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Conserved domains on  [gi|90111439|ref|NP_416952|]
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putative ethanolamine catabolic microcompartment shell protein EutM [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

BMC domain-containing protein( domain architecture ID 10794174)

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
PRK15474 PRK15474
ethanolamine utilization microcompartment protein EutM;
1-97 9.42e-49

ethanolamine utilization microcompartment protein EutM;


:

Pssm-ID: 185371  Cd Length: 97  Bit Score: 149.81  E-value: 9.42e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439   1 MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHG 80
Cdd:PRK15474  1 MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHG 80

                        90
                ....*....|....*..
gi 90111439  81 DLEEVFPIGLKGDSSNL 97
Cdd:PRK15474 81 DLEEVFPIGLKGDSSNL 97
 
Name Accession Description Interval E-value
PRK15474 PRK15474
ethanolamine utilization microcompartment protein EutM;
1-97 9.42e-49

ethanolamine utilization microcompartment protein EutM;


Pssm-ID: 185371  Cd Length: 97  Bit Score: 149.81  E-value: 9.42e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439   1 MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHG 80
Cdd:PRK15474  1 MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHG 80

                        90
                ....*....|....*..
gi 90111439  81 DLEEVFPIGLKGDSSNL 97
Cdd:PRK15474 81 DLEEVFPIGLKGDSSNL 97
CcmK COG4577
Carboxysome shell and ethanolamine utilization microcompartment protein CcmL/EutN [Secondary ...
 1-85 3.65e-35

Carboxysome shell and ethanolamine utilization microcompartment protein CcmL/EutN [Secondary metabolites biosynthesis, transport and catabolism, Energy production and conversion];


Pssm-ID: 443634  Cd Length: 86  Bit Score: 114.82  E-value: 3.65e-35
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439  1 MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHG 80
Cdd:COG4577  2 GKALGLIETKGLAAAIEAADAMLKAANVELVGYEKIGSGKVTVIVRGDVAAVKAAVDAGAAAAERVGELVSSHVIPRPHP 81


               ....*
gi 90111439 81 DLEEV 85
Cdd:COG4577 82 EVEAA 86
BMC_CcmK_like cd07045
Carbon dioxide concentrating mechanism K (CcmK)-like proteins, Bacterial Micro-Compartment ...
 3-86 3.14e-31

Carbon dioxide concentrating mechanism K (CcmK)-like proteins, 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). Potential functional differences between the two types are not yet fully understood. 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 shells at present no experimental evidence directly supports this view.


Pssm-ID: 132885  Cd Length: 84  Bit Score: 104.93  E-value: 3.14e-31
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439  3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHGDL 82
Cdd:cd07045  1 ALGLIETRGLVAAIEAADAALKAANVTLVGYEKVGGGLVTVKITGDVAAVKAAVEAGAAAAERIGELVSSHVIPRPHDEV 80


               ....
gi 90111439 83 EEVF 86
Cdd:cd07045 81 EKIL 84
BMC pfam00936
BMC domain; Bacterial microcompartments are primitive organelles composed entirely of protein ...
 3-76 1.15e-24

BMC domain; 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: 425954 [Multi-domain]  Cd Length: 74  Bit Score: 87.89  E-value: 1.15e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111439    3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIP 76
Cdd:pfam00936  1 ALGLIETRGLAAGIEAADAMLKAANVELVGYELIGGGKVTVIITGDVAAVKAAVEAGVEAAERIGELVSSHVIP 74
BMC smart00877
Bacterial microcompartments are primitive organelles composed entirely of protein subunits; ...
 3-78 2.90e-21

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: 79.54  E-value: 2.90e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111439     3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGeLVSVHVIPRP 78
Cdd:smart00877  1 ALGIIETRGAAAAIEAADAALKAANVELVGYESIGGGKVTVIITGDVAAVRAAVEAGLEAAERLG-LVSSHVIPRP 75
 
Name Accession Description Interval E-value
PRK15474 PRK15474
ethanolamine utilization microcompartment protein EutM;
1-97 9.42e-49

ethanolamine utilization microcompartment protein EutM;


Pssm-ID: 185371  Cd Length: 97  Bit Score: 149.81  E-value: 9.42e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439   1 MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHG 80
Cdd:PRK15474  1 MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHG 80

                        90
                ....*....|....*..
gi 90111439  81 DLEEVFPIGLKGDSSNL 97
Cdd:PRK15474 81 DLEEVFPIGLKGDSSNL 97
CcmK COG4577
Carboxysome shell and ethanolamine utilization microcompartment protein CcmL/EutN [Secondary ...
 1-85 3.65e-35

Carboxysome shell and ethanolamine utilization microcompartment protein CcmL/EutN [Secondary metabolites biosynthesis, transport and catabolism, Energy production and conversion];


Pssm-ID: 443634  Cd Length: 86  Bit Score: 114.82  E-value: 3.65e-35
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439  1 MEALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHG 80
Cdd:COG4577  2 GKALGLIETKGLAAAIEAADAMLKAANVELVGYEKIGSGKVTVIVRGDVAAVKAAVDAGAAAAERVGELVSSHVIPRPHP 81


               ....*
gi 90111439 81 DLEEV 85
Cdd:COG4577 82 EVEAA 86
BMC_CcmK_like cd07045
Carbon dioxide concentrating mechanism K (CcmK)-like proteins, Bacterial Micro-Compartment ...
 3-86 3.14e-31

Carbon dioxide concentrating mechanism K (CcmK)-like proteins, 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). Potential functional differences between the two types are not yet fully understood. 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 shells at present no experimental evidence directly supports this view.


Pssm-ID: 132885  Cd Length: 84  Bit Score: 104.93  E-value: 3.14e-31
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439  3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHGDL 82
Cdd:cd07045  1 ALGLIETRGLVAAIEAADAALKAANVTLVGYEKVGGGLVTVKITGDVAAVKAAVEAGAAAAERIGELVSSHVIPRPHDEV 80


               ....
gi 90111439 83 EEVF 86
Cdd:cd07045 81 EKIL 84
BMC_PduA cd07059
1,2-propanediol utilization protein A (PduA), Bacterial Micro-Compartment (BMC) domain; PduA ...
 3-87 1.51e-29

1,2-propanediol utilization protein A (PduA), Bacterial Micro-Compartment (BMC) domain; PduA is encoded within the 1,2-propanediol utilization (pdu) operon along with other homologous carboxysome shell proteins PduB, B', J, K, T, and U. PduA is thought to be required for the formation of the outer shell of bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduA might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles, like PduU does, at present no experimental evidence directly supports this view.


Pssm-ID: 132899  Cd Length: 85  Bit Score: 100.71  E-value: 1.51e-29
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439  3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHGDL 82
Cdd:cd07059  1 ALGMIETKGLVGAIEAADAMVKAANVTLVGKEQIGGGLVTVMVRGDVGAVKAATDAGAAAAERVGELVSVHVIPRPHTEV 80


               ....*
gi 90111439 83 EEVFP 87
Cdd:cd07059 81 EKILP 85
BMC_CcmK cd07057
Carbon dioxide concentrating mechanism (CcmK); Bacterial Micro-Compartment (BMC) domain; ...
 3-88 1.73e-27

Carbon dioxide concentrating mechanism (CcmK); Bacterial Micro-Compartment (BMC) domain; CcmK1-4 and CcmL proteins found in Synechocystis sp. strain PCC 6803 make up the beta carboxysome shell. These CcmK proteins have been shown to form hexameric units, while the CcmL proteins have been shown to form pentameric units. Together these proteins further assemble into the flat facets of the polyhedral carboxysome shell. The structures suggest that the central pores and the gaps between hexamers limit the transport of metabolites into and out of the the carboxysome.


Pssm-ID: 132897  Cd Length: 88  Bit Score: 95.82  E-value: 1.73e-27
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439  3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQR--IGELVSVHVIPRPHG 80
Cdd:cd07057  1 AVGMIETLGFPAVLAAADAMVKAARVTLVGYEKIGSGRCTVIVRGDVAEVKAAVEAGIEAAERvhGGEVLSHTIIPRPHE 80


               ....*...
gi 90111439 81 DLEEVFPI 88
Cdd:cd07057 81 NLEAVLPI 88
BMC pfam00936
BMC domain; Bacterial microcompartments are primitive organelles composed entirely of protein ...
 3-76 1.15e-24

BMC domain; 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: 425954 [Multi-domain]  Cd Length: 74  Bit Score: 87.89  E-value: 1.15e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111439    3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIP 76
Cdd:pfam00936  1 ALGLIETRGLAAGIEAADAMLKAANVELVGYELIGGGKVTVIITGDVAAVKAAVEAGVEAAERIGELVSSHVIP 74
BMC smart00877
Bacterial microcompartments are primitive organelles composed entirely of protein subunits; ...
 3-78 2.90e-21

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: 79.54  E-value: 2.90e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111439     3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGeLVSVHVIPRP 78
Cdd:smart00877  1 ALGIIETRGAAAAIEAADAALKAANVELVGYESIGGGKVTVIITGDVAAVRAAVEAGLEAAERLG-LVSSHVIPRP 75
BMC_CsoS1 cd07058
Carboxysome Shell 1 (CsoS1); Bacterial Micro-Compartment (BMC) domain; The cso operon in ...
 3-87 5.88e-20

Carboxysome Shell 1 (CsoS1); Bacterial Micro-Compartment (BMC) domain; The cso operon in Halothiobacillus neapolitanus contains the genes involved in alpha carboxysome function including those for the carboxysome shell proteins: CsoS1A, CsoS1B, and CsoS1C. CsoS1A has been shown to form hexameric units which further assemble into the flat facets of the polyhedral carboxysome shell. The structures suggest that the central pores and the gaps between hexamers limit the transport of metabolites into and out of the the carboxysome. Although it has been suggested that other homologous proteins, CsoS1B and CsoS1C, in this family might also form hexamers and play similar functional roles in the construction of carboxysome outer shell at present no experimental evidence directly supports this view.


Pssm-ID: 132898  Cd Length: 88  Bit Score: 76.56  E-value: 5.88e-20
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439  3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGE-LVSVHVIPRPHGD 81
Cdd:cd07058  3 ALGMIETRGLVPAIEAADAMTKAAEVRLIGRQFVGGGYVTVLVRGETGAVNAAVRAGADACERVGDgLVAAHIIARVHSE 82


               ....*.
gi 90111439 82 LEEVFP 87
Cdd:cd07058 83 VENILP 88
PRK15466 PRK15466
ethanolamine utilization microcompartment protein EutK;
3-83 1.02e-14

ethanolamine utilization microcompartment protein EutK;


Pssm-ID: 185363 [Multi-domain]  Cd Length: 166  Bit Score: 65.39  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111439    3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRPHGDL 82
Cdd:PRK15466   4 ALGLLEVDGMVAAIDAADAMLKAANVRLLSHEVLDPGRLTLVVEGDLAACRAALDAGCAAAMRTGRVISRKEIGRPDDDT 83


                 .
gi 90111439   83 E 83
Cdd:PRK15466  84 Q 84
BMC_PduK cd07056
1,2-propanediol utilization protein K (PduK), Bacterial Micro-Compartment (BMC) domain repeat ...
 3-78 9.31e-11

1,2-propanediol utilization protein K (PduK), Bacterial Micro-Compartment (BMC) domain repeat 1l; PduK proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduK might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles at present no experimental evidence directly supports this view.


Pssm-ID: 132896  Cd Length: 77  Bit Score: 52.79  E-value: 9.31e-11
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111439  3 ALGMIETRGLVALIEASDAMVKAARVKLVGV-KQIGGGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRP 78
Cdd:cd07056  1 SLGLLEVSGLSGAIVVADRMAKTANVRLLGLeNTKGSGWMTVKISGDVAAVNAAIEAGKQTAGASDGYVASTVIARP 77
BMC cd06169
Bacterial Micro-Compartment (BMC) domain; Bacterial micro-compartments are primitive ...
 3-53 1.40e-10

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: 51.88  E-value: 1.40e-10
                       10        20        30        40        50
               ....*....|....*....|....*....|....*....|....*....|..
gi 90111439  3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQI-GGGLCTAMVRGDVAACK 53
Cdd:cd06169  1 ALGLLEVRGLAAAIVAADAAVKAADVELVGIERAgGGGLVTLIIRGDVSAVK 52
BMC_PduT_repeat1 cd07053
1,2-propanediol utilization protein T (PduT), Bacterial Micro-Compartment (BMC) domain repeat ...
 3-79 9.32e-08

1,2-propanediol utilization protein T (PduT), Bacterial Micro-Compartment (BMC) domain repeat 1; PduT proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduT might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles at present no experimental evidence directly supports this view. PduT proteins contain two tandem BMC domains repeats. This CD contains repeat 1 (the first BMC domain of PduT) as well as carboxysome shell protein sequence homolog, EutM protein, are also included in this CD. They too might exist as hexamers and might play similar functional roles in the construction of the eut organelle outer shell which still remains poorly understood.


Pssm-ID: 132893  Cd Length: 76  Bit Score: 45.24  E-value: 9.32e-08
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111439  3 ALGMIETRGLVALIEASDAMVKAARVKLVGVKQIGGGLCTAMVRGDVAACKAATDAGAAAAQriGELVSVHVIPRPH 79
Cdd:cd07053  1 AIGLLELNSIAKGIEAADAMLKAANVELVLAKTICPGKYIIIVSGDVGAVQAAVDAGKEIGG--KYVVDSFVLPNVH 75
BMC_PduT_repeat2 cd07054
1,2-propanediol utilization protein T (PduT), Bacterial Micro-Compartment (BMC) domain repeat ...
 3-78 1.56e-07

1,2-propanediol utilization protein T (PduT), Bacterial Micro-Compartment (BMC) domain repeat 2; PduT proteins are homologs of the carboxysome shell protein. They are encoded within the pdu operon and might be required for the formation of the outer shell of the bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduT might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles, at present no experimental evidence directly supports this view. PduT proteins contain two tandem BMC domains repeats. This CD contains repeat 2 (the second BMC domain of PduT) as well as carboxysome shell protein sequence homolog, EutM protein, are also included in this CD. They too might exist as hexamers and might play similar functional roles in the construction of the eut organelle outer shell which still remains poorly understood.


Pssm-ID: 132894  Cd Length: 78  Bit Score: 44.47  E-value: 1.56e-07
                       10        20        30        40        50        60        70
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111439  3 ALGMIETRGLVALIEASDAMVKAARVKLVGVkQIG---GGLCTAMVRGDVAACKAATDAGAAAAQRIGELVSVHVIPRP 78
Cdd:cd07054  1 ALGVIETFSVASGIVAADAALKAADVQLIEI-RLAmgiGGKSFVVLTGDVSAVEAAVEAAEAVVGEKGLLVDSVVIPSP 78
 
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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