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Conserved domains on  [gi|52353308|ref|NP_476556|]
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tropomyosin alpha-3 chain isoform Tpm3.4cy [Rattus norvegicus]

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 2.36e-68

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


:

Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 210.27  E-value: 2.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    12 RKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    92 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52353308   172 EAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELKLTLHGL 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 2.36e-68

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


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 210.27  E-value: 2.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    12 RKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    92 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52353308   172 EAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELKLTLHGL 245
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAEL 234
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-229 1.62e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   6 TIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVT 165
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52353308 166 NNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLE 229
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-245 3.93e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.46  E-value: 3.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTN 166
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    167 NLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEER---LYSQLERNRLLSNELKLTLH 243
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrseLRRELEELREKLAQLELRLE 932


                   ..
gi 52353308    244 GL 245
Cdd:TIGR02168  933 GL 934
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 13-238 1.71e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.51  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    13 KIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVAS--LNRRI-----QLVEE------ELDRAQE---RLATALQK 76
Cdd:PRK10929   66 RAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTdaLEQEIlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQ 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    77 LEEAEKAADESERGMKVIENRALKDEEkmelqeiqlkeakhiAEEADRKYEEVARKLVIIEGDLE------RTE---ERA 147
Cdd:PRK10929  146 QTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAESAALKALVDELELAqlsannRQElarLRS 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   148 ELAESKCSELEEELKNVTNNLKSLEaqaekysQKEdkyeeeikiltdklkeaetrAEFAERSVAKLEKTIDDLEERLYSQ 227
Cdd:PRK10929  211 ELAKKRSQQLDAYLQALRNQLNSQR-------QRE--------------------AERALESTELLAEQSGDLPKSIVAQ 263

                         250
                  ....*....|.
gi 52353308   228 LERNRLLSNEL 238
Cdd:PRK10929  264 FKINRELSQAL 274
 
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 2.36e-68

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


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 210.27  E-value: 2.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    12 RKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    92 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52353308   172 EAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELKLTLHGL 245
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAEL 234
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-229 1.62e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   6 TIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVT 165
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52353308 166 NNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLE 229
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-240 1.44e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 1.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQ-------LVEEELDRAQERLATALQKLEE 79
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyELLAELARLEQDIARLEERRRE 313

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  80 AEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEE 159
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308 160 ELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELK 239
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473


                .
gi 52353308 240 L 240
Cdd:COG1196 474 L 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-245 3.93e-12

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.46  E-value: 3.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTN 166
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    167 NLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEER---LYSQLERNRLLSNELKLTLH 243
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrseLRRELEELREKLAQLELRLE 932


                   ..
gi 52353308    244 GL 245
Cdd:TIGR02168  933 GL 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-238 2.11e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 2.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   5 TTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  85 DESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNV 164
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52353308 165 TNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNEL 238
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 8-242 7.56e-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: 7.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   8 EAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  88 ERGMKV-------IENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEE 160
Cdd:COG1196 301 EQDIARleerrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308 161 LKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELKL 240
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460


                ..
gi 52353308 241 TL 242
Cdd:COG1196 461 LL 462
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 7-116 8.06e-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: 8.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEaevaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:pfam12718  37 IKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEH 112

                          90       100       110
                  ....*....|....*....|....*....|
gi 52353308    87 SERGMKVIENRALKDEEKMELQEIQLKEAK 116
Cdd:pfam12718 113 LERKVQALEQERDEWEKKYEELEEKYKEAK 142
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-210 2.75e-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: 57.00  E-value: 2.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02169  303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTN 166
Cdd:TIGR02169  383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 52353308    167 NLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSV 210
Cdd:TIGR02169  463 DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-239 6.37e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 6.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   7 IEAVKRKIQVLQQQADDAEE----RAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 82
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  83 AADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELK 162
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52353308 163 NVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELK 239
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-240 1.16e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      2 AGSTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     82 KAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEEL 161
Cdd:TIGR02168  337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52353308    162 KNVTNNLKSLEAQAEkySQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELKL 240
Cdd:TIGR02168  417 ERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-230 1.49e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.38  E-value: 1.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   1 MAGSTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4942  16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  81 EKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTeeRAELAESKcSELEEE 160
Cdd:COG4942  96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD--LAELAALR-AELEAE 172

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308 161 LKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLER 230
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-190 6.96e-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: 6.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   6 TIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVT 165
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                       170       180
                ....*....|....*....|....*
gi 52353308 166 NNLKSLEAQAEKYSQKEDKYEEEIK 190
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEA 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 13-224 8.76e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 8.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     13 KIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEaekaadesergmk 92
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR------------- 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     93 vIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLE 172
Cdd:TIGR02168  300 -LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 52353308    173 AQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERL 224
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-222 1.15e-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: 52.38  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEEL------------DRAQERLATAL 74
Cdd:TIGR02169  718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleealndleaRLSHSRIPEIQ 797

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     75 QKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKC 154
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52353308    155 SELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEE 222
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-230 1.40e-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: 51.98  E-value: 1.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      7 IEAVKRKIQVLQQQAddaeERAERLQREVEGERrareqaEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  195 LNELERQLKSLERQA----EKAERYKELKAELR------ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTN 166
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52353308    167 NLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLER 230
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-239 2.13e-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: 51.21  E-value: 2.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      4 STTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168  280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     84 ADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELeeELKN 163
Cdd:TIGR02168  360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKE 437

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52353308    164 VTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELK 239
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 32-224 2.75e-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: 51.21  E-value: 2.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     32 QREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQ 111
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    112 LKEAKHIAEEADRKYE-------EVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDK 184
Cdd:TIGR02168  756 LTELEAEIEELEERLEeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 52353308    185 YEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERL 224
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 8-242 4.46e-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: 50.45  E-value: 4.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      8 EAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     88 ERGMKVIENR-----ALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEG-------DLERTEERAELAESKCS 155
Cdd:TIGR02169  757 KSELKELEARieeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlreieqKLNRLTLEKEYLEKEIQ 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    156 ELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEER---LYSQLERNR 232
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKieeLEAQIEKKR 916

                          250
                   ....*....|
gi 52353308    233 LLSNELKLTL 242
Cdd:TIGR02169  917 KRLSELKAKL 926
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-239 5.40e-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: 50.07  E-value: 5.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     87 SERGMKVIENRAL-----KDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEEL 161
Cdd:TIGR02169  777 LEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52353308    162 KNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELK 239
Cdd:TIGR02169  857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-239 8.45e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 8.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      7 IEAVKRKIQVLQQQADDAEERAERLQRE-------------------------VEGERRAREQAEAEVASLNRRIQLVEE 61
Cdd:TIGR02169  179 LEEVEENIERLDLIIDEKRQQLERLRRErekaeryqallkekreyegyellkeKEALERQKEAIERQLASLEEELEKLTE 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     62 ELDRAQERLATALQKLEEaekaadESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLE 141
Cdd:TIGR02169  259 EISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEID 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    142 RTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLE 221
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412

                          250
                   ....*....|....*...
gi 52353308    222 ERLYSQLERNRLLSNELK 239
Cdd:TIGR02169  413 EELQRLSEELADLNAAIA 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-224 1.26e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTN 166
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 52353308    167 NLKSLEAQAEKYSQKEDKYEEEIKIL-TDKLKEAETRAEFAERSVAKLEKTIDDLEERL 224
Cdd:TIGR02168  923 KLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-176 1.66e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.51  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308      7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     87 SERGMKviENRALKDEEKMELQEIQLKEA---KHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSEL------ 157
Cdd:TIGR02168  913 LRRELE--ELREKLAQLELRLEGLEVRIDnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnla 990

                          170       180
                   ....*....|....*....|
gi 52353308    158 -EEELKNVTNNLKSLEAQAE 176
Cdd:TIGR02168  991 aIEEYEELKERYDFLTAQKE 1010
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 13-238 1.71e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 48.51  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    13 KIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVAS--LNRRI-----QLVEE------ELDRAQE---RLATALQK 76
Cdd:PRK10929   66 RAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTdaLEQEIlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQ 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    77 LEEAEKAADESERGMKVIENRALKDEEkmelqeiqlkeakhiAEEADRKYEEVARKLVIIEGDLE------RTE---ERA 147
Cdd:PRK10929  146 QTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAESAALKALVDELELAqlsannRQElarLRS 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   148 ELAESKCSELEEELKNVTNNLKSLEaqaekysQKEdkyeeeikiltdklkeaetrAEFAERSVAKLEKTIDDLEERLYSQ 227
Cdd:PRK10929  211 ELAKKRSQQLDAYLQALRNQLNSQR-------QRE--------------------AERALESTELLAEQSGDLPKSIVAQ 263

                         250
                  ....*....|.
gi 52353308   228 LERNRLLSNEL 238
Cdd:PRK10929  264 FKINRELSQAL 274
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
5-206 3.18e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    5 TTIEAVKRKIQVLQQQAD-----DAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATA-LQKLE 78
Cdd:COG4913  262 ERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLE 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   79 EAEKAADESERGMKVIENRALKDEEKmeLQEIQLkEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELE 158
Cdd:COG4913  342 QLEREIERLERELEERERRRARLEAL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 52353308  159 EELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKiltDKLKEAETRAEFA 206
Cdd:COG4913  419 RELRELEAEIASLERRKSNIPARLLALRDALA---EALGLDEAELPFV 463
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-233 3.30e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   11 KRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 90
Cdd:COG4913  609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   91 MKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESkcSELEEELKNvtnnlks 170
Cdd:COG4913  687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAA------- 757

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52353308  171 lEAQAEKYSQKEDKYEEEIKILTDKLKEAETR-----AEFAER---SVAKLEKTIDDLEE--RLYSQLERNRL 233
Cdd:COG4913  758 -ALGDAVERELRENLEERIDALRARLNRAEEEleramRAFNREwpaETADLDADLESLPEylALLDRLEEDGL 829
PTZ00121 PTZ00121
MAEBL; Provisional
 11-232 3.41e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    11 KRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    91 MKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVtNNLKS 170
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-EQLKK 1640

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52353308   171 LEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNR 232
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-192 7.34e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 7.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    7 IEAVKRKIQVLQQQADDAEERAERLQR----EVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 82
Cdd:COG4913  244 LEDAREQIELLEPIRELAERYAAARERlaelEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   83 AADESERgmkVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKL-VIIEGDLERTEERAELAESKCSELEEEL 161
Cdd:COG4913  324 ELDELEA---QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALgLPLPASAEEFAALRAEAAALLEALEEEL 400

                        170       180       190
                 ....*....|....*....|....*....|.
gi 52353308  162 KNVTNNLKSLEAQAEKYSQKEDKYEEEIKIL 192
Cdd:COG4913  401 EALEEALAEAEAALRDLRRELRELEAEIASL 431
PTZ00121 PTZ00121
MAEBL; Provisional
 23-223 1.01e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    23 DAEERAERLQREVEgERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDE 102
Cdd:PTZ00121 1179 EAARKAEEVRKAEE-LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKF 1257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   103 EKMELQEIQLKEAKHIAEEAdRKYEEVARKLVIIEGDLERTEERAELAES---------KCSELEEELKNVTNNLKSLEA 173
Cdd:PTZ00121 1258 EEARMAHFARRQAAIKAEEA-RKADELKKAEEKKKADEAKKAEEKKKADEakkkaeeakKADEAKKKAEEAKKKADAAKK 1336

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 52353308   174 QAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEER 223
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 5-211 1.11e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   5 TTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3883  16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  85 DESERGMKVIE------------NRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAES 152
Cdd:COG3883  96 YRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 52353308 153 KCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVA 211
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
8-224 1.52e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   8 EAVKRKIQVLQQQADDAEERAERLQREVEGERRARE--QAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  86 ESERGMKVIENRALKDEEKMELQEIQLKEAkhiaeEADRKYEEVARKLVIIEgdlertEERAELAESKCSELEEELKNVT 165
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQLAELEAELA-----ELSARYTPNHPDVIALR------AQIAALRAQLQQEAQRILASLE 319

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 52353308 166 NNLKSLEAQAEKYSQKEDKYEEEIKiltdKLKEAETRAEFAERSVAKLEKTIDDLEERL 224
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRL 374
PTZ00121 PTZ00121
MAEBL; Provisional
 11-215 2.59e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    11 KRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErg 90
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-- 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    91 mKVIENRALKDEEKMELQEIQLK-EAKHIAEEADRKYEEVARKlviieGDLERTEERAELAESKCSELEEELKNVTNNLK 169
Cdd:PTZ00121 1392 -KADEAKKKAEEDKKKADELKKAaAAKKKADEAKKKAEEKKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 52353308   170 SLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEK 215
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
6-93 4.89e-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: 4.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   6 TIEAVKRKIQVLQQQADDAEERAERLQREVE---GERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 82
Cdd:COG2433 421 QVERLEAEVEELEAELEEKDERIERLERELSearSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500

                        90
                ....*....|.
gi 52353308  83 AADESERGMKV 93
Cdd:COG2433 501 LWKLEHSGELV 511
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 13-239 6.50e-05

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: 43.79  E-value: 6.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   13 KIQVLQQQADDAEERAERLQREVEG------ERRAR-EQAEAEVASLNRRIQLVEEELDRAQER---LATALQKLEEAEK 82
Cdd:COG3096  348 KIERYQEDLEELTERLEEQEEVVEEaaeqlaEAEARlEAAEEEVDSLKSQLADYQQALDVQQTRaiqYQQAVQALEKARA 427

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   83 AADESERGMKVIENRALKDEEKMELQEIQLKEAKH---IAEEADRKYEEVARKLVIIEGDLERTEeraelAESKCSELEE 159
Cdd:COG3096  428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERSQ-----AWQTARELLR 502

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  160 ---ELKNVTNNLKSLEAQ---AEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRL 233
Cdd:COG3096  503 ryrSQQALAQRLQQLRAQlaeLEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSE 582


                 ....*.
gi 52353308  234 LSNELK 239
Cdd:COG3096  583 LRQQLE 588
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-176 1.14e-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: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   5 TTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  85 DESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNV 164
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552

                       170
                ....*....|..
gi 52353308 165 TNNLKSLEAQAE 176
Cdd:COG1196 553 VEDDEVAAAAIE 564
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-232 1.15e-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: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    7 IEAVKRKIQVLQQQADDAEERAERLQR--EVEGERRAREQAEAEVASLNRRIQLVEE---ELDRAQERLATALQKLEEAE 81
Cdd:COG4913  626 LAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELE 705

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   82 KAADESERGMKVIENR-----ALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLV------IIEGDLERTEERAELA 150
Cdd:COG4913  706 EELDELKGEIGRLEKEleqaeEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVerelreNLEERIDALRARLNRA 785

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  151 ESKCSELEEELKNV-TNNLKSLEAQAEKYSQKEDKYEeeiKILTDKLKEAEtrAEFAErsvAKLEKTIDDLEErLYSQLE 229
Cdd:COG4913  786 EEELERAMRAFNREwPAETADLDADLESLPEYLALLD---RLEEDGLPEYE--ERFKE---LLNENSIEFVAD-LLSKLR 856


                 ...
gi 52353308  230 RNR 232
Cdd:COG4913  857 RAI 859
PTZ00121 PTZ00121
MAEBL; Provisional
 25-223 1.18e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    25 EERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALqKLEEAEKAADESERGMKVIENRALKDEEK 104
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI-KAEEARKADELKKAEEKKKADEAKKAEEK 1301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   105 MELQEIQLK-EAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSleaqAEKYSQKED 183
Cdd:PTZ00121 1302 KKADEAKKKaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA----AEKKKEEAK 1377

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 52353308   184 KYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEER 223
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
13-147 1.37e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 42.34  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  13 KIQVLQQQADDAEERAERLQREVEGERRaREQAEAEVASLNRRIQLVEEELDRAQ---ERLATALQKLEEAEKAADESER 89
Cdd:COG1566  84 ALAQAEAQLAAAEAQLARLEAELGAEAE-IAAAEAQLAAAQAQLDLAQRELERYQalyKKGAVSQQELDEARAALDAAQA 162

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 52353308  90 GMKVIENRALKDEEKMELQEIQlkeakhiaEEADRKYEEVARKLVIIEGDLERTEERA 147
Cdd:COG1566 163 QLEAAQAQLAQAQAGLREEEEL--------AAAQAQVAQAEAALAQAELNLARTTIRA 212
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 7-219 1.81e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.51  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRiqlVEEELDRAQERLATALQKLE-------- 78
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEE---LEEKKEKLQEEEDKLLEEAEkeaqqaik 580

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   79 EAEKAADESERGMKVIENRALKDEEKMELQEIQ--LKEAKHIAEEAdrKYEEVARKLVIIEGD------LERTEERAELA 150
Cdd:PRK00409 581 EAKKEADEIIKELRQLQKGGYASVKAHELIEARkrLNKANEKKEKK--KKKQKEKQEELKVGDevkylsLGQKGEVLSIP 658

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52353308  151 ESKCSELEEELKNVTNNLKSLeaqaEKYSQKEDKYEEEIKILTDKLKEAET----RAEFAERSVAKLEKTIDD 219
Cdd:PRK00409 659 DDKEAIVQAGIMKMKVPLSDL----EKIQKPKKKKKKKPKTVKPKPRTVSLeldlRGMRYEEALERLDKYLDD 727
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
46-230 1.88e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   46 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALK---DEEKMELQEIQLKEAKHIAEEA 122
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETiaeTEREREELAEEVRDLRERLEEL 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  123 DRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETR 202
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371

                        170       180
                 ....*....|....*....|....*...
gi 52353308  203 AEFAERSVAKLEKTIDDLEERLYSQLER 230
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRER 399
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-224 2.55e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    8 EAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   88 ERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAES-------KCSELEEE 160
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREerdelreREAELEAT 434

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52353308  161 LKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERL 224
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERL 498
PTZ00121 PTZ00121
MAEBL; Provisional
 19-233 2.73e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    19 QQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRA 98
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    99 LKDEEKMELQEIQLKEakhiaEEADRKYEEVARKlviiegdlertEERAELAESKCSELEEELKNVTNNLKSLEAQAEKY 178
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAE-----EENKIKAAEEAKK-----------AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 52353308   179 SQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRL 233
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-224 3.20e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 3.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    2 AGSTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEE-- 79
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEElr 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   80 ----------AEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHI--AEEADRKYEEVARKLVIIEGDLERTEERA 147
Cdd:PRK02224 419 eerdelrereAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERL 498

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52353308  148 ELAESkCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERL 224
Cdd:PRK02224 499 ERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
45-224 4.34e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   45 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEiqLKEAKHIAEEADR 124
Cdd:COG4913  608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE--LEAELERLDASSD 685

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  125 KYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEikiLTDKLKEAETRAE 204
Cdd:COG4913  686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA---LLEERFAAALGDA 762

                        170       180
                 ....*....|....*....|
gi 52353308  205 FAERSVAKLEKTIDDLEERL 224
Cdd:COG4913  763 VERELRENLEERIDALRARL 782
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 2-225 4.83e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.07  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    2 AGSTTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVE--------EELDRAQERLATA 73
Cdd:PRK05771  69 LNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldLSLLLGFKYVSVF 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   74 LQKLEEAEKAADESERGMKVIENRAlKDEEKMELQEIQLKEAKHIAEEADRKYEevARKLVIIEGdlerteeraELAESK 153
Cdd:PRK05771 149 VGTVPEDKLEELKLESDVENVEYIS-TDKGYVYVVVVVLKELSDEVEEELKKLG--FERLELEEE---------GTPSEL 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  154 CSELEEELKNVTNNLKSLEAQAEKYSQkedKYEEEIKILTDKL----KEAETRAEFA-------------ERSVAKLEKT 216
Cdd:PRK05771 217 IREIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielERAEALSKFLktdktfaiegwvpEDRVKKLKEL 293


                 ....*....
gi 52353308  217 IDDLEERLY 225
Cdd:PRK05771 294 IDKATGGSA 302
PTZ00121 PTZ00121
MAEBL; Provisional
 8-211 7.66e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 7.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     8 EAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEA--EVASLNRRIQLVEEELDRAQE-RLATALQKLEEAEKAA 84
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKA 1446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    85 DESERGM---KVIENRALKDEEKMELQEIQLK-EAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEE 160
Cdd:PTZ00121 1447 DEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 52353308   161 LKNVTNNLKSLEAQA--EKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVA 211
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
7-206 8.21e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 8.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4372  40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAelAESKCSELEEELKNVTN 166
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE--AEQALDELLKEANRNAE 197

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 52353308 167 NLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFA 206
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 18-223 9.59e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 39.93  E-value: 9.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   18 QQQADDA----EERAERLQREvEGERRAReQAEAEVASLNRRIQLVEEELDRAQERLATALQKL-EEAEKAADESERGMK 92
Cdd:PRK05035 445 KKKAEEAkarfEARQARLERE-KAAREAR-HKKAAEARAAKDKDAVAAALARVKAKKAAATQPIvIKAGARPDNSAVIAA 522

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   93 VIENRALKDEEKMELQEiqlkeakhiAEEADRKYEEVArklviieGDLERTEER--AELAESKCSELEEELKNVTNNLKS 170
Cdd:PRK05035 523 REARKAQARARQAEKQA---------AAAADPKKAAVA-------AAIARAKAKkaAQQAANAEAEEEVDPKKAAVAAAI 586

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 52353308  171 LEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEER 223
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEE 639
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
7-233 1.01e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   7 IEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4372  96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTN 166
Cdd:COG4372 176 LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52353308 167 NLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRL 233
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
9-199 1.02e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.06  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   9 AVKRKIQVLQQQADDAEERAERLQREVEgerrareqaeaEVASLNrrIQLVE-EELDRAQERLATA---LQKLEEAEKAA 84
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLE-----------ELEAAA--LQPGEeEELEEERRRLSNAeklREALQEALEAL 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  85 DESERG--------MKVIENRALKDEEKMELQEiQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEER---------- 146
Cdd:COG0497 236 SGGEGGaldllgqaLRALERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFDPERLEEVEERlallrrlark 314

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 52353308 147 -----AELAEsKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEA 199
Cdd:COG0497 315 ygvtvEELLA-YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
PTZ00121 PTZ00121
MAEBL; Provisional
 8-222 1.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308     8 EAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEE---AEKAA 84
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    85 DESERGMKVIENRALKDEEKMELQEIQLK-EAKHIAEEADRKYEEVARKlviieGDLERTEERAELAESKCSELEEELKn 163
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKA-----DEAKKKAEEAKKAEEAKKKAEEAKK- 1471

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 52353308   164 vTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEE 222
Cdd:PTZ00121 1472 -ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
mukB PRK04863
chromosome partition protein MukB;
13-239 1.16e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    13 KIQVLQQQADDAEERAE------RLQREVEGERRAR-EQAEAEVASLNRRIQLVEEELDRAQERLAT---ALQKLEEAEK 82
Cdd:PRK04863  349 KIERYQADLEELEERLEeqnevvEEADEQQEENEARaEAAEEEVDELKSQLADYQQALDVQQTRAIQyqqAVQALERAKQ 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    83 ---AADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERtEERAELAESKCSELEE 159
Cdd:PRK04863  429 lcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSR-SEAWDVARELLRRLRE 507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   160 ElKNVTNNLKSLEAQ---AEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSN 236
Cdd:PRK04863  508 Q-RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586


                  ...
gi 52353308   237 ELK 239
Cdd:PRK04863  587 QLE 589
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
14-240 1.49e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  14 IQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 93
Cdd:COG4372  26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  94 IENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEA 173
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52353308 174 QAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELKL 240
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
PRK12705 PRK12705
hypothetical protein; Provisional
 14-181 1.93e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.92  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   14 IQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQ-ERLATALQKLEEAEKAADESERGMK 92
Cdd:PRK12705  22 VVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRErEELQREEERLVQKEEQLDARAEKLD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   93 VIENRALKDEEKMELQEIQLKEAKHiaeeadrkyeEVARKLVIIEGdLERTEERAELAESKCSELEEELKNVTN-NLKSL 171
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEK----------QLDNELYRVAG-LTPEQARKLLLKLLDAELEEEKAQRVKkIEEEA 170

                        170
                 ....*....|
gi 52353308  172 EAQAEKYSQK 181
Cdd:PRK12705 171 DLEAERKAQN 180
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 68-234 2.21e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.88  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    68 ERLATALQKLEEAEKAADESERGMKVIEN-----RALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLER 142
Cdd:PRK10929   48 EALQSALNWLEERKGSLERAKQYQQVIDNfpklsAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   143 TEERA-ELAES------KCSELEEELKNVTNNLKSLE-------------AQAEKYSQKEDKYEEEIKILTDKLKE--AE 200
Cdd:PRK10929  128 EQDRArEISDSlsqlpqQQTEARRQLNEIERRLQTLGtpntplaqaqltaLQAESAALKALVDELELAQLSANNRQelAR 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 52353308   201 TRAEFAERSVAKLEKTIDDLEERLYSQ--------LERNRLL 234
Cdd:PRK10929  208 LRSELAKKRSQQLDAYLQALRNQLNSQrqreaeraLESTELL 249
PTZ00121 PTZ00121
MAEBL; Provisional
 19-190 2.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    19 QQADDAEERAERLQREvEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEE----AEKAADESERGMKVI 94
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKKAA 1691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    95 ENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSelEEELKNVTNNLKSLEAQ 174
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD--EEEKKKIAHLKKEEEKK 1769

                         170
                  ....*....|....*..
gi 52353308   175 AEKY-SQKEDKYEEEIK 190
Cdd:PTZ00121 1770 AEEIrKEKEAVIEEELD 1786
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 12-230 2.85e-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: 38.57  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    12 RKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam17380 325 RQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKV 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    92 KVIEnralkdEEKMELQEIQLKEAKHIAEEADRKYEEVARKLviiEGDLERTEERAELAESKCSELEEELKNVTNNLKSL 171
Cdd:pfam17380 405 KILE------EERQRKIQQQKVEMEQIRAEQEEARQREVRRL---EEERAREMERVRLEEQERQQQVERLRQQEEERKRK 475

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   172 EAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAK-LEKTIDDLEERLYSQLER 230
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKlLEKEMEERQKAIYEEERR 535
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
42-238 3.09e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 3.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  42 REQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEE--AEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIA 119
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308 120 EEADRKYEEVARKLVIIEGDLERTEERAELAESKcSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILtdkLKEA 199
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELE-AELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI---LASL 318

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 52353308 200 ETRAEFAERSVAKLEKTIDDLEERL---------YSQLERNRLLSNEL 238
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLaelpeleaeLRRLEREVEVAREL 366
PTZ00121 PTZ00121
MAEBL; Provisional
 11-232 3.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    11 KRKIQVLQQQADDAEERAERLQREVEGERRARE--QAEAEVASLNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADES 87
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAE 1671

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    88 ERGMKVIENR-ALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKcselEEELKNVTN 166
Cdd:PTZ00121 1672 EDKKKAEEAKkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAE 1747

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52353308   167 NLKSLEAQAEKYSQ---KEDKYEEEIKILTDKLKEAETRAEfAERSVAKLEKTIDDLEERLYSQLERNR 232
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHlkkEEEKKAEEIRKEKEAVIEEELDEE-DEKRRMEVDKKIKDIFDNFANIIEGGK 1815
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 33-201 4.26e-03

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 38.06  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    33 REVEGERRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDE---------E 103
Cdd:pfam05262 192 KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPkpadtsspkE 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   104 KMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLER-TEERAELAESKCSELEEELKNVTNNLKSL--EAQAEKYSQ 180
Cdd:pfam05262 272 DKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQKTkpQVEAQPTSL 351

                         170       180
                  ....*....|....*....|.
gi 52353308   181 KEDKYEEEIKILTDKLKEAET 201
Cdd:pfam05262 352 NEDAIDSSNPVYGLKVVDPIT 372
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
5-225 4.46e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 4.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308    5 TTIEAVKRKIQVLQQQADDAEERAERLQREVEGERRAREQAEAEVASLNRRIQLVEEELDRAqERLATALQKLEEAEKAA 84
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEI 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   85 DE------------SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAES 152
Cdd:PRK02224 609 ERlrekrealaelnDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52353308  153 KCSELE---EELKNVTNNLKSLEAQAEKYSQKEDKYeeeikiltdklkeAETRAEFAERSVAKLEKTIDDLEERLY 225
Cdd:PRK02224 689 ELEELEelrERREALENRVEALEALYDEAEELESMY-------------GDLRAELRQRNVETLERMLNETFDLVY 751
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 41-239 5.88e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 37.44  E-value: 5.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  41 AREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKhiaE 120
Cdd:COG4942  21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR---A 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308 121 EADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAE 200
Cdd:COG4942  98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 52353308 201 TRAEFAERSVAKLEKTIDDLEERLYSQLERNRLLSNELK 239
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 63-192 6.94e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 37.21  E-value: 6.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   63 LDRAQERLATALQKLEEAEkaadesergmkvIENraLKDEEKMELQEIQLKEAKHIAEEAD--RKYEEVARKLVIIEGDL 140
Cdd:PRK05771  14 LKSYKDEVLEALHELGVVH------------IED--LKEELSNERLRKLRSLLTKLSEALDklRSYLPKLNPLREEKKKV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 52353308  141 E--RTEERAELAESKCSELEEELKNVTNNLKSLEAqaekysqKEDKYEEEIKIL 192
Cdd:PRK05771  80 SvkSLEELIKDVEEELEKIEKEIKELEEEISELEN-------EIKELEQEIERL 126
PRK12704 PRK12704
phosphodiesterase; Provisional
 113-230 8.97e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.07  E-value: 8.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308  113 KEAKHIAEEADRKYEEVARKLViiegdLERTEERAELAeskcSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKIL 192
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKKEAL-----LEAKEEIHKLR----NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 52353308  193 TDKLKEAETRAEFAERSVAKLEKTIDDLEERLYSQLER 230
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
PRK12472 PRK12472
hypothetical protein; Provisional
 24-124 9.32e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 36.77  E-value: 9.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52353308   24 AEERAERLQREVEGERRAREQAEAEVAslnrriqlveeELDRAQERLATALQKLEEAEKAAD-ESERGMKVIENrALKDE 102
Cdd:PRK12472 188 APARAETLAREAEDAARAADEAKTAAA-----------AAAREAAPLKASLRKLERAKARADaELKRADKALAA-AKTDE 255

                         90       100
                 ....*....|....*....|..
gi 52353308  103 EKMELQEIQLKEAKHIAEEADR 124
Cdd:PRK12472 256 AKARAEERQQKAAQQAAEAATQ 277
 
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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