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Conserved domains on  [gi|528522056|ref|XP_005174442|]
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tropomyosin alpha-1 chain isoform X11 [Danio rerio]

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 ...
 11-243 2.49e-66

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: 205.26  E-value: 2.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   11 RKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 90
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   91 KVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSL 170
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528522056  171 EAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELRMALNE 243
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAE 233
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 11-243 2.49e-66

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: 205.26  E-value: 2.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   11 RKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 90
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   91 KVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSL 170
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528522056  171 EAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELRMALNE 243
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAE 233
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-228 3.04e-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: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   2 AATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 81
Cdd:COG1196  272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  82 AADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELK 161
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528522056 162 TVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLE 228
Cdd:COG1196  432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-243 6.93e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.61  E-value: 6.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     1 MAATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAE 80
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    81 KAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEEL 160
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   161 KTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDR---LYQQLEKNRLLSNEL 237
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrseLRRELEELREKLAQL 927


                   ....*.
gi 528522056   238 RMALNE 243
Cdd:TIGR02168  928 ELRLEG 933
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 29-237 6.74e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.59  E-value: 6.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   29 KLQKELAHERKARETAEGDVAS--LNRRI-----QLVEE------ELDRAQE---RLATALQKLEEAEKAADESERGMKV 92
Cdd:PRK10929   83 ELRQQLNNERDEPRSVPPNMSTdaLEQEIlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQT 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   93 IENRALKDEEkmeiqeiqlkeakhiAEEADRKYEEVARKLVIVEGELE------RTE---ERAELNESKCSELEEELKTV 163
Cdd:PRK10929  163 LGTPNTPLAQ---------------AQLTALQAESAALKALVDELELAqlsannRQElarLRSELAKKRSQQLDAYLQAL 227

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528522056  164 TNNLKSLEaqaekysQKEdkyeeeikvltdklkeaetrAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNEL 237
Cdd:PRK10929  228 RNQLNSQR-------QRE--------------------AERALESTELLAEQSGDLPKSIVAQFKINRELSQAL 274
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 11-243 2.49e-66

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: 205.26  E-value: 2.49e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   11 RKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 90
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   91 KVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSL 170
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528522056  171 EAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELRMALNE 243
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAE 233
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-228 3.04e-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: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   2 AATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 81
Cdd:COG1196  272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  82 AADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELK 161
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528522056 162 TVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLE 228
Cdd:COG1196  432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-244 2.26e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 2.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   6 LEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQ-------LVEEELDRAQERLATALQKLEE 78
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  79 AEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEE 158
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056 159 ELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELR 238
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473


                 ....*.
gi 528522056 239 MALNED 244
Cdd:COG1196  474 LLEAAL 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-243 6.93e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.61  E-value: 6.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     1 MAATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAE 80
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    81 KAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEEL 160
Cdd:TIGR02168  768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   161 KTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDR---LYQQLEKNRLLSNEL 237
Cdd:TIGR02168  848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrseLRRELEELREKLAQL 927


                   ....*.
gi 528522056   238 RMALNE 243
Cdd:TIGR02168  928 ELRLEG 933
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 11-115 1.62e-10

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: 57.31  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   11 RKIKLLQEQADGAEDKAEKLQKELAHERKARETAEgdvaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 90
Cdd:pfam12718  42 HKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKV 117

                          90       100
                  ....*....|....*....|....*
gi 528522056   91 KVIENRALKDEEKMEIQEIQLKEAK 115
Cdd:pfam12718 118 QALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-243 6.72e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 6.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   7 EAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 86
Cdd:COG1196  221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  87 ERGMKV-------IENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEE 159
Cdd:COG1196  301 EQDIARleerrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056 160 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELRM 239
Cdd:COG1196  381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460


                 ....
gi 528522056 240 ALNE 243
Cdd:COG1196  461 LLEL 464
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-225 5.97e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 5.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     1 MAATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQL-------VEEELDRAQERLATAL 73
Cdd:TIGR02168  250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIlrerlanLERQLEELEAQLEELE 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    74 QKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKC 153
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528522056   154 SELEEELKTVTNNLKSL-----EAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQ 225
Cdd:TIGR02168  410 ERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-223 1.19e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     2 AATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 81
Cdd:TIGR02168  717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    82 AADESERGMKVIEN-------RALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCS 154
Cdd:TIGR02168  797 ELKALREALDELRAeltllneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528522056   155 ELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRL 223
Cdd:TIGR02168  877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 6-223 1.24e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     6 LEAVKRKIKLLQEQADgaedKAEKLQKELAHERKAretaegDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 85
Cdd:TIGR02168  195 LNELERQLKSLERQAE----KAERYKELKAELREL------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    86 SERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTN 165
Cdd:TIGR02168  265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 528522056   166 NLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRL 223
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 9-243 1.38e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   9 VKRKIKLLQEQADGAED----KAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 84
Cdd:COG1196  198 LERQLEPLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  85 ESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVT 164
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528522056 165 NNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELRMALNE 243
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-229 2.91e-07

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.53  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   2 AATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 81
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  82 AADESErgmKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELK 161
Cdd:COG4942   98 ELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528522056 162 TVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEK 229
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-214 9.15e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 9.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   6 LEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 85
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  86 SERGmkviENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTN 165
Cdd:COG1196  391 ALRA----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528522056 166 NLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEK 214
Cdd:COG1196  467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-243 1.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    12 KIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEaekaadesergmk 91
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR------------- 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    92 vIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLE 171
Cdd:TIGR02168  300 -LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528522056   172 AQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLY-QQLEKNRLLSNELRMALNE 243
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEE 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 5-222 1.97e-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: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     5 SLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 84
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    85 ESERgmKVIENRALKDEEKMEIQEIQlkeakhiaEEADRKYEEVARKlvivEGELERTEERAELNESKCSELEEELKTVT 164
Cdd:TIGR02169  382 ETRD--ELKDYREKLEKLKREINELK--------RELDRLQEELQRL----SEELADLNAAIAGIEAKINELEEEKEDKA 447

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 528522056   165 NNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDR 222
Cdd:TIGR02169  448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 29-237 6.74e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.59  E-value: 6.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   29 KLQKELAHERKARETAEGDVAS--LNRRI-----QLVEE------ELDRAQE---RLATALQKLEEAEKAADESERGMKV 92
Cdd:PRK10929   83 ELRQQLNNERDEPRSVPPNMSTdaLEQEIlqvssQLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQT 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   93 IENRALKDEEkmeiqeiqlkeakhiAEEADRKYEEVARKLVIVEGELE------RTE---ERAELNESKCSELEEELKTV 163
Cdd:PRK10929  163 LGTPNTPLAQ---------------AQLTALQAESAALKALVDELELAqlsannRQElarLRSELAKKRSQQLDAYLQAL 227

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528522056  164 TNNLKSLEaqaekysQKEdkyeeeikvltdklkeaetrAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNEL 237
Cdd:PRK10929  228 RNQLNSQR-------QRE--------------------AERALESTELLAEQSGDLPKSIVAQFKINRELSQAL 274
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 10-238 6.90e-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: 46.60  E-value: 6.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    10 KRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERg 89
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ- 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    90 mKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKS 169
Cdd:TIGR02169  752 -EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528522056   170 LEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELR 238
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
7-225 1.23e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   7 EAVKRKIKLLQEQADGAEDKAEKLQKELAHERkaretAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 86
Cdd:COG3206  171 EEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  87 ERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEAD--RKYEEVARKLVIVEgelertEERAELNESKCSELEEELKTVT 164
Cdd:COG3206  246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsARYTPNHPDVIALR------AQIAALRAQLQQEAQRILASLE 319

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528522056 165 NNLKSLEAQAEKYSQKEDKYEEEIKvltdKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQ 225
Cdd:COG3206  320 AELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLEE 376
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 15-238 1.94e-05

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: 45.14  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  15 LLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIE 94
Cdd:COG4942   10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  95 NRALKDEEKMEIQEIQLKEakhIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQA 174
Cdd:COG4942   90 KEIAELRAELEAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528522056 175 EKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELR 238
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
10-232 1.97e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   10 KRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 89
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   90 MKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESkcSELEEELKTvtnnlks 169
Cdd:COG4913   687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAA------- 757

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528522056  170 lEAQAEKYSQKEDKYEEEIKVLTDKLKEAETR-----AEFAER---SVAKLEKTIDDLED--RLYQQLEKNRL 232
Cdd:COG4913   758 -ALGDAVERELRENLEERIDALRARLNRAEEEleramRAFNREwpaETADLDADLESLPEylALLDRLEEDGL 829
PTZ00121 PTZ00121
MAEBL; Provisional
 7-222 5.15e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    7 EAVKRKIKLLQEQADGAEDKAEKLQKELAHE-RKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 85
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAEElRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   86 SERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNES--------KCSELE 157
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAkkkaeeakKADEAK 1321

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528522056  158 EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDR 222
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
PTZ00121 PTZ00121
MAEBL; Provisional
 10-231 9.08e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 9.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   10 KRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 89
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   90 MKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVtNNLKS 169
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-EQLKK 1640

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528522056  170 LEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNR 231
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-220 1.06e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     6 LEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEEL-----DRAQERLATALQKLEEAE 80
Cdd:TIGR02169  725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLE 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    81 KAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEEL 160
Cdd:TIGR02169  805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   161 KTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLE 220
Cdd:TIGR02169  885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 1-224 2.96e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   1 MAATSLEAVKRKIKLLQE--QADGAEDKAEKLQKELAHErKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEE 78
Cdd:PRK05771  47 KLRSLLTKLSEALDKLRSylPKLNPLREEKKKVSVKSLE-ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  79 AEKAAD--------ESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVA---RKLVIVEGELERTE-ERA 146
Cdd:PRK05771 126 LEPWGNfdldlsllLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVvlkELSDEVEEELKKLGfERL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056 147 ELNESKC-----SELEEELKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLTDKL----KEAETRAEFA------------ 205
Cdd:PRK05771 206 ELEEEGTpseliREIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielERAEALSKFLktdktfaiegwv 282

                        250       260
                 ....*....|....*....|
gi 528522056 206 -ERSVAKLEKTIDDLEDRLY 224
Cdd:PRK05771 283 pEDRVKKLKELIDKATGGSA 302
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 5-223 4.14e-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: 41.21  E-value: 4.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     5 SLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 84
Cdd:TIGR02169  710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    85 ESERGMKVIENRALKD-----EEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEE 159
Cdd:TIGR02169  790 HSRIPEIQAELSKLEEevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528522056   160 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRL 223
Cdd:TIGR02169  870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
6-222 4.36e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    6 LEAVKRKIKLLqEQADGAEDKAEKLQKELAHERKARET-----AEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAE 80
Cdd:COG4913   244 LEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALR 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   81 KAADESERgmkvienralkdeekmEIQEIQLKEAKHIAEEADRKyeevarklvivEGELERTEERAELNESKCSELEEel 160
Cdd:COG4913   323 EELDELEA----------------QIRGNGGDRLEQLEREIERL-----------ERELEERERRRARLEALLAALGL-- 373

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528522056  161 kTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDR 222
Cdd:COG4913   374 -PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-145 4.78e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    2 AATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAE--------GDVASLNRRIQLVEEELDRAQERLATAL 73
Cdd:COG4913   286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLE 365

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528522056   74 QKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHiaeEADRKYEEVARKLVIVEGELERTEER 145
Cdd:COG4913   366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLERR 434
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
26-223 5.98e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  26 KAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALK---DEE 102
Cdd:PRK02224 193 KAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETiaeTER 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056 103 KMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKED 182
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAD 352

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528522056 183 KYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRL 223
Cdd:PRK02224 353 DLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 2-210 9.39e-04

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: 9.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   2 AATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 81
Cdd:COG3883   14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  82 AADESERGMKVIE------------NRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELN 149
Cdd:COG3883   94 ALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528522056 150 ESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVA 210
Cdd:COG3883  174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
13-229 1.42e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  13 IKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 92
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  93 IENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAE-----LNESKCSELEEELKTVTN-- 165
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaealLEAGKCPECGQPVEGSPHve 468

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528522056 166 -------NLKSLEAQAEKYSQKEDKYEEEIKVLTDkLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEK 229
Cdd:PRK02224 469 tieedreRVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRER 538
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-229 1.80e-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: 39.28  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     3 ATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQ-LVEEELDRAQERLATALQKLEEAEK 81
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLER 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    82 AADESERGMKVIENRALKDEEKM------------EIQEIQLKEAKHIAE----------------EADRKYEEVARKLV 133
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIdkllaeieelerEIEEERKRRDKLTEEyaelkeeledlraeleEVDKEFAETRDELK 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   134 IVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLE 213
Cdd:TIGR02169  389 DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468

                          250
                   ....*....|....*.
gi 528522056   214 KTIDDLEDRlYQQLEK 229
Cdd:TIGR02169  469 QELYDLKEE-YDRVEK 483
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 30-238 1.82e-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: 39.28  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    30 LQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEaekaadESERGMKVIENRALKDEEKMEIQEI 109
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGELEA 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   110 QLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEaqaekysqkedkyeEEIK 189
Cdd:TIGR02169  302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK--------------EELE 367

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 528522056   190 VLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELR 238
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ 416
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
13-232 2.32e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  13 IKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 92
Cdd:COG4372   26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  93 IENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEA 172
Cdd:COG4372  106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056 173 QAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRL 232
Cdd:COG4372  186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
60-238 3.69e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   60 EELDRAQERLATALQKLE----------EAEKAADESERGMKVIE-NRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEV 128
Cdd:COG4913   235 DDLERAHEALEDAREQIEllepirelaeRYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAELARLEAELERL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  129 ARKLVIVEGELERTEE-RAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQK----EDKYEEEIKVLTDKLKEAETRAE 203
Cdd:COG4913   315 EARLDALREELDELEAqIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLE 394

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 528522056  204 FAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELR 238
Cdd:COG4913   395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 39-192 4.51e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.88  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  39 KARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkviENRALKDEEKMEIQEiQLKEAKHIA 118
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEE-----KKEKLQEEEDKLLEE-AEKEAQQAI 579

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528522056 119 EEADRKYEEVARKLvivegeleRTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYE--EEIKVLT 192
Cdd:PRK00409 580 KEAKKEADEIIKEL--------RQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKvgDEVKYLS 647
PTZ00121 PTZ00121
MAEBL; Provisional
 18-236 4.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   18 EQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRA 97
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   98 LKDEEKMEIQEIQLKEAKHI--AEEADRKYEEVARKlviveGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAE 175
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKK-----AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528522056  176 KYSQKEDKYEEEIKVltdKLKEAETRAEFAERSVAKLEKtiDDLEDRLYQQLEKNRLLSNE 236
Cdd:PTZ00121 1716 KKAEELKKAEEENKI---KAEEAKKEAEEDKKKAEEAKK--DEEEKKKIAHLKKEEEKKAE 1771
PRK12704 PRK12704
phosphodiesterase; Provisional
 112-229 4.88e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 4.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056 112 KEAKHIAEEADRKYEEVARKLVivegeLERTEERAELNEskcsELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVL 191
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKKEAL-----LEAKEEIHKLRN----EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 528522056 192 TDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEK 229
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
PTZ00121 PTZ00121
MAEBL; Provisional
 2-210 5.44e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    2 AATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEG--DVASLNRRIQLVEEELDRAQE--RLATALQKLE 77
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKKADEakKKAEEKKKAD 1434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   78 EAEKAADESERG---------MKVIENRALKDEEKMEIQEIQLK-EAKHIAEEADRKYEEVARKLVIVEGELERTEERAE 147
Cdd:PTZ00121 1435 EAKKKAEEAKKAdeakkkaeeAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528522056  148 LNESKCSELEEELKTVTNNLKSLEAQA--EKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVA 210
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-244 7.37e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.19  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   2 AATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 81
Cdd:COG4372   92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  82 AADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELK 161
Cdd:COG4372  172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056 162 TVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQLEKNRLLSNELRMAL 241
Cdd:COG4372  252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331


                 ...
gi 528522056 242 NED 244
Cdd:COG4372  332 LAI 334
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
28-226 7.78e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.19  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  28 EKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAekaadesergmkvienralkdEEKMEIQ 107
Cdd:COG4372    6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQA---------------------REELEQL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056 108 EIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEE 187
Cdd:COG4372   65 EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE 144

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 528522056 188 IKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDRLYQQ 226
Cdd:COG4372  145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 6-208 7.98e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 37.26  E-value: 7.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056     6 LEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 85
Cdd:pfam02463  302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    86 SERGmkvIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNESKCSELEEELKTVTN 165
Cdd:pfam02463  382 ESER---LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 528522056   166 NLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERS 208
Cdd:pfam02463  459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
PTZ00121 PTZ00121
MAEBL; Provisional
 3-222 8.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 8.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056    3 ATSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDvASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 82
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK-AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   83 ADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKlvivegelERTEERAELNESKCSELE--EEL 160
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA--------DEAKKKAEEDKKKADELKkaAAA 1416

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528522056  161 KTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDR 222
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
4-225 8.86e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 36.94  E-value: 8.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056   4 TSLEAVKRKIKLLQEQADGAEDKAEKLQKELAHERKARETAEGDVASLNRRIQLVEEELDRAqERLATALQKLEEAEKAA 83
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEI 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522056  84 D------------ESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNES 151
Cdd:PRK02224 609 ErlrekrealaelNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528522056 152 KCSELE---EELKTVTNNLKSLEAQAEKYSQKEDKYeeeikvltdklkeAETRAEFAERSVAKLEKTIDDLEDRLYQ 225
Cdd:PRK02224 689 ELEELEelrERREALENRVEALEALYDEAEELESMY-------------GDLRAELRQRNVETLERMLNETFDLVYQ 752
 
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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