakdown products. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.


Pssm-ID: 240562  Cd Length: 93  Bit Score: 50.44  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 151 AWAYVPGAYQ-GWEPSTADSLISATGNGIYTGTILFTpGNLEFKITPAKSWDIAYGDAGDGNISTSA-SANLVAPGAGSY 228
Cdd:cd12956     1 TWGIVGSATPnGWDGPPDKPFTYDATDGTFVSYATLA-GDGEIKFRPNNDWGENYGDDGDDGTFLSSgGDNIAVSAGGTY 79

                          90
                  ....*....|...
gi 1033842012 229 QITANFNDNTYSI 241
Cdd:cd12956    80 KITLNLNNNTYTI 92
X25_BaPul_like cd12962
X25 domain of Bacillus acidopullulyticus pullulanase and similar proteins; Pullulanase (EC 3.2. ...
 155-241 8.44e-06

X25 domain of Bacillus acidopullulyticus pullulanase and similar proteins; Pullulanase (EC 3.2.1.41) cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. BaPul is used industrially in the production of high fructose corn syrup, high maltose content syrups and low calorie and ''light'' beers. Pullulanases, in addition to the catalytic domain, include several carbohydrate-binding domains (CBMs) as well as domains of unknown function (termed ''X'' modules). X25 was identified in Bacillus acidopullulyticus pullulanase, and splits another domain of unknown function (X45). X25 is present in multiple copy in some pullulanases. It has been suggested that X25 and X45 are CBMs which target mixed alpha-1,6/alpha-1,4 linked D-glucan polysaccharides.


Pssm-ID: 240568 [Multi-domain]  Cd Length: 95  Bit Score: 43.77  E-value: 8.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 155 VPGAYQG-------WEPSTADSLISATGN-GIYTGTILFTPGNLEFKITPAKSWDIAYGDAG---DGNIStsasanLVAP 223
Cdd:cd12962     4 LVGSFQSelgcagdWDPDCLATQLTDDGNdGVYTFTTTLPAGDYEYKVALNGSWDENYGAGGapdGANIP------LTLP 77

                          90
                  ....*....|....*...
gi 1033842012 224 GAGSYQITanFNDNTYSI 241
Cdd:cd12962    78 AGAEVTFT--YDPATHEV 93
CBM-Eb_CBM-Fb cd12965
carbohydrate-binding modules Eb and Fb from SusE and SusF, respectively, and similar CBMs; ...
 248-332 1.37e-05

carbohydrate-binding modules Eb and Fb from SusE and SusF, respectively, and similar CBMs; Included in this subgroup are CBM-Eb and CBM-Fb, starch-specific carbohydrate-binding modules of SusE and SusF, cell surface lipoproteins within the Sus (Starch-utilization system)system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they contribute differently to binding insoluble starch. CBM-Fb and CBM-Fc both bind insoluble starch, deletion of one or the other results in a decrease in the overall affinity of SusF for starch. Both CBM-Eb and CBM-Ec are needed for SusE to bind tightly to starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.


Pssm-ID: 240564  Cd Length: 98  Bit Score: 43.10  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 248 IIGDAtAGGWNADTDMKF---NNGDSTWSVVAALTAGGSVKFRYNHDWGVNYGGSAGTLK-------LNGDNIPITTTGT 317
Cdd:cd12965     4 MTGSF-FGNWNWDGWKEMtpvNGGDGEFWSIVYFDAGAGFKFNTSKAWDGDFGGFDATIAgeagagvSDGGNIVVANAGW 82

                          90
                  ....*....|....*
gi 1033842012 318 YSIKMDLPHLKYTIT 332
Cdd:cd12965    83 YLVYVTADVYKYTVI 97
E_set_pullulanase_like cd02861
Early set domain associated with the catalytic domain of pullulanase-like proteins; E or ...
 137-231 9.67e-04

Early set domain associated with the catalytic domain of pullulanase-like proteins; E or "early" set domains are associated with the catalytic domain of pullulanase at either the N-terminal or C-terminal end, and in a few instances at both ends. Pullulanase (also called dextrinase or alpha-dextrin endo-1,6-alpha glucosidase) is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. The E set domain of pullulanase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199891 [Multi-domain]  Cd Length: 88  Bit Score: 37.68  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 137 SNVVPLTITTYqaiawaYVPGAYQGWepSTADSLISAtGNGIYTGTILFTPGNLEFKITPAkSW-DIAYGDAGDGNISTS 215
Cdd:cd02861     3 SDEEPFGGTTV------YVRGSMNGW--GEDDALTYQ-GNGVYSVTITLAAGSYEFKVASA-DWsTVNFGSGSSDVLVAT 72

                          90
                  ....*....|....*.
gi 1033842012 216 ASANLVAPGAGSYQIT 231
Cdd:cd02861    73 GTLETLAAGGDNLSLT 88
X25_BaPul_like cd12962
X25 domain of Bacillus acidopullulyticus pullulanase and similar proteins; Pullulanase (EC 3.2. ...
 254-316 1.71e-03

X25 domain of Bacillus acidopullulyticus pullulanase and similar proteins; Pullulanase (EC 3.2.1.41) cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. BaPul is used industrially in the production of high fructose corn syrup, high maltose content syrups and low calorie and ''light'' beers. Pullulanases, in addition to the catalytic domain, include several carbohydrate-binding domains (CBMs) as well as domains of unknown function (termed ''X'' modules). X25 was identified in Bacillus acidopullulyticus pullulanase, and splits another domain of unknown function (X45). X25 is present in multiple copy in some pullulanases. It has been suggested that X25 and X45 are CBMs which target mixed alpha-1,6/alpha-1,4 linked D-glucan polysaccharides.


Pssm-ID: 240568 [Multi-domain]  Cd Length: 95  Bit Score: 37.22  E-value: 1.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033842012 254 AGGW---NADTDMKFNNGDSTWSVVAALTAGG-SVKFRYNHDWGVNYGGSAgtlKLNGDNIPITTTG 316
Cdd:cd12962    15 AGDWdpdCLATQLTDDGNDGVYTFTTTLPAGDyEYKVALNGSWDENYGAGG---APDGANIPLTLPA 78
CBM-Fa cd12964
carbohydrate-binding module Fa from Bacteroides thetaiotaomicron SusE, and similar CBMs; ...
 154-241 1.82e-03

carbohydrate-binding module Fa from Bacteroides thetaiotaomicron SusE, and similar CBMs; CBM-Fa is the first of three starch-specific CBM (carbohydrate-binding modules) of SusF, a cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. The precise mechanistic role of SusF in starch metabolism is unclear. SusF has an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by three tandem starch-binding CBMs: CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus. These CBMs have no enzymatic activity. Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These three CBMs show differences in their affinity for various different starch oligosaccharides, and they contribute differently to binding insoluble starch. CBM-Fa does not bind insoluble starch, and can bind smaller maltooligosaccharides. Proteins in this subgroup are present in the species of the Gram-negative Bacteroidetes phylum.


Pssm-ID: 240563  Cd Length: 110  Bit Score: 37.39  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033842012 154 YVPGAYQGWEPSTADSLI-SATGNGIY---TGTILFTPGNLEFKITPAK------SWDIAYG-------DAGDGNISTSA 216
Cdd:cd12964     3 YLVGDINGWDANNPIKFNhSGKDVYDDpvfTETLTTTASDQYFKIIPASnidaanDWDEALGasavdgdDSAEGFLAWTG 82

                          90       100
                  ....*....|....*....|....*...
gi 1033842012 217 SANLVAP---GAGSYQITANFNDNTYSI 241
Cdd:cd12964    83 SFGVGAGkiaGAGKYKITLNMMDYTYTV 110
 
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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