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Conserved domains on  [gi|45553375|ref|NP_996216|]
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tropomyosin 1, isoform L [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 5.99e-56

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: 180.22  E-value: 5.99e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    48 KKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   128 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553375   208 EVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEMEATLHDIQ 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 5.99e-56

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: 180.22  E-value: 5.99e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    48 KKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   128 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553375   208 EVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEMEATLHDIQ 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-275 1.06e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  21 RALVCEQEARDANTRA---EKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEE 97
Cdd:COG1196 216 RELKEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  98 DLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLE 177
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 178 RSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                       250
                ....*....|....*...
gi 45553375 258 DDLLNVRGKNKLLQEEME 275
Cdd:COG1196 456 EEEEALLELLAELLEEAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-283 4.04e-13

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: 69.32  E-value: 4.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    106 LGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    186 SESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVL-------DHSLKEAEARAEFAERSVQKLQKEVDRLED 258
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlneraslEEALALLRSELEELSEELRELESKRSELRR 915

                          250       260
                   ....*....|....*....|....*
gi 45553375    259 DLLNVRGKNKLLQEEMEATLHDIQN 283
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLEVRIDN 940
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
28-197 3.03e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.66  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   28 EARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLG 107
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  108 SATAKLSEASQAADESERIRKALE--------------NRTNMEDDKVALLENQLAQAKLIAEEADKKYEEvARKLVLME 173
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAE 508

                        170       180
                 ....*....|....*....|....
gi 45553375  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 5.99e-56

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: 180.22  E-value: 5.99e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    48 KKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIR 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   128 KALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553375   208 EVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEMEATLHDIQ 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 5.66e-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: 5.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     7 KMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESeva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEN--- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553375    87 aLNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAK 152
Cdd:pfam12718  78 -LTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-275 1.06e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  21 RALVCEQEARDANTRA---EKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEE 97
Cdd:COG1196 216 RELKEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  98 DLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLE 177
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 178 RSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                       250
                ....*....|....*...
gi 45553375 258 DDLLNVRGKNKLLQEEME 275
Cdd:COG1196 456 EEEEALLELLAELLEEAA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 26-283 4.04e-13

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: 69.32  E-value: 4.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    106 LGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    186 SESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVL-------DHSLKEAEARAEFAERSVQKLQKEVDRLED 258
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlneraslEEALALLRSELEELSEELRELESKRSELRR 915

                          250       260
                   ....*....|....*....|....*
gi 45553375    259 DLLNVRGKNKLLQEEMEATLHDIQN 283
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGLEVRIDN 940
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-276 6.52e-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: 6.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 106 LGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 186 SESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRG 265
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                       250
                ....*....|.
gi 45553375 266 KNKLLQEEMEA 276
Cdd:COG1196 478 ALAELLEELAE 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-275 2.01e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 2.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   7 KMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVA 86
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  87 ALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVA 166
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 167 RKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSV 246
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472

                       250       260
                ....*....|....*....|....*....
gi 45553375 247 QKLQKEVDRLEDDLLNVRGKNKLLQEEME 275
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEA 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 35-282 2.89e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.80  E-value: 2.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 115 EASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELE 194
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 195 EELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEM 274
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458


                ....*...
gi 45553375 275 EATLHDIQ 282
Cdd:COG1196 459 EALLELLA 466
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-282 2.46e-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: 60.84  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    115 EASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELE 194
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    195 EELRVVGNNLKSLEV-----SEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKL 269
Cdd:TIGR02168  393 LQIASLNNEIERLEArlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472

                          250
                   ....*....|...
gi 45553375    270 LQEEMEATLHDIQ 282
Cdd:TIGR02168  473 AEQALDAAERELA 485
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-283 5.15e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 5.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  36 AEKAEEeARQLQKKIQTVENELdqTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSE 115
Cdd:COG1196 209 AEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 116 ASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEE 195
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 196 ELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEME 275
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445


                ....*...
gi 45553375 276 ATLHDIQN 283
Cdd:COG1196 446 EAAEEEAE 453
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 35-252 1.91e-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: 58.14  E-value: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:TIGR02168  219 KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    115 EASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELE 194
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 45553375    195 EELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKE 252
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-232 4.93e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 4.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  82 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKK 161
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553375 162 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSL 232
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-266 8.85e-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: 56.22  E-value: 8.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375      1 MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQN 80
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     81 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADK 160
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    161 KYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAE 240
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          250       260
                   ....*....|....*....|....*.
gi 45553375    241 FAERSVQKLQKEVDRLEDDLLNVRGK 266
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRIDNLQER 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 7-259 1.46e-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: 55.46  E-value: 1.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375      7 KMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVA 86
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     87 ALNRRIQLLEEDLERSEERLGSATAKLS---------EASQAADESERIRKAL---ENRTNMEDDKVALLENQLAQAKLI 154
Cdd:TIGR02169  762 ELEARIEELEEDLHKLEEALNDLEARLShsripeiqaELSKLEEEVSRIEARLreiEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    155 AEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKE 234
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          250       260
                   ....*....|....*....|....*
gi 45553375    235 AEARAEFAERSVQKLQKEVDRLEDD 259
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEDEEI 946
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
28-197 3.03e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.66  E-value: 3.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   28 EARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLG 107
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  108 SATAKLSEASQAADESERIRKALE--------------NRTNMEDDKVALLENQLAQAKLIAEEADKKYEEvARKLVLME 173
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAE 508

                        170       180
                 ....*....|....*....|....
gi 45553375  174 QDLERSEEKVELSESKIVELEEEL 197
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETI 532
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
18-193 4.33e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 4.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   18 ALERALV-CEQEARDANTRAEKAEEEARQLQKKIQT---------VENELDQTQEALTlvtgKLEEKNKALQNAESEVAA 87
Cdd:COG4913  614 ALEAELAeLEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIA----ELEAELERLDASSDDLAA 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   88 LNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVAR 167
Cdd:COG4913  690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769

                        170       180
                 ....*....|....*....|....*.
gi 45553375  168 KLvlmEQDLERSEEKVELSESKIVEL 193
Cdd:COG4913  770 NL---EERIDALRARLNRAEEELERA 792
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 22-252 1.40e-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: 52.07  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  22 ALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLER 101
Cdd:COG4942   8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 102 SEERLGSATAKLSEasQAADESERIRkALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEE 181
Cdd:COG4942  88 LEKEIAELRAELEA--QKEELAELLR-ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553375 182 KVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKE 252
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-276 2.74e-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: 2.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375      1 MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQN 80
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     81 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADK 160
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    161 KYEEVARKLVLMEQDLERSEEKVELSESKIVELeeELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAE 240
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 45553375    241 FAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEMEA 276
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-284 1.77e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     50 IQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEAsqaadesERIRKA 129
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL-------EAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    130 LENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEV 209
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553375    210 SEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEMEATLHDIQNM 284
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-214 2.42e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 2.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQ-TQEALTLVTGKLEEKNKALQN 80
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEElAEELLEALRAAAELAAQLEEL 405

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  81 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADK 160
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 45553375 161 KYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKA 214
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 54-283 2.80e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  54 ENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEE----RLGSATAKLSEASQAADESERIRKA 129
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAEllllKLRELEAELEELEAELEELEAELEE 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 130 LENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEV 209
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553375 210 SEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEMEATLHDIQN 283
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 26-257 2.90e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     26 EQEARDANTRAEK-AEEEARQLQKKIQTVENELDQTQealtlvtGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEE 104
Cdd:TIGR02169  271 EQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLE-------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    105 RLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVE 184
Cdd:TIGR02169  344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553375    185 LSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:TIGR02169  424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 32-217 7.01e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 7.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  32 ANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATA 111
Cdd:COG3883  14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 112 KLSEASQAADESERI------------RKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERS 179
Cdd:COG3883  94 ALYRSGGSVSYLDVLlgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 45553375 180 EEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQK 217
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-230 1.13e-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: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   37 EKAEEEARQLQKKIQTVEnELDQTQEALTLVTGKLEEKNKALQNAESEVAAlnRRIQLLEEDLERSEERLGSATAKLSEA 116
Cdd:COG4913  238 ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  117 SQAADE-SERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEE----KVELSESKIV 191
Cdd:COG4913  315 EARLDAlREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaaLRAEAAALLE 394

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 45553375  192 ELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDH 230
Cdd:COG4913  395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-193 1.57e-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: 1.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     27 QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERL 106
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    107 GSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQ-AKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:TIGR02168  897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976


                   ....*...
gi 45553375    186 SESKIVEL 193
Cdd:TIGR02168  977 LENKIKEL 984
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
70-199 1.04e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   70 KLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLgSATAKLSEAS-------QAADESERIRKALENRTNmEDDKVA 142
Cdd:COG4913  611 KLAALEAELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSwdeidvaSAEREIAELEAELERLDA-SSDDLA 688

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 45553375  143 LLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRV 199
Cdd:COG4913  689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
90-283 1.23e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   90 RRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNM--EDDKVALLENQLAQAKLIAEEADKKYEEVAR 167
Cdd:COG4913  610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswDEIDVASAEREIAELEAELERLDASSDDLAA 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  168 klvlMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQ 247
Cdd:COG4913  690 ----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVER 765

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 45553375  248 KLQKevdRLEDDLLNVRGKNKLLQEEMEATLHDIQN 283
Cdd:COG4913  766 ELRE---NLEERIDALRARLNRAEEELERAMRAFNR 798
mukB PRK04863
chromosome partition protein MukB;
29-272 1.59e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.02  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    29 ARDANTRAEKAEEeARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQL------LEEDLERS 102
Cdd:PRK04863  275 MRHANERRVHLEE-ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLvqtalrQQEKIERY 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   103 EERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLA--QAKLIAEE--------ADKKYEEVARKLVLM 172
Cdd:PRK04863  354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyQQALDVQQtraiqyqqAVQALERAKQLCGLP 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   173 EQDLERSEEKVELSESKIVELEEELRVVGNNLKsleVSEEKATQKEETFETQIKVLDH-----------SLKEAEARAEF 241
Cdd:PRK04863  434 DLTADNAEDWLEEFQAKEQEATEELLSLEQKLS---VAQAAHSQFEQAYQLVRKIAGEvsrseawdvarELLRRLREQRH 510

                         250       260       270
                  ....*....|....*....|....*....|.
gi 45553375   242 AERSVQKLQKEVDRLEDDLLNVRGKNKLLQE 272
Cdd:PRK04863  511 LAEQLQQLRMRLSELEQRLRQQQRAERLLAE 541
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
26-283 1.80e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:COG4372  51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 106 LGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVEL 185
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIE 210

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 186 SESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRG 265
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290

                       250
                ....*....|....*...
gi 45553375 266 KNKLLQEEMEATLHDIQN 283
Cdd:COG4372 291 AALELKLLALLLNLAALS 308
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
27-276 3.06e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 3.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  27 QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERL 106
Cdd:COG4372  38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 107 GSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELS 186
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 187 ESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGK 266
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277

                       250
                ....*....|
gi 45553375 267 NKLLQEEMEA 276
Cdd:COG4372 278 LEIAALELEA 287
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 26-204 3.37e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEK-NKALQNAESEVAALNRRIQLLE--EDLERS 102
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQkgGYASVK 605

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  103 EERLGSATAKLSEASQAADESERIRKAlENRTNMEDDKVALLenQLAQAKLIAEEADKKYEEV---ARKLVLMEQDLERS 179
Cdd:PRK00409 606 AHELIEARKRLNKANEKKEKKKKKQKE-KQEELKVGDEVKYL--SLGQKGEVLSIPDDKEAIVqagIMKMKVPLSDLEKI 682

                        170       180
                 ....*....|....*....|....*
gi 45553375  180 EEKVELSESKIVELEEELRVVGNNL 204
Cdd:PRK00409 683 QKPKKKKKKKPKTVKPKPRTVSLEL 707
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-262 3.43e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   1 MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQN 80
Cdd:COG4372  40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  81 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVAL--LENQLAQAKLIAEEA 158
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEqaLDELLKEANRNAEKE 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 159 DKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEAR 238
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279

                       250       260
                ....*....|....*....|....
gi 45553375 239 AEFAERSVQKLQKEVDRLEDDLLN 262
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLN 303
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
26-229 3.58e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 3.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQ---------TQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLE 96
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  97 EDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDD---------KVALLENQLAQ-AKLIAEEADKKYEEVA 166
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdvialraQIAALRAQLQQeAQRILASLEAELEALQ 326

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553375 167 RKLVLMEQDLERSEEKVEL---SESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLD 229
Cdd:COG3206 327 AREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
PTZ00121 PTZ00121
MAEBL; Provisional
 2-219 4.13e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    82 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKK 161
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 45553375   162 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEE 219
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 26-168 4.55e-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: 40.68  E-value: 4.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEE--KNKALQNAESEVAALNRRIQLLEEDLERSE 103
Cdd:COG1579  37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILELM 116

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 104 ERLGSATAKLSEASQAADESERIRKALENR-----TNMEDDKVALLENQLAQAKLIAEEADKKYEEVARK 168
Cdd:COG1579 117 ERIEELEEELAELEAELAELEAELEEKKAEldeelAELEAELEELEAEREELAAKIPPELLALYERIRKR 186
PRK11281 PRK11281
mechanosensitive channel MscK;
35-224 5.49e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.44  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTG--------------------KLEEKNKALQNAESEVAALNRRIQL 94
Cdd:PRK11281   74 KIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDdndeetretlstlslrqlesRLAQTLDQLQNAQNDLAEYNSQLVS 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    95 LEEDLERseerlgsATAKLSEASQAADEserIRKALENRTNMEDDKVALLENQLaQAKLIAEEADKKYE--EVARKLVLm 172
Cdd:PRK11281  154 LQTQPER-------AQAALYANSQRLQQ---IRNLLKGGKVGGKALRPSQRVLL-QAEQALLNAQNDLQrkSLEGNTQL- 221

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 45553375   173 eQDLErsEEKVELSESKIVELEEELRVVGN--NLKSLEVSEEKATQKEETFETQ 224
Cdd:PRK11281  222 -QDLL--QKQRDYLTARIQRLEHQLQLLQEaiNSKRLTLSEKTVQEAQSQDEAA 272
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1-158 5.86e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 5.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    1 MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQ-KKIQTVENELDQTQEALTLVTGKLEEKNKALQ 79
Cdd:COG4913  290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLA 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   80 NAESEV-----------AALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQL 148
Cdd:COG4913  370 ALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449

                        170
                 ....*....|
gi 45553375  149 AQAKLIAEEA 158
Cdd:COG4913  450 AEALGLDEAE 459
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-199 6.18e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 6.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  27 QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAEsevaaLNRRIQLLEEDLERSEERL 106
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELAELPERL 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 107 GSATAKLSEASQAADESERIRKALENrtnMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELS 186
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225

                       170
                ....*....|...
gi 45553375 187 ESKIVELEEELRV 199
Cdd:COG4717 226 EEELEQLENELEA 238
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
51-282 6.37e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 6.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  51 QTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQL--LEEDLERSEERLGSATAKLSEASQAADESERIRK 128
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 129 ALENRTNMEDDKVALLENQLAQAKLIAEEAdkkyeEVARKLVLMEQDLERSEEKVELSESKIVELEEELRV-VGNNLKSL 207
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLA-----ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQeAQRILASL 318

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553375 208 EVSEEKATQKEETFETQIKvldhSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEMEATLHDIQ 282
Cdd:COG3206 319 EAELEALQAREASLQAQLA----QLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
27-204 1.15e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.06  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  27 QEARDANTRAEKAEEEARQLQKKIQTVE---NELdqtqEALTLVTG---KLEEKNKALQNAESEVAALNRRIQLLEEDLE 100
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRfqlEEL----EAAALQPGeeeELEEERRRLSNAEKLREALQEALEALSGGEG 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375 101 RSEERLGSATAKLSEASQAADESERIRKALEN---------------RTNMEDDKVAL--LENQLAQAKLIAeeadKKY- 162
Cdd:COG0497 241 GALDLLGQALRALERLAEYDPSLAELAERLESalieleeaaselrryLDSLEFDPERLeeVEERLALLRRLA----RKYg 316

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 45553375 163 ---EEVARKLVLMEQDLER---SEEKVELSESKIVELEEELRVVGNNL 204
Cdd:COG0497 317 vtvEELLAYAEELRAELAElenSDERLEELEAELAEAEAELLEAAEKL 364
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 35-216 1.33e-03

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: 40.21  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERS--------EERL 106
Cdd:pfam12128  605 RLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAlaerkdsaNERL 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    107 GS--ATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVE 184
Cdd:pfam12128  685 NSleAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLG 764

                          170       180       190
                   ....*....|....*....|....*....|..
gi 45553375    185 LSESKIVELEEELRVVGNNLKSLEVSEEKATQ 216
Cdd:pfam12128  765 VDPDVIAKLKREIRTLERKIERIAVRRQEVLR 796
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 2-220 1.35e-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: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:COG3883  19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  82 ESEVAALNrrIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKK 161
Cdd:COG3883  99 GGSVSYLD--VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 45553375 162 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEET 220
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
18-196 1.40e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   18 ALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEaltlvtgKLEEKNKALQNAESEVAALNRRIQLLEE 97
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE-------RAEELRERAAELEAEAEEKREAAAEAEE 565

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   98 DLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLME---- 173
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAefde 645

                        170       180       190
                 ....*....|....*....|....*....|
gi 45553375  174 -------QDLERSEEKVELSESKIVELEEE 196
Cdd:PRK02224 646 arieearEDKERAEEYLEQVEEKLDELREE 675
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 82-283 1.43e-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: 40.05  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     82 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKK 161
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    162 YEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEetFETQIKVLDHSLKEAEARAEF 241
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR--IEARLREIEQKLNRLTLEKEY 830

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 45553375    242 AERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEMEATLHDIQN 283
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-276 3.61e-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: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     66 LVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLE 145
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    146 NQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEvsEEKATQKEETFETQI 225
Cdd:TIGR02168  740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR--EALDELRAELTLLNE 817

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 45553375    226 KVLDHS--LKEAEARAEFAERSVQKLQKEVDRLEDDLLNVRGKNKLLQEEMEA 276
Cdd:TIGR02168  818 EAANLRerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 45-281 3.98e-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: 38.51  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     45 QLQKKIQTVENELDQTQEALTLVTGKLEEKN--------------------------------KALQNAESEVAALNRRI 92
Cdd:TIGR02169  167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqlerlrrerekaeryqallkekreyegyellKEKEALERQKEAIERQL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     93 QLLEEDLERSEERLGSATAKLSEASQAADE-SERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVL 171
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    172 MEQDLERSEEKVELSESKIVELEEELRVVGNNLKSLEVSEEKATQKEETFETQIKVLDHSLKEAEARAEFAERSVQKLQK 251
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406

                          250       260       270
                   ....*....|....*....|....*....|
gi 45553375    252 EVDRLEDDLLNVRGKNKLLQEEMEATLHDI 281
Cdd:TIGR02169  407 ELDRLQEELQRLSEELADLNAAIAGIEAKI 436
PRK09039 PRK09039
peptidoglycan -binding protein;
18-135 4.57e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.02  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   18 ALERALVCEQEARDANTRAEKAEEEArqLQKKIQTVENELDQTQEALTlvtGKLEEKNKALQNAESEVAALNRRIQLLEE 97
Cdd:PRK09039  70 SLERQGNQDLQDSVANLRASLSAAEA--ERSRLQALLAELAGAGAAAE---GRAGELAQELDSEKQVSARALAQVELLNQ 144

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 45553375   98 DLERSEERLGSATAKLsEASQAADESERIRKA-LENRTN 135
Cdd:PRK09039 145 QIAALRRQLAALEAAL-DASEKRDRESQAKIAdLGRRLN 182
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 25-265 5.56e-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: 38.13  E-value: 5.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375     25 CEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEE 104
Cdd:TIGR02169  306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    105 RLGSATAKLSEASQAADESERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVE 184
Cdd:TIGR02169  386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    185 LSESKIVELEEELRVVGNNLKSLEvseekatqkeetfetqikvldHSLKEAEARAEFAERSVQKLQKEVDRLEDDLLNVR 264
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEKELSKLQ---------------------RELAEAEAQARASEERVRGGRAVEEVLKASIQGVH 524


                   .
gi 45553375    265 G 265
Cdd:TIGR02169  525 G 525
PTZ00121 PTZ00121
MAEBL; Provisional
 27-226 8.58e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 8.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375    27 QEARDANTRAEKAEE--EARQLQKKIQTVENELDQTQEaltlvtgKLEEKNKALQNAESEVAALnrriqllEEDLERSEE 104
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEakKADEAKKKAEEAKKKADAAKK-------KAEEAKKAAEAAKAEAEAA-------ADEAEAAEE 1364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   105 RLGSATAKLSEASQAADE----SERIRKALENRTNMEDDKVALLE-NQLAQAKLIAEEADKKYEEVARKlvlmEQDLERS 179
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAakkkAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKA----DEAKKKA 1440

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 45553375   180 EEKVELSESKIVELE----EELRVVGNNLKSLEVSEEKATQKEETFETQIK 226
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEakkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
35-198 8.62e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.71  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375   35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  115 EASQAADESERIRKALEN-----RTNMEDDKVAL------LENQLAQAKLIAEEADKKYEEVARklvlMEQDLERSEEKV 183
Cdd:PRK02224 304 LDDADAEAVEARREELEDrdeelRDRLEECRVAAqahneeAESLREDADDLEERAEELREEAAE----LESELEEAREAV 379

                        170
                 ....*....|....*
gi 45553375  184 ELSESKIVELEEELR 198
Cdd:PRK02224 380 EDRREEIEELEEEIE 394
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 42-198 9.53e-03

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: 36.83  E-value: 9.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553375  42 EARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATaklseasqaad 121
Cdd:COG1579  18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR----------- 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553375 122 eSERIRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEEKVELSESKIVELEEELR 198
Cdd:COG1579  87 -NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
 
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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