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Conserved domains on  [gi|2156426651|ref|WP_230324878|]
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hypothetical protein [Bacteroides clarus]

Protein Classification

cadherin repeat domain-containing protein( domain architecture ID 736143)

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

CATH:  2.60.40.60
Gene Ontology:  GO:0005509
PubMed:  28268172
SCOP:  4007535

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CBM_SusE-F_like super family cl28889
carbohydrate-binding modules from Bacteroides thetaiotaomicron SusE, SusF and similar proteins; ...
477-563 3.90e-05

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.


The actual alignment was detected with superfamily member cd12967:

Pssm-ID: 475118  Cd Length: 91  Bit Score: 42.66  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156426651 477 GTAQSWQPESALPLVRVGDSFVYEGTCYV-----------FSWAGDiafiltnptgntkvelpNENFDANSSVLSGNPTH 545
Cdd:cd12967     6 GNYQGWNPATAPALYSPNGDGKYEGYVYLpgnfefkfttaPNWDGD-----------------YGGDGGGGGLLDGGGGN 68
                          90
                  ....*....|....*...
gi 2156426651 546 FSLPTTeGYYKISVDLKE 563
Cdd:cd12967    69 IKAPEA-GYYKVTVDLND 85
 
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 ...
477-563 3.90e-05

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: 42.66  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156426651 477 GTAQSWQPESALPLVRVGDSFVYEGTCYV-----------FSWAGDiafiltnptgntkvelpNENFDANSSVLSGNPTH 545
Cdd:cd12967     6 GNYQGWNPATAPALYSPNGDGKYEGYVYLpgnfefkfttaPNWDGD-----------------YGGDGGGGGLLDGGGGN 68
                          90
                  ....*....|....*...
gi 2156426651 546 FSLPTTeGYYKISVDLKE 563
Cdd:cd12967    69 IKAPEA-GYYKVTVDLND 85
 
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 ...
477-563 3.90e-05

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: 42.66  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2156426651 477 GTAQSWQPESALPLVRVGDSFVYEGTCYV-----------FSWAGDiafiltnptgntkvelpNENFDANSSVLSGNPTH 545
Cdd:cd12967     6 GNYQGWNPATAPALYSPNGDGKYEGYVYLpgnfefkfttaPNWDGD-----------------YGGDGGGGGLLDGGGGN 68
                          90
                  ....*....|....*...
gi 2156426651 546 FSLPTTeGYYKISVDLKE 563
Cdd:cd12967    69 IKAPEA-GYYKVTVDLND 85
 
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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