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Conserved domains on  [gi|488854229|ref|WP_002766539|]
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MULTISPECIES: hypothetical protein [Microcystis]

Protein Classification

BMC domain-containing protein( domain architecture ID 10162515)

BMC (Bacterial Micro-Compartment) domain-containing protein similar to Clostridium difficile EutS protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BMC_like_1_repeat1 cd07051
Bacterial Micro-Compartment (BMC)-like domain 1 repeat 1; BMC-like domains exist in ...
4-114 1.41e-63

Bacterial Micro-Compartment (BMC)-like domain 1 repeat 1; BMC-like domains exist in cyanobacteria, proteobacteria, and actinobacteria and are homologs of the carboxysome shell proteins. They might be encoded from putative organelles involved in unknown metabolic process. Although it has been suggested that these carboxysome shell protein homologs form hexamers and further assemble into the flat facets of the polyhedral bacterial organelles shell at present no experimental evidence exists to directly support this view. Proteins in this CD contain two tandem BMC domains. This CD includes repeat 1 (the first BMC domain of BMC like 1 proteins).


:

Pssm-ID: 132891  Cd Length: 111  Bit Score: 192.51  E-value: 1.41e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488854229   4 ELRSYVYLDNLQLQHAAYIGTVAQGFLPLPGDASLWIEISPGIEINRITDIALKSAVVRPGVLFVERLYGLLELHSSSQG 83
Cdd:cd07051    1 ELRTYVFIDRLQPQLAAYMGTVSQGFLPVAGDASLWIEVAPGLAIHRVTDIALKAANVRPGVQVVERQFGLLELHSRSQS 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488854229  84 EVRAAGQAILQYLGVSQRDCLKPQIVSSQII 114
Cdd:cd07051   81 EVLAAGDAVLDALGLTEEDRLKPKILSSQII 111
BMC_like_1_repeat2 cd07052
Bacterial Micro-Compartment (BMC)-like domain 1 repeat 2; BMC-like domains exist in ...
121-199 1.47e-34

Bacterial Micro-Compartment (BMC)-like domain 1 repeat 2; BMC-like domains exist in cyanobacteria, proteobacteria, and actinobacteria and are homologs of the carboxysome shell proteins. They might be encoded from putative organelles involved in unknown metabolic process. Although it has been suggested that these carboxysome shell protein homologs form hexamers and further assemble into the flat facets of the polyhedral bacterial organelles shell at present no experimental evidence exists to directly support this view. Proteins in this CD contain two tandem BMC domains. This CD includes repeat 2 (the second BMC domain of BMC like 1 proteins).


:

Pssm-ID: 132892  Cd Length: 79  Bit Score: 117.82  E-value: 1.47e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488854229 121 QAQLINRSSRGMMLMAGQTLYVLEVQPAAYASLAANQAEKAALINILHVTSVGSFGRLYLGGEERDIIAGSRAAVSALE 199
Cdd:cd07052    1 HAQLINRNRRGSMLLPGQSLFVLEVEPAAYASLAANEAEKAAPITLVDVRMVGAFGRLYLSGTEADVRAARDAAIAALE 79
 
Name Accession Description Interval E-value
BMC_like_1_repeat1 cd07051
Bacterial Micro-Compartment (BMC)-like domain 1 repeat 1; BMC-like domains exist in ...
4-114 1.41e-63

Bacterial Micro-Compartment (BMC)-like domain 1 repeat 1; BMC-like domains exist in cyanobacteria, proteobacteria, and actinobacteria and are homologs of the carboxysome shell proteins. They might be encoded from putative organelles involved in unknown metabolic process. Although it has been suggested that these carboxysome shell protein homologs form hexamers and further assemble into the flat facets of the polyhedral bacterial organelles shell at present no experimental evidence exists to directly support this view. Proteins in this CD contain two tandem BMC domains. This CD includes repeat 1 (the first BMC domain of BMC like 1 proteins).


Pssm-ID: 132891  Cd Length: 111  Bit Score: 192.51  E-value: 1.41e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488854229   4 ELRSYVYLDNLQLQHAAYIGTVAQGFLPLPGDASLWIEISPGIEINRITDIALKSAVVRPGVLFVERLYGLLELHSSSQG 83
Cdd:cd07051    1 ELRTYVFIDRLQPQLAAYMGTVSQGFLPVAGDASLWIEVAPGLAIHRVTDIALKAANVRPGVQVVERQFGLLELHSRSQS 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488854229  84 EVRAAGQAILQYLGVSQRDCLKPQIVSSQII 114
Cdd:cd07051   81 EVLAAGDAVLDALGLTEEDRLKPKILSSQII 111
BMC_like_1_repeat2 cd07052
Bacterial Micro-Compartment (BMC)-like domain 1 repeat 2; BMC-like domains exist in ...
121-199 1.47e-34

Bacterial Micro-Compartment (BMC)-like domain 1 repeat 2; BMC-like domains exist in cyanobacteria, proteobacteria, and actinobacteria and are homologs of the carboxysome shell proteins. They might be encoded from putative organelles involved in unknown metabolic process. Although it has been suggested that these carboxysome shell protein homologs form hexamers and further assemble into the flat facets of the polyhedral bacterial organelles shell at present no experimental evidence exists to directly support this view. Proteins in this CD contain two tandem BMC domains. This CD includes repeat 2 (the second BMC domain of BMC like 1 proteins).


Pssm-ID: 132892  Cd Length: 79  Bit Score: 117.82  E-value: 1.47e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488854229 121 QAQLINRSSRGMMLMAGQTLYVLEVQPAAYASLAANQAEKAALINILHVTSVGSFGRLYLGGEERDIIAGSRAAVSALE 199
Cdd:cd07052    1 HAQLINRNRRGSMLLPGQSLFVLEVEPAAYASLAANEAEKAAPITLVDVRMVGAFGRLYLSGTEADVRAARDAAIAALE 79
BMC smart00877
Bacterial microcompartments are primitive organelles composed entirely of protein subunits; ...
139-205 6.68e-08

Bacterial microcompartments are primitive organelles composed entirely of protein subunits; The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. These proteins for hexameric structure.


Pssm-ID: 197945  Cd Length: 75  Bit Score: 47.95  E-value: 6.68e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488854229   139 TLYVLEVQPAAYASLAANQAEKAALINILHVTSVGSF-GRLYLGGEERDIIAGSRAAVSALENIQGRA 205
Cdd:smart00877   1 ALGIIETRGAAAAIEAADAALKAANVELVGYESIGGGkVTVIITGDVAAVRAAVEAGLEAAERLGLVS 68
 
Name Accession Description Interval E-value
BMC_like_1_repeat1 cd07051
Bacterial Micro-Compartment (BMC)-like domain 1 repeat 1; BMC-like domains exist in ...
4-114 1.41e-63

Bacterial Micro-Compartment (BMC)-like domain 1 repeat 1; BMC-like domains exist in cyanobacteria, proteobacteria, and actinobacteria and are homologs of the carboxysome shell proteins. They might be encoded from putative organelles involved in unknown metabolic process. Although it has been suggested that these carboxysome shell protein homologs form hexamers and further assemble into the flat facets of the polyhedral bacterial organelles shell at present no experimental evidence exists to directly support this view. Proteins in this CD contain two tandem BMC domains. This CD includes repeat 1 (the first BMC domain of BMC like 1 proteins).


Pssm-ID: 132891  Cd Length: 111  Bit Score: 192.51  E-value: 1.41e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488854229   4 ELRSYVYLDNLQLQHAAYIGTVAQGFLPLPGDASLWIEISPGIEINRITDIALKSAVVRPGVLFVERLYGLLELHSSSQG 83
Cdd:cd07051    1 ELRTYVFIDRLQPQLAAYMGTVSQGFLPVAGDASLWIEVAPGLAIHRVTDIALKAANVRPGVQVVERQFGLLELHSRSQS 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488854229  84 EVRAAGQAILQYLGVSQRDCLKPQIVSSQII 114
Cdd:cd07051   81 EVLAAGDAVLDALGLTEEDRLKPKILSSQII 111
BMC_like_1_repeat2 cd07052
Bacterial Micro-Compartment (BMC)-like domain 1 repeat 2; BMC-like domains exist in ...
121-199 1.47e-34

Bacterial Micro-Compartment (BMC)-like domain 1 repeat 2; BMC-like domains exist in cyanobacteria, proteobacteria, and actinobacteria and are homologs of the carboxysome shell proteins. They might be encoded from putative organelles involved in unknown metabolic process. Although it has been suggested that these carboxysome shell protein homologs form hexamers and further assemble into the flat facets of the polyhedral bacterial organelles shell at present no experimental evidence exists to directly support this view. Proteins in this CD contain two tandem BMC domains. This CD includes repeat 2 (the second BMC domain of BMC like 1 proteins).


Pssm-ID: 132892  Cd Length: 79  Bit Score: 117.82  E-value: 1.47e-34
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488854229 121 QAQLINRSSRGMMLMAGQTLYVLEVQPAAYASLAANQAEKAALINILHVTSVGSFGRLYLGGEERDIIAGSRAAVSALE 199
Cdd:cd07052    1 HAQLINRNRRGSMLLPGQSLFVLEVEPAAYASLAANEAEKAAPITLVDVRMVGAFGRLYLSGTEADVRAARDAAIAALE 79
BMC cd06169
Bacterial Micro-Compartment (BMC) domain; Bacterial micro-compartments are primitive ...
36-96 6.55e-08

Bacterial Micro-Compartment (BMC) domain; Bacterial micro-compartments are primitive protein-based organelles that sequester specific metabolic pathways in bacterial cells. The prototypical bacterial microcompartment is the carboxysome shell, a bacterial polyhedral organelle which increase the efficiency of CO2 fixation by encapsulating RuBisCO and carbonic anhydrase. They can be divided into two types: alpha-type carboxysomes (alpha-cyanobacteria and proteobacteria) and beta-type carboxysomes (beta-cyanobacteria). In addition to these proteins there are several homologous shell proteins including those found in pdu organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol and eut organelles involved in the cobalamin-dependent degradation of ethanolamine. Structure evidence shows that several carboxysome shell proteins and their homologs (Csos1A, CcmK1,2,4, and PduU) exist as hexamers which might further assemble into extended, tightly packed layers hypothesized to represent the flat facets of the polyhedral organelles outer shell. Although it has been suggested that other homologous proteins in this family might also form hexamers and play similar functional roles in the construction of their corresponding organelle outer shell at present no experimental evidence directly supports this view.


Pssm-ID: 132884  Cd Length: 62  Bit Score: 47.64  E-value: 6.55e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488854229  36 ASLWIEISPGIEINRITDIALKSAVVRPGVLFVER--LYGLLELHSSSqGEVRAAGQAILQYL 96
Cdd:cd06169    1 ALGLLEVRGLAAAIVAADAAVKAADVELVGIERAGggGLVTLIIRGDV-SAVKAAVEAAEQAA 62
BMC smart00877
Bacterial microcompartments are primitive organelles composed entirely of protein subunits; ...
139-205 6.68e-08

Bacterial microcompartments are primitive organelles composed entirely of protein subunits; The prototypical bacterial microcompartment is the carboxysome, a protein shell for sequestering carbon fixation reactions. These proteins for hexameric structure.


Pssm-ID: 197945  Cd Length: 75  Bit Score: 47.95  E-value: 6.68e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488854229   139 TLYVLEVQPAAYASLAANQAEKAALINILHVTSVGSF-GRLYLGGEERDIIAGSRAAVSALENIQGRA 205
Cdd:smart00877   1 ALGIIETRGAAAAIEAADAALKAANVELVGYESIGGGkVTVIITGDVAAVRAAVEAGLEAAERLGLVS 68
 
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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