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Conserved domains on  [gi|1039764806|ref|XP_017175166|]
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tropomyosin alpha-3 chain isoform X3 [Mus musculus]

Protein Classification

tropomyosin( domain architecture ID 11991670)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-246 1.52e-67

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: 208.34  E-value: 1.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  12 RKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  92 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039764806 172 SAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMT 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-246 1.52e-67

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: 208.34  E-value: 1.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  12 RKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  92 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039764806 172 SAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMT 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-228 6.70e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.65  E-value: 6.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   6 TIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMD 165
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039764806 166 QNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQK 228
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-248 8.29e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.69  E-value: 8.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQ 166
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  167 NLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMT 246
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932


                   ..
gi 1039764806  247 SI 248
Cdd:TIGR02168  933 GL 934
PTZ00121 PTZ00121
MAEBL; Provisional
 11-241 1.09e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   11 KRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErg 90
Cdd:PTZ00121  1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-- 1391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   91 mKVIENRALKDEEKMELQEIQLK-EAKHIAEEADRKYEEVARKlviieGDLERTEERAELAESRCREMDEQIRLMDQNLK 169
Cdd:PTZ00121  1392 -KADEAKKKAEEDKKKADELKKAaAAKKKADEAKKKAEEKKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039764806  170 clsaAEEKYSQKEDKYEEEIKiltDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHA 241
Cdd:PTZ00121  1466 ----AEEAKKADEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-246 1.52e-67

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: 208.34  E-value: 1.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  12 RKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  92 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039764806 172 SAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMT 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-228 6.70e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.65  E-value: 6.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   6 TIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMD 165
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039764806 166 QNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQK 228
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-248 8.29e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 64.69  E-value: 8.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQ 166
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  167 NLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMT 246
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932


                   ..
gi 1039764806  247 SI 248
Cdd:TIGR02168  933 GL 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-242 1.74e-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: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQ 166
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764806 167 NLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHAL 242
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 7-116 8.16e-11

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


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 58.47  E-value: 8.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEaevaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:pfam12718  37 IKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEH 112

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039764806  87 SERGMKVIENRALKDEEKMELQEIQLKEAK 116
Cdd:pfam12718 113 LERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-241 2.52e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 2.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   4 TTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  84 ADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRL 163
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039764806 164 MDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHA 241
Cdd:COG1196   412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 8-238 6.37e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 6.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   8 EAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG1196   221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  88 ERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQN 167
Cdd:COG1196   301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039764806 168 LKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDEL 238
Cdd:COG1196   381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-224 1.69e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    2 AGTTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   82 KAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQI 161
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039764806  162 RLMDQNLKCL-----SAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 224
Cdd:TIGR02168  417 ERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-216 1.85e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.61  E-value: 1.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   87 SERgmKVIENRALKDEEKMELQEIQlKEAKHIAEEADRKYEEVARklviIEGDLERTEERAELAESRCREMDEQIRLMDQ 166
Cdd:TIGR02169  383 TRD--ELKDYREKLEKLKREINELK-RELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEW 455

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039764806  167 NLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKT 216
Cdd:TIGR02169  456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-242 3.73e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   7 IEAVKRKIQVLQQQADDAEE-----------RAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQ 75
Cdd:COG1196   195 LGELERQLEPLERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  76 KLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCR 155
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806 156 EMDEQIRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAIS 235
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434


                  ....*..
gi 1039764806 236 DELDHAL 242
Cdd:COG1196   435 EEEEEEE 441
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-190 4.57e-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: 4.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   6 TIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMD 165
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                         170       180
                  ....*....|....*....|....*
gi 1039764806 166 QNLKCLSAAEEKYSQKEDKYEEEIK 190
Cdd:COG1196   477 AALAELLEELAEAAARLLLLLEAEA 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-223 5.33e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 5.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    2 AGTTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   82 KAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERaeLAESRCREMDEQI 161
Cdd:TIGR02168  880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER--LSEEYSLTLEEAE 957

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039764806  162 RLMDQNLKCLSAAEEKYSQKEDKYE----------EEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDE 223
Cdd:TIGR02168  958 ALENKIEDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-235 6.91e-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: 49.38  E-value: 6.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   1 MAGTTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  81 EKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTeeRAELAESRcREMDEQ 160
Cdd:COG4942    96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD--LAELAALR-AELEAE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039764806 161 IRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAIS 235
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 8-241 2.13e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    8 EAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   88 ERGMKviENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQN 167
Cdd:TIGR02169  757 KSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039764806  168 LKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHA 241
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-247 5.23e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 5.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQ 166
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  167 NLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAefAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMT 246
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478


                   .
gi 1039764806  247 S 247
Cdd:TIGR02168  479 A 479
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-240 7.06e-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: 7.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   87 SERGMKVIENRAL-----KDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQI 161
Cdd:TIGR02169  777 LEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039764806  162 RLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDH 240
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
PTZ00121 PTZ00121
MAEBL; Provisional
 11-241 1.09e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   11 KRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErg 90
Cdd:PTZ00121  1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-- 1391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   91 mKVIENRALKDEEKMELQEIQLK-EAKHIAEEADRKYEEVARKlviieGDLERTEERAELAESRCREMDEQIRLMDQNLK 169
Cdd:PTZ00121  1392 -KADEAKKKAEEDKKKADELKKAaAAKKKADEAKKKAEEKKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039764806  170 clsaAEEKYSQKEDKYEEEIKiltDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHA 241
Cdd:PTZ00121  1466 ----AEEAKKADEAKKKAEEA---KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
PTZ00121 PTZ00121
MAEBL; Provisional
 8-237 1.65e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    8 EAVKRKIQVLQQQADDAEE--RAERLQREVEgERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:PTZ00121  1162 DARKAEEARKAEDAKKAEAarKAEEVRKAEE-LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEAD-----RKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQ 160
Cdd:PTZ00121  1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkadelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  161 IRLMDQNLKCLSAAEEKYSQKEDKYE---EEIKILTDKLKEAETRAEFAERSVAKLEKTIDDL----EDELYAQKLKYKA 233
Cdd:PTZ00121  1321 KKKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAkkkaEEKKKADEAKKKA 1400


                   ....
gi 1039764806  234 ISDE 237
Cdd:PTZ00121  1401 EEDK 1404
PTZ00121 PTZ00121
MAEBL; Provisional
 11-200 2.55e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   11 KRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121  1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   91 MKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREmDEQIRLMDQNLKC 170
Cdd:PTZ00121  1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKK 1640

                          170       180       190
                   ....*....|....*....|....*....|
gi 1039764806  171 LSAAEEKYSQKEDKYEEEIKILTDKLKEAE 200
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-213 2.59e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   11 KRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELD--RAQERLATALQKLEEAEKAADESE 88
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   89 rgmkvienralkdeekmELQEiQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQnl 168
Cdd:COG4913    689 -----------------ALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR-- 748

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1039764806  169 kclSAAEEKYSQ--KEDKYEEEIKILTDKLKEAETRAEFAERSVAKL 213
Cdd:COG4913    749 ---ALLEERFAAalGDAVERELRENLEERIDALRARLNRAEEELERA 792
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
6-93 4.27e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   6 TIEAVKRKIQVLQQQADDAEERAERLQREVE---GERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 82
Cdd:COG2433   421 QVERLEAEVEELEAELEEKDERIERLERELSearSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500

                          90
                  ....*....|.
gi 1039764806  83 AADESERGMKV 93
Cdd:COG2433   501 LWKLEHSGELV 511
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-244 5.00e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  26 ERAERLQREVEGeRRAREQAEAEVAslnRRIQLVEEELDRAQERLAtaLQKLEEAEKAADESERGMKVIENRALKDEEKM 105
Cdd:COG1196   189 ERLEDILGELER-QLEPLERQAEKA---ERYRELKEELKELEAELL--LLKLRELEAELEELEAELEELEAELEELEAEL 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806 106 ELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDKY 185
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039764806 186 EEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALND 244
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-166 5.69e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 5.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    7 IEAVKRKIQVLQQQADDAEERAERLQR--EVEGERRAREQAEAEVASLNRRIQLVEE---ELDRAQERLATALQKLEEAE 81
Cdd:COG4913    626 LAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELE 705

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   82 KAADESERGMKVIENR-----ALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCRE 156
Cdd:COG4913    706 EELDELKGEIGRLEKEleqaeEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785

                          170
                   ....*....|
gi 1039764806  157 MDEQIRLMDQ 166
Cdd:COG4913    786 EEELERAMRA 795
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 11-248 5.75e-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: 43.89  E-value: 5.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   11 KRKIQVLQQ--QADDAEERAERLQREVEGE-RRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:TIGR02168  172 ERRKETERKleRTRENLDRLEDILNELERQlKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   88 ERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQN 167
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  168 LKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMTS 247
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411


                   .
gi 1039764806  248 I 248
Cdd:TIGR02168  412 L 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-224 1.09e-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: 43.13  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    7 IEAVKRKIQVLQQQADDAEERAERLQRE-------------------------VEGERRAREQAEAEVASLNRRIQLVEE 61
Cdd:TIGR02169  179 LEEVEENIERLDLIIDEKRQQLERLRRErekaeryqallkekreyegyellkeKEALERQKEAIERQLASLEEELEKLTE 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   62 ELDRAQERLATALQKLEEaekaadESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLE 141
Cdd:TIGR02169  259 EISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  142 RTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLE 221
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412


                   ...
gi 1039764806  222 DEL 224
Cdd:TIGR02169  413 EEL 415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 33-248 1.11e-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: 43.12  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   33 REVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEE----AEKAADESERGMKVIENRALKDEEKMELQ 108
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleqLRKELEELSRQISALRKDLARLEAEVEQL 745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  109 EIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDKYEEE 188
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  189 IKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMTSI 248
Cdd:TIGR02168  826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-192 1.33e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    7 IEAVKRKIQVLQQQADDAEERAERLQR----EVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 82
Cdd:COG4913    244 LEDAREQIELLEPIRELAERYAAARERlaelEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   83 AADESERgmkVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKL-VIIEGDLERTEERAELAESRCREMDEQI 161
Cdd:COG4913    324 ELDELEA---QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALgLPLPASAEEFAALRAEAAALLEALEEEL 400

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039764806  162 RLMDQNLKCLSAAEEKYSQKEDKYEEEIKIL 192
Cdd:COG4913    401 EALEEALAEAEAALRDLRRELRELEAEIASL 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-151 2.00e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   5 TTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039764806  85 DESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAE 151
Cdd:COG1196   473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
13-147 2.19e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 41.57  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  13 KIQVLQQQADDAEERAERLQREVEGERRaREQAEAEVASLNRRIQLVEEELDRAQ---ERLATALQKLEEAEKAADESER 89
Cdd:COG1566    84 ALAQAEAQLAAAEAQLARLEAELGAEAE-IAAAEAQLAAAQAQLDLAQRELERYQalyKKGAVSQQELDEARAALDAAQA 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039764806  90 GMKVIENRALKDEEKMELQEIQlkeakhiaEEADRKYEEVARKLVIIEGDLERTEERA 147
Cdd:COG1566   163 QLEAAQAQLAQAQAGLREEEEL--------AAAQAQVAQAEAALAQAELNLARTTIRA 212
PTZ00121 PTZ00121
MAEBL; Provisional
 19-200 2.29e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   19 QQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRA 98
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   99 LKDEEKMELQEIQLKEAKHI--AEEADRKYEEVARKlviiEGDLERTEERAELAESRCREMDEQIRLMDQnLKCLSAAEE 176
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKK----AEEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEK 1715

                          170       180
                   ....*....|....*....|....
gi 1039764806  177 KYSQKEDKYEEEIKILTDKLKEAE 200
Cdd:PTZ00121  1716 KKAEELKKAEEENKIKAEEAKKEA 1739
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 7-219 5.07e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.97  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRiqlVEEELDRAQERLATALQKLE-------- 78
Cdd:PRK00409  504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEE---LEEKKEKLQEEEDKLLEEAEkeaqqaik 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  79 EAEKAADESERGMKVIENRALKDEEKMELQEIQ--LKEAKHIAEEAdrKYEEVARKLVIIEGD---LERTEERAE-LAES 152
Cdd:PRK00409  581 EAKKEADEIIKELRQLQKGGYASVKAHELIEARkrLNKANEKKEKK--KKKQKEKQEELKVGDevkYLSLGQKGEvLSIP 658

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039764806 153 RCREMDEQIRLMDQNLKcLSAAEEKYSQKEDKyEEEIKILTDKLKEAET----RAEFAERSVAKLEKTIDD 219
Cdd:PRK00409  659 DDKEAIVQAGIMKMKVP-LSDLEKIQKPKKKK-KKKPKTVKPKPRTVSLeldlRGMRYEEALERLDKYLDD 727
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
7-230 5.37e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 5.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQiRLMDQ 166
Cdd:COG4372   106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA-EAEQA 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039764806 167 NLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLK 230
Cdd:COG4372   185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
PTZ00121 PTZ00121
MAEBL; Provisional
 7-233 5.70e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 5.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRARE--QAEAEVASLNRRIQLVEEELDRAQE--RLATALQKLEEAEK 82
Cdd:PTZ00121  1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAAAKKKADEakKKAEEKKKADEAKK 1438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   83 AADESERG---------MKVIENRALKDEEKMELQEIQLK-EAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAES 152
Cdd:PTZ00121  1439 KAEEAKKAdeakkkaeeAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  153 RCREMDEQIRLMDQNLKC--LSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVA--------KLEKTIDDLED 222
Cdd:PTZ00121  1519 EEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAlrkaeeakKAEEARIEEVM 1598

                          250
                   ....*....|.
gi 1039764806  223 ELYAQKLKYKA 233
Cdd:PTZ00121  1599 KLYEEEKKMKA 1609
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5-162 6.75e-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: 6.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    5 TTIEAVKRKIQVLQQQAD-----DAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATA-LQKLE 78
Cdd:COG4913    262 ERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLE 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   79 EAEKAADESERGMKVIENRALKDEEKmeLQEIQLkEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMD 158
Cdd:COG4913    342 QLEREIERLERELEERERRRARLEAL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418


                   ....
gi 1039764806  159 EQIR 162
Cdd:COG4913    419 RELR 422
PTZ00121 PTZ00121
MAEBL; Provisional
 19-190 7.26e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 7.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   19 QQADDAEERAERLQREvEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEE----AEKAADESERGMKVI 94
Cdd:PTZ00121  1613 KKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAA 1691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   95 ENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREmDEQIRLMDQNLKCLSAA 174
Cdd:PTZ00121  1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEKKA 1770

                          170
                   ....*....|....*.
gi 1039764806  175 EEKYSQKEDKYEEEIK 190
Cdd:PTZ00121  1771 EEIRKEKEAVIEEELD 1786
PTZ00121 PTZ00121
MAEBL; Provisional
 18-208 8.38e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 8.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   18 QQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERlatALQKLEEAEKAADESERGmkvieNR 97
Cdd:PTZ00121  1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE---AKKKADEAKKAAEAKKKA-----DE 1514

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   98 ALKDEEKMELQEIQLKEAKHIAEEAdRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEK 177
Cdd:PTZ00121  1515 AKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039764806  178 YSQKEDKYEEEIKILTDKLKEAETRAEFAER 208
Cdd:PTZ00121  1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-239 9.15e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   2 AGTTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEE-- 79
Cdd:PRK02224  339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEElr 418

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  80 ----------AEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHI--AEEADRKYEEVARKLVIIEGDLERTEERA 147
Cdd:PRK02224  419 eerdelrereAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERL 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806 148 ELAESRCREMDEQIRLMDQnlkcLSAAEEKYSQKEDKYEEEIKILTDKLKEA---ETRAEFAERSVAKLEKTIDDLEDEL 224
Cdd:PRK02224  499 ERAEDLVEAEDRIERLEER----REDLEELIAERRETIEEKRERAEELRERAaelEAEAEEKREAAAEAEEEAEEAREEV 574

                         250
                  ....*....|....*
gi 1039764806 225 YAQKLKYKAISDELD 239
Cdd:PRK02224  575 AELNSKLAELKERIE 589
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 5-211 1.15e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   5 TTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  85 DESERGMKVIENRALKDE-----EKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDE 159
Cdd:COG3883    96 YRSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039764806 160 QIRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVA 211
Cdd:COG3883   176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 13-224 1.49e-03

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: 39.55  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   13 KIQVLQQQADDAEERAERLQREVEG------ERRAR-EQAEAEVASLNRRIQLVEEELDRAQER---LATALQKLEEAEK 82
Cdd:COG3096    348 KIERYQEDLEELTERLEEQEEVVEEaaeqlaEAEARlEAAEEEVDSLKSQLADYQQALDVQQTRaiqYQQAVQALEKARA 427

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   83 AADESERGMKVIENRALKDEEKMELQEIQLKEAKH---IAEEADRKYEEVARKLVIIEGDLERTE--ERAELAESRCREM 157
Cdd:COG3096    428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQ 507

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039764806  158 DEQIRLMDQNLKCLSAAEEKYSQKEDKyEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 224
Cdd:COG3096    508 QALAQRLQQLRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 12-233 1.50e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  12 RKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam17380 325 RQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKV 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  92 KVIEnralkdEEKMELQEIQLKEAKHIAEEADRKYEEVARKLviiEGDLERTEERAELAESRCREMDEQIRLMDQNLKCL 171
Cdd:pfam17380 405 KILE------EERQRKIQQQKVEMEQIRAEQEEARQREVRRL---EEERAREMERVRLEEQERQQQVERLRQQEEERKRK 475

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039764806 172 SAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAK-LEKTIDDLEDELYAQKLKYKA 233
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERRREA 538
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
17-221 1.73e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   17 LQQQADDAEERAERLQREVE-GERRAREQAEAEVAS----------LNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG4913    240 AHEALEDAREQIELLEPIRElAERYAAARERLAELEylraalrlwfAQRRLELLEAELEELRAELARLEAELERLEARLD 319

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   86 ESERgmkvienralkdeekmelQEIQLKEAkhIAEEADRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMD 165
Cdd:COG4913    320 ALRE------------------ELDELEAQ--IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764806  166 QNLKclsAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLE 221
Cdd:COG4913    380 EEFA---ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
23-239 1.94e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   23 DAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVE--EELDRAQERLAT-----ALQKLEEAEKAADESERGMKVIE 95
Cdd:COG4913    222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRElaERYAAARERLAEleylrAALRLWFAQRRLELLEAELEELR 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   96 NRALKDEEKMELQEIQLKEAKHIAEEADRKYEEV-ARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLkclsaa 174
Cdd:COG4913    302 AELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL------ 375

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039764806  175 eekysqkedkyEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELD 239
Cdd:COG4913    376 -----------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
6-245 2.04e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   6 TIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEE--RAELAESRCREMDEQIRL 163
Cdd:COG4372   112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAEAEQALDELLKE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806 164 MDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALN 243
Cdd:COG4372   192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271


                  ..
gi 1039764806 244 DM 245
Cdd:COG4372   272 DT 273
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
14-230 2.80e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  14 IQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 93
Cdd:PRK02224  309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  94 IENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAE-----LAESRCREMD---------E 159
Cdd:PRK02224  389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaealLEAGKCPECGqpvegsphvE 468

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039764806 160 QIRLMDQNLKCLSAAEEKYSQKEDKYEEEIKILTDkLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLK 230
Cdd:PRK02224  469 TIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRER 538
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4-140 3.03e-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: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806    4 TTTIEAVKRKIQVLQQQADDAE-ERAERLQREVEGERRAREQAEAEVASLNRRIQ-------LVEEELDRAQERLATALQ 75
Cdd:COG4913    315 EARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAEAAALLE 394

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039764806   76 KLEEAEKAADESERGMKVIENRALKDEEKMElQEIQLKEAKH--IAEEADRKYEEVARKLVIIEGDL 140
Cdd:COG4913    395 ALEEELEALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnIPARLLALRDALAEALGLDEAEL 460
PTZ00121 PTZ00121
MAEBL; Provisional
 25-222 3.14e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   25 EERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEElDRAQERLATALQKLEEAEKAadesERGMKVIENRALKDEEK 104
Cdd:PTZ00121  1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA-KKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKK 1606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  105 MELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAElaesRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDK 184
Cdd:PTZ00121  1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1039764806  185 YEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLED 222
Cdd:PTZ00121  1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
PTZ00121 PTZ00121
MAEBL; Provisional
 25-241 3.85e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806   25 EERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESergmKVIENRALKDEEK 104
Cdd:PTZ00121  1150 DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER----KAEEARKAEDAKK 1225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  105 MELQEiQLKEAKHIAEEAdRKYEEVARKLVIIEGDLERTEERAELAESRCREMDEQIRLMDQNLKCLSAAEEKYSQKEDK 184
Cdd:PTZ00121  1226 AEAVK-KAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039764806  185 YEEEIKILTDKLK--EAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHA 241
Cdd:PTZ00121  1304 ADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
15-198 5.78e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 37.69  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  15 QVLQQQADDAEERAERLQREVEGERRAREQAEAEVA---------SLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764806  86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEAD--RKYEEVARKLVIIEgdlertEERAELAESRCREMDEQIRL 163
Cdd:COG3206   244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsARYTPNHPDVIALR------AQIAALRAQLQQEAQRILAS 317

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039764806 164 MDQNLKCLSAAEEKYSQKEDKYEEEIKILTDKLKE 198
Cdd:COG3206   318 LEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
 
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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