NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|506359047|ref|WP_015878766|]
View 

propanediol utilization microcompartment protein PduB [Tolumonas auensis]

Protein Classification

propanediol utilization microcompartment protein PduB( domain architecture ID 11487782)

propanediol utilization microcompartment protein PduB is a major shell protein of Pdu metabolosomes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK15415 PRK15415
propanediol utilization microcompartment protein PduB;
2-268 0e+00

propanediol utilization microcompartment protein PduB;


:

Pssm-ID: 185313 [Multi-domain]  Cd Length: 266  Bit Score: 504.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047   2 SQDNLVEQIMAQVMAKVSDQTAATAPQTtQRGKTMAEKSCSLTEFVGTAIGDTIGLVIANVDQQLLDAMKLEKRYRSIGI 81
Cdd:PRK15415   1 MSNELVEQIMAEVMKKVEAQAAPKNPQP-IRETAMAEKSCGLTEFVGTAIGDTIGLVIANVDSALLEAMKLEKKYRSIGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  82 LGARTGAGPHIMAADEAVKGTNTEVVSIELPRDTKGGAGHGSLIVFGGEDVSDVKRAVEVALKELDRTFGDVYANEAGHI 161
Cdd:PRK15415  80 LGARTGAGPQIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIIFGAEDVSDVRRAVEVALKELDRTFGDVYGNEAGHL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047 162 ELQYSARASYALEKAFGAPLGKACGVIVGAPASVGVLMADTAVKSANVDVVAYSSPAHGTSFSNEVILIVSGDSGAVRQA 241
Cdd:PRK15415 160 ELQYTARASYALEKAFGAPLGKAFGIIVGAPAGIGVVMADTALKSANVDVVAYSSPAHGTSFSNEVILTISGDSGAVRQA 239

                        250       260
                 ....*....|....*....|....*..
gi 506359047 242 VISAREIGKTLLSALGDEPTNTRPSYI 268
Cdd:PRK15415 240 VIAAREVGLTLLATLGSEPKSDTPPYI 266
 
Name Accession Description Interval E-value
PRK15415 PRK15415
propanediol utilization microcompartment protein PduB;
2-268 0e+00

propanediol utilization microcompartment protein PduB;


Pssm-ID: 185313 [Multi-domain]  Cd Length: 266  Bit Score: 504.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047   2 SQDNLVEQIMAQVMAKVSDQTAATAPQTtQRGKTMAEKSCSLTEFVGTAIGDTIGLVIANVDQQLLDAMKLEKRYRSIGI 81
Cdd:PRK15415   1 MSNELVEQIMAEVMKKVEAQAAPKNPQP-IRETAMAEKSCGLTEFVGTAIGDTIGLVIANVDSALLEAMKLEKKYRSIGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  82 LGARTGAGPHIMAADEAVKGTNTEVVSIELPRDTKGGAGHGSLIVFGGEDVSDVKRAVEVALKELDRTFGDVYANEAGHI 161
Cdd:PRK15415  80 LGARTGAGPQIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIIFGAEDVSDVRRAVEVALKELDRTFGDVYGNEAGHL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047 162 ELQYSARASYALEKAFGAPLGKACGVIVGAPASVGVLMADTAVKSANVDVVAYSSPAHGTSFSNEVILIVSGDSGAVRQA 241
Cdd:PRK15415 160 ELQYTARASYALEKAFGAPLGKAFGIIVGAPAGIGVVMADTALKSANVDVVAYSSPAHGTSFSNEVILTISGDSGAVRQA 239

                        250       260
                 ....*....|....*....|....*..
gi 506359047 242 VISAREIGKTLLSALGDEPTNTRPSYI 268
Cdd:PRK15415 240 VIAAREVGLTLLATLGSEPKSDTPPYI 266
microcomp_PduB TIGR04501
microcompartment protein PduB; Members of this family are PduB, a protein of bacterial ...
 44-268 6.23e-157

microcompartment protein PduB; Members of this family are PduB, a protein of bacterial microcompartments for coenzyme B(12)-dependent utilization of 1,2-propanediol (hence pdu) or glycerol. The most closely related protein in ethanolamine utilization microcompartments is EutL (TIGR04502).


Pssm-ID: 275294 [Multi-domain]  Cd Length: 225  Bit Score: 435.60  E-value: 6.23e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047   44 TEFVGTAIGDTIGLVIANVDQQLLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKGTNTEVVSIELPRDTKGGAGHGS 123
Cdd:TIGR04501   1 TEFVGTAIGDTIGLVIANVDSQLHEAMGLDKKYRSIGIISARTGAGPQIMAADEAVKATNTEVVSIELPRDTKGGAGHGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  124 LIVFGGEDVSDVKRAVEVALKELDRTFGDVYANEAGHIELQYSARASYALEKAFGAPLGKACGVIVGAPASVGVLMADTA 203
Cdd:TIGR04501  81 LIIFGAEDVSDVRRAVEVALKELDRTFGDVYGNDAGHLEFQYTARASYALNKAFGAPVGKAFGLIVGAPAAIGVVMADTA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506359047  204 VKSANVDVVAYSSPAHGTSFSNEVILIVSGDSGAVRQAVISAREIGKTLLSALGDEPTNTRPSYI 268
Cdd:TIGR04501 161 VKSANVEVVGYASPGHGTSFSNEVIITISGDSGAVRQAVIAAREVGLKLLGAMGSEPKSPTTPYI 225
EutL COG4816
Ethanolamine utilization protein EutL, microcompartment shell protein [Amino acid transport ...
 58-263 5.92e-90

Ethanolamine utilization protein EutL, microcompartment shell protein [Amino acid transport and metabolism];


Pssm-ID: 443844 [Multi-domain]  Cd Length: 216  Bit Score: 265.57  E-value: 5.92e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  58 VIANVDQQLLDAMKLEKRYRSIGILGARTGAGPHImAADEAVKGTNTEVVsieLPRDTKGGAGHGS-------LIVFGGE 130
Cdd:COG4816   14 VIANVDPDLAEKLGLDPKYRSIGIITADTDDVPYI-AADEATKAANVEVV---YARSFYGGAGHASgplagevIGILAGP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047 131 DVSDVKRAVEVALKELDRTFGDVYANEAGHIEL--QYSARASYALEKAFGAPLGKACGVIVgAPASVGVLMADTAVKSAN 208
Cdd:COG4816   90 DPAEVRSGLEAALDFLENTAGFVSANDDGHIEFyaHYISRTGSYLSKAAGIPEGEAFAYLI-APPLEAVYGLDAALKAAD 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 506359047 209 VDVVAYSSPAHGTSFSNEViliVSGDSGAVRQAVISAREIGKTllsaLGDEPTNT 263
Cdd:COG4816  169 VEVVVFYGPPSETNFSGEL---LTGSQSACRAACDAFREAVLK----VAENPKSY 216
BMC_PduB_repeat1 cd07047
1,2-propanediol utilization protein B (PduB), Bacterial Micro-Compartment (BMC) domain repeat ...
 44-177 3.15e-81

1,2-propanediol utilization protein B (PduB), Bacterial Micro-Compartment (BMC) domain repeat 1; PduB 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 involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduB 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. PduB proteins contain two tandem BMC domains repeats. This CD contains repeat 1 (the first BMC domain of PduB).


Pssm-ID: 132887  Cd Length: 134  Bit Score: 240.43  E-value: 3.15e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  44 TEFVGTAIGDTIGLVIANVDQQLLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKGTNTEVVSIELPRDTKGGAGHGS 123
Cdd:cd07047    1 TEFVGTAIGDTIGLVIANVDPLLLEKMKLDKKYRSIGILGARTGAGPQIMAADEAVKATNTEVISIELPRDTKGGAGHGS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 506359047 124 LIVFGGEDVSDVKRAVEVALKELDRTFGDVYANEAGHIELQYSARASYALEKAF 177
Cdd:cd07047   81 LILFGAEDVSDVRRAVEVALSETEKTFGDVYGSEAGHIELQYTARASYALNKAF 134
BMC pfam00936
BMC domain; Bacterial microcompartments are primitive organelles composed entirely of protein ...
 184-250 2.64e-12

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: 60.93  E-value: 2.64e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506359047  184 ACGVIVGAPASVGVLMADTAVKSANVDVVAYSSPAHGtsfsnEVILIVSGDSGAVRQAVISAREIGK 250
Cdd:pfam00936   1 ALGLIETRGLAAGIEAADAMLKAANVELVGYELIGGG-----KVTVIITGDVAAVKAAVEAGVEAAE 62
BMC smart00877
Bacterial microcompartments are primitive organelles composed entirely of protein subunits; ...
 184-253 1.43e-11

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: 58.74  E-value: 1.43e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047   184 ACGVIVGAPASVGVLMADTAVKSANVDVVAYSSPahgtsFSNEVILIVSGDSGAVRQAVISAREIGKTLL 253
Cdd:smart00877   1 ALGIIETRGAAAAIEAADAALKAANVELVGYESI-----GGGKVTVIITGDVAAVRAAVEAGLEAAERLG 65
 
Name Accession Description Interval E-value
PRK15415 PRK15415
propanediol utilization microcompartment protein PduB;
2-268 0e+00

propanediol utilization microcompartment protein PduB;


Pssm-ID: 185313 [Multi-domain]  Cd Length: 266  Bit Score: 504.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047   2 SQDNLVEQIMAQVMAKVSDQTAATAPQTtQRGKTMAEKSCSLTEFVGTAIGDTIGLVIANVDQQLLDAMKLEKRYRSIGI 81
Cdd:PRK15415   1 MSNELVEQIMAEVMKKVEAQAAPKNPQP-IRETAMAEKSCGLTEFVGTAIGDTIGLVIANVDSALLEAMKLEKKYRSIGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  82 LGARTGAGPHIMAADEAVKGTNTEVVSIELPRDTKGGAGHGSLIVFGGEDVSDVKRAVEVALKELDRTFGDVYANEAGHI 161
Cdd:PRK15415  80 LGARTGAGPQIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIIFGAEDVSDVRRAVEVALKELDRTFGDVYGNEAGHL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047 162 ELQYSARASYALEKAFGAPLGKACGVIVGAPASVGVLMADTAVKSANVDVVAYSSPAHGTSFSNEVILIVSGDSGAVRQA 241
Cdd:PRK15415 160 ELQYTARASYALEKAFGAPLGKAFGIIVGAPAGIGVVMADTALKSANVDVVAYSSPAHGTSFSNEVILTISGDSGAVRQA 239

                        250       260
                 ....*....|....*....|....*..
gi 506359047 242 VISAREIGKTLLSALGDEPTNTRPSYI 268
Cdd:PRK15415 240 VIAAREVGLTLLATLGSEPKSDTPPYI 266
microcomp_PduB TIGR04501
microcompartment protein PduB; Members of this family are PduB, a protein of bacterial ...
 44-268 6.23e-157

microcompartment protein PduB; Members of this family are PduB, a protein of bacterial microcompartments for coenzyme B(12)-dependent utilization of 1,2-propanediol (hence pdu) or glycerol. The most closely related protein in ethanolamine utilization microcompartments is EutL (TIGR04502).


Pssm-ID: 275294 [Multi-domain]  Cd Length: 225  Bit Score: 435.60  E-value: 6.23e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047   44 TEFVGTAIGDTIGLVIANVDQQLLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKGTNTEVVSIELPRDTKGGAGHGS 123
Cdd:TIGR04501   1 TEFVGTAIGDTIGLVIANVDSQLHEAMGLDKKYRSIGIISARTGAGPQIMAADEAVKATNTEVVSIELPRDTKGGAGHGS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  124 LIVFGGEDVSDVKRAVEVALKELDRTFGDVYANEAGHIELQYSARASYALEKAFGAPLGKACGVIVGAPASVGVLMADTA 203
Cdd:TIGR04501  81 LIIFGAEDVSDVRRAVEVALKELDRTFGDVYGNDAGHLEFQYTARASYALNKAFGAPVGKAFGLIVGAPAAIGVVMADTA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506359047  204 VKSANVDVVAYSSPAHGTSFSNEVILIVSGDSGAVRQAVISAREIGKTLLSALGDEPTNTRPSYI 268
Cdd:TIGR04501 161 VKSANVEVVGYASPGHGTSFSNEVIITISGDSGAVRQAVIAAREVGLKLLGAMGSEPKSPTTPYI 225
EutL COG4816
Ethanolamine utilization protein EutL, microcompartment shell protein [Amino acid transport ...
 58-263 5.92e-90

Ethanolamine utilization protein EutL, microcompartment shell protein [Amino acid transport and metabolism];


Pssm-ID: 443844 [Multi-domain]  Cd Length: 216  Bit Score: 265.57  E-value: 5.92e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  58 VIANVDQQLLDAMKLEKRYRSIGILGARTGAGPHImAADEAVKGTNTEVVsieLPRDTKGGAGHGS-------LIVFGGE 130
Cdd:COG4816   14 VIANVDPDLAEKLGLDPKYRSIGIITADTDDVPYI-AADEATKAANVEVV---YARSFYGGAGHASgplagevIGILAGP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047 131 DVSDVKRAVEVALKELDRTFGDVYANEAGHIEL--QYSARASYALEKAFGAPLGKACGVIVgAPASVGVLMADTAVKSAN 208
Cdd:COG4816   90 DPAEVRSGLEAALDFLENTAGFVSANDDGHIEFyaHYISRTGSYLSKAAGIPEGEAFAYLI-APPLEAVYGLDAALKAAD 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 506359047 209 VDVVAYSSPAHGTSFSNEViliVSGDSGAVRQAVISAREIGKTllsaLGDEPTNT 263
Cdd:COG4816  169 VEVVVFYGPPSETNFSGEL---LTGSQSACRAACDAFREAVLK----VAENPKSY 216
BMC_PduB_repeat1 cd07047
1,2-propanediol utilization protein B (PduB), Bacterial Micro-Compartment (BMC) domain repeat ...
 44-177 3.15e-81

1,2-propanediol utilization protein B (PduB), Bacterial Micro-Compartment (BMC) domain repeat 1; PduB 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 involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduB 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. PduB proteins contain two tandem BMC domains repeats. This CD contains repeat 1 (the first BMC domain of PduB).


Pssm-ID: 132887  Cd Length: 134  Bit Score: 240.43  E-value: 3.15e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  44 TEFVGTAIGDTIGLVIANVDQQLLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKGTNTEVVSIELPRDTKGGAGHGS 123
Cdd:cd07047    1 TEFVGTAIGDTIGLVIANVDPLLLEKMKLDKKYRSIGILGARTGAGPQIMAADEAVKATNTEVISIELPRDTKGGAGHGS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 506359047 124 LIVFGGEDVSDVKRAVEVALKELDRTFGDVYANEAGHIELQYSARASYALEKAF 177
Cdd:cd07047   81 LILFGAEDVSDVRRAVEVALSETEKTFGDVYGSEAGHIELQYTARASYALNKAF 134
BMC_PduB_repeat2 cd07048
1,2-propanediol utilization protein B (PduB), Bacterial Micro-Compartment (BMC) domain repeat ...
 184-253 9.69e-32

1,2-propanediol utilization protein B (PduB), Bacterial Micro-Compartment (BMC) domain repeat 2; PduB 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 involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduB might form hexamers and further assemble into the flat facets of the polyhedral outer shell of the pdu organelles at present no experimental evidence directly supports this view. PduB proteins contain two tandem BMC domains repeats. This CD contains repeat 2 (the second BMC domain of PduB).


Pssm-ID: 132888 [Multi-domain]  Cd Length: 70  Bit Score: 112.05  E-value: 9.69e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047 184 ACGVIVGAPASVGVLMADTAVKSANVDVVAYSSPAHGTSFSNEVILIVSGDSGAVRQAVISAREIGKTLL 253
Cdd:cd07048    1 AFGIIVGAPAAIGLLMADTALKAANVDIVGYASPSGGTSFSNEVILTISGDSGAVRQALIAAREVGLQLL 70
PRK15405 PRK15405
ethanolamine utilization microcompartment protein EutL;
58-224 2.09e-12

ethanolamine utilization microcompartment protein EutL;


Pssm-ID: 185303 [Multi-domain]  Cd Length: 217  Bit Score: 64.72  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  58 VIANVDQQLLDAMKLEKRYRSIGILGARTGAGPHImAADEAVKGTNTEVVsieLPRDTKGGAGHGS-------LIVFGGE 130
Cdd:PRK15405  15 VIANVNAGLARELKLPPHIRSLGLITADSDDVTYT-ALDEATKQAMVEVV---YARSFYAGAAHAStplagevIGILAGP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047 131 DVSDVKRAVEVALKELDRTFGDVYANEAGHIEL---QYSARASYaLEKAFGAPLGKACGVIVGAP--ASVGVlmaDTAVK 205
Cdd:PRK15405  91 NPAEVRAGLDAMVAFIENGAAFQSANDDDSTAFfahVVSRTGSY-LSKTAGIAEGEPLAYLIAPPleAMYGI---DAALK 166

                        170
                 ....*....|....*....
gi 506359047 206 SANVDVVAYSSPAHGTSFS 224
Cdd:PRK15405 167 AADVQLVTFVGPPSETNFG 185
BMC pfam00936
BMC domain; Bacterial microcompartments are primitive organelles composed entirely of protein ...
 184-250 2.64e-12

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: 60.93  E-value: 2.64e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506359047  184 ACGVIVGAPASVGVLMADTAVKSANVDVVAYSSPAHGtsfsnEVILIVSGDSGAVRQAVISAREIGK 250
Cdd:pfam00936   1 ALGLIETRGLAAGIEAADAMLKAANVELVGYELIGGG-----KVTVIITGDVAAVKAAVEAGVEAAE 62
BMC smart00877
Bacterial microcompartments are primitive organelles composed entirely of protein subunits; ...
 184-253 1.43e-11

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: 58.74  E-value: 1.43e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047   184 ACGVIVGAPASVGVLMADTAVKSANVDVVAYSSPahgtsFSNEVILIVSGDSGAVRQAVISAREIGKTLL 253
Cdd:smart00877   1 ALGIIETRGAAAAIEAADAALKAANVELVGYESI-----GGGKVTVIITGDVAAVRAAVEAGLEAAERLG 65
BMC smart00877
Bacterial microcompartments are primitive organelles composed entirely of protein subunits; ...
 78-151 9.44e-11

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: 56.43  E-value: 9.44e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506359047    78 SIGILGARtGAGPHIMAADEAVKGTNTEVVSIELPrdtkgGAGHGSLIVFGgeDVSDVKRAVEVALKELDRTFG 151
Cdd:smart00877   1 ALGIIETR-GAAAAIEAADAALKAANVELVGYESI-----GGGKVTVIITG--DVAAVRAAVEAGLEAAERLGL 66
BMC cd06169
Bacterial Micro-Compartment (BMC) domain; Bacterial micro-compartments are primitive ...
 184-249 2.65e-09

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: 52.26  E-value: 2.65e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506359047 184 ACGVIVGAPASVGVLMADTAVKSANVDVVAYSSPAHGtsfsNEVILIVSGDSGAVRQAVISAREIG 249
Cdd:cd06169    1 ALGLLEVRGLAAAIVAADAAVKAADVELVGIERAGGG----GLVTLIIRGDVSAVKAAVEAAEQAA 62
BMC pfam00936
BMC domain; Bacterial microcompartments are primitive organelles composed entirely of protein ...
 78-148 6.59e-07

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: 45.91  E-value: 6.59e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506359047   78 SIGILGARTGAGPhIMAADEAVKGTNTEVVSIELPRDTKggaghgSLIVFGGeDVSDVKRAVEVALKELDR 148
Cdd:pfam00936   1 ALGLIETRGLAAG-IEAADAMLKAANVELVGYELIGGGK------VTVIITG-DVAAVKAAVEAGVEAAER 63
BMC cd06169
Bacterial Micro-Compartment (BMC) domain; Bacterial micro-compartments are primitive ...
 78-146 6.15e-06

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: 43.02  E-value: 6.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506359047  78 SIGILGARtGAGPHIMAADEAVKGTNTEVVSIELPrdtkGGAGHGSLIVFGgeDVSDVKRAVEVALKEL 146
Cdd:cd06169    1 ALGLLEVR-GLAAAIVAADAAVKAADVELVGIERA----GGGGLVTLIIRG--DVSAVKAAVEAAEQAA 62
CcmK COG4577
Carboxysome shell and ethanolamine utilization microcompartment protein CcmL/EutN [Secondary ...
 196-250 1.66e-05

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: 42.40  E-value: 1.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 506359047 196 GVLMADTAVKSANVDVVAYSSPAHGtsfsnEVILIVSGDSGAVRQAVISAREIGK 250
Cdd:COG4577   16 AIEAADAMLKAANVELVGYEKIGSG-----KVTVIVRGDVAAVKAAVDAGAAAAE 65
BMC_PduT_repeat1 cd07053
1,2-propanediol utilization protein T (PduT), Bacterial Micro-Compartment (BMC) domain repeat ...
 196-250 7.01e-05

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: 40.23  E-value: 7.01e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 506359047 196 GVLMADTAVKSANVDVVAYSspahgTSFSNEVILIVSGDSGAVRQAVISAREIGK 250
Cdd:cd07053   13 GIEAADAMLKAANVELVLAK-----TICPGKYIIIVSGDVGAVQAAVDAGKEIGG 62
BMC_EutL_repeat1 cd07049
ethanolamine utilization protein S (EutS), Bacterial Micro-Compartment (BMC) domain repeat 1; ...
 58-147 2.26e-04

ethanolamine utilization protein S (EutS), Bacterial Micro-Compartment (BMC) domain repeat 1; EutL proteins are homologs of the carboxysome shell protein. They are encoded within the eut operon and might be required for the formation of the outer shell of the bacterial eut polyhedral organelles which are involved in the cobalamin-dependent degradation of ethanolamine. Although it has been suggested that EutL might form hexamers and further assemble into the flat facets of the polyhedral outer shell of the eut organelles at present no experimental evidence directly supports this view. EutL proteins contain two tandem BMC domains. This CD includes domain 1 (the first BMC domain of EutL).


Pssm-ID: 132889  Cd Length: 103  Bit Score: 39.70  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506359047  58 VIANVDQQLLDAMKLEKRYRSIGILGARTGAGPHImAADEAVKGTNTEVVsieLPRDTKGGAGHGS-------LIVFGGE 130
Cdd:cd07049    6 VIPNVDPDLAKELSLPPHHRSLGIITADSDDVTYT-ALDEATKAAEVEVV---YARSFYAGAAHAStplagevIGILAGP 81

                         90
                 ....*....|....*..
gi 506359047 131 DVSDVKRAVEVALKELD 147
Cdd:cd07049   82 SPAEVRSGLNAAIDFIE 98
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH