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Conserved domains on  [gi|1069317129|ref|XP_018088639|]
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tropomyosin 4 S homeolog isoform X2 [Xenopus laevis]

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 ...
 12-245 2.43e-63

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: 197.56  E-value: 2.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  12 KKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  92 KVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069317129 172 EAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRTLQEL 245
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAEL 234
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-245 2.43e-63

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: 197.56  E-value: 2.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  12 KKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  92 KVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069317129 172 EAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRTLQEL 245
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAEL 234
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-230 1.48e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   6 SLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  86 ESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVT 165
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069317129 166 NNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEE 230
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-230 3.80e-10

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: 59.69  E-value: 3.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    7 LEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   87 SERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEvselkcsDLEEELKNVTN 166
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069317129  167 NLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEE 230
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
PRK09039 PRK09039
peptidoglycan -binding protein;
2-85 1.38e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   2 AGVNSLEAVKKKIQAL----QQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIqlveEELDRAQERLATALQKL 77
Cdd:PRK09039   88 ASLSAAEAERSRLQALlaelAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI----AALRRQLAALEAALDAS 163


                  ....*...
gi 1069317129  78 EEAEKAAD 85
Cdd:PRK09039  164 EKRDRESQ 171
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-245 2.43e-63

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: 197.56  E-value: 2.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  12 KKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  92 KVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069317129 172 EAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRTLQEL 245
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAEL 234
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-230 1.48e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   6 SLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  86 ESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVT 165
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069317129 166 NNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEE 230
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-248 7.14e-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: 7.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   7 LEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  87 SERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTN 166
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129 167 NLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRTLQELG 246
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487


                  ..
gi 1069317129 247 SL 248
Cdd:COG1196   488 EA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-247 1.01e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   7 LEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196   262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  87 SERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTN 166
Cdd:COG1196   342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129 167 NLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRTLQELG 246
Cdd:COG1196   422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501


                  .
gi 1069317129 247 S 247
Cdd:COG1196   502 D 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-230 3.80e-10

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: 59.69  E-value: 3.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    7 LEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   87 SERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEvselkcsDLEEELKNVTN 166
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069317129  167 NLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEE 230
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-245 4.56e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   7 LEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  87 SERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTN 166
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1069317129 167 NLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRTLQEL 245
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 5-116 1.02e-09

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: 55.39  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   5 NSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEgdvaALNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:pfam12718  35 QEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKA 110

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1069317129  85 DESERGMKVIENRAMKDEEKMDVQEMQLKEAK 116
Cdd:pfam12718 111 EHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-228 2.03e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 2.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    7 LEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   87 SERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTN 166
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1069317129  167 NLKSL-----EAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAK 228
Cdd:TIGR02168  422 EIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-210 7.30e-09

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.84  E-value: 7.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    6 SLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   86 ESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVT 165
Cdd:TIGR02169  382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1069317129  166 NNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTV 210
Cdd:TIGR02169  462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 8-248 8.93e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 8.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   8 EAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  88 ERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNN 167
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129 168 LKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRTLQELGS 247
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460


                  .
gi 1069317129 248 L 248
Cdd:COG1196   461 L 461
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-248 3.24e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   4 VNSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLV---EEELDRAQERLATAL----QK 76
Cdd:COG1196   231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeEYELLAELARLEQDIarleER 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  77 LEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSD 156
Cdd:COG1196   311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129 157 LEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQ 236
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                         250
                  ....*....|..
gi 1069317129 237 VLDRTLQELGSL 248
Cdd:COG1196   471 EAALLEAALAEL 482
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-207 9.04e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 9.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   4 VNSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  84 ADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKN 163
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1069317129 164 VTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAE 207
Cdd:COG1196   454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-248 5.00e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 5.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   5 NSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQ---ERLATALQKLEEAE 81
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEerlEELEEELAELEEEL 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  82 KAADESERGmkvIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEEL 161
Cdd:COG1196   333 EELEEELEE---LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129 162 KNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRT 241
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489


                  ....*..
gi 1069317129 242 LQELGSL 248
Cdd:COG1196   490 AARLLLL 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-230 8.38e-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: 48.99  E-value: 8.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   1 MAGVNSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  81 EKAADESErgmKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEE 160
Cdd:COG4942    96 RAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129 161 LKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEE 230
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 5-221 3.88e-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: 47.76  E-value: 3.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    5 NSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEEL-----DRAQERLATALQKLEE 79
Cdd:TIGR02169  723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSK 802

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   80 AEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEE 159
Cdd:TIGR02169  803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1069317129  160 ELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLE 221
Cdd:TIGR02169  883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-238 3.91e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 3.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    5 NSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLatalQKLEEAEKAA 84
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL----KALREALDEL 808

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   85 DESERGMKVienRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNV 164
Cdd:TIGR02168  809 RAELTLLNE---EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1069317129  165 TNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVL 238
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEAL 959
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-230 8.61e-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: 46.60  E-value: 8.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    6 SLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKaad 85
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ--- 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   86 esergmKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVT 165
Cdd:TIGR02169  752 ------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1069317129  166 NNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEE 230
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-248 9.09e-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: 46.60  E-value: 9.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    4 VNSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQ-LVEEELDRAQERLATALQKLEEAEK 82
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLER 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   83 AADESERGMKVIENRAMKDEEKMDVQEMQLKE-AKHIAEEADRK------YEEVARKLVILEGELERAEERAEVSELKCS 155
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEElEREIEEERKRRdklteeYAELKEELEDLRAELEEVDKEFAETRDELK 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  156 DLEEELKNVTN-------NLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAK 228
Cdd:TIGR02169  389 DYREKLEKLKReinelkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468

                          250       260
                   ....*....|....*....|
gi 1069317129  229 EENLGMHQVLDRTLQELGSL 248
Cdd:TIGR02169  469 QELYDLKEEYDRVEKELSKL 488
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-131 1.85e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    7 LEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEG---------DVAALNRRIQLVEEELDRAQE---RLATAL 74
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALE 691

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1069317129   75 QKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVAR 131
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-133 7.59e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 7.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    7 LEAVKKKIQALQQQADDAEERAQLLQR-------------------ELDSEREMREKAEGDVAALNRRIQLVEEELDRAQ 67
Cdd:COG4913    626 LAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaereiaELEAELERLDASSDDLAALEEQLEELEAELEELE 705

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069317129   68 ERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKL 133
Cdd:COG4913    706 EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-248 1.31e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  10 VKKKIQALQQQADDAEeRAQLLQRELDseremrekaEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 89
Cdd:COG1196   198 LERQLEPLERQAEKAE-RYRELKEELK---------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  90 GMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLK 169
Cdd:COG1196   268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1069317129 170 SLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRTLQELGSL 248
Cdd:COG1196   348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
PRK09039 PRK09039
peptidoglycan -binding protein;
2-85 1.38e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.26  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   2 AGVNSLEAVKKKIQAL----QQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIqlveEELDRAQERLATALQKL 77
Cdd:PRK09039   88 ASLSAAEAERSRLQALlaelAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI----AALRRQLAALEAALDAS 163


                  ....*...
gi 1069317129  78 EEAEKAAD 85
Cdd:PRK09039  164 EKRDRESQ 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-138 1.53e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    7 LEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGD-VAALNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG4913    297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1069317129   86 ESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAE----EADRKYEEVARKLVILEG 138
Cdd:COG4913    377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEaalrDLRRELRELEAEIASLER 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-204 3.15e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   11 KKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 90
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   91 MKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELkcSDLEEELKNvtnnlks 170
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAA------- 757

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1069317129  171 lEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAE 204
Cdd:COG4913    758 -ALGDAVERELRENLEERIDALRARLNRAEEELE 790
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
24-206 3.17e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   24 AEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATA-LQKLEEAEKAADESERGMKVIENRAMKDE 102
Cdd:COG4913    286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  103 EKMDVQEMQLKEAkhiAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKE 182
Cdd:COG4913    366 ALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442

                          170       180
                   ....*....|....*....|....
gi 1069317129  183 DKYEEEIKiltDKLKEAETRAEFA 206
Cdd:COG4913    443 LALRDALA---EALGLDEAELPFV 463
PTZ00121 PTZ00121
MAEBL; Provisional
 8-216 3.71e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    8 EAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERlATALQKLEEAEKAADES 87
Cdd:PTZ00121  1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-AEEKKKADEAKKKAEED 1403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   88 ErgmKVIENRAMKDEEKMDVQEMQLK-EAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTN 166
Cdd:PTZ00121  1404 K---KKADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1069317129  167 NLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKA 216
Cdd:PTZ00121  1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
PTZ00121 PTZ00121
MAEBL; Provisional
 11-244 8.30e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 8.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   11 KKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121  1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   91 MKVIENRAMKDEEKMDVQEMQLKEAKHIAEeadRKYEEVARKLVILEGELERAEERAEVSELKCSDL--EEELKNVTNNL 168
Cdd:PTZ00121  1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEE---ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQL 1638

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1069317129  169 KSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEENLGMHQVLDRTLQE 244
Cdd:PTZ00121  1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-230 1.16e-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: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   31 LQRELDSEREMREKAEgdvAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEM 110
Cdd:TIGR02168  198 LERQLKSLERQAEKAE---RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  111 QLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIK 190
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1069317129  191 ILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKEE 230
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 7-204 1.41e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   7 LEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG3883    18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  87 SERGMKVIE------------NRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKC 154
Cdd:COG3883    98 SGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1069317129 155 SDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAE 204
Cdd:COG3883   178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 33-128 1.46e-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: 39.60  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  33 RELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMDVQEMql 112
Cdd:pfam05262 192 KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSP-- 269

                          90
                  ....*....|....*.
gi 1069317129 113 KEAKHIAEEADRKYEE 128
Cdd:pfam05262 270 KEDKQVAENQKREIEK 285
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-223 1.95e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   2 AGVNSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:COG4372    35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  82 KAADESERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKcsDLEEEL 161
Cdd:COG4372   115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD--ELLKEA 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1069317129 162 KNVTNNLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDK 223
Cdd:COG4372   193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-226 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 1069317129    7 LEAVKKKIQALQQQADDAEERAQLLQReLDSEREMREKAegDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4913    244 LEDAREQIELLEPIRELAERYAAARER-LAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDA 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   87 SERgmKVIENRAMKDEEKMDvqemQLKEAKHIAEEADRKYEEVARKLVILEGEleraeeraevselkCSDLEEELknvTN 166
Cdd:COG4913    321 LRE--ELDELEAQIRGNGGD----RLEQLEREIERLERELEERERRRARLEAL--------------LAALGLPL---PA 377

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  167 NLKSLEAQSEKYSEKEDKYEEEIKILTDKLKEAETRaefaertVTKLEKAIDDLEDKLAS 226
Cdd:COG4913    378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAA-------LRDLRRELRELEAEIAS 430
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
7-93 3.22e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   7 LEAVKKKIQALQQQADDAEERAQLLQRELDSER-EMREKAEGD--VAALNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:COG2433   422 VERLEAEVEELEAELEEKDERIERLERELSEARsEERREIRKDreISRLDREIERLERELEEERERIEELKRKLERLKEL 501

                          90
                  ....*....|
gi 1069317129  84 ADESERGMKV 93
Cdd:COG2433   502 WKLEHSGELV 511
PTZ00121 PTZ00121
MAEBL; Provisional
 8-229 5.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 5.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    8 EAVKKKIQALQQQADDAEE-RAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:PTZ00121  1162 DARKAEEARKAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   87 SERGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEAD-----RKYEEVARKLVILEGELERAEERAEVSELKCSDLEEEL 161
Cdd:PTZ00121  1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkadelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1069317129  162 KNVTNNLKSLEAQSEKYSEKEDKYE---EEIKILTDKLKEAETRAEFAERTVTKLEKAIDDLEDKLASAKE 229
Cdd:PTZ00121  1322 KKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
PTZ00121 PTZ00121
MAEBL; Provisional
 2-216 5.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    2 AGVNSLEAVKKKIQALQQQADDAEERAQLLQRELDSER---EMREKAEGDVAALNRrIQLVEEELDRAQE--RLATALQK 76
Cdd:PTZ00121  1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadEAKKKAEEDKKKADE-LKKAAAAKKKADEakKKAEEKKK 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   77 LEEAEKAADESERG---------MKVIENRAMKDEEKMDVQEMQLK-EAKHIAEEADRKYEEVARKLVILEGELERAEER 146
Cdd:PTZ00121  1433 ADEAKKKAEEAKKAdeakkkaeeAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1069317129  147 AEVSELKCSDLEEELKNVTNNLKSLEAQ--SEKYSEKEDKYEEEIKILTDKLKEAETRAEfAERTVTKLEKA 216
Cdd:PTZ00121  1513 DEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKA 1583
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-172 8.09e-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: 37.34  E-value: 8.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129    5 NSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   85 DESERgMKVIENRAMKDEEKMDVQEmQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSELKCSDLEEELKNV 164
Cdd:TIGR02168  431 EEAEL-KELQAELEELEEELEELQE-ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508


                   ....*...
gi 1069317129  165 TNNLKSLE 172
Cdd:TIGR02168  509 KALLKNQS 516
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 5-188 9.77e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 36.73  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129   5 NSLEAVKKKIQALQQQADDAEERAQLLQRELDSEREMREKAEGDVAALNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3883    23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1069317129  85 DESE------------RGMKVIENRAMKDEEKMDVQEMQLKEAKHIAEEADRKYEEVARKLVILEGELERAEERAEVSEL 152
Cdd:COG3883   103 SYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1069317129 153 KCSDLEEELKNVTNNLKSLEAQSEKYSEKEDKYEEE 188
Cdd:COG3883   183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
 
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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