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Conserved domains on  [gi|281361832|ref|NP_001163619|]
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tropomyosin 1, isoform N [Drosophila melanogaster]

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 ...
 48-282 2.29e-60

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: 191.40  E-value: 2.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   48 KKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  128 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281361832  208 EVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKERYKDIGDDLDTAFVELI 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 48-282 2.29e-60

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: 191.40  E-value: 2.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   48 KKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  128 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281361832  208 EVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKERYKDIGDDLDTAFVELI 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-277 2.63e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  21 RALVCEQEARDANTRA---EKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEE 97
Cdd:COG1196  216 RELKEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  98 DLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLE 177
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 178 RSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                        250       260
                 ....*....|....*....|
gi 281361832 258 DDLVLEKERYKDIGDDLDTA 277
Cdd:COG1196  456 EEEEALLELLAELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-281 7.47e-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: 7.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   106 LGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   186 SESKIVELEEELRV-------VGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLED 258
Cdd:TIGR02168  836 TERRLEDLEEQIEElsediesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                          250       260
                   ....*....|....*....|...
gi 281361832   259 DLVLEKERYKDIGDDLDTAFVEL 281
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLEVRI 938
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
28-197 6.85e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 6.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  28 EARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLG 107
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 108 SATAKLSEASQAADESERIRKALE--------------NRTNMEDDKVALLENQLAQAKLIAEEADKKYEEvARKLVLME 173
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAE 508

                        170       180
                 ....*....|....*....|....
gi 281361832 174 QDLERSEEKVELSESKIVELEEEL 197
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETI 532
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 48-282 2.29e-60

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: 191.40  E-value: 2.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   48 KKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  128 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281361832  208 EVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKERYKDIGDDLDTAFVELI 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 7-152 5.40e-19

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: 81.20  E-value: 5.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    7 KMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESeva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEN--- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281361832   87 aLNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAK 152
Cdd:pfam12718  78 -LTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-277 2.63e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.05  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  21 RALVCEQEARDANTRA---EKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEE 97
Cdd:COG1196  216 RELKEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  98 DLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLE 177
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 178 RSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                        250       260
                 ....*....|....*....|
gi 281361832 258 DDLVLEKERYKDIGDDLDTA 277
Cdd:COG1196  456 EEEEALLELLAELLEEAALL 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-268 1.44e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.65  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   7 KMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVA 86
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  87 ALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVA 166
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 167 RKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSV 246
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                        250       260
                 ....*....|....*....|..
gi 281361832 247 QKLQKEVDRLEDDLVLEKERYK 268
Cdd:COG1196  473 ALLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-281 7.47e-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: 7.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   106 LGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   186 SESKIVELEEELRV-------VGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLED 258
Cdd:TIGR02168  836 TERRLEDLEEQIEElsediesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                          250       260
                   ....*....|....*....|...
gi 281361832   259 DLVLEKERYKDIGDDLDTAFVEL 281
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLEVRI 938
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-271 1.47e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  82 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKK 161
Cdd:COG1196  322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 162 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEF 241
Cdd:COG1196  402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481

                        250       260       270
                 ....*....|....*....|....*....|
gi 281361832 242 AERSVQKLQKEVDRLEDDLVLEKERYKDIG 271
Cdd:COG1196  482 LLEELAEAAARLLLLLEAEADYEGFLEGVK 511
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-281 7.06e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.77  E-value: 7.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   115 EASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELE 194
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   195 EELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRL-----KEAEARAEFAERSVQKLQKEVDRLEDDLVLEKERYKD 269
Cdd:TIGR02168  393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelKELQAELEELEEELEELQEELERLEEALEELREELEE 472

                          250
                   ....*....|..
gi 281361832   270 IGDDLDTAFVEL 281
Cdd:TIGR02168  473 AEQALDAAEREL 484
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-252 6.79e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 6.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:TIGR02168  219 KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   115 EASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELE 194
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 281361832   195 EELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKE 252
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-260 1.20e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.91  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832     2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:TIGR02168  694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    82 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMeddkvalLENQLAQAKLIAEEADKK 161
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES-------LERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   162 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEF 241
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926

                          250
                   ....*....|....*....
gi 281361832   242 AERSVQKLQKEVDRLEDDL 260
Cdd:TIGR02168  927 LELRLEGLEVRIDNLQERL 945
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-259 1.06e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.84  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832     7 KMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVA 86
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    87 ALNRRIQLLEEDLERSEERLGSATAKLS---------EASQAADESERIRKAL---ENRTNMEDDKVALLENQLAQAKLI 154
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLEARLShsripeiqaELSKLEEEVSRIEARLreiEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   155 AEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKE 234
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          250       260
                   ....*....|....*....|....*
gi 281361832   235 AEARAEFAERSVQKLQKEVDRLEDD 259
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEDEEI 946
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 22-258 4.10e-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: 53.61  E-value: 4.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  22 ALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLER 101
Cdd:COG4942    8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 102 SEERLGSATAKLSEasQAADESERIRKALENRTNmedDKVALLENQlaqakliaeeadKKYEEVARKLVLMEQDLERSEE 181
Cdd:COG4942   88 LEKEIAELRAELEA--QKEELAELLRALYRLGRQ---PPLALLLSP------------EDFLDAVRRLQYLKYLAPARRE 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281361832 182 KVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLED 258
Cdd:COG4942  151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
28-197 6.85e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 53.51  E-value: 6.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  28 EARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLG 107
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 108 SATAKLSEASQAADESERIRKALE--------------NRTNMEDDKVALLENQLAQAKLIAEEADKKYEEvARKLVLME 173
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAE 508

                        170       180
                 ....*....|....*....|....
gi 281361832 174 QDLERSEEKVELSESKIVELEEEL 197
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETI 532
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-260 7.36e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 7.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   106 LGSATAKLSEASQAADEserirkaLENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:TIGR02168  332 LDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   186 SESKIVELEEELRVVGNNLKSLEVSEEKANQRE-----EEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDL 260
Cdd:TIGR02168  405 LEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-193 8.69e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   18 ALERALV-CEQEARDANTRAEKAEEEARQLQKKIQT---------VENELDQTQEALTlvtgKLEEKNKALQNAESEVAA 87
Cdd:COG4913   614 ALEAELAeLEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIA----ELEAELERLDASSDDLAA 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   88 LNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVAR 167
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769

                         170       180
                  ....*....|....*....|....*.
gi 281361832  168 KLvlmEQDLERSEEKVELSESKIVEL 193
Cdd:COG4913   770 NL---EERIDALRARLNRAEEELERA 792
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-233 2.65e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 2.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832     1 MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKK-------IQTVENELDQTQEALTLVTGKLEE 73
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    74 KNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKL 153
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   154 IAEEADKKYEEVARKL------------VLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEY 221
Cdd:TIGR02168  401 EIERLEARLERLEDRRerlqqeieellkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480

                          250
                   ....*....|..
gi 281361832   222 KNQIKTLNTRLK 233
Cdd:TIGR02168  481 ERELAQLQARLD 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-226 8.06e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.06  E-value: 8.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832     3 AIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAE 82
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    83 SEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLiaEEADKKY 162
Cdd:TIGR02168  372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEEL 449

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281361832   163 EEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIK 226
Cdd:TIGR02168  450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
51-270 2.42e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  51 QTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQL--LEEDLERSEERLGSATAKLSEASQAADESERIRK 128
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 129 ALENRTNMEDDKVALLENQLAQAKLIAEEAdkkyeEVARKLVLMEQDLERSEEKVELSESKIVELEEELRV-VGNNLKSL 207
Cdd:COG3206  244 ALRAQLGSGPDALPELLQSPVIQQLRAQLA-----ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASL 318

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281361832 208 EVSEEKANQREEEYKNQIKTLNTRLKeaearaefaerSVQKLQKEVDRLEDDLVLEKERYKDI 270
Cdd:COG3206  319 EAELEALQAREASLQAQLAQLEARLA-----------ELPELEAELRRLEREVEVARELYESL 370
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-214 3.76e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQ-TQEALTLVTGKLEEKNKALQN 80
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEElAEELLEALRAAAELAAQLEEL 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  81 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADK 160
Cdd:COG1196  406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 281361832 161 KYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKA 214
Cdd:COG1196  486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 32-221 4.19e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  32 ANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATA 111
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 112 KLSEASQAADESERI------------RKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERS 179
Cdd:COG3883   94 ALYRSGGSVSYLDVLlgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 281361832 180 EEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEY 221
Cdd:COG3883  174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-231 5.96e-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: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   37 EKAEEEARQLQKKIQTVEnELDQTQEALTLVTGKLEEKNKALQNAESEVAAlnRRIQLLEEDLERSEERLGSATAKLSEA 116
Cdd:COG4913   238 ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  117 SQAADE-SERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEE----KVELSESKIV 191
Cdd:COG4913   315 EARLDAlREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaaLRAEAAALLE 394

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 281361832  192 ELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTR 231
Cdd:COG4913   395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 54-267 6.37e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 6.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  54 ENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERseeRLGSATAKLSEASQAADESERIRKALENR 133
Cdd:COG1196  178 ERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKEL---EAELLLLKLRELEAELEELEAELEELEAE 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 134 TNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEK 213
Cdd:COG1196  255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 281361832 214 ANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKERY 267
Cdd:COG1196  335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 26-257 7.09e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 7.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    26 EQEARDANTRAEK-AEEEARQLQKKIQTVENELDQTQealtlvtGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEE 104
Cdd:TIGR02169  271 EQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLE-------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   105 RLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVE 184
Cdd:TIGR02169  344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281361832   185 LSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:TIGR02169  424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-233 1.71e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    27 QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERL 106
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   107 GSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQ-AKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 281361832   186 SESKIVELeeelrvvGN-NLKSLEVSEEKaNQREEEYKNQIKTLNTRLK 233
Cdd:TIGR02168  977 LENKIKEL-------GPvNLAAIEEYEEL-KERYDFLTAQKEDLTEAKE 1017
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-276 4.43e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   70 KLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLgSATAKLSEASQAADESERIRKALENRTNM------EDDKVAL 143
Cdd:COG4913   611 KLAALEAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEIDVASAEREIAELEAElerldaSSDDLAA 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  144 LENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKN 223
Cdd:COG4913   690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281361832  224 QIktlntrlkeaearaefaERSVQKLQKEVDRLEDDLVLE----KERYKDIGDDLDT 276
Cdd:COG4913   770 NL-----------------EERIDALRARLNRAEEELERAmrafNREWPAETADLDA 809
PTZ00121 PTZ00121
MAEBL; Provisional
 2-222 2.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   82 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKK 161
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281361832  162 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYK 222
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 35-259 2.86e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.13  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERS--------EERL 106
Cdd:pfam12128  605 RLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAlaerkdsaNERL 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   107 GS--ATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVE 184
Cdd:pfam12128  685 NSleAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLG 764

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281361832   185 LSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKeaeARAEFAERSVQKLQKEVDRLEDD 259
Cdd:pfam12128  765 VDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA---TQLSNIERAISELQQQLARLIAD 836
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
26-282 3.58e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:COG4372   58 REELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 106 LGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:COG4372  138 IAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELA 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 186 SESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKE 265
Cdd:COG4372  218 EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297

                        250
                 ....*....|....*..
gi 281361832 266 RYKDIGDDLDTAFVELI 282
Cdd:COG4372  298 LALLLNLAALSLIGALE 314
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 26-204 3.91e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEK-NKALQNAESEVAALNRRIQLLE--EDLERS 102
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQkgGYASVK 605

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 103 EERLGSATAKLSEASQAADESERIRKAlENRTNMEDDKVALLenQLAQAKLIAEEADKKYEEV---ARKLVLMEQDLERS 179
Cdd:PRK00409 606 AHELIEARKRLNKANEKKEKKKKKQKE-KQEELKVGDEVKYL--SLGQKGEVLSIPDDKEAIVqagIMKMKVPLSDLEKI 682

                        170       180
                 ....*....|....*....|....*
gi 281361832 180 EEKVELSESKIVELEEELRVVGNNL 204
Cdd:PRK00409 683 QKPKKKKKKKPKTVKPKPRTVSLEL 707
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
26-277 4.33e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTL-------VTGKLEEKNKALQNAESEVAALNRRIQLLEED 98
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarseleqLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  99 LERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLER 178
Cdd:COG4372  110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 179 SEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLED 258
Cdd:COG4372  190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269

                        250
                 ....*....|....*....
gi 281361832 259 DLVLEKERYKDIGDDLDTA 277
Cdd:COG4372  270 EKDTEEEELEIAALELEAL 288
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-260 4.45e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 4.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    66 LVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLE 145
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   146 NQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQI 225
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 281361832   226 KTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDL 260
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
mukB PRK04863
chromosome partition protein MukB;
29-222 6.50e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 6.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   29 ARDANTRAEKAEEeARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQL------LEEDLERS 102
Cdd:PRK04863  275 MRHANERRVHLEE-ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLvqtalrQQEKIERY 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  103 EERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLA--QAKLIAEE--------ADKKYEEVARKLVLM 172
Cdd:PRK04863  354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyQQALDVQQtraiqyqqAVQALERAKQLCGLP 433

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 281361832  173 EQDLERSEEKVELSESKIVELEEELRVVGNNLKsleVSEEKANQREEEYK 222
Cdd:PRK04863  434 DLTADNAEDWLEEFQAKEQEATEELLSLEQKLS---VAQAAHSQFEQAYQ 480
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-199 7.77e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  27 QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAEsevaaLNRRIQLLEEDLERSEERL 106
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELAELPERL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 107 GSATAKLSEASQAADESERIRKALENrtnMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELS 186
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225

                        170
                 ....*....|...
gi 281361832 187 ESKIVELEEELRV 199
Cdd:COG4717  226 EEELEQLENELEA 238
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 26-168 8.15e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEE--KNKALQNAESEVAALNRRIQLLEEDLERSE 103
Cdd:COG1579   37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILELM 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 104 ERLGSATAKLSEASQAADESERIRKALENR-----TNMEDDKVALLENQLAQAKLIAEEADKKYEEVARK 168
Cdd:COG1579  117 ERIEELEEELAELEAELAELEAELEEKKAEldeelAELEAELEELEAEREELAAKIPPELLALYERIRKR 186
PRK11281 PRK11281
mechanosensitive channel MscK;
2-224 8.16e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    2 DAIKKKMQAMKVDKDGALERALVCE--QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTG---------- 69
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAEDKLVQQdlEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDdndeetretl 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   70 ----------KLEEKNKALQNAESEVAALNRRIQLLEEDLERseerlgsATAKLSEASQAADEserIRKALENRTNMEDD 139
Cdd:PRK11281  119 stlslrqlesRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPER-------AQAALYANSQRLQQ---IRNLLKGGKVGGKA 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  140 KVALLENQLaQAKLIAEEADKKYE--EVARKLVLmeQDLErsEEKVELSESKIVELEEELRVVGN--NLKSLEVSEEKAN 215
Cdd:PRK11281  189 LRPSQRVLL-QAEQALLNAQNDLQrkSLEGNTQL--QDLL--QKQRDYLTARIQRLEHQLQLLQEaiNSKRLTLSEKTVQ 263


                  ....*....
gi 281361832  216 QREEEYKNQ 224
Cdd:PRK11281  264 EAQSQDEAA 272
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 45-274 8.26e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 8.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    45 QLQKKIQTVENELDQTQEALTLVTGKLEEKN--------------------------------KALQNAESEVAALNRRI 92
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqlerlrrerekaeryqallkekreyegyellKEKEALERQKEAIERQL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    93 QLLEEDLERSEERLGSATAKLSEASQAADE-SERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVL 171
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   172 MEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQK 251
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                          250       260
                   ....*....|....*....|...
gi 281361832   252 EVDRLEDDLVLEKERYKDIGDDL 274
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAI 429
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1-158 9.60e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 9.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    1 MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQ-KKIQTVENELDQTQEALTLVTGKLEEKNKALQ 79
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLA 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   80 NAESEV-----------AALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQL 148
Cdd:COG4913   370 ALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449

                         170
                  ....*....|
gi 281361832  149 AQAKLIAEEA 158
Cdd:COG4913   450 AEALGLDEAE 459
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
27-204 1.16e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.06  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  27 QEARDANTRAEKAEEEARQLQKKIQTVE---NELdqtqEALTLVTG---KLEEKNKALQNAESEVAALNRRIQLLEEDLE 100
Cdd:COG0497  165 RAWRALKKELEELRADEAERARELDLLRfqlEEL----EAAALQPGeeeELEEERRRLSNAEKLREALQEALEALSGGEG 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 101 RSEERLGSATAKLSEASQAADESERIRKALEN---------------RTNMEDDKVAL--LENQLAQAKLIAeeadKKY- 162
Cdd:COG0497  241 GALDLLGQALRALERLAEYDPSLAELAERLESalieleeaaselrryLDSLEFDPERLeeVEERLALLRRLA----RKYg 316

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 281361832 163 ---EEVARKLVLMEQDLER---SEEKVELSESKIVELEEELRVVGNNL 204
Cdd:COG0497  317 vtvEELLAYAEELRAELAElenSDERLEELEAELAEAEAELLEAAEKL 364
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 2-220 1.25e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  82 ESEVAALNrrIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKK 161
Cdd:COG3883   99 GGSVSYLD--VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 281361832 162 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEE 220
Cdd:COG3883  177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
25-255 1.44e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  25 CEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEE 104
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 105 RLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKL--------------IAEEADKKYEEVARKLV 170
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegsphveTIEEDRERVEELEAELE 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 171 LMEQDLERSEEKVELSESkIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQ 250
Cdd:PRK02224 486 DLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE 564


                 ....*
gi 281361832 251 KEVDR 255
Cdd:PRK02224 565 EEAEE 569
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
26-221 2.20e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  26 EQEARDANTRAEKAEEEARQLQKKiqtveNELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:COG3206  181 EEQLPELRKELEEAEAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 106 LGSATAKLSEASQAADESERIRKALENRTNMEDD--KVALLENQLAQAKliaeeaDKKYEEVARKLVLMEQDLERSEEKV 183
Cdd:COG3206  256 LPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpDVIALRAQIAALR------AQLQQEAQRILASLEAELEALQARE 329

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 281361832 184 ELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEY 221
Cdd:COG3206  330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY 367
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
36-196 2.66e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  36 AEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSE 115
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 116 ASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLME-----------QDLERSEEKVE 184
Cdd:PRK02224 584 LKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAefdearieearEDKERAEEYLE 663

                        170
                 ....*....|..
gi 281361832 185 LSESKIVELEEE 196
Cdd:PRK02224 664 QVEEKLDELREE 675
PTZ00121 PTZ00121
MAEBL; Provisional
 38-273 3.15e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   38 KAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATA---KLS 114
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekKKA 1649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  115 EASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKlvlMEQDLERSEEKVELSESKIVELE 194
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK---AEELKKKEAEEKKKAEELKKAEE 1726

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  195 EELRVVGNNLKSLEVSEEKANQ--REEEYKNQIKTLNTRLKEAEARAEFAERSVqkLQKEVDRLEDDLVLEKER-YKDIG 271
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEakKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKkIKDIF 1804


                  ..
gi 281361832  272 DD 273
Cdd:PTZ00121 1805 DN 1806
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 82-266 3.57e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832    82 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKK 161
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   162 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRvvGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEF 241
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830

                          170       180
                   ....*....|....*....|....*
gi 281361832   242 AERSVQKLQKEVDRLEDDLVLEKER 266
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKE 855
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-250 4.81e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 115 EASQAADESERIRKALEN-----RTNMEDDKVAL------LENQLAQAKLIAEEADKKYEEVARklvlMEQDLERSEEKV 183
Cdd:PRK02224 304 LDDADAEAVEARREELEDrdeelRDRLEECRVAAqahneeAESLREDADDLEERAEELREEAAE----LESELEEAREAV 379

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281361832 184 ELSESKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQ 250
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE 446
PRK12705 PRK12705
hypothetical protein; Provisional
 88-225 5.09e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.15  E-value: 5.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  88 LNRRIQLLEEDLERSEERLGSATAKLSEASQAADES-ERIRKALENRTNMEDDKVALLENQLAQAKliaEEADKKYEeva 166
Cdd:PRK12705  25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELlLRERNQQRQEARREREELQREEERLVQKE---EQLDARAE--- 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 281361832 167 rKLVLMEQDLERSEEKVELSESKIVELEEELRvvgnnlkslEVSEEKANQREEEYKNQI 225
Cdd:PRK12705  99 -KLDNLENQLEEREKALSARELELEELEKQLD---------NELYRVAGLTPEQARKLL 147
PRK09039 PRK09039
peptidoglycan -binding protein;
18-135 5.17e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.02  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  18 ALERALVCEQEARDANTRAEKAEEEArqLQKKIQTVENELDQTQEALTlvtGKLEEKNKALQNAESEVAALNRRIQLLEE 97
Cdd:PRK09039  70 SLERQGNQDLQDSVANLRASLSAAEA--ERSRLQALLAELAGAGAAAE---GRAGELAQELDSEKQVSARALAQVELLNQ 144

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 281361832  98 DLERSEERLGSATAKLsEASQAADESERIRKA-LENRTN 135
Cdd:PRK09039 145 QIAALRRQLAALEAAL-DASEKRDRESQAKIAdLGRRLN 182
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
113-277 5.17e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 5.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  113 LSEASQAADESERIRKAL----ENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSES 188
Cdd:COG4913   237 LERAHEALEDAREQIELLepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  189 KIVELEEELRVVGNNLKSLEvseekaNQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLVLEKERYK 268
Cdd:COG4913   317 RLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390


                  ....*....
gi 281361832  269 DIGDDLDTA 277
Cdd:COG4913   391 ALLEALEEE 399
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 37-265 7.82e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 37.60  E-value: 7.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  37 EKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKAlqnaesEVAALNRRIQLLEEDLERSEERLGSATAKLSEA 116
Cdd:PRK05771  39 ELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKV------SVKSLEELIKDVEEELEKIEKEIKELEEEISEL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832 117 SQAADESERIRKALENRTNMEDDKVALLENQLAQAKL--IAEEADKKYEEVARKLVLMEqdLERSEEKVEL----SESKI 190
Cdd:PRK05771 113 ENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgtVPEDKLEELKLESDVENVEY--ISTDKGYVYVvvvvLKELS 190

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281361832 191 VELEEELRVVGnnLKSLEVSEEK-ANQREEEYKNQIKTLNTRLKEAEAraefaersvqKLQKEVDRLEDDLVLEKE 265
Cdd:PRK05771 191 DEVEEELKKLG--FERLELEEEGtPSELIREIKEELEEIEKERESLLE----------ELKELAKKYLEELLALYE 254
46 PHA02562
endonuclease subunit; Provisional
 26-227 8.04e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 37.69  E-value: 8.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  26 EQEARDANTRAEKaEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQN-------AESEVAALNRRIQLLEE- 97
Cdd:PHA02562 206 EQRKKNGENIARK-QNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntaaakIKSKIEQFQKVIKMYEKg 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  98 --------DLERSEERLGSATAKLSEASQaadeseRIRKALENRtnmedDKVALLENQLAQAKLIAEEADKKYEEVARKL 169
Cdd:PHA02562 285 gvcptctqQISEGPDRITKIKDKLKELQH------SLEKLDTAI-----DELEEIMDEFNEQSKKLLELKNKISTNKQSL 353

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 281361832 170 VLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKslEVSEEKANQREEEYKNQIKT 227
Cdd:PHA02562 354 ITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD--KIVKTKSELVKEKYHRGIVT 409
PTZ00121 PTZ00121
MAEBL; Provisional
 27-268 8.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832   27 QEARDANTRAEKAEE--EARQLQKKIQTVENELDQTQEaltlvtgKLEEKNKALQNAESEVAALnrriqllEEDLERSEE 104
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKK-------AAEAKKKADEAKKAEEAKK-------ADEAKKAEE 1532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  105 RLGSATAKLSEASQAADE---SERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLE---- 177
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADElkkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeea 1612

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281361832  178 RSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKANQ-REEEYKNQIKTlnTRLKEAEARAEFAERSVQKLQKEVDRL 256
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKA--AEEAKKAEEDKKKAEEAKKAEEDEKKA 1690

                         250
                  ....*....|..
gi 281361832  257 EDDLVLEKERYK 268
Cdd:PTZ00121 1691 AEALKKEAEEAK 1702
 
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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