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Conserved domains on  [gi|1539091041|ref|NP_001354767|]
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tropomyosin alpha-4 chain isoform 5 [Homo sapiens]

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 ...
 42-243 7.20e-68

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: 209.11  E-value: 7.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:pfam00261  34 AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:pfam00261 114 KYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAE 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1539091041 202 FAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 243
Cdd:pfam00261 194 FAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 42-243 7.20e-68

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: 209.11  E-value: 7.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:pfam00261  34 AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:pfam00261 114 KYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAE 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1539091041 202 FAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 243
Cdd:pfam00261 194 FAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-227 1.30e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:COG1196   380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                         170       180
                  ....*....|....*....|....*.
gi 1539091041 202 FAERTVAKLEKTIDDLEEKLAQAKEE 227
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEE 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-227 1.47e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   40 TLAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEA 119
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  120 DRKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETR 199
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888

                          170       180
                   ....*....|....*....|....*...
gi 1539091041  200 AEFAERTVAKLEKTIDDLEEKLAQAKEE 227
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRE 916
PTZ00121 PTZ00121
MAEBL; Provisional
 56-226 1.24e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   56 VEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEAD-----RKYEEVARKL 130
Cdd:PTZ00121  1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkadelKKAEEKKKAD 1293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  131 VILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYE---EEIKLLSDKLKEAETRAEFAERTV 207
Cdd:PTZ00121  1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKK 1373

                          170
                   ....*....|....*....
gi 1539091041  208 AKLEKTIDDLEEKLAQAKE 226
Cdd:PTZ00121  1374 EEAKKKADAAKKKAEEKKK 1392
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 42-243 7.20e-68

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: 209.11  E-value: 7.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:pfam00261  34 AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:pfam00261 114 KYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAE 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1539091041 202 FAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 243
Cdd:pfam00261 194 FAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 48-113 2.51e-13

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: 65.02  E-value: 2.51e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1539091041  48 ALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAK 113
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-227 1.30e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:COG1196   380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                         170       180
                  ....*....|....*....|....*.
gi 1539091041 202 FAERTVAKLEKTIDDLEEKLAQAKEE 227
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEE 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 40-227 1.47e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   40 TLAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEA 119
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  120 DRKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETR 199
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888

                          170       180
                   ....*....|....*....|....*...
gi 1539091041  200 AEFAERTVAKLEKTIDDLEEKLAQAKEE 227
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRE 916
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-243 1.77e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1539091041 202 FAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 243
Cdd:COG1196   446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 41-242 2.06e-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: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  41 LAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEAD 120
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 121 RKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRA 200
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1539091041 201 EFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNEL 242
Cdd:COG1196   403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-227 2.22e-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: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                         170       180
                  ....*....|....*....|....*.
gi 1539091041 202 FAERTVAKLEKTIDDLEEKLAQAKEE 227
Cdd:COG1196   474 LLEAALAELLEELAEAAARLLLLLEA 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 41-242 1.72e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  41 LAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEAD 120
Cdd:COG1196   250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 121 RKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRA 200
Cdd:COG1196   330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1539091041 201 EFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNEL 242
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
51-227 1.64e-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: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   51 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQE-----MQLKEAKHIAEEADRKYEE 125
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiAELEAELERLDASSDDLAA 689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  126 VARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEkysEKEDKYEEEIKLLSDKLKEAETRAEFAER 205
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFAAALGDAVERE 766

                          170       180
                   ....*....|....*....|..
gi 1539091041  206 TVAKLEKTIDDLEEKLAQAKEE 227
Cdd:COG4913    767 LRENLEERIDALRARLNRAEEE 788
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 66-242 4.29e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  66 RLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAE 145
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 146 VSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAK 225
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                         170
                  ....*....|....*..
gi 1539091041 226 EENVGLHQTLDQTLNEL 242
Cdd:COG1196   393 RAAAELAAQLEELEEAE 409
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 34-237 5.66e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 5.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  34 APPPRPTLAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADEsergmkvIENRAMKDEEKMEIQEMQLKEAK 113
Cdd:COG3883     6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDKLQAEIAEAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 114 HIAEEADRKYEEVARKL-----------VILEGeleraeerAEVSEL--KCGDLEEELKNVTNNLKSLEAASEKYSEKED 180
Cdd:COG3883    79 AEIEERREELGERARALyrsggsvsyldVLLGS--------ESFSDFldRLSALSKIADADADLLEELKADKAELEAKKA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539091041 181 KYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQ 237
Cdd:COG3883   151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-243 5.74e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  58 EELDRAQERLAtaLQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGEL 137
Cdd:COG1196   220 EELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 138 ERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDL 217
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180
                  ....*....|....*....|....*.
gi 1539091041 218 EEKLAQAKEENVGLHQTLDQTLNELN 243
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLE 403
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-227 1.18e-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: 1.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   54 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVIL 133
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  134 EGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKT 213
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                          170
                   ....*....|....
gi 1539091041  214 IDDLEEKLAQAKEE 227
Cdd:TIGR02168  381 LETLRSKVAQLELQ 394
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 42-227 2.58e-05

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: 45.06  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR-----AMKDEEKMEIQEMQLKEAKHIA 116
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARieeleEDLHKLEEALNDLEARLSHSRI 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  117 EEADRKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEA 196
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL 873

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1539091041  197 ETRAEFAERTVAKLEKTIDDLEEKLAQAKEE 227
Cdd:TIGR02169  874 EAALRDLESRLGDLKKERDELEAQLRELERK 904
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-207 2.80e-05

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: 45.06  E-value: 2.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   43 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRK 122
Cdd:TIGR02169  342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  123 YEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEF 202
Cdd:TIGR02169  422 LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501


                   ....*
gi 1539091041  203 AERTV 207
Cdd:TIGR02169  502 SEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 42-236 2.85e-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: 45.05  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1539091041  202 FAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLD 236
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 42-243 3.04e-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: 44.66  E-value: 3.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLE-------------------AASEKYSEKEDKY 182
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLElqiaslnneierlearlerLEDRRERLQQEIE 424

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1539091041  183 EEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNELN 243
Cdd:TIGR02168  425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 42-222 4.05e-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: 44.28  E-value: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkvienRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE-------EAANLRERLESLERRIAATERRLEDLEE 845

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925

                          170       180
                   ....*....|....*....|.
gi 1539091041  202 FAERTVAKLEKTIDDLEEKLA 222
Cdd:TIGR02168  926 QLELRLEGLEVRIDNLQERLS 946
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 23-237 4.86e-05

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: 44.29  E-value: 4.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   23 ARRIEGWNSNEAPPPRPTLAE--GDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER--GMKVIENRAMKD 98
Cdd:TIGR02169  278 NKKIKDLGEEEQLRVKEKIGEleAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEReiEEERKRRDKLTE 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   99 EEKMEIQEMQLKEAKhiAEEADRKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEK 178
Cdd:TIGR02169  358 EYAELKEELEDLRAE--LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1539091041  179 EDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQ 237
Cdd:TIGR02169  436 INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
49-233 9.95e-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: 9.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  49 LNRRIQLVEEELDRA----QERLATALQKLEEAEKAADE--SERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRK 122
Cdd:COG3206   162 LEQNLELRREEARKAleflEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 123 YEEVARKLVILEGELERAEERAEVSELKC------GDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLsdkLKEA 196
Cdd:COG3206   242 LAALRAQLGSGPDALPELLQSPVIQQLRAqlaeleAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI---LASL 318

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1539091041 197 ETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQ 233
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
PTZ00121 PTZ00121
MAEBL; Provisional
 56-226 1.24e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   56 VEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEAD-----RKYEEVARKL 130
Cdd:PTZ00121  1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkadelKKAEEKKKAD 1293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  131 VILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYE---EEIKLLSDKLKEAETRAEFAERTV 207
Cdd:PTZ00121  1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKK 1373

                          170
                   ....*....|....*....
gi 1539091041  208 AKLEKTIDDLEEKLAQAKE 226
Cdd:PTZ00121  1374 EEAKKKADAAKKKAEEKKK 1392
PTZ00121 PTZ00121
MAEBL; Provisional
 51-226 1.56e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   51 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARkl 130
Cdd:PTZ00121  1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-- 1392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  131 vilegeleraeeraeVSELKcgDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKL 210
Cdd:PTZ00121  1393 ---------------ADEAK--KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455

                          170
                   ....*....|....*.
gi 1539091041  211 EKTIDDLEEKLAQAKE 226
Cdd:PTZ00121  1456 AKKAEEAKKKAEEAKK 1471
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 42-242 1.78e-04

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: 42.06  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAmkDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:COG4942    25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--AALEAELAELEKEIAELRAELEAQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 122 KyEEVARKLVILEGELERAEERAEVSElkcgdleEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:COG4942   103 K-EELAELLRALYRLGRQPPLALLLSP-------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1539091041 202 FAERTVAKLEKtiddLEEKLAQAKEENVGLHQTLDQTLNEL 242
Cdd:COG4942   175 ELEALLAELEE----ERAALEALKAERQKLLARLEKELAEL 211
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 37-242 2.48e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  37 PRPTLAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEakhIA 116
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---RA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 117 EEADRKYEEVARKLVILEGELEraeeraevselkcGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEA 196
Cdd:COG3883    93 RALYRSGGSVSYLDVLLGSESF-------------SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1539091041 197 ETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNEL 242
Cdd:COG3883   160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 169-241 3.13e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539091041 169 EAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNE 241
Cdd:PRK00409  505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
PTZ00121 PTZ00121
MAEBL; Provisional
 58-228 3.54e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 3.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   58 EELDRAQERLATALQKLEEAEKAadESERGMKVIenRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEgeL 137
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKA--EEARIEEVM--KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK--K 1640

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  138 ERAEERAEVSELKcgDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDL 217
Cdd:PTZ00121  1641 KEAEEKKKAEELK--KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718

                          170
                   ....*....|.
gi 1539091041  218 EEkLAQAKEEN 228
Cdd:PTZ00121  1719 EE-LKKAEEEN 1728
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 52-237 3.74e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.48  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   52 RIQLVEEELDRAQERLA-----------------TALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKH 114
Cdd:COG3096    383 RLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQ 462

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  115 ---IAEEADRKYEEVARKLVILEGELERAEERAEVSELkcgdLEE--ELKNVTNNLKSLEAA---SEKYSEKEDKYEEEI 186
Cdd:COG3096    463 klsVADAARRQFEKAYELVCKIAGEVERSQAWQTAREL----LRRyrSQQALAQRLQQLRAQlaeLEQRLRQQQNAERLL 538

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1539091041  187 KLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQ 237
Cdd:COG3096    539 EEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 70-221 5.10e-04

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: 41.21  E-value: 5.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   70 ALQKLEEAEKAADESErGMKVIENRAMKDEEKmeiQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSEL 149
Cdd:TIGR02169  669 SRSEPAELQRLRERLE-GLKRELSSLQSELRR---IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1539091041  150 KCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKL-----KEAETRAEFAERTVAKLEKTIDDLEEKL 221
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKL 821
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
51-227 6.32e-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: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   51 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKD--EEKMEIQEmQLKEAKHIAEEADRKYEEVAR 128
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLER-EIERLERELEERERRRARLEA 366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  129 KLVILEgeleraeeraevselkcGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVA 208
Cdd:COG4913    367 LLAALG-----------------LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429

                          170
                   ....*....|....*....
gi 1539091041  209 KLEKTIDDLEEKLAQAKEE 227
Cdd:COG4913    430 SLERRKSNIPARLLALRDA 448
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 156-242 6.98e-04

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: 40.13  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 156 EELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTL 235
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99


                  ....*..
gi 1539091041 236 DQTLNEL 242
Cdd:COG4942   100 EAQKEEL 106
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 52-242 8.50e-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: 40.43  E-value: 8.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   52 RIQLVEEELDRAQERL------ATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIA--------- 116
Cdd:TIGR02168  190 RLEDILNELERQLKSLerqaekAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAelqeleekl 269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  117 EEADRKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEA 196
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1539091041  197 ET-------RAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNEL 242
Cdd:TIGR02168  350 KEelesleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-236 9.30e-04

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: 9.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   43 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRK 122
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  123 YEEVARKLVILEGELERAEERAEVSELKCGDLEEELknvtnnlksLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEF 202
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARL---------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1539091041  203 AERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLD 236
Cdd:TIGR02169  824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 43-225 1.05e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   43 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRK 122
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  123 YEEVARK--------------LVILEGELEraeeraevselkcgDLEEELKNVTNNLKSL-----EAASEKYSEKEDKYE 183
Cdd:TIGR02168  381 LETLRSKvaqlelqiaslnneIERLEARLE--------------RLEDRRERLQQEIEELlkkleEAELKELQAELEELE 446

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1539091041  184 EEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAK 225
Cdd:TIGR02168  447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-242 1.27e-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: 39.67  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   43 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEaekaadESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRK 122
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  123 YEEVARKLVILEgeleraeeraevselkcgdleEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEF 202
Cdd:TIGR02169  317 LEDAEERLAKLE---------------------AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1539091041  203 AERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQTLNEL 242
Cdd:TIGR02169  376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 51-125 1.64e-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: 39.22  E-value: 1.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539091041  51 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMqlKEAKHIAEEADRKYEE 125
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSP--KEDKQVAENQKREIEK 285
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
52-227 1.97e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  52 RIQLVEEELDRAQERLATALQKLEEAEKAAdESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLV 131
Cdd:PRK02224  476 RVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 132 ILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDkYEEEIKLLSDKLKEAETRAEFAERTVAKLE 211
Cdd:PRK02224  555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKR 633

                         170
                  ....*....|....*.
gi 1539091041 212 KTIDDLEEKLAQAKEE 227
Cdd:PRK02224  634 ERKRELEAEFDEARIE 649
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 49-225 2.03e-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: 39.28  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   49 LNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVAR 128
Cdd:TIGR02169  320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  129 KLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVA 208
Cdd:TIGR02169  400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479

                          170
                   ....*....|....*..
gi 1539091041  209 KLEKTIDDLEEKLAQAK 225
Cdd:TIGR02169  480 RVEKELSKLQRELAEAE 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 42-230 2.20e-03

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: 38.59  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  42 AEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADR 121
Cdd:COG4942    60 LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVR 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 122 KYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAE 201
Cdd:COG4942   137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216

                         170       180
                  ....*....|....*....|....*....
gi 1539091041 202 FAERTVAKLEKTIDDLEEKLAQAKEENVG 230
Cdd:COG4942   217 ELQQEAEELEALIARLEAEAAAAAERTPA 245
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 42-243 2.60e-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: 38.90  E-value: 2.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   42 AEGDVAALNRRIQ-LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLkeakhiaEEAD 120
Cdd:TIGR02169  270 IEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI-------EELE 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  121 RKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEK-------EDKYEEEIKLLSDKL 193
Cdd:TIGR02169  343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREinelkreLDRLQEELQRLSEEL 422

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539091041  194 KEAETRAEFAERTVAKLEKTIDDL-------EEKLAQAKEENVGLHQTLDQTLNELN 243
Cdd:TIGR02169  423 ADLNAAIAGIEAKINELEEEKEDKaleikkqEWKLEQLAADLSKYEQELYDLKEEYD 479
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 49-190 2.64e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  49 LNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmKVIENRAMKDEEKMEiqemQLKEAKHIAEEADRKYEEVAR 128
Cdd:PRK00409  518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEE--KKEKLQEEEDKLLEE----AEKEAQQAIKEAKKEADEIIK 591

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1539091041 129 KLVILEgeleraeeRAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYE--EEIKLLS 190
Cdd:PRK00409  592 ELRQLQ--------KGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKvgDEVKYLS 647
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
41-226 3.20e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  41 LAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEAD 120
Cdd:PRK02224  304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 121 RKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAaseKYSEKEDKYEEEIKLLS---------- 190
Cdd:PRK02224  384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA---TLRTARERVEEAEALLEagkcpecgqp 460

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1539091041 191 -------DKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKE 226
Cdd:PRK02224  461 vegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
mukB PRK04863
chromosome partition protein MukB;
41-237 3.66e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.40  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   41 LAEGDVAALNRRIQLVEEELDRAQERLA-----------------TALQKLEEAEKAADESERGMKVIENR--AMKDEEK 101
Cdd:PRK04863   373 EADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQLCGLPDLTADNAEDWleEFQAKEQ 452

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  102 MEIQEM-QLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELkCGDLEEElKNVTNNLKSLEAaseKYSEKED 180
Cdd:PRK04863   453 EATEELlSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVAREL-LRRLREQ-RHLAEQLQQLRM---RLSELEQ 527

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1539091041  181 KYEEE---IKLLSD---KLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGLHQTLDQ 237
Cdd:PRK04863   528 RLRQQqraERLLAEfckRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
PTZ00121 PTZ00121
MAEBL; Provisional
 57-219 3.81e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   57 EEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIAEEADRKYEEVARKLVILEGE 136
Cdd:PTZ00121  1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK 1736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  137 LERAEERAEVSELKcgdLEEELKNVTNNLKSLE--AASEKYSEKEDKYEEEIKllsdklKEAETRAEFAERTVAKLEKTI 214
Cdd:PTZ00121  1737 KEAEEDKKKAEEAK---KDEEEKKKIAHLKKEEekKAEEIRKEKEAVIEEELD------EEDEKRRMEVDKKIKDIFDNF 1807


                   ....*
gi 1539091041  215 DDLEE 219
Cdd:PTZ00121  1808 ANIIE 1812
PTZ00121 PTZ00121
MAEBL; Provisional
 23-226 4.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   23 ARRIEGWNSNEAPPPrptLAEGDVAALNRRIQLVEEEldraQERLATALQKLEEAEKA--ADESERGMKVIENRAmKDEE 100
Cdd:PTZ00121  1242 AKKAEEERNNEEIRK---FEEARMAHFARRQAAIKAE----EARKADELKKAEEKKKAdeAKKAEEKKKADEAKK-KAEE 1313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  101 KMEIQEMQLK--EAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCGDLE---EELKNVTNNLKSlEAASEKY 175
Cdd:PTZ00121  1314 AKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkEEAKKKADAAKK-KAEEKKK 1392

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1539091041  176 SEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLE--KTIDDLEEKLAQAKE 226
Cdd:PTZ00121  1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEEAKK 1445
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
153-227 4.74e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 37.92  E-value: 4.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539091041 153 DLEEELKNVTNnlKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEE 227
Cdd:COG2433   384 ELIEKELPEEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE 456
mukB PRK04863
chromosome partition protein MukB;
88-227 6.09e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 37.63  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041   88 MKVIENRAMKDEEKMEIQEmQLKEAKHIAEEADRKYEEVARKLVILEGELeraeeraevselkcGDLEEELKNVTNNLKS 167
Cdd:PRK04863   275 MRHANERRVHLEEALELRR-ELYTSRRQLAAEQYRLVEMARELAELNEAE--------------SDLEQDYQAASDHLNL 339

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1539091041  168 LEAAsEKYSEKEDKYEEEIKLLSDKLKEA-ETRAEFAERtvaklektIDDLEEKLAQAKEE 227
Cdd:PRK04863   340 VQTA-LRQQEKIERYQADLEELEERLEEQnEVVEEADEQ--------QEENEARAEAAEEE 391
PRK12704 PRK12704
phosphodiesterase; Provisional
 110-231 6.33e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.45  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 110 KEAKHIAEEADRKYEEVaRKLVILEGELERAEERAevselkcgDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLL 189
Cdd:PRK12704   38 EEAKRILEEAKKEAEAI-KKEALLEAKEEIHKLRN--------EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1539091041 190 SDKLKEAETRAEFAERTVAKLEKTIDDLEEKLAQAKEENVGL 231
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL 150
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
43-227 6.37e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.71  E-value: 6.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  43 EGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMK---DEEKMEIQEMQLKEAKHIAEEA 119
Cdd:PRK02224  212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETiaeTEREREELAEEVRDLRERLEEL 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 120 DRKYEEVARKLVILEGELERAEERAEVSELKCGDLEEELKNVTNNLKSLEAASEKYSEKEDKYEEEIKLLSDKLKEAETR 199
Cdd:PRK02224  292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                         170       180
                  ....*....|....*....|....*...
gi 1539091041 200 AEFAERTVAKLEKTIDDLEEKLAQAKEE 227
Cdd:PRK02224  372 LEEAREAVEDRREEIEELEEEIEELRER 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 37-220 6.77e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.61  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041  37 PRPTLAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMEIQEMQLKEAKHIA 116
Cdd:COG1196   658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539091041 117 EEADRKYEEVARKLVILEGELERAEEraevselkcgDLEEELKNVTNNLKSLEA----ASEKYSEKEDKYEEeiklLSDK 192
Cdd:COG1196   738 LEELLEEEELLEEEALEELPEPPDLE----------ELERELERLEREIEALGPvnllAIEEYEELEERYDF----LSEQ 803

                         170       180
                  ....*....|....*....|....*...
gi 1539091041 193 LKEaetraefAERTVAKLEKTIDDLEEK 220
Cdd:COG1196   804 RED-------LEEARETLEEAIEEIDRE 824
 
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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