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Conserved domains on  [gi|156113273|gb|EDO14854|]
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hypothetical protein Kpol_345p2 [Vanderwaltozyma polyspora DSM 70294]

Protein Classification

CBM21 domain-containing protein( domain architecture ID 10505868)

CBM21 domain-containing protein carries a family 21 carbohydrate-binding module (CBM21), such as found in many eukaryotic proteins involved in glycogen metabolism, which might mediate interactions with glycogen; similar to regulatory subunits 3A, 3B, 3C, 3E, 3F, and 3G of protein phosphatase 1

Gene Ontology:  GO:0005515
PubMed:  16262690
SCOP:  4007352

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBM_21 pfam03370
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 240-354 4.98e-24

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


:

Pssm-ID: 427265  Cd Length: 112  Bit Score: 97.31  E-value: 4.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156113273  240 YLNNQNIRLHSLKQLPNETdKIYGLIYVNNLNFEKFIEIKFSFNNWQDIHYVTASFNKSINS-----NIDEFKFVIDLNS 314
Cdd:pfam03370   1 RLQGQPVCLERLFLSDDKK-SLVGTVRVKNLAFEKRVAVRYTFDNWKTISDVPAEYVPDARSsldgdNYDRFKFKIPLPP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 156113273  315 LKYTLQFKgliyndfnsnspitncnlnVNLCCRYDVNNET 354
Cdd:pfam03370  80 LLNLEGKT-------------------LEFCIRYEVNGQE 100
 
Name Accession Description Interval E-value
CBM_21 pfam03370
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 240-354 4.98e-24

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


Pssm-ID: 427265  Cd Length: 112  Bit Score: 97.31  E-value: 4.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156113273  240 YLNNQNIRLHSLKQLPNETdKIYGLIYVNNLNFEKFIEIKFSFNNWQDIHYVTASFNKSINS-----NIDEFKFVIDLNS 314
Cdd:pfam03370   1 RLQGQPVCLERLFLSDDKK-SLVGTVRVKNLAFEKRVAVRYTFDNWKTISDVPAEYVPDARSsldgdNYDRFKFKIPLPP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 156113273  315 LKYTLQFKgliyndfnsnspitncnlnVNLCCRYDVNNET 354
Cdd:pfam03370  80 LLNLEGKT-------------------LEFCIRYEVNGQE 100
 
Name Accession Description Interval E-value
CBM_21 pfam03370
Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic ...
 240-354 4.98e-24

Carbohydrate/starch-binding module (family 21); This family consists of several eukaryotic proteins that are thought to be involved in the regulation of glycogen metabolism. For instance, the mouse PTG protein has been shown to interact with glycogen synthase, phosphorylase kinase, phosphorylase a: these three enzymes have key roles in the regulation of glycogen metabolism. PTG also binds the catalytic subunit of protein phosphatase 1 (PP1C) and localizes it to glycogen. Subsets of similar interactions have been observed with several other members of this family, such as the yeast PIG1, PIG2, GAC1 and GIP2 proteins. While the precise function of these proteins is not known, they may serve a scaffold function, bringing together the key enzymes in glycogen metabolism. This family is a carbohydrate binding domain.


Pssm-ID: 427265  Cd Length: 112  Bit Score: 97.31  E-value: 4.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156113273  240 YLNNQNIRLHSLKQLPNETdKIYGLIYVNNLNFEKFIEIKFSFNNWQDIHYVTASFNKSINS-----NIDEFKFVIDLNS 314
Cdd:pfam03370   1 RLQGQPVCLERLFLSDDKK-SLVGTVRVKNLAFEKRVAVRYTFDNWKTISDVPAEYVPDARSsldgdNYDRFKFKIPLPP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 156113273  315 LKYTLQFKgliyndfnsnspitncnlnVNLCCRYDVNNET 354
Cdd:pfam03370  80 LLNLEGKT-------------------LEFCIRYEVNGQE 100
 
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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