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Conserved domains on  [gi|568961237|ref|XP_006511113|]
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tropomyosin alpha-1 chain isoform X11 [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 7.47e-66

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: 204.11  E-value: 7.47e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961237  172 MAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 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 7.47e-66

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: 204.11  E-value: 7.47e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961237  172 MAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-228 2.31e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   6 SLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMD 165
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961237 166 QTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQK 228
Cdd:COG1196  435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-238 1.83e-11

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: 63.54  E-value: 1.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237     5 SSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIM 164
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961237   165 DQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEEL 238
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
PTZ00121 PTZ00121
MAEBL; Provisional
 8-233 4.58e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    8 EAVRRKIRSLQEQADAAEE-RAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD-----RKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQL 161
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkadelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961237  162 RIMDQTLKALMAAEDKYSQKEDKYE---EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDL----EDELYAQKLKYKA 233
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKA 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 7.47e-66

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: 204.11  E-value: 7.47e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961237  172 MAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMT 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-228 2.31e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   6 SLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMD 165
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961237 166 QTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQK 228
Cdd:COG1196  435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-242 8.48e-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: 8.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196  248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961237 167 TLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHAL 242
Cdd:COG1196  408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-238 1.83e-11

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: 63.54  E-value: 1.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237     5 SSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIM 164
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961237   165 DQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEEL 238
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-241 7.34e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.88  E-value: 7.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196  255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:COG1196  335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961237 167 TLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 241
Cdd:COG1196  415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
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 568961237   12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEadvaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam12718  42 HKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKV 117

                          90       100
                  ....*....|....*....|....*
gi 568961237   92 KVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:pfam12718 118 QALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-243 3.18e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:COG1196  342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961237 167 TLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALN 243
Cdd:COG1196  422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 31-242 2.60e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  31 LQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEI 110
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237 111 QLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIK 190
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568961237 191 VLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHAL 242
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-215 4.67e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  87 SERGmkviESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:COG1196  391 ALRA----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568961237 167 TLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEK 215
Cdd:COG1196  467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-239 5.57e-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: 53.14  E-value: 5.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    24 AEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEE 103
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   104 KMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALmaAEDKYSQKED 183
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL--LKKLEEAELK 436

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568961237   184 KYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 239
Cdd:TIGR02168  437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-224 1.00e-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: 52.37  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237     4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRI 163
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961237   164 MDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDEL 224
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-239 1.21e-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: 51.99  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237     2 AGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    82 KAADESERGMKVIESR-----AQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQ 156
Cdd:TIGR02169  751 QEIENVKSELKELEARieeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   157 LEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISE 236
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910


                   ...
gi 568961237   237 ELD 239
Cdd:TIGR02169  911 QIE 913
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-235 2.11e-07

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: 50.92  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   1 MAGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4942   16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  81 EKAADESErgmKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQ 160
Cdd:COG4942   96 RAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961237 161 LRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAIS 235
Cdd:COG4942  173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 21-239 3.20e-07

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: 50.53  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  21 ADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQK 100
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237 101 DEEKMEIQEIQLKEakhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQ 180
Cdd:COG4942   95 LRAELEAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568961237 181 KEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 239
Cdd:COG4942  172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-210 1.19e-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: 49.30  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237     4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02169  300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRI 163
Cdd:TIGR02169  380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 568961237   164 MDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSV 210
Cdd:TIGR02169  460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-162 1.51e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRET---------AEADVASLNRRIQLVEEELDRAQE---RLATAL 74
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDAssdDLAALE 691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   75 QKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLViiesDLERAEERAELSEGQV 154
Cdd:COG4913   692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVEREL 767


                  ....*....
gi 568961237  155 R-QLEEQLR 162
Cdd:COG4913   768 ReNLEERID 776
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-238 1.70e-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: 48.51  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237     7 LEAVRRKIRSLQEQADAAEEragslQRELDQERKlretaEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAER-----YKELKAELR-----ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    87 SERgmKVIESRAQKDEEKMEIQEIQlkeakhiaedadRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:TIGR02168  265 LEE--KLEELRLEVSELEEEIEELQ------------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568961237   167 TLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEEL 238
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-223 2.00e-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: 48.51  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237     2 AGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    82 KAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERaeLSEGQVRQLEEQL 161
Cdd:TIGR02168  880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER--LSEEYSLTLEEAE 957

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568961237   162 RIMDQTLKALMAAEDKYSQKEDKYE----------EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDE 223
Cdd:TIGR02168  958 ALENKIEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-204 2.50e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 90
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsEGQVRQLEEQLrimdqtlkA 170
Cdd:COG4913   687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF--------A 756

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568961237  171 LMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAE 204
Cdd:COG4913   757 AALGDAVERELRENLEERIDALRARLNRAEEELE 790
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-224 1.25e-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: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237     4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    84 ADESERGMKVIESRAQKDEEKMeiqeiqlkeakhiaEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRi 163
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQL--------------ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE- 424

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961237   164 mDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDEL 224
Cdd:TIGR02168  425 -ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-162 3.19e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQ-ERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG4913   297 LEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961237   86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHiaeDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLR 162
Cdd:COG4913   377 ASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-224 3.79e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    7 LEAVRRKIRSLqEQADAAEERAGSLQRELDQERKLRETAEADVASlnRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4913   244 LEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDA 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   87 SErgmkviESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:COG4913   321 LR------EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568961237  167 TLKALMAAedkysqkedkyeeeikvlsdkLKEAETRAEFAERsvtKLEKSIDDLEDEL 224
Cdd:COG4913   395 ALEEELEA---------------------LEEALAEAEAALR---DLRRELRELEAEI 428
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-171 3.89e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 3.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    7 LEAVRRKIRSLQEQADA-----AEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATA-LQKLEEA 80
Cdd:COG4913   264 YAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQL 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   81 EKAADESERGMKVIESRAQKDEEKmeIQEIQLkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQ 160
Cdd:COG4913   344 EREIERLERELEERERRRARLEAL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420

                         170
                  ....*....|.
gi 568961237  161 LRIMDQTLKAL 171
Cdd:COG4913   421 LRELEAEIASL 431
PTZ00121 PTZ00121
MAEBL; Provisional
 8-233 4.58e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    8 EAVRRKIRSLQEQADAAEE-RAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD-----RKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQL 161
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkadelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961237  162 RIMDQTLKALMAAEDKYSQKEDKYE---EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDL----EDELYAQKLKYKA 233
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKA 1400
PTZ00121 PTZ00121
MAEBL; Provisional
 9-216 5.10e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    9 AVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEAD----VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKlviiesdlERAEERAELSEGQVRQLEEQLRIM 164
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA--------DEAKKKAEEDKKKADELKKAAAAK 1417

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568961237  165 DQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKS 216
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
PTZ00121 PTZ00121
MAEBL; Provisional
 15-222 7.06e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   15 RSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEElDRAQERLATALQKLEEAEKAadesERGMKVI 94
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA-KKAEEDKNMALRKAEEAKKA----EEARIEE 1596

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   95 ESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsegQVRQLEEQLRIMDQTLKALMAA 174
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEE 1672

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568961237  175 EDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
PTZ00121 PTZ00121
MAEBL; Provisional
 11-236 8.83e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 8.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQtLKA 170
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-LKK 1640

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961237  171 LMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISE 236
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
7-205 9.13e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 9.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   7 LEAVRRKIRSLQEQAD--AAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3206  191 LEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  85 DESERGMKVIESRAQKDEEKMEIQEIQLKeakhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIM 164
Cdd:COG3206  271 QLAELEAELAELSARYTPNHPDVIALRAQ----IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 568961237 165 DQTLKALMAAEDKYSQKEDKYEEeikvLSDKLKEAETRAEF 205
Cdd:COG3206  347 PELEAELRRLEREVEVARELYES----LLQRLEEARLAEAL 383
PRK09039 PRK09039
peptidoglycan -binding protein;
2-85 2.76e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.49  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   2 AGSSSLEAVRRKIRSL----QEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIqlveEELDRAQERLATALQKL 77
Cdd:PRK09039  88 ASLSAAEAERSRLQALlaelAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI----AALRRQLAALEAALDAS 163


                 ....*...
gi 568961237  78 EEAEKAAD 85
Cdd:PRK09039 164 EKRDRESQ 171
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 47-241 3.23e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  47 ADVASLNRRIQLVEEELDRAQERlatalqkLEEAEKAADESERGMKVIESRAQKDEE----KMEIQEIQLKEAKHIAEDA 122
Cdd:COG1196  165 AGISKYKERKEEAERKLEATEEN-------LERLEDILGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLREL 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237 123 DRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETR 202
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568961237 203 AEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 241
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-248 4.98e-04

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: 41.20  E-value: 4.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    66 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEiQLKEAKHIA-----EDADRKYEEVARKLVIIESDL 140
Cdd:TIGR02168  177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKA-ELRELELALlvlrlEELREELEELQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   141 ERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDL 220
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                          170       180
                   ....*....|....*....|....*...
gi 568961237   221 EDELYAQKLKYKAISEELDHALNDMTSM 248
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAELEEL 363
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
61-239 6.87e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 6.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   61 EELDRAQERLATALQKLEEAEKAADESERgmkviesrAQKDEEKMEIQEIQLKEAKHiaEDADRKYEEVARKLVIIESDL 140
Cdd:COG4913   235 DDLERAHEALEDAREQIELLEPIRELAER--------YAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELRAEL 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  141 ERAEERAELSEGQVRQLEEQLRimdqTLKALMAAEDkySQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDL 220
Cdd:COG4913   305 ARLEAELERLEARLDALREELD----ELEAQIRGNG--GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378

                         170
                  ....*....|....*....
gi 568961237  221 EDELYAQKLKYKAISEELD 239
Cdd:COG4913   379 AEEFAALRAEAAALLEALE 397
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
14-167 7.10e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 7.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  14 IRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 93
Cdd:COG4372   26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961237  94 IESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQT 167
Cdd:COG4372  106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
33-224 8.37e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   33 RELDQERKLRE------TAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKME 106
Cdd:COG4913   590 HEKDDRRRIRSryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE 669

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  107 IQEiqLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLrimDQTLKALMAAEDKYSQKEDKYE 186
Cdd:COG4913   670 IAE--LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLEAAEDLAR 744

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568961237  187 EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDEL 224
Cdd:COG4913   745 LELRALLEERFAAALGDAVERELRENLEERIDALRARL 782
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 12-239 1.17e-03

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: 40.05  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA----EKAADES 87
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaiERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    88 ERGMKVIESRAQKDEEKMEIQEIQLKE-AKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961237   167 TLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELD 239
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
PTZ00121 PTZ00121
MAEBL; Provisional
 19-190 1.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   19 EQADAAEERAGSLQ--RELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEE----AEKAADESERGMK 92
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKK 1689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   93 VIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQlEEQLRIMDQTLKALM 172
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEK 1768

                         170
                  ....*....|....*...
gi 568961237  173 AAEDKYSQKEDKYEEEIK 190
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELD 1786
mukB PRK04863
chromosome partition protein MukB;
7-241 2.00e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLretaeaDVASLNRRIQLVEEELDRAQErlatALQKLEEAEKAADE 86
Cdd:PRK04863  853 LADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLL------ADETLADRVEEIREQLDEAEE----AKRFVQQHGNALAQ 922

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   87 SERGMKVIesraQKDEEKMEIQEIQLKEAKHIAEDADRK---------------YEEVARKLV-------IIESDLERAE 144
Cdd:PRK04863  923 LEPIVSVL----QSDPEQFEQLKQDYQQAQQTQRDAKQQafaltevvqrrahfsYEDAAEMLAknsdlneKLRQRLEQAE 998

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  145 ERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKV-------------------LSDKLKEAETRAEF 205
Cdd:PRK04863  999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpadsgaeerararrdeLHARLSANRSRRNQ 1078

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568961237  206 AERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 241
Cdd:PRK04863 1079 LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 5-204 2.00e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   5 SSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  85 DESERGMKVIE------------SRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG 152
Cdd:COG3883   96 YRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568961237 153 QVRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAE 204
Cdd:COG3883  176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 7-92 2.08e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.91  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   7 LEAVRRKIRSLQ--------EQADAAEERAGSLQRELDQERKLRETAEADVAS---LNRRIQLVEEELDRAQERLATALQ 75
Cdd:COG0542  413 LDELERRLEQLEiekealkkEQDEASFERLAELRDELAELEEELEALKARWEAekeLIEEIQELKEELEQRYGKIPELEK 492

                         90
                 ....*....|....*..
gi 568961237  76 KLEEAEKAADESERGMK 92
Cdd:COG0542  493 ELAELEEELAELAPLLR 509
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 14-219 2.23e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  14 IRSLQEQADAAEERAGSLQRELDQERKLREtaeadvaSLNRRIQLVEEELDRAQERLA-TALQKLEEAEKAADESERGMK 92
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKE-------ELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELR 594

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  93 VIESRAQKDEEKMEIQEIQ--LKEAKHIAEDADRKYEEVARKL-----VIIESDLERAEeraELSEGQVRQLEEQLRIMD 165
Cdd:PRK00409 595 QLQKGGYASVKAHELIEARkrLNKANEKKEKKKKKQKEKQEELkvgdeVKYLSLGQKGE---VLSIPDDKEAIVQAGIMK 671

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568961237 166 QTLKalmAAEDKYSQKEDKYEEE-IKVLSDKLKEAET----RAEFAERSVTKLEKSIDD 219
Cdd:PRK00409 672 MKVP---LSDLEKIQKPKKKKKKkPKTVKPKPRTVSLeldlRGMRYEEALERLDKYLDD 727
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-245 2.40e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   1 MAGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4372   27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  81 EKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQ--VRQLE 158
Cdd:COG4372  107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaEQALD 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237 159 EQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEEL 238
Cdd:COG4372  187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266


                 ....*..
gi 568961237 239 DHALNDM 245
Cdd:COG4372  267 ILVEKDT 273
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
121-241 2.68e-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: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  121 DADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRI------MDQTLKALMAAEDKYSQKEDKYEEeIKVLSD 194
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeYSWDEIDVASAEREIAELEAELER-LDASSD 685

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568961237  195 KLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 241
Cdd:COG4913   686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 7-238 2.71e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.80  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237     7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:pfam02463  232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEER-----------AELSEGQVR 155
Cdd:pfam02463  312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLeeellakkkleSERLSSAAK 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   156 QLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAIS 235
Cdd:pfam02463  392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471


                   ...
gi 568961237   236 EEL 238
Cdd:pfam02463  472 DLL 474
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-222 2.80e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   8 EAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEEL--------------DRAQERLATA 73
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeecrvaaqahneeaESLREDADDL 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  74 LQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQ 153
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961237 154 VRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-140 3.20e-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: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    7 LEAVRRKIRSLQEQADAAE-ERAGSLQRELDQERKLRETAEADVASLNRRIQ-------LVEEELDRAQERLATALQKLE 78
Cdd:COG4913   318 LDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAEAAALLEALE 397

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961237   79 EAEKAADESERGMKVIESRAQKDEEKMEiQEIQLKEAKH--IAEDADRKYEEVARKLVIIESDL 140
Cdd:COG4913   398 EELEALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnIPARLLALRDALAEALGLDEAEL 460
PTZ00121 PTZ00121
MAEBL; Provisional
 2-233 3.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    2 AGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERK---LRETAEADVASLNRrIQLVEEELDRAQE--RLATALQK 76
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADE-LKKAAAAKKKADEakKKAEEKKK 1432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   77 LEEAEKAADESERG---------MKVIESRAQKDEEKMEIQEIQLK-EAKHIAEDADRKYEEVARKLVIIESDLERAEER 146
Cdd:PTZ00121 1433 ADEAKKKAEEAKKAdeakkkaeeAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  147 AELSEGQVRQLEEQLRIMDQTLKA--LMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVT--------KLEKS 216
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeakKAEEA 1592

                         250
                  ....*....|....*..
gi 568961237  217 IDDLEDELYAQKLKYKA 233
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKA 1609
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
14-222 4.54e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  14 IRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 93
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  94 IESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsEGQVRQLEEQLRIMDQTLKALMA 173
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE--EAEALLEAGKCPECGQPVEGSPH 466

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568961237 174 AE--DKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVtKLEKSIDDLED 222
Cdd:PRK02224 467 VEtiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEE 516
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 8-172 4.73e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 38.10  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    8 EAVRRKIRSLQEQADAAEEragSLQReLDQERK-LRETAEadvaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:pfam10168 557 EEIQKRVKLLKLQKEQQLQ---ELQS-LEEERKsLSERAE----KLAEKYEEIKDKQEKLMRRCKKVLQRLNSQLPVLSD 628

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   87 SERGMKvieSRAQKDEEKMEIQEIQLKEAKhiaedadRKYEEVARKLVIIESDLERAEerAELSEGQVRQLEEQLRIMDQ 166
Cdd:pfam10168 629 AEREMK---KELETINEQLKHLANAIKQAK-------KKMNYQRYQIAKSQSIRKKSS--LSLSEKQRKTIKEILKQLGS 696


                  ....*.
gi 568961237  167 TLKALM 172
Cdd:pfam10168 697 EIDELI 702
PTZ00121 PTZ00121
MAEBL; Provisional
 14-223 5.16e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   14 IRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAadESERGMKV 93
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKA 1663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   94 IESRAQKDEEKMEIQEI-QLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsegQVRQLEEQLRIMDQTLKALM 172
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAkKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEA 1739

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568961237  173 AAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDE 223
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
PTZ00121 PTZ00121
MAEBL; Provisional
 7-241 5.59e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237    7 LEAVRR--KIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:PTZ00121 1130 AEEARKaeDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   85 DESergmKVIESRAQKDEEKMEIQEiQLKEAKHIAEDAdRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIM 164
Cdd:PTZ00121 1210 EER----KAEEARKAEDAKKAEAVK-KAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL 1283

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961237  165 DQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLK--EAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHA 241
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-221 6.04e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  17 LQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIqlveEELDRAQERLATALQKLEEAEKAADESERGMKVIES 96
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEE 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  97 RAQKDEEKMEIQEIQLKEAKHIAEDADRK------YEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKA 170
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568961237 171 LMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 24-236 6.31e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 37.80  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   24 AEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEE 103
Cdd:pfam17380 337 AEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQ 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  104 KMEIQEIQLKEAKHIAEDadrkyeevaRKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKED 183
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQ---------REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568961237  184 KYEEEIKVLSDKLKEAETRAEFAERSVTK-LEKSIDDLEDELYAQKLKYKAISE 236
Cdd:pfam17380 488 RAEEQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERRREAEEE 541
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 33-160 6.37e-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: 37.29  E-value: 6.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   33 RELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIql 112
Cdd:pfam05262 192 KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSP-- 269

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568961237  113 KEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQ 160
Cdd:pfam05262 270 KEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEK 317
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-239 6.72e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.71  E-value: 6.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   8 EAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  88 ERGMKVIESRAQKDEEKMEIQEIQLKEAK--------------HIAEDADRKYEEVARKLVIIESDLERAEERAELSEgQ 153
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-D 503

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237 154 VRQLEEQLRIMDQTLKALMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKA 233
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583


                 ....*.
gi 568961237 234 ISEELD 239
Cdd:PRK02224 584 LKERIE 589
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
7-223 8.47e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 37.14  E-value: 8.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERklretaeadvaslnRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG2433  408 LTEEEEEIRRLEEQVERLEAEVEELEAELEEKD--------------ERIERLERELSEARSEERREIRKDREISRLDRE 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  87 SERgmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDaDRKYEEVARKLV--IIESDLERAEERAELSEGQVRQLEEQL--- 161
Cdd:COG2433  474 IER----LERELEEERERIEELKRKLERLKELWKL-EHSGELVPVKVVekFTKEAIRRLEEEYGLKEGDVVYLRDASgag 548

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568961237 162 -----RIMDQTLKALMAAEDKYSQKEDKY-EEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDE 223
Cdd:COG2433  549 rstaeLLAEAGPRAVIVPGELSEAADEVLfEEGIPVLPAEDVTIQEVDDLAVVDEEELEAAIEDWEER 616
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-224 8.76e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.22  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:COG1196  573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRkyEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKA 170
Cdd:COG1196  653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAE--RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568961237 171 LMAAEDKYSQKEDKYEEEIKVLSDKLKEAETRAEfaersvtkLEKSIDDLEDEL 224
Cdd:COG1196  731 EAEREELLEELLEEEELLEEEALEELPEPPDLEE--------LERELERLEREI 776
mukB PRK04863
chromosome partition protein MukB;
11-116 9.18e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 37.24  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELdRAQERLATALQKLEEAEKAADESERG 90
Cdd:PRK04863  292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQADLEELEERLEEQNEV 370

                          90       100
                  ....*....|....*....|....*.
gi 568961237   91 MKVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:PRK04863  371 VEEADEQQEENEARAEAAEEEVDELK 396
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 14-243 9.88e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 36.96  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   14 IRSLQEQADAAEERAGSL------QRELDQERKLRETAEADVASLNRRIQLVEEEL---DRAQERLATALQKLEEAEKAA 84
Cdd:PRK10929   47 VEALQSALNWLEERKGSLerakqyQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMstdALEQEILQVSSQLLEKSRQAQ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237   85 DESERGMKVIESRAQKDEEKMEIQEiQLKEAKH-------------IAEDADRKYEEVARKLVIIESDLER--AEERAEL 149
Cdd:PRK10929  127 QEQDRAREISDSLSQLPQQQTEARR-QLNEIERrlqtlgtpntplaQAQLTALQAESAALKALVDELELAQlsANNRQEL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961237  150 SEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEdkyeeeikvlsdklkeaetrAEFAERSVTKLEKSIDDLEDELYAQkL 229
Cdd:PRK10929  206 ARLRSELAKKRSQQLDAYLQALRNQLNSQRQRE--------------------AERALESTELLAEQSGDLPKSIVAQ-F 264

                         250
                  ....*....|....
gi 568961237  230 KykaISEELDHALN 243
Cdd:PRK10929  265 K---INRELSQALN 275
 
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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