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Conserved domains on  [gi|528522044|ref|XP_005174436|]
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tropomyosin alpha-1 chain isoform X4 [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 ...
 48-282 1.75e-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: 207.19  E-value: 1.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   48 KKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  128 KVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528522044  208 KASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKAISEELDHALNDMT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 48-282 1.75e-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: 207.19  E-value: 1.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   48 KKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  128 KVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528522044  208 KASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKAISEELDHALNDMT 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-264 1.48e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.43  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   1 MDAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  81 AEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADR 160
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 161 KYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                        250       260
                 ....*....|....*....|....
gi 528522044 241 FAERSVAKLEKTIDDLEDELYSQK 264
Cdd:COG1196  474 LLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-259 8.49e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 8.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    15 KENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQL 94
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    95 VEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKM-------EIQEIQLKEAKHIAEEADRKYEEVAR 167
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALallrselEELSEELRELESKRSELRRELEELRE 922

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   168 KLVIVEGELERTE-ERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVL-------TDKLKEAETRA 239
Cdd:TIGR02168  923 KLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERY 1002

                          250       260
                   ....*....|....*....|....*..
gi 528522044   240 EF-------AERSVAKLEKTIDDLEDE 259
Cdd:TIGR02168 1003 DFltaqkedLTEAKETLEEAIEEIDRE 1029
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-275 1.37e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  82 EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAadesergmkVIENRALKDEEKMEIQEIQLKEAKHI--AEEAD 159
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDR 474

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 160 RKYEEVARKLVIVEGELERTEERAELNERCnRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRA 239
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 528522044 240 EFAERSVAKLEKTIDDLEDELYSQKLKYKAISEELD 275
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 48-282 1.75e-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: 207.19  E-value: 1.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   48 KKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 127
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  128 KVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSL 207
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528522044  208 KASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKAISEELDHALNDMT 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 1.53e-25

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: 98.53  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    7 KMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEgdva 86
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528522044   87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAK 152
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-264 1.48e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.43  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   1 MDAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  81 AEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADR 160
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 161 KYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                        250       260
                 ....*....|....*....|....
gi 528522044 241 FAERSVAKLEKTIDDLEDELYSQK 264
Cdd:COG1196  474 LLEAALAELLEELAEAAARLLLLL 497
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 30-274 8.60e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 8.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  30 KAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATA 109
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 110 LQKLEEAEKAADEsergmkvIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERC 189
Cdd:COG1196  315 EERLEELEEELAE-------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 190 NRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKA 269
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467


                 ....*
gi 528522044 270 ISEEL 274
Cdd:COG1196  468 LLEEA 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-259 8.49e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.30  E-value: 8.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    15 KENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQL 94
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    95 VEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKM-------EIQEIQLKEAKHIAEEADRKYEEVAR 167
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALallrselEELSEELRELESKRSELRRELEELRE 922

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   168 KLVIVEGELERTE-ERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVL-------TDKLKEAETRA 239
Cdd:TIGR02168  923 KLAQLELRLEGLEvRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERY 1002

                          250       260
                   ....*....|....*....|....*..
gi 528522044   240 EF-------AERSVAKLEKTIDDLEDE 259
Cdd:TIGR02168 1003 DFltaqkedLTEAKETLEEAIEEIDRE 1029
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 18-247 2.91e-09

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: 57.08  E-value: 2.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  18 ALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEE 97
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  98 ELDRAQERLATALQKleeAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELE 177
Cdd:COG4942   98 ELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 178 RTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVA 247
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-270 1.39e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044     2 DAIKKKMQMLKLDKENALDRAEqaegdkkaaedrskQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIA--------------QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    82 EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRK 161
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   162 YEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKE-AETRAE 240
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeYSLTLE 954

                          250       260       270
                   ....*....|....*....|....*....|
gi 528522044   241 FAERSVAKLEKTIDDLEDELYSQKLKYKAI 270
Cdd:TIGR02168  955 EAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-278 3.37e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 3.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  48 KKLKGTEDELDKYSEALKD--AQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG1196  216 RELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 126 GMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYK 205
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528522044 206 SLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKAISEELDHAL 278
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-266 6.19e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 6.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    24 QAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQ 103
Cdd:TIGR02168  208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   104 ERLATALQKLEEaekaadesergmkvIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERA 183
Cdd:TIGR02168  288 KELYALANEISR--------------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   184 ELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQ 263
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433


                   ...
gi 528522044   264 KLK 266
Cdd:TIGR02168  434 ELK 436
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 30-277 7.02e-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: 53.53  E-value: 7.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    30 KAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATA 109
Cdd:TIGR02169  663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   110 LQKLEEAEKAADESERGMKviENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERC 189
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   190 NRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKA 269
Cdd:TIGR02169  821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900


                   ....*...
gi 528522044   270 ISEELDHA 277
Cdd:TIGR02169  901 LERKIEEL 908
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-277 3.34e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 3.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044     1 MDAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD 80
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    81 AEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADR 160
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   161 KYEEVARKLVIVEGELERTEERAELNERcnRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 528522044   241 FAERSVAKLEKTIDDLEDELYSQKLKYKAISEELDHA 277
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 15-277 8.96e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 8.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    15 KENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELA-EKKATDAEGDVASLNRRIQ 93
Cdd:TIGR02169  232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIA 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    94 LVEEELDRAQERLATALQKLEEAEKAADESER--GMKVIENRALKDEEKMEIQEIQLKEAKhiAEEADRKYEEVARKLVI 171
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELEReiEEERKRRDKLTEEYAELKEELEDLRAE--LEEVDKEFAETRDELKD 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   172 VEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEK 251
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469

                          250       260
                   ....*....|....*....|....*.
gi 528522044   252 TIDDLEDELYSQKLKYKAISEELDHA 277
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKLQRELAEA 495
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
2-275 1.37e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 49.27  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  82 EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAadesergmkVIENRALKDEEKMEIQEIQLKEAKHI--AEEAD 159
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDR 474

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 160 RKYEEVARKLVIVEGELERTEERAELNERCnRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRA 239
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 528522044 240 EFAERSVAKLEKTIDDLEDELYSQKLKYKAISEELD 275
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 43-260 1.39e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  43 LLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 122
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 123 SERGMK----VIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERCNRRLQDELR 198
Cdd:COG4942   95 LRAELEaqkeELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528522044 199 VLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDEL 260
Cdd:COG4942  175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1-236 4.74e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 4.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044     1 MDAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKL-----ELAE 75
Cdd:TIGR02169  704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhkleeALND 783

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    76 KKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEE--AEKAADESERGMKVIENRALKDEEKMEIQEIqlkeakh 153
Cdd:TIGR02169  784 LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI------- 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   154 iaEEADRKYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLK 233
Cdd:TIGR02169  857 --ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934


                   ...
gi 528522044   234 EAE 236
Cdd:TIGR02169  935 EIE 937
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-125 5.26e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQL---------EDDLLALQKKLKGTEDELDKYSEA---LKDAQE 69
Cdd:COG4913   613 AALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdEIDVASAEREIAELEAELERLDASsddLAALEE 692

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528522044   70 KLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 125
Cdd:COG4913   693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-275 1.23e-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: 46.59  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    47 QKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEG-----------DVASLNRRIQLVEEELDRAQERLATALQKLEE 115
Cdd:TIGR02168  178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEE 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   116 AEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERCNRRLQD 195
Cdd:TIGR02168  258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   196 ELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKAISEELD 275
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-223 1.82e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   32 AEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEK--KATDAEGDVASLNRRIQLVEEELDRAQE---RL 106
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAssdDL 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  107 ATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEAdrkyeevarklviveGELERTEERAELN 186
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---------------EDLARLELRALLE 752

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 528522044  187 ERCNRRLQDEL--RVLDQTYKSLKASEEQYSQKEDKYEE 223
Cdd:COG4913   753 ERFAAALGDAVerELRENLEERIDALRARLNRAEEELER 791
PTZ00121 PTZ00121
MAEBL; Provisional
 5-244 2.07e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    5 KKKMQMLKLDKENALDRAEQ---AEGDKKAAEDRSKQLEDDLLAlqKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADElkkAAAAKKKADEAKKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   82 EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGmkvieNRALKDEEKMEIQEIQLKEAKHIAEEAdRK 161
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA-----DEAKKAEEAKKADEAKKAEEAKKADEA-KK 1541

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  162 YEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEF 241
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621


                  ...
gi 528522044  242 AER 244
Cdd:PTZ00121 1622 AEE 1624
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
66-240 2.94e-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: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   66 DAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLAT--ALQKLEEAEKAADESERGMKVIEN---RALKDEEK 140
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIAELEAeleRLDASSDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  141 MEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRV-----LDQTYKSLKAsEEQYS 215
Cdd:COG4913   687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAALG-DAVER 765

                         170       180
                  ....*....|....*....|....*
gi 528522044  216 QKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:COG4913   766 ELRENLEERIDALRARLNRAEEELE 790
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 105-279 3.73e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 105 RLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAE 184
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 185 LNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQK 264
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170
                 ....*....|....*
gi 528522044 265 lkyKAISEELDHALN 279
Cdd:COG1196  393 ---RAAAELAAQLEE 404
PTZ00121 PTZ00121
MAEBL; Provisional
 6-269 5.69e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    6 KKMQMLKLDKENA--LDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKySEALKDAQEKLELAEKKATDAEG 83
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKKADEAK 1308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   84 DVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYE 163
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  164 EVaRKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAE 243
Cdd:PTZ00121 1389 EK-KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467

                         250       260
                  ....*....|....*....|....*.
gi 528522044  244 RSvAKLEKTIDDLEDELYSQKLKYKA 269
Cdd:PTZ00121 1468 EA-KKADEAKKKAEEAKKADEAKKKA 1492
mukB PRK04863
chromosome partition protein MukB;
23-257 8.12e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.18  E-value: 8.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   23 EQAEGDKKAAEDR-------SKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLV 95
Cdd:PRK04863  351 ERYQADLEELEERleeqnevVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLC 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   96 EE---ELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEI-----QEIQLKEAKHIAEEADRKYEE--- 164
Cdd:PRK04863  431 GLpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLvrkiaGEVSRSEAWDVARELLRRLREqrh 510

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  165 VARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYkslkASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAER 244
Cdd:PRK04863  511 LAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNL----DDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586

                         250
                  ....*....|...
gi 528522044  245 SVAKLEKTIDDLE 257
Cdd:PRK04863  587 QLEQLQARIQRLA 599
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 33-277 1.01e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.79  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   33 EDRSKQLEDDLLA-------LQKKLKGTEdELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQER 105
Cdd:COG3096   319 SARESDLEQDYQAasdhlnlVQTALRQQE-KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQ 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  106 LA-----------------TALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKH---IAEEADRKYEEV 165
Cdd:COG3096   398 LAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKA 477

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  166 ARKLVIVEGELERTE--ERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKyEEEIKVLTDKLKEAETRAEFAE 243
Cdd:COG3096   478 YELVCKIAGEVERSQawQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNA-ERLLEEFCQRIGQQLDAAEELE 556

                         250       260       270
                  ....*....|....*....|....*....|....
gi 528522044  244 RSVAKLEKTIDDLEDELYSQKLKYKAISEELDHA 277
Cdd:COG3096   557 ELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL 590
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 24-247 1.06e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  24 QAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRA- 102
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 103 -----QERLATALQKLEEAEKAADESERgMKVIENRALKDEEKMEiqeiQLKEAKHIAEEADRKYEEVARKLVIVEGELE 177
Cdd:COG3883   93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEALKAELE 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 178 RTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVA 247
Cdd:COG3883  168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 23-261 1.24e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.38  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  23 EQAEGDKKAAEDRSK--QLEDDLLALQKKLKGTEDELDKYS-----EALKDAQEKLELAEKKATDAEGDVASLNRRIQLV 95
Cdd:PRK05771  40 LSNERLRKLRSLLTKlsEALDKLRSYLPKLNPLREEKKKVSvksleELIKDVEEELEKIEKEIKELEEEISELENEIKEL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  96 EEELDRAQ---------------ERLATALQKLEEAEKAADESERGMKVIENRAlKDEEKMEIQEIQLKEAKHIAEEADR 160
Cdd:PRK05771 120 EQEIERLEpwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYIS-TDKGYVYVVVVVLKELSDEVEEELK 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 161 KYEevARKLVIVEG-----ELERTEERAELNERCNRRLQDELRVLDQTYKSLK-ASEEQYSQKEDKYEEeikvltdKLKE 234
Cdd:PRK05771 199 KLG--FERLELEEEgtpseLIREIKEELEEIEKERESLLEELKELAKKYLEELlALYEYLEIELERAEA-------LSKF 269

                        250       260       270
                 ....*....|....*....|....*....|...
gi 528522044 235 AETRAEFA------ERSVAKLEKTIDDLEDELY 261
Cdd:PRK05771 270 LKTDKTFAiegwvpEDRVKKLKELIDKATGGSA 302
PTZ00121 PTZ00121
MAEBL; Provisional
 2-250 1.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAE-KKATD 80
Cdd:PTZ00121 1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElRKAED 1198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   81 A-EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEAD 159
Cdd:PTZ00121 1199 ArKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR 1278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  160 RKYEEVARKLVIVEGELERTEERAELNERcnRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRA 239
Cdd:PTZ00121 1279 KADELKKAEEKKKADEAKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356

                         250
                  ....*....|.
gi 528522044  240 EFAERSVAKLE 250
Cdd:PTZ00121 1357 DEAEAAEEKAE 1367
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
15-229 1.92e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  15 KENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLK---------GTEDELDKYSEALKDAQEKLELAEKKATDAEGDV 85
Cdd:COG3206  163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  86 ASLNRRIQLVEEEL-----DRAQERLATALQKLE--EAEKAADESERGMKVIENRALKDEEKMEIQEiqlkEAKHIAEEA 158
Cdd:COG3206  243 AALRAQLGSGPDALpellqSPVIQQLRAQLAELEaeLAELSARYTPNHPDVIALRAQIAALRAQLQQ----EAQRILASL 318

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528522044 159 DRKYEEVARKLVIVEGELERTEERAEL---NERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLT 229
Cdd:COG3206  319 EAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
2-152 2.61e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 41.96  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLlalqkklkGTEDELDKYSEALKDAQEKLELAEKkatda 81
Cdd:COG1566   65 DRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAEL--------GAEAEIAAAEAQLAAAQAQLDLAQR----- 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528522044  82 egdvaSLNRRIQLVE------EELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEiQLKEAK 152
Cdd:COG1566  132 -----ELERYQALYKkgavsqQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAE 202
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
52-275 5.53e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  52 GTEDELDKYSEALKDAQEklELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErgmkviE 131
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------E 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 132 NRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAE--LNERCNRRLQDELRVLDQTYKSLKA 209
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEagLDDADAEAVEARREELEDRDEELRD 328

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528522044 210 SEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKAISEELD 275
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
7-269 6.31e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 6.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   7 KMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVA 86
Cdd:COG4372   39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEkmEIQEIQLKEAKHIAEEADRKYEEVA 166
Cdd:COG4372  119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ--ELQALSEAEAEQALDELLKEANRNA 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 167 RKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSV 246
Cdd:COG4372  197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276

                        250       260
                 ....*....|....*....|...
gi 528522044 247 AKLEKTIDDLEDELYSQKLKYKA 269
Cdd:COG4372  277 ELEIAALELEALEEAALELKLLA 299
PTZ00121 PTZ00121
MAEBL; Provisional
 14-226 8.14e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   14 DKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQ 93
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   94 LVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVE 173
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 528522044  174 GELERTEERAELnERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIK 226
Cdd:PTZ00121 1735 AKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
52-235 1.09e-03

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 40.06  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  52 GTEDELDKYSEALKDAQEklelAEKKATDAEGDVASLNRRIQLVE---EELDRA------QERLATALQKLEEAEK---- 118
Cdd:COG0497  152 GLEELLEEYREAYRAWRA----LKKELEELRADEAERARELDLLRfqlEELEAAalqpgeEEELEEERRRLSNAEKlrea 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 119 ------AADESERG--------MKVIENRALKDEEKMEIQEiQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEER-- 182
Cdd:COG0497  228 lqealeALSGGEGGaldllgqaLRALERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFDPERLEEVEERla 306

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528522044 183 -------------AELNERCNRrLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEA 235
Cdd:COG0497  307 llrrlarkygvtvEELLAYAEE-LRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
mukB PRK04863
chromosome partition protein MukB;
57-275 1.41e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.94  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   57 LDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLA-----------------TALQKLEEAEKA 119
Cdd:PRK04863  350 IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQL 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  120 ADESERGMKVIENR--ALKDEEKMEIQEI-QLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERCnRRLQdE 196
Cdd:PRK04863  430 CGLPDLTADNAEDWleEFQAKEQEATEELlSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELL-RRLR-E 507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  197 LRVLDQTYKSLKA--SE-EQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKAISEE 273
Cdd:PRK04863  508 QRHLAEQLQQLRMrlSElEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587


                  ..
gi 528522044  274 LD 275
Cdd:PRK04863  588 LE 589
PRK12704 PRK12704
phosphodiesterase; Provisional
 109-240 1.97e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 109 ALQKLEEAEKAADEsergmkvienraLKDEEKMEIQEIQlKEAKHIA-EEADRKYEEVARKLVIVEGELERTEERAELNE 187
Cdd:PRK12704  29 AEAKIKEAEEEAKR------------ILEEAKKEAEAIK-KEALLEAkEEIHKLRNEFEKELRERRNELQKLEKRLLQKE 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 528522044 188 rcnRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAE 240
Cdd:PRK12704  96 ---ENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE 145
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 23-218 2.20e-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: 39.67  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    23 EQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRA 102
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   103 QERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEER 182
Cdd:TIGR02169  384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD 463

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 528522044   183 AELNERCNRRLQDELRVLDqtyKSLKASEEQYSQKE 218
Cdd:TIGR02169  464 LSKYEQELYDLKEEYDRVE---KELSKLQRELAEAE 496
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
13-242 2.32e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   13 LDKENALDRAEQA-------EGDKKAAEDRSKQLE--DDLLALQKKLKGTEDELDKYSE-----ALKDAQEKLELAEKKA 78
Cdd:COG4913   218 LEEPDTFEAADALvehfddlERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   79 TDAEGDVASLNRRIQLVEEELDRAQERLATA--------LQKLEEAEKAADESERGMKVIENRALKDEEKmeIQEIQLkE 150
Cdd:COG4913   298 EELRAELARLEAELERLEARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEAL--LAALGL-P 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  151 AKHIAEEADRKYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKvltD 230
Cdd:COG4913   375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA---E 451

                         250
                  ....*....|..
gi 528522044  231 KLKEAETRAEFA 242
Cdd:COG4913   452 ALGLDEAELPFV 463
PTZ00121 PTZ00121
MAEBL; Provisional
 2-277 2.42e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGteDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA--DAAKKKAEEAKKAAEAAKAEAEAAADE 1358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   82 EGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLK--------EAKH 153
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaeekkkadEAKK 1438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  154 IAEEAdRKYEEVARKL---VIVEGELERTEERAELNERcnRRLQDELRVLDQTYKslKASEEQYSQKEDKYEEEIKVLTD 230
Cdd:PTZ00121 1439 KAEEA-KKADEAKKKAeeaKKAEEAKKKAEEAKKADEA--KKKAEEAKKADEAKK--KAEEAKKKADEAKKAAEAKKKAD 1513

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 528522044  231 KLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYKAISEELDHA 277
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKA 1560
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-176 2.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   12 KLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEA---------------LKDAQEKLELAEK 76
Cdd:COG4913   280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleqlereIERLERELEERER 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   77 KATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEiQEIQLKEAKH--I 154
Cdd:COG4913   360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnI 438

                         170       180
                  ....*....|....*....|..
gi 528522044  155 AEEADRKYEEVARKLVIVEGEL 176
Cdd:COG4913   439 PARLLALRDALAEALGLDEAEL 460
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1-133 3.31e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    1 MDAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLE--------DDLLALQKKLKGTEDELDKYSEALKDAQEKLE 72
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLA 369

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528522044   73 LAEKKATDAEGDVASLNRRIQL----VEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR 133
Cdd:COG4913   370 ALGLPLPASAEEFAALRAEAAAlleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
54-259 3.33e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  54 EDELDKYSEALKDAQEKLELAEKKATDAEgDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR 133
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 134 ALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELN---ERCNRRLQDELRVLDQTYKSLKAS 210
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEdeiERLREKREALAELNDERRERLAEK 632

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 528522044 211 EEQYSQKEDKYEEeikvltDKLKEAETRAEFAERSVAKLEKTIDDLEDE 259
Cdd:PRK02224 633 RERKRELEAEFDE------ARIEEAREDKERAEEYLEQVEEKLDELREE 675
PTZ00121 PTZ00121
MAEBL; Provisional
 2-258 3.42e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDA 81
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   82 EGDVASLNRRIQLVEEELDRAQE-RLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADR 160
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEkKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  161 KYEEVARKLVIVEGELERTEERAELNERCNRRLQDELRVLDQTYKSLKASEE------QYSQKEDKYEEEIKVLTDKLKE 234
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEekkkiaHLKKEEEKKAEEIRKEKEAVIE 1782

                         250       260
                  ....*....|....*....|....
gi 528522044  235 AETRAEfAERSVAKLEKTIDDLED 258
Cdd:PTZ00121 1783 EELDEE-DEKRRMEVDKKIKDIFD 1805
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 3-156 3.58e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 38.87  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044    3 AIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRSKQLEDDLLALQKKlkgTEDELDKYSEALKDAQEKLELAekkaTDAE 82
Cdd:pfam10168 558 EIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEEIKDK---QEKLMRRCKKVLQRLNSQLPVL----SDAE 630

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528522044   83 GDVASLNRRIQLVEEELDRaqeRLATALQKLEEAEK--AADESERGMKVIEnraLKDEEKMEIQEIQLKEAKHIAE 156
Cdd:pfam10168 631 REMKKELETINEQLKHLAN---AIKQAKKKMNYQRYqiAKSQSIRKKSSLS---LSEKQRKTIKEILKQLGSEIDE 700
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
87-260 5.28e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.07  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  87 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE--SERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEE 164
Cdd:COG3206  165 NLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 165 VARKLVIVEGELERTEERAELNERCNR--RLQDELRVLDQTYK----SLKASEEQYSQKEDKYEEEIKVLtdkLKEAETR 238
Cdd:COG3206  245 LRAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQRI---LASLEAE 321

                        170       180
                 ....*....|....*....|..
gi 528522044 239 AEFAERSVAKLEKTIDDLEDEL 260
Cdd:COG3206  322 LEALQAREASLQAQLAQLEARL 343
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
2-129 7.79e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 37.53  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   2 DAIKKKMQMLKLDKENALDRAEQAEGDKKAAEDRS-KQLE---DDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKK 77
Cdd:COG2433  380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEeqvERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528522044  78 ATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 129
Cdd:COG2433  460 EIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELV 511
PTZ00121 PTZ00121
MAEBL; Provisional
 20-251 8.22e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 8.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044   20 DRAEQAEGDKKAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEEL 99
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  100 DRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARklvIVEGELERT 179
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK---IKAAEEAKK 1669

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528522044  180 EERAELNERCNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEK 251
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 91-278 9.09e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.61  E-value: 9.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  91 RIQLVEEELDRAQERLAtalqklEEAEKA--ADESERGMKVIENRALKDeeKMEIQEIQLKEAKHIAEEADRKYEEVARK 168
Cdd:COG1196  190 RLEDILGELERQLEPLE------RQAEKAerYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAE 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 169 LVIVEGELERTE-ERAELNERCNRRLQDELRV------LDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEF 241
Cdd:COG1196  262 LAELEAELEELRlELEELELELEEAQAEEYELlaelarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 528522044 242 AERSVAKLEKTIDDLEDELYSQKLKYKAISEELDHAL 278
Cdd:COG1196  342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
30-274 9.29e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 37.19  E-value: 9.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044  30 KAAEDRSKQLEDDLLALQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATA 109
Cdd:COG4372   34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 110 LQKLEEAEKAADESERGMKVIENRALKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKL-VIVEGELERTEERAELNER 188
Cdd:COG4372  114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELqALSEAEAEQALDELLKEAN 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528522044 189 CNRRLQDELRVLDQTYKSLKASEEQYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYSQKLKYK 268
Cdd:COG4372  194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273


                 ....*.
gi 528522044 269 AISEEL 274
Cdd:COG4372  274 EEEELE 279
 
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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