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Conserved domains on  [gi|1953282154|ref|XP_038538034|]
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tropomyosin beta chain isoform X3 [Canis lupus familiaris]

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 1.46e-61

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: 194.48  E-value: 1.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  48 KKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 128 KVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953282154 208 EAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEETLASAKEENVEIHQTLDQTLLELN 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 1.46e-61

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: 194.48  E-value: 1.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  48 KKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 128 KVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953282154 208 EAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEETLASAKEENVEIHQTLDQTLLELN 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-266 4.85e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 4.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   5 KKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEAD 84
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEE 164
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 165 VARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAER 244
Cdd:COG1196   384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                         250       260
                  ....*....|....*....|..
gi 1953282154 245 SVAKLEKTIDDLEETLASAKEE 266
Cdd:COG1196   464 LLAELLEEAALLEAALAELLEE 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 30-284 1.80e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   30 KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATA 109
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  110 LQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESK 189
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  190 CGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEET-------LAS 262
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEE 919

                          250       260
                   ....*....|....*....|..
gi 1953282154  263 AKEENVEIHQTLDQTLLELNNL 284
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRIDNL 941
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-257 3.23e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.28  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  22 AEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDR 101
Cdd:PRK02224  344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 102 AQERLATALQKLEEAEKAADESERGMKV--------------IENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEvAR 167
Cdd:PRK02224  424 LREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-AE 502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 168 KLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVA 247
Cdd:PRK02224  503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582

                         250
                  ....*....|
gi 1953282154 248 KLEKTIDDLE 257
Cdd:PRK02224  583 ELKERIESLE 592
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 7-220 3.07e-07

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 51.76  E-value: 3.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    7 KMQMLKLDKENAIDRAEQ-AEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESvkdAQEKLEQAEKKATDAEA-- 83
Cdd:NF012221  1541 SQQADAVSKHAKQDDAAQnALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQN---ALETNGQAQRDAILEESra 1617

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   84 ---DVASLNRRIQLVEEE-------------------LDRAQERLATALQKLEEA-EKAADESERGMKVIENRAMKDEEK 140
Cdd:NF012221  1618 vtkELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAG 1697

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  141 MELQEMQLKEAKhiAEDSDRKYEEVARKLvilegELERSEERAEVAESKCGDLEEELK------IVTNNLKSLEAQADKY 214
Cdd:NF012221  1698 VAQGEQNQANAE--QDIDDAKADAEKRKD-----DALAKQNEAQQAESDANAAANDAQsrgeqdASAAENKANQAQADAK 1770


                   ....*.
gi 1953282154  215 STKEDK 220
Cdd:NF012221  1771 GAKQDE 1776
 
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 1.46e-61

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: 194.48  E-value: 1.46e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  48 KKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 128 KVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953282154 208 EAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEETLASAKEENVEIHQTLDQTLLELN 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 5.43e-26

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: 99.69  E-value: 5.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   7 KMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEadva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953282154  87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAK 152
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 5-266 4.85e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 4.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   5 KKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEAD 84
Cdd:COG1196   224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEE 164
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 165 VARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAER 244
Cdd:COG1196   384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                         250       260
                  ....*....|....*....|..
gi 1953282154 245 SVAKLEKTIDDLEETLASAKEE 266
Cdd:COG1196   464 LLAELLEEAALLEAALAELLEE 485
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-269 5.89e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 68.81  E-value: 5.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 161 KYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                         250       260
                  ....*....|....*....|....*....
gi 1953282154 241 FAERSVAKLEKTIDDLEETLASAKEENVE 269
Cdd:COG1196   474 LLEAALAELLEELAEAAARLLLLLEAEAD 502
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 24-284 6.47e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 6.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  24 QAEADKKQAE---DRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELD 100
Cdd:COG1196   219 KEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 101 RAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSE 180
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 181 ERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEETL 260
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                         250       260
                  ....*....|....*....|....
gi 1953282154 261 ASAKEENVEIHQTLDQTLLELNNL 284
Cdd:COG1196   459 EALLELLAELLEEAALLEAALAEL 482
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 30-284 1.80e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   30 KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATA 109
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  110 LQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESK 189
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  190 CGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEET-------LAS 262
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselrreLEE 919

                          250       260
                   ....*....|....*....|..
gi 1953282154  263 AKEENVEIHQTLDQTLLELNNL 284
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRIDNL 941
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-284 1.73e-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: 55.45  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    4 IKKKMQMLKLDKENAID----RAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKAT 79
Cdd:TIGR02168  198 LERQLKSLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   80 DAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSD 159
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  160 RKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQ-----ADKYSTKEDKYEEEIKLLEEKLKE 234
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlerleDRRERLQQEIEELLKKLEEAELKE 437

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1953282154  235 AETRAEFAERSVAKLEKTIDDLEETLASAKEENVEIHQTLDQTLLELNNL 284
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-274 1.75e-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: 55.45  E-value: 1.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   20 DRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEEL 99
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  100 DRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERS 179
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  180 EERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEET 259
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944

                          250
                   ....*....|....*
gi 1953282154  260 LASAKEENVEIHQTL 274
Cdd:TIGR02168  945 LSEEYSLTLEEAEAL 959
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-257 3.23e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.28  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  22 AEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDR 101
Cdd:PRK02224  344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDE 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 102 AQERLATALQKLEEAEKAADESERGMKV--------------IENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEvAR 167
Cdd:PRK02224  424 LREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLER-AE 502

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 168 KLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVA 247
Cdd:PRK02224  503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLA 582

                         250
                  ....*....|
gi 1953282154 248 KLEKTIDDLE 257
Cdd:PRK02224  583 ELKERIESLE 592
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 18-213 1.07e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.46  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  18 AIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEE 97
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  98 ELDRAQERLATALQKLEEAEKA-----------ADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVA 166
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1953282154 167 RKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADK 213
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-264 1.71e-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: 52.37  E-value: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKhiaedsdR 160
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE-------L 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  161 KYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKivtnnlkslEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEELERLEEALE 464

                          250       260
                   ....*....|....*....|....
gi 1953282154  241 FAERSVAKLEKTIDDLEETLASAK 264
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQ 488
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 7-220 3.07e-07

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 51.76  E-value: 3.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    7 KMQMLKLDKENAIDRAEQ-AEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESvkdAQEKLEQAEKKATDAEA-- 83
Cdd:NF012221  1541 SQQADAVSKHAKQDDAAQnALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQN---ALETNGQAQRDAILEESra 1617

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   84 ---DVASLNRRIQLVEEE-------------------LDRAQERLATALQKLEEA-EKAADESERGMKVIENRAMKDEEK 140
Cdd:NF012221  1618 vtkELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAG 1697

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  141 MELQEMQLKEAKhiAEDSDRKYEEVARKLvilegELERSEERAEVAESKCGDLEEELK------IVTNNLKSLEAQADKY 214
Cdd:NF012221  1698 VAQGEQNQANAE--QDIDDAKADAEKRKD-----DALAKQNEAQQAESDANAAANDAQsrgeqdASAAENKANQAQADAK 1770


                   ....*.
gi 1953282154  215 STKEDK 220
Cdd:NF012221  1771 GAKQDE 1776
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 23-276 7.30e-07

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 50.44  E-value: 7.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   23 EQAEADKKQAEdrckqlEEEQQALQKKL------KGTEDEVEKYSESVKD---------AQEKLEQAEKKATDAEADVAS 87
Cdd:PRK10929    33 EQAKAAKTPAQ------AEIVEALQSALnwleerKGSLERAKQYQQVIDNfpklsaelrQQLNNERDEPRSVPPNMSTDA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   88 LNRRI-----QLVEE------ELDRAQE---RLATALQKLEEAEKAADESERGMKVIENRAMKDEEkmelqemqlkeakh 153
Cdd:PRK10929   107 LEQEIlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ-------------- 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  154 iAEDSDRKYEEVARKLVILEGEL---------ERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQAdkystkedkyeee 224
Cdd:PRK10929   173 -AQLTALQAESAALKALVDELELaqlsannrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQRE------------- 238

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1953282154  225 iklleeklkeaetrAEFAERSVAKLEKTIDDLEETLASAKEENVEIHQTLDQ 276
Cdd:PRK10929   239 --------------AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQ 276
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-216 9.13e-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: 50.06  E-value: 9.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDA 81
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADEsergmkvieNRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER---------LQQEIEELLKKLEEAELKELQAELEELEEE 448

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953282154  162 YEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYST 216
Cdd:TIGR02168  449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-259 9.98e-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: 9.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQL-EEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   81 AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDR 160
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  161 KYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAE 240
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486

                          250
                   ....*....|....*....
gi 1953282154  241 FAERSVAKLEKTIDDLEET 259
Cdd:TIGR02169  487 KLQRELAEAEAQARASEER 505
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 9-276 1.51e-06

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: 49.57  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    9 QMLKLDKENAIDRAEQAEADKKQAE--DRCKQLEEEQQALQKKLKGTED-------------EVEKYSESVKDAQEKLEQ 73
Cdd:COG3096    286 RALELRRELFGARRQLAEEQYRLVEmaRELEELSARESDLEQDYQAASDhlnlvqtalrqqeKIERYQEDLEELTERLEE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   74 AEKKATDAEADVASLNRRIQLVEEELDRAQERLA-----------------TALQKLEEAEKAADESERGMKVIENRAMK 136
Cdd:COG3096    366 QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAA 445

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  137 DEEKMELQEMQLKEAKH---IAEDSDRKYEEVARKLVILEGELERSE-------------------ERAEVAESKCGDLE 194
Cdd:COG3096    446 FRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERSQawqtarellrryrsqqalaQRLQQLRAQLAELE 525

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  195 EELkivtNNLKSLEAQADKYSTKEDKyeeeiklleeklkeAETRAEFAERSVAKLEKTIDDLEETLASAKEENVEIHQTL 274
Cdd:COG3096    526 QRL----RQQQNAERLLEEFCQRIGQ--------------QLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587


                   ..
gi 1953282154  275 DQ 276
Cdd:COG3096    588 EQ 589
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 22-263 2.46e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  22 AEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDR 101
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 102 AQERLATALQKLEEAEKAADESERgmkvienramKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEE 181
Cdd:COG4942    95 LRAELEAQKEELAELLRALYRLGR----------QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 182 RAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEETLA 261
Cdd:COG4942   165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244


                  ..
gi 1953282154 262 SA 263
Cdd:COG4942   245 AA 246
mukB PRK04863
chromosome partition protein MukB;
15-276 3.23e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 48.41  E-value: 3.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   15 KENAIDRAEQA-EADKKQAEDRCkQLEEEQQALQKKLkgtedevEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQ 93
Cdd:PRK04863   315 ELAELNEAESDlEQDYQAASDHL-NLVQTALRQQEKI-------ERYQADLEELEERLEEQNEVVEEADEQQEENEARAE 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   94 LVEEELDRAQERLA-----------------TALQKLEEAEK---AADESERGMKVIENRAMKDEEKMELQEMQLKEAKH 153
Cdd:PRK04863   387 AAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS 466

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  154 IAEDSDRKYEEVARKLVILEGELERSEErAEVAESKCGDLEEElKIVTNNLKSLEAQ---ADKYSTKEDKYEEEIKLLEE 230
Cdd:PRK04863   467 VAQAAHSQFEQAYQLVRKIAGEVSRSEA-WDVARELLRRLREQ-RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCK 544

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1953282154  231 KLKEAETRAEFAERSVAKLEKTIDDLEETLASAKEENVEIHQTLDQ 276
Cdd:PRK04863   545 RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 30-276 3.96e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.14  E-value: 3.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   30 KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATA 109
Cdd:TIGR02169  663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  110 LQKLEEAEKAADESERGMKviENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESK 189
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  190 CGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEETLASAKEENVE 269
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900


                   ....*..
gi 1953282154  270 IHQTLDQ 276
Cdd:TIGR02169  901 LERKIEE 907
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
6-176 8.60e-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: 8.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    6 KKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTE-DEVEKYSESVKDAQEKLEQAEKKATDAEAD 84
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEAL 367

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   85 VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKM--ELQEMQLKeAKHIAEDSDRKY 162
Cdd:COG4913    368 LAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaEIASLERR-KSNIPARLLALR 446

                          170
                   ....*....|....
gi 1953282154  163 EEVARKLVILEGEL 176
Cdd:COG4913    447 DALAEALGLDEAEL 460
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-258 1.17e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    7 KMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVA 86
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   87 SLNRRIQLVEEEL------------DRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHI 154
Cdd:TIGR02169  762 ELEARIEELEEDLhkleealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  155 AEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKE 234
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          250       260
                   ....*....|....*....|....
gi 1953282154  235 AETRAEFAERSVAKLEKTIDDLEE 258
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEDEE 945
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-125 1.43e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDR---CKQLEEEQ------QALQKKLKGTEDEVEKYSES---VKDAQE 69
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERreaLQRLAEYSwdeidvASAEREIAELEAELERLDASsddLAALEE 692

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953282154   70 KLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-182 1.76e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   12 KLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEAD-VASLNR 90
Cdd:COG4913    266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLER 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   91 RIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHiaeDSDRKYEEVARKLV 170
Cdd:COG4913    346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELR 422

                          170
                   ....*....|..
gi 1953282154  171 ILEGELERSEER 182
Cdd:COG4913    423 ELEAEIASLERR 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 18-259 1.78e-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: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   18 AIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEE 97
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   98 ELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELE 177
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  178 RSEER-AEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEF-------AERSVAKL 249
Cdd:TIGR02168  940 NLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFltaqkedLTEAKETL 1019

                          250
                   ....*....|
gi 1953282154  250 EKTIDDLEET 259
Cdd:TIGR02168 1020 EEAIEEIDRE 1029
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
12-129 4.64e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  12 KLDKENAIDRAEQAEADK--KQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKatdaEADVASLN 89
Cdd:COG2433   396 EAEREKEHEERELTEEEEeiRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRK----DREISRLD 471

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953282154  90 RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 129
Cdd:COG2433   472 REIERLERELEEERERIEELKRKLERLKELWKLEHSGELV 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
66-266 6.05e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 6.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   66 DAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLAtALQKLEEaekaADESERGMKVIENRAmkdeekmelqe 145
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAEREI----------- 670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  146 MQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYstkEDKYEEEI 225
Cdd:COG4913    671 AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLEL 747

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1953282154  226 KLLEEKLKEAETRAEFAERSVAKLEKTIDDLEETLASAKEE 266
Cdd:COG4913    748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
2-125 1.54e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 42.73  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDR-------------CKQLEEEQQALQKKLKGTEDEVEKYSESVKD-- 66
Cdd:COG1566    65 DRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQlarleaelgaeaeIAAAEAQLAAAQAQLDLAQRELERYQALYKKga 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  67 -AQEKLEQAEKKATDAEADVASLNRRIQLVEEELdRAQERLATALQKLEEAEKAADESER 125
Cdd:COG1566   145 vSQQELDEARAALDAAQAQLEAAQAQLAQAQAGL-REEEELAAAQAQVAQAEAALAQAEL 203
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
22-210 1.92e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  22 AEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKY---------SESVKDAQEKLEQAEKKATDAEADVASLNRRI 92
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  93 QLVEEELDRAQERLATALQ--------------KLEEAEKAADESERGMKVIENRAMKDEEKMELQEmqlkEAKHIAEDS 158
Cdd:COG3206   243 AALRAQLGSGPDALPELLQspviqqlraqlaelEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ----EAQRILASL 318

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953282154 159 DRKYEEVARKLVILEGELERSEERAEV---AESKCGDLEEELKIVTNNLKSLEAQ 210
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQR 373
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1-277 1.94e-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: 42.75  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:TIGR02169  704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND 783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   81 AEADVA-----SLNRRIQLVEEELDRAQERLATALQKLEE-------AEKAADESERGMKVIENRAMKDEEKMELQEMQL 148
Cdd:TIGR02169  784 LEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  149 KEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLL 228
Cdd:TIGR02169  864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953282154  229 EEKLKEAETRAEFAERSVAKLE--------------------KTIDDLEETLASAKEENVEIHQTLDQT 277
Cdd:TIGR02169  944 EEIPEEELSLEDVQAELQRVEEeiralepvnmlaiqeyeevlKRLDELKEKRAKLEEERKAILERIEEY 1012
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
23-283 2.82e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  23 EQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRA 102
Cdd:COG4372    55 EQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 103 QERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEER 182
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 183 AEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEETLAS 262
Cdd:COG4372   215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294

                         250       260
                  ....*....|....*....|.
gi 1953282154 263 AKEENVEIHQTLDQTLLELNN 283
Cdd:COG4372   295 LKLLALLLNLAALSLIGALED 315
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-187 4.44e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDA 81
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:COG1196   413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492

                         170       180
                  ....*....|....*....|....*.
gi 1953282154 162 YEEVARKLVILEGELERSEERAEVAE 187
Cdd:COG1196   493 LLLLLEAEADYEGFLEGVKAALLLAG 518
PTZ00121 PTZ00121
MAEBL; Provisional
 6-184 5.01e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 5.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    6 KKMQMLKLDKENA--IDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKySESVKDAQEKLEQAEKKATDAEA 83
Cdd:PTZ00121  1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYE 163
Cdd:PTZ00121  1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388

                          170       180
                   ....*....|....*....|.
gi 1953282154  164 EVaRKLVILEGELERSEERAE 184
Cdd:PTZ00121  1389 EK-KKADEAKKKAEEDKKKAD 1408
PTZ00121 PTZ00121
MAEBL; Provisional
 20-272 6.64e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 6.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   20 DRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTE---DEVEKYSESVKDAQEK-----LEQAEKKATDAEADVASLNRR 91
Cdd:PTZ00121  1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAEELKK 1559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   92 IQLVE--EELDRAQERLATALQKLEEAEKAadesERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKL 169
Cdd:PTZ00121  1560 AEEKKkaEEAKKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  170 VILEGELERSEERAEVAESKcgdlEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKL 249
Cdd:PTZ00121  1636 EQLKKKEAEEKKKAEELKKA----EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711

                          250       260
                   ....*....|....*....|...
gi 1953282154  250 EKTIDDLEETLASAKEENVEIHQ 272
Cdd:PTZ00121  1712 AEEKKKAEELKKAEEENKIKAEE 1734
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
15-207 7.02e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  15 KENAIDRAEQAE---ADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRR 91
Cdd:PRK02224  229 REQARETRDEADevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  92 IQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVI 171
Cdd:PRK02224  309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1953282154 172 LEGELERSEERAEVAESKCGDLEEELKIVTNNLKSL 207
Cdd:PRK02224  389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
PTZ00121 PTZ00121
MAEBL; Provisional
 5-265 9.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 9.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    5 KKKMQMLKLDKENAIDRAEQ---AEADKKQAEDRCKQLEEEQQAlqKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDA 81
Cdd:PTZ00121  1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRK 161
Cdd:PTZ00121  1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  162 YEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEF 241
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627

                          250       260
                   ....*....|....*....|....
gi 1953282154  242 AERSVAKLEKTIDDLEETLASAKE 265
Cdd:PTZ00121  1628 AEEEKKKVEQLKKKEAEEKKKAEE 1651
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 24-213 1.01e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  24 QAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRA- 102
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 103 -----QERLATALQKLEEAEKAADESERgMKVIENRAMKDEEKMElqemQLKEAKHIAEDSDRKYEEVARKLVILEGELE 177
Cdd:COG3883    93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEALKAELE 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1953282154 178 RSEERAE----VAESKCGDLEEELKIVTNNLKSLEAQADK 213
Cdd:COG3883   168 AAKAELEaqqaEQEALLAQLSAEEAAAEAQLAELEAELAA 207
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
20-116 1.22e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   20 DRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEEL 99
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771

                           90
                   ....*....|....*..
gi 1953282154  100 DRAQERLATALQKLEEA 116
Cdd:COG4913    772 EERIDALRARLNRAEEE 788
PTZ00121 PTZ00121
MAEBL; Provisional
 5-192 1.22e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    5 KKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKL---KGTEDEVEKYSESVKDAQEKLEQAEKKATDA 81
Cdd:PTZ00121  1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM---KVIENRAMKDEEKMELQEMQLK--------E 150
Cdd:PTZ00121  1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeeaKKAEEAKKKAEEAKKADEAKKKaeeakkadE 1487

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1953282154  151 AKHIAEDSDRKYEEVARKlvilEGELERSEERAEVAESKCGD 192
Cdd:PTZ00121  1488 AKKKAEEAKKKADEAKKA----AEAKKKADEAKKAEEAKKAD 1525
PTZ00121 PTZ00121
MAEBL; Provisional
 2-269 1.77e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    2 DAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEE-EQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKkATD 80
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-LKK 1627

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   81 AEADVASLNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGMKVIENR-AMKDEEKMELQEMQLKEAKHIAEDS 158
Cdd:PTZ00121  1628 AEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKkAEEDEKKAAEALKKEAEEAKKAEEL 1707

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  159 DRKYEEVARKLVILEGELERSEERAEVAESKcgdlEEELKIVTNNLKSLEAQADK--YSTKEDKYEEEIKLLEEKLKEAE 236
Cdd:PTZ00121  1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKiaHLKKEEEKKAEEIRKEKEAVIEE 1783

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1953282154  237 TRAEFAERSVAKLEKTIDDLEETLASAKEENVE 269
Cdd:PTZ00121  1784 ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 27-128 1.78e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.68  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  27 ADKKQAEDRCKQLEEEQQALQK-KLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVAslnrRIQLVEEELDRAQER 105
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKeQDEASFERLAELRDELAELEEELEALKARWEAEKELIE----EIQELKEELEQRYGK 486

                          90       100
                  ....*....|....*....|...
gi 1953282154 106 LATALQKLEEAEKAADESERGMK 128
Cdd:COG0542   487 IPELEKELAELEEELAELAPLLR 509
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-257 2.41e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   48 KKLKGTEDEVEKYSESVK------DAQEKLEQAEKKATDAEADVASLN-----RRIQLVEEELDRAQERLATALQKLEEA 116
Cdd:COG4913    235 DDLERAHEALEDAREQIEllepirELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  117 EKAADESERgmkvienramkdeekmelQEMQLKEAkhIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEE 196
Cdd:COG4913    315 EARLDALRE------------------ELDELEAQ--IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953282154  197 lkiVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLE 257
Cdd:COG4913    375 ---LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 74-284 2.47e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  74 AEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKh 153
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 154 iaEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLK 233
Cdd:COG4942    97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953282154 234 EAETRAEFAERSVAKLEKTIDDLEETLASAKEENVEIHQTLDQTLLELNNL 284
Cdd:COG4942   175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-177 3.14e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154    1 MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATD 80
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   81 AEADVASLNRRIQLVEEELDRAQERLATALQKL-EEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSD 159
Cdd:TIGR02168  913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992

                          170
                   ....*....|....*...
gi 1953282154  160 RKYEEVARKLVILEGELE 177
Cdd:TIGR02168  993 EEYEELKERYDFLTAQKE 1010
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 54-156 3.52e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  54 EDEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLA-TALQKLEEAEKAADESERGMKVIEN 132
Cdd:PRK00409  519 NELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELRQLQK 598

                          90       100
                  ....*....|....*....|....*.
gi 1953282154 133 RAMKDEEKMELQEMQ--LKEAKHIAE 156
Cdd:PRK00409  599 GGYASVKAHELIEARkrLNKANEKKE 624
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
 22-101 4.72e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 37.17  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  22 AEQAEADKKQAEDRCKQLEEEQQALQKKLKgteDEVEKYSESVKDAQEKLEQAEKKATDaeaDVASLNRRIQLVEEELDR 101
Cdd:pfam10211 114 ALQAEQGKAELEKKIADLEEEKEELEKQVA---ELKAKCEAIEKREEERRQAEEKKHAE---EIAFLKKTNQQLKAQLER 187
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
14-274 6.17e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.10  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  14 DKENAIDRAEQAEADKKQAEdrckqLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLEQAEKKATDAEADVAslnrRIQ 93
Cdd:PRK02224  184 DQRGSLDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELE 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  94 LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILE 173
Cdd:PRK02224  255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154 174 GELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTI 253
Cdd:PRK02224  335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414

                         250       260
                  ....*....|....*....|.
gi 1953282154 254 DDLEETLASAKEENVEIHQTL 274
Cdd:PRK02224  415 EELREERDELREREAELEATL 435
PRK11281 PRK11281
mechanosensitive channel MscK;
11-152 8.09e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 37.58  E-value: 8.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154   11 LKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQK------KLKGTEDEVEKY---SESVKDAQEKLEQAEKKATDA 81
Cdd:PRK11281    61 VQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQaqaeleALKDDNDEETREtlsTLSLRQLESRLAQTLDQLQNA 140

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953282154   82 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmkvIENRAMKDEEKMELQ-EMQLKEAK 152
Cdd:PRK11281   141 QNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGK-----VGGKALRPSQRVLLQaEQALLNAQ 207
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
55-198 8.58e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 37.36  E-value: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  55 DEVEKYSESVKDAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLAT--ALQK---------LEEAEKAADES 123
Cdd:COG0497   254 ERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEERLALlrRLARkygvtveelLAYAEELRAEL 333

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953282154 124 ERgmkvIENramkDEEKMELQEMQLKEAKhiaedsdRKYEEVARKLvilegelerSEERAEVAESKCGDLEEELK 198
Cdd:COG0497   334 AE----LEN----SDERLEELEAELAEAE-------AELLEAAEKL---------SAARKKAAKKLEKAVTAELA 384
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
16-219 9.09e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.33  E-value: 9.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  16 ENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKDAQEKLE--------QAEKKATDAEAdVAS 87
Cdd:PRK02224  394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgQPVEGSPHVET-IEE 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953282154  88 LNRRIQLVEEELDRAQERLATALQKLEEAEkAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVAR 167
Cdd:PRK02224  473 DRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953282154 168 KLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKED 219
Cdd:PRK02224  552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD 603
 
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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