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Conserved domains on  [gi|256000792|ref|NP_001157726|]
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tropomyosin alpha-1 chain isoform Tpm1.13 [Mus musculus]

Protein Classification

tropomyosin( domain architecture ID 11991670)

tropomyosin binds to actin filaments in muscle and non-muscle cells and plays a central role in regulating striated and smooth muscle contraction; forms a homodimer or a heterodimer between tropomyosin alpha and beta chains

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-246 4.99e-71

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


:

Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 217.20  E-value: 4.99e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256000792  172 EAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-246 4.99e-71

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 217.20  E-value: 4.99e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256000792  172 EAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-228 3.20e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   6 SLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVT 165
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256000792 166 NNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQK 228
Cdd:COG1196  435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-248 3.93e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.46  E-value: 3.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsegkcaELEEELKTVTN 166
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 246
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932


                   ..
gi 256000792   247 SI 248
Cdd:TIGR02168  933 GL 934
PTZ00121 PTZ00121
MAEBL; Provisional
 15-233 6.11e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   15 RSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI 94
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   95 ESRAQKDEEKMEIQEIQLKEAKHIAEDAdRKYEEVARKLVIIESD-LERAEERAELSEG--------KCAELEEELKTVT 165
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEA-RKADELKKAEEKKKADeAKKAEEKKKADEAkkkaeeakKADEAKKKAEEAK 1328

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256000792  166 NNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDL----EDELYAQKLKYKA 233
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKA 1400
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-246 4.99e-71

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 217.20  E-value: 4.99e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256000792  172 EAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-228 3.20e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   6 SLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVT 165
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256000792 166 NNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQK 228
Cdd:COG1196  435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-248 3.93e-12

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.46  E-value: 3.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsegkcaELEEELKTVTN 166
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 246
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932


                   ..
gi 256000792   247 SI 248
Cdd:TIGR02168  933 GL 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-242 7.24e-12

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 7.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196  248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256000792 167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHAL 242
Cdd:COG1196  408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-239 9.67e-12

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 9.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196  269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256000792 167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 239
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 12-116 1.02e-10

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 58.08  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEadvaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam12718  42 HKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKV 117

                          90       100
                  ....*....|....*....|....*
gi 256000792   92 KVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:pfam12718 118 QALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 8-238 4.56e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 4.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   8 EAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  88 ERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNN 167
Cdd:COG1196  301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256000792 168 LKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEEL 238
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-242 4.74e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 4.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  10 VRRKIRSLQEQADAAEE-----------RAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLE 78
Cdd:COG1196  198 LERQLEPLERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  79 EAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELE 158
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792 159 EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEEL 238
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437


                 ....
gi 256000792 239 DHAL 242
Cdd:COG1196  438 EEEE 441
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-239 3.73e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 3.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     2 AGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    82 KAADESERGMKVIESR-----AQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAE 156
Cdd:TIGR02169  751 QEIENVKSELKELEARieeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   157 LEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISE 236
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910


                   ...
gi 256000792   237 ELD 239
Cdd:TIGR02169  911 QIE 913
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-244 4.87e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 4.87e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    32 QRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQ 111
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   112 LKEAKHIAEDADRKYE-------EVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDK 184
Cdd:TIGR02168  756 LTELEAEIEELEERLEeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   185 YEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELyAQKLKYKAISEELDHALND 244
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRS 894
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-230 5.64e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 5.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    13 KIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEaekaadesergmk 92
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR------------- 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    93 vIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLE 172
Cdd:TIGR02168  300 -LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 256000792   173 AQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLK 230
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-210 1.87e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.69  E-value: 1.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02169  300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKT 163
Cdd:TIGR02169  380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 256000792   164 VTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSV 210
Cdd:TIGR02169  460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 6-247 2.70e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.29  E-value: 2.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     6 SLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    86 ESERGMKVIESRAQKDEEKMEIQ-------EIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELE 158
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   159 EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAefAERSVTKLEKSIDDLEDELYAQKLKYKAISEEL 238
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREEL 470


                   ....*....
gi 256000792   239 DHALNDMTS 247
Cdd:TIGR02168  471 EEAEQALDA 479
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-235 4.06e-08

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   1 MAGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  81 EKAADESErgmKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 160
Cdd:COG4942   96 RAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256000792 161 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAIS 235
Cdd:COG4942  173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-215 6.93e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 6.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  87 SERGmkviESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196  391 ALRA----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 256000792 167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEK 215
Cdd:COG1196  467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-248 6.82e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 6.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     7 LEAVRRKIRSLQEQADAAEEragslQRELDQERKlretaEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAER-----YKELKAELR-----ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    87 SErgMKVIESRAQKDEEKMEIQEIQlkeakhiaedadRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:TIGR02168  265 LE--EKLEELRLEVSELEEEIEELQ------------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 246
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410


                   ..
gi 256000792   247 SI 248
Cdd:TIGR02168  411 RL 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-224 9.99e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 9.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELdrAQERLATALQKLEEAEKA 83
Cdd:TIGR02169  715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL--HKLEEALNDLEARLSHSR 792

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKT 163
Cdd:TIGR02169  793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256000792   164 VTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDEL 224
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-177 1.11e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRET---------AEADVASLNRRIQLVEEELDRAQE---RLATAL 74
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDAssdDLAALE 691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   75 QKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLViiesDLERAEERAELSEGKC 154
Cdd:COG4913   692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVEREL 767

                         170       180
                  ....*....|....*....|....
gi 256000792  155 AE-LEEELKTVTNNLKSLEAQAEK 177
Cdd:COG4913   768 REnLEERIDALRARLNRAEEELER 791
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-204 1.31e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 90
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGkcAELEEELKTvtnnlks 170
Cdd:COG4913   687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAA------- 757

                         170       180       190
                  ....*....|....*....|....*....|....
gi 256000792  171 lEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 204
Cdd:COG4913   758 -ALGDAVERELRENLEERIDALRARLNRAEEELE 790
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-223 2.29e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 2.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEEL-----DRAQERLATALQKLE 78
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELS 801

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    79 EAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELE 158
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256000792   159 EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDE 223
Cdd:TIGR02169  882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-241 4.57e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 4.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELeeELKT 163
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKE 437

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256000792   164 VTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 241
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-206 7.03e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    7 LEAVRRKIRSLQEQADA-----AEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATA-LQKLEEA 80
Cdd:COG4913   264 YAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQL 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   81 EKAADESERGMKVIESRAQKDEEKmeIQEIQLkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 160
Cdd:COG4913   344 EREIERLERELEERERRRARLEAL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 256000792  161 LKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLSDKLKEAETRAEFA 206
Cdd:COG4913   421 LRELEAEIASLERRKSNIPA---RLLALRDALAEALGLDEAELPFV 463
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-157 1.16e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792     7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256000792    87 SERGMKviESRAQKDEEKMEIQEIQLKEA---KHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAEL 157
Cdd:TIGR02168  913 LRRELE--ELREKLAQLELRLEGLEVRIDnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
8-198 5.31e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   8 EAVRRKIRSLQEQADAAEERAGSLQRELDQ-ERKLRE-TAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEaEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAkhiaeDADRKYEEVARKL-----VIIESDLERAEERAELSEgkcaELEEE 160
Cdd:COG3206  244 ALRAQLGSGPDALPELLQSPVIQQLRAQLA-----ELEAELAELSARYtpnhpDVIALRAQIAALRAQLQQ----EAQRI 314

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 256000792 161 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKE 198
Cdd:COG3206  315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
PTZ00121 PTZ00121
MAEBL; Provisional
 15-233 6.11e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   15 RSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI 94
Cdd:PTZ00121 1170 RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   95 ESRAQKDEEKMEIQEIQLKEAKHIAEDAdRKYEEVARKLVIIESD-LERAEERAELSEG--------KCAELEEELKTVT 165
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEA-RKADELKKAEEKKKADeAKKAEEKKKADEAkkkaeeakKADEAKKKAEEAK 1328

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256000792  166 NNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDL----EDELYAQKLKYKA 233
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKA 1400
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
33-224 7.45e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   33 RELDQERKLRE------TAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKME 106
Cdd:COG4913   590 HEKDDRRRIRSryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  107 IQEiqLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYE 186
Cdd:COG4913   670 IAE--LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 256000792  187 EEikvLSDKLKEAETRAEFAERSVTKLEKSIDDLEDEL 224
Cdd:COG4913   748 RA---LLEERFAAALGDAVERELRENLEERIDALRARL 782
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 13-225 7.68e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.38  E-value: 7.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  13 KIRSLQEQADAAEERAGSLQRELDQERKLRET-AEADVASLNRRIQLVEEELDRAQERLATALQKLEE--AEKAADESE- 88
Cdd:PRK05771  44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISEleNEIKELEQEi 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  89 -------------------RGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA---RKLVIIESDLERAE-E 145
Cdd:PRK05771 124 erlepwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVvlkELSDEVEEELKKLGfE 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792 146 RAELSEGKC-----AELEEELKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLSDKL----KEAETRAEFA---------- 206
Cdd:PRK05771 204 RLELEEEGTpseliREIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielERAEALSKFLktdktfaieg 280

                        250       260
                 ....*....|....*....|..
gi 256000792 207 ---ERSVTKLEKSIDDLEDELY 225
Cdd:PRK05771 281 wvpEDRVKKLKELIDKATGGSA 302
PRK09039 PRK09039
peptidoglycan -binding protein;
2-85 1.57e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   2 AGSSSLEAVRRKIRSL----QEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIqlveEELDRAQERLATALQKL 77
Cdd:PRK09039  88 ASLSAAEAERSRLQALlaelAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI----AALRRQLAALEAALDAS 163


                 ....*...
gi 256000792  78 EEAEKAAD 85
Cdd:PRK09039 164 EKRDRESQ 171
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-224 1.57e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  46 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI-ESRAQKDEEKMEIQEI--QLKEAKHIAEDA 122
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIeDLRETIAETEREREELaeEVRDLRERLEEL 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792 123 DRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETR 202
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                        170       180
                 ....*....|....*....|..
gi 256000792 203 AEFAERSVTKLEKSIDDLEDEL 224
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEI 393
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 5-204 2.15e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   5 SSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  85 DESERGMKVIE------------SRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG 152
Cdd:COG3883   96 YRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 256000792 153 KCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 204
Cdd:COG3883  176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-239 2.95e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    7 LEAVRRKIRSLqEQADAAEERAGSLQRELDQERKLRETAEADVASlnRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4913   244 LEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDA 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   87 SERgmkviesraqkdeekmeiQEIQLKEAkhIAEDADRKYEEVARKLviiesdleraeeraelsegkcAELEEELKTVTN 166
Cdd:COG4913   321 LRE------------------ELDELEAQ--IRGNGGDRLEQLEREI---------------------ERLERELEERER 359

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256000792  167 NLKSLEAQAEKYSQkedKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 239
Cdd:COG4913   360 RRARLEALLAALGL---PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-177 3.23e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   8 EAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  88 ERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNN 167
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434

                        170
                 ....*....|
gi 256000792 168 LKSLEAQAEK 177
Cdd:PRK02224 435 LRTARERVEE 444
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-239 3.41e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   58 LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEkmeIQEIQLKEAKHIAEDADRKYEEVARKLVIIE 137
Cdd:COG4913   218 LEEPDTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAER---YAAARERLAELEYLRAALRLWFAQRRLELLE 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  138 SDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKS 216
Cdd:COG4913   295 AELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374

                         170       180
                  ....*....|....*....|...
gi 256000792  217 IDDLEDELYAQKLKYKAISEELD 239
Cdd:COG4913   375 LPASAEEFAALRAEAAALLEALE 397
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-239 3.97e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   8 EAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  88 ERGMKVIESRAQKDEEKMEIQEIQLKEAK--------------HIAEDADRKYEEVARKLVIIESDLERAEERAELSEgK 153
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-D 503

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792 154 CAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKA 233
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583


                 ....*.
gi 256000792 234 ISEELD 239
Cdd:PRK02224 584 LKERIE 589
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
11-193 9.65e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 9.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEEL-----DRAQERLATALQKLE--EAEKA 83
Cdd:COG3206  204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEaeLAELS 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  84 ADESERGMKVIESRAQKDEEKMEIQEiqlkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAEL---SEGKCAELEEE 160
Cdd:COG3206  284 ARYTPNHPDVIALRAQIAALRAQLQQ----EAQRILASLEAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLERE 359

                        170       180       190
                 ....*....|....*....|....*....|...
gi 256000792 161 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLS 193
Cdd:COG3206  360 VEVARELYESLLQRLEEARLAEALTVGNVRVID 392
PTZ00121 PTZ00121
MAEBL; Provisional
 11-236 1.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVtNNLKS 170
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-EQLKK 1640

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256000792  171 LEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISE 236
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-221 1.04e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:COG1196  573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADrkyEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKS 170
Cdd:COG1196  653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELA---ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 256000792 171 LEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG1196  730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
5-224 1.05e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   5 SSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLREtaeadvaslnrRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----------ELETLEAEIEDLRETIAETEREREELAEEV 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTV 164
Cdd:PRK02224 282 RDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792 165 TNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDEL 224
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
14-239 1.39e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  14 IRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 93
Cdd:COG4372   26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  94 IESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELktvtNNLKSLEA 173
Cdd:COG4372  106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL----QALSEAEA 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256000792 174 QAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 239
Cdd:COG4372  182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 8-197 1.41e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.65  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    8 EAVRRKIRSLQEqADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEEL---DRAQERLATALQKLEEAEKAA 84
Cdd:PRK10929   48 EALQSALNWLEE-RKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMstdALEQEILQVSSQLLEKSRQAQ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   85 DESERGMKVIESRAQKDEEKMEIQEiQLKEAKH-------------IAEDADRKYEEVARKLVIIESDL---------ER 142
Cdd:PRK10929  127 QEQDRAREISDSLSQLPQQQTEARR-QLNEIERrlqtlgtpntplaQAQLTALQAESAALKALVDELELaqlsannrqEL 205

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  143 AEERAELSEGKCAELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEI----KVLSDKLK 197
Cdd:PRK10929  206 ARLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgdlpKSIVAQFK 265
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 7-92 1.77e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.29  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   7 LEAVRRKIRSLQ--------EQADAAEERAGSLQRELDQERKLRETAEADVAS---LNRRIQLVEEELDRAQERLATALQ 75
Cdd:COG0542  413 LDELERRLEQLEiekealkkEQDEASFERLAELRDELAELEEELEALKARWEAekeLIEEIQELKEELEQRYGKIPELEK 492

                         90
                 ....*....|....*..
gi 256000792  76 KLEEAEKAADESERGMK 92
Cdd:COG0542  493 ELAELEEELAELAPLLR 509
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 14-219 1.81e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  14 IRSLQEQADAAEERAGSLQRELDQERKLREtaeadvaSLNRRIQLVEEELDRAQERLA-TALQKLEEAEKAADESERGMK 92
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKE-------ELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELR 594

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  93 VIESRAQKDEEKMEIQEIQ--LKEAKHIAEDADRKYEEVARKL-----VIIESDLERAeERAELSEGKCAELEEELKTVT 165
Cdd:PRK00409 595 QLQKGGYASVKAHELIEARkrLNKANEKKEKKKKKQKEKQEELkvgdeVKYLSLGQKG-EVLSIPDDKEAIVQAGIMKMK 673

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 256000792 166 NNLKSLeaqaEKYSQKEDKYEEEIKVLSDKLKEAET----RAEFAERSVTKLEKSIDD 219
Cdd:PRK00409 674 VPLSDL----EKIQKPKKKKKKKPKTVKPKPRTVSLeldlRGMRYEEALERLDKYLDD 727
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
7-199 1.83e-03

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 39.29  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   7 LEAVR---RKIRSLQEQADAAEERAGSLQRELDQ-ERKLRETAEADVASLNrriqlvEEELDRAQERLATA---LQKLEE 79
Cdd:COG0497  157 LEEYReayRAWRALKKELEELRADEAERARELDLlRFQLEELEAAALQPGE------EEELEEERRRLSNAeklREALQE 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  80 AEKAADESERG--------MKVIESRAQKDEEKMEIQEiQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEER----- 146
Cdd:COG0497  231 ALEALSGGEGGaldllgqaLRALERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFDPERLEEVEERlallr 309

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256000792 147 ----------AELSEgKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEA 199
Cdd:COG0497  310 rlarkygvtvEELLA-YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 47-241 2.30e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  47 ADVASLNRRIQLVEEELDRAQERlatalqkLEEAEKAADESERGMKVIESRAQKDEE----KMEIQEIQLKEAKHIAEDA 122
Cdd:COG1196  165 AGISKYKERKEEAERKLEATEEN-------LERLEDILGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLREL 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792 123 DRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETR 202
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 256000792 203 AEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 241
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 33-201 2.31e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 38.83  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   33 RELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDE---------E 103
Cdd:pfam05262 192 KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPkpadtsspkE 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  104 KMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLER-AEERAELSEGKCAELEEELKTVTNNLKSL--EAQAEKYSQ 180
Cdd:pfam05262 272 DKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQKTkpQVEAQPTSL 351

                         170       180
                  ....*....|....*....|.
gi 256000792  181 KEDKYEEEIKVLSDKLKEAET 201
Cdd:pfam05262 352 NEDAIDSSNPVYGLKVVDPIT 372
PTZ00121 PTZ00121
MAEBL; Provisional
 15-222 2.42e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   15 RSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEElDRAQERLATALQKLEEAEKAadesERGMKVI 94
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA-KKAEEDKNMALRKAEEAKKA----EEARIEE 1596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   95 ESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsegKCAELEEELKTVTNNLKSLEAQ 174
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEE 1672

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 256000792  175 AEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
14-221 2.63e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   14 IRSLQEQAD---AAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:COG4913   227 ADALVEHFDdleRAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   91 MKVIESRAQKDEEKMEIQEIQLKEAkhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEelkTVTNNLKS 170
Cdd:COG4913   307 LEAELERLEARLDALREELDELEAQ--IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL---PLPASAEE 381

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 256000792  171 LEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG4913   382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-245 2.68e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   1 MAGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  81 EKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEE--RAELSEGKCAELE 158
Cdd:COG4372  107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAEAEQALD 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792 159 EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEEL 238
Cdd:COG4372  187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266


                 ....*..
gi 256000792 239 DHALNDM 245
Cdd:COG4372  267 ILVEKDT 273
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
7-205 2.73e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   7 LEAVRRKIRSLQEQAD--AAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3206  191 LEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  85 DESERGMKVIESRAQKDEEKMEIQEIQLKeakhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTV 164
Cdd:COG3206  271 QLAELEAELAELSARYTPNHPDVIALRAQ----IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 256000792 165 TNNLKSLEAQAEKYSQKEDKYEEeikvLSDKLKEAETRAEF 205
Cdd:COG3206  347 PELEAELRRLEREVEVARELYES----LLQRLEEARLAEAL 383
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 108-203 2.94e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 38.78  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  108 QEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEE 187
Cdd:PRK11448  140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219

                          90
                  ....*....|....*....
gi 256000792  188 EIKVLSDK---LKEAETRA 203
Cdd:PRK11448  220 EITDQAAKrleLSEEETRI 238
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-239 3.69e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.50  E-value: 3.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    66 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQE-----------IQLKEAKHIAEDADRKYEEVARKLV 134
Cdd:TIGR02168  177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAelrelelallvLRLEELREELEELQEELKEAEEELE 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   135 IIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLE 214
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336

                          170       180
                   ....*....|....*....|....*
gi 256000792   215 KSIDDLEDELYAQKLKYKAISEELD 239
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELE 361
PTZ00121 PTZ00121
MAEBL; Provisional
 8-241 3.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792    8 EAVRR--KIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEK--A 83
Cdd:PTZ00121 1125 EDARKaeEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKaeA 1204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   84 ADESERGMKVIESRAQKDEEKMEIQEiQLKEAKHIAEDAdRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKT 163
Cdd:PTZ00121 1205 ARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE 1282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  164 VTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLK--EAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 241
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
mukB PRK04863
chromosome partition protein MukB;
11-116 6.04e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 37.63  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELdRAQERLATALQKLEEAEKAADESERG 90
Cdd:PRK04863  292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQADLEELEERLEEQNEV 370

                          90       100
                  ....*....|....*....|....*.
gi 256000792   91 MKVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:PRK04863  371 VEEADEQQEENEARAEAAEEEVDELK 396
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
55-224 7.22e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.33  E-value: 7.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  55 RIQLVEEELDRAQERLATALQKLEEAEKAAdESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLV 134
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792 135 IIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDkYEEEIKVLSDKLKEAETRAEFAERSVTKLE 214
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKR 633

                        170
                 ....*....|
gi 256000792 215 KSIDDLEDEL 224
Cdd:PRK02224 634 ERKRELEAEF 643
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 54-202 7.44e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.50  E-value: 7.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  54 RRIQLVEEELDRAQERLATALQKLEEaekaadesergmkVIESRaqkdEEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 133
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKLNE-------------LIASL----EELERELEQKAEEAEALLKEAEKLKEELEEKK 557

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792 134 VIIESDLERAEERAELS-EGKCAELEEELKTVTNNLKSLEaQAEKYSQKEDKYEEEIKVLSDKLKEAETR 202
Cdd:PRK00409 558 EKLQEEEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKK 626
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
7-85 8.06e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 37.14  E-value: 8.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKlRETAEADVASLNR---RIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:COG3524  237 LAALRSYLSPNSPQVRQLRRRIAALEKQIAAERA-RLTGASGGDSLASllaEYERLELEREFAEKAYTSALAALEQARIE 315


                 ..
gi 256000792  84 AD 85
Cdd:COG3524  316 AA 317
PRK12704 PRK12704
phosphodiesterase; Provisional
 73-193 8.12e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.07  E-value: 8.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792  73 ALQKLEEAEKAADEsergmKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEE----RAE 148
Cdd:PRK12704  29 AEAKIKEAEEEAKR-----ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldrKLE 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 256000792 149 LSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLS 193
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
7-93 9.77e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 36.76  E-value: 9.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256000792   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRET---AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:COG2433  422 VERLEAEVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLERELEEERERIEELKRKLERLKEL 501

                         90
                 ....*....|
gi 256000792  84 ADESERGMKV 93
Cdd:COG2433  502 WKLEHSGELV 511
 
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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