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Conserved domains on  [gi|1622825854|ref|XP_028701337|]
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tropomyosin alpha-3 chain isoform X3 [Macaca mulatta]

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 ...
 49-283 8.81e-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: 8.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  49 KKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 128
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 129 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSL 208
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825854 209 EAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQTLLDLN 283
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 ...
 49-283 8.81e-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: 8.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  49 KKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 128
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 129 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSL 208
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825854 209 EAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQTLLDLN 283
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-262 9.74e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 9.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   2 MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD 81
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  82 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADR 161
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 162 KYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                         250       260
                  ....*....|....*....|.
gi 1622825854 242 FAERSVAKLEKTIDDLEDKLK 262
Cdd:COG1196   474 LLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-285 3.78e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.32  E-value: 3.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   27 EAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQER 106
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  107 LATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAEL 186
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  187 AESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKE 266
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                          250
                   ....*....|....*....
gi 1622825854  267 EHLCTQRMLDQTLLDLNEM 285
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGL 934
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
3-261 7.26e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:PRK02224  324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV--------------IENRALKDEEKMELQEIQ 148
Cdd:PRK02224  404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAE 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 149 LKEAKHIAEEADRKYEEvARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKi 228
Cdd:PRK02224  484 LEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA- 561

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1622825854 229 ltdklkEAETRAEFAERSVAKLEKTIDDLEDKL 261
Cdd:PRK02224  562 ------EAEEEAEEAREEVAELNSKLAELKERI 588
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 17-221 3.03e-05

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


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 45.60  E-value: 3.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   17 ENALDRAEQAEAE-QKQAEERSKQLeDELAAMQKKLKGTEDE-LDKYSEALKDA-QEKLELAEKKAADAEAEVASLNRRI 93
Cdd:NF012221  1558 QNALADKERAEADrQRLEQEKQQQL-AAISGSQSQLESTDQNaLETNGQAQRDAiLEESRAVTKELTTLAQGLDALDSQA 1636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   94 QLVEEELDRAQERLATAL-----QKLEEAEKAADES-ERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVA 167
Cdd:NF012221  1637 TYAGESGDQWRNPFAGGLldrvqEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAK 1716

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  168 RKLVIIEGDLERTEERAELAESKCSELEEELKN------VTNNLKSLEAQAEKYSQKEDK 221
Cdd:NF012221  1717 ADAEKRKDDALAKQNEAQQAESDANAAANDAQSrgeqdaSAAENKANQAQADAKGAKQDE 1776
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 49-283 8.81e-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: 8.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  49 KKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 128
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 129 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSL 208
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825854 209 EAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQTLLDLN 283
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 8-153 1.12e-23

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: 93.52  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   8 KMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEaeva 87
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE---- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622825854  88 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAK 153
Cdd:pfam12718  77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-262 9.74e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 9.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   2 MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD 81
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  82 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADR 161
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 162 KYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:COG1196   394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473

                         250       260
                  ....*....|....*....|.
gi 1622825854 242 FAERSVAKLEKTIDDLEDKLK 262
Cdd:COG1196   474 LLEAALAELLEELAEAAARLL 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-285 3.78e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 69.32  E-value: 3.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   27 EAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQER 106
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  107 LATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAEL 186
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  187 AESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKE 266
Cdd:TIGR02168  836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915

                          250
                   ....*....|....*....
gi 1622825854  267 EHLCTQRMLDQTLLDLNEM 285
Cdd:TIGR02168  916 ELEELREKLAQLELRLEGL 934
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 25-262 2.39e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  25 QAEAEQKQAEERS---KQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELD 101
Cdd:COG1196   219 KEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 102 RAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTE 181
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 182 ERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKL 261
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458


                  .
gi 1622825854 262 K 262
Cdd:COG1196   459 E 459
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-227 2.08e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:COG1196   277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRK 162
Cdd:COG1196   357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825854 163 YEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIK 227
Cdd:COG1196   437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 19-248 3.11e-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: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  19 ALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEE 98
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  99 ELDRAQERLATALQKleeAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLE 178
Cdd:COG4942    98 ELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 179 RTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVA 248
Cdd:COG4942   175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-262 1.92e-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: 55.06  E-value: 1.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   25 QAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQ 104
Cdd:TIGR02168  208 QAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  105 ERLATALQKLEEaekaadesergmkvIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERA 184
Cdd:TIGR02168  288 KELYALANEISR--------------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825854  185 ELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLK 262
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-262 2.83e-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: 54.68  E-value: 2.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    1 MMEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAA 80
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   81 DAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMEL-------QEIQLKEAK 153
Cdd:TIGR02168  793 QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieeLEELIEELE 872

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  154 HIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKIL-TDK 232
Cdd:TIGR02168  873 SELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLT 952

                          250       260       270
                   ....*....|....*....|....*....|
gi 1622825854  233 LKEAETRAEFAERSVAKLEKTIDDLEDKLK 262
Cdd:TIGR02168  953 LEEAEALENKIEDDEEEARRRLKRLENKIK 982
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-261 4.02e-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: 54.29  E-value: 4.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   24 EQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRA 103
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  104 QERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEER 183
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  184 AELA---------------------ESKCSELEEELKNVTN-------NLKSLEAQAEKYSQKEDKYEEEIKILTDKLKE 235
Cdd:TIGR02168  840 LEDLeeqieelsedieslaaeieelEELIEELESELEALLNerasleeALALLRSELEELSEELRELESKRSELRRELEE 919

                          250       260
                   ....*....|....*....|....*.
gi 1622825854  236 AETRAEFAERSVAKLEKTIDDLEDKL 261
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-259 8.90e-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: 8.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    2 MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD 81
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   82 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADR 161
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  162 KYEEVARKLVIIEGDLERTEER--------AELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKL 233
Cdd:TIGR02168  923 KLAQLELRLEGLEVRIDNLQERlseeysltLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERY 1002

                          250       260
                   ....*....|....*....|....*.
gi 1622825854  234 KEAETRAEFAERSVAKLEKTIDDLED 259
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAIEEIDR 1028
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-258 1.50e-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: 52.38  E-value: 1.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    2 MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALkdAQEKLELAEKKAAD 81
Cdd:TIGR02169  711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL--HKLEEALNDLEARL 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   82 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEE--AEKAADESERGMKVIENRALKDEEKMELQEIQLkeakhiaeea 159
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN---------- 858

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  160 drkyeevarklviIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETR 239
Cdd:TIGR02169  859 -------------LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925

                          250
                   ....*....|....*....
gi 1622825854  240 AEFAERSVAKLEKTIDDLE 258
Cdd:TIGR02169  926 LEALEEELSEIEDPKGEDE 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 27-247 1.84e-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: 52.38  E-value: 1.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   27 EAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQER 106
Cdd:TIGR02169  286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  107 LATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAEL 186
Cdd:TIGR02169  366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622825854  187 AESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSV 247
Cdd:TIGR02169  446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-259 3.17e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 3.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    2 MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD 81
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   82 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADR 161
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  162 KYEEVARKLVIIEGDLERTEERAELAESKCSELeeELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478

                          250
                   ....*....|....*...
gi 1622825854  242 FAERSVAKLEKTIDDLED 259
Cdd:TIGR02168  479 AAERELAQLQARLDSLER 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 22-267 7.77e-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: 50.45  E-value: 7.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   22 RAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELaekkaadaeaevasLNRRIQLVEEELD 101
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE--------------IEKEIEQLEQEEE 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  102 RAQERLATALQKLEEAEKAADESERGMKVIENR-----ALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGD 176
Cdd:TIGR02169  734 KLKERLEELEEDLSSLEQEIENVKSELKELEARieeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEAR 813

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  177 LERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDD 256
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          250
                   ....*....|.
gi 1622825854  257 LEDKLKCTKEE 267
Cdd:TIGR02169  894 LEAQLRELERK 904
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
23-262 8.69e-07

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 8.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  23 AEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEalkdaQEKLELAEKKAADAEAEVASLNRRIQLVEEELDR 102
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 103 AQERLATALQKLEEAEKAADEsergmkVIENRALKDEEKmELQEIQLKEAkhiaeEADRKYEEVARKLVIIEgdlertEE 182
Cdd:COG3206   238 AEARLAALRAQLGSGPDALPE------LLQSPVIQQLRA-QLAELEAELA-----ELSARYTPNHPDVIALR------AQ 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 183 RAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKiltdKLKEAETRAEFAERSVAKLEKTIDDLEDKLK 262
Cdd:COG3206   300 IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLE 375
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 10-277 1.17e-06

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 49.57  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   10 QMLKLDKENALDRAEQAEAEQKQAE---------ERSKQLE-------DELAAMQKKLKGTEdELDKYSEALKDAQEKLE 73
Cdd:COG3096    286 RALELRRELFGARRQLAEEQYRLVEmareleelsARESDLEqdyqaasDHLNLVQTALRQQE-KIERYQEDLEELTERLE 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   74 LAEKKAADAEAEVASLNRRIQLVEEELDRAQERLA-----------------TALQKLEEAEKAADESERGMKVIENRAL 136
Cdd:COG3096    365 EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLA 444

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  137 KDEEKMELQEIQLKEAKH---IAEEADRKYEEVARKLVIIEGDLERTEeraelAESKCSELEE---ELKNVTNNLKSLEA 210
Cdd:COG3096    445 AFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERSQ-----AWQTARELLRryrSQQALAQRLQQLRA 519

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  211 Q---AEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQ 277
Cdd:COG3096    520 QlaeLEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-216 1.71e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADEsergmkvieNRALKDEEKMELQEIQLKEAKHIAEEADRK 162
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER---------LQQEIEELLKKLEEAELKELQAELEELEEE 448

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622825854  163 YEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYS 216
Cdd:TIGR02168  449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
3-261 7.26e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:PRK02224  324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV--------------IENRALKDEEKMELQEIQ 148
Cdd:PRK02224  404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAE 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 149 LKEAKHIAEEADRKYEEvARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKi 228
Cdd:PRK02224  484 LEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA- 561

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1622825854 229 ltdklkEAETRAEFAERSVAKLEKTIDDLEDKL 261
Cdd:PRK02224  562 ------EAEEEAEEAREEVAELNSKLAELKERI 588
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
12-153 2.94e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 44.65  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  12 LKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAmQKKLKGTEDELDKYSEALKDAQEKLElaekkaadaeaevaslnR 91
Cdd:COG1566    74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELE-----------------R 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825854  92 RIQLVE------EELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEiQLKEAK 153
Cdd:COG1566   136 YQALYKkgavsqQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAE 202
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 17-221 3.03e-05

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


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 45.60  E-value: 3.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   17 ENALDRAEQAEAE-QKQAEERSKQLeDELAAMQKKLKGTEDE-LDKYSEALKDA-QEKLELAEKKAADAEAEVASLNRRI 93
Cdd:NF012221  1558 QNALADKERAEADrQRLEQEKQQQL-AAISGSQSQLESTDQNaLETNGQAQRDAiLEESRAVTKELTTLAQGLDALDSQA 1636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   94 QLVEEELDRAQERLATAL-----QKLEEAEKAADES-ERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVA 167
Cdd:NF012221  1637 TYAGESGDQWRNPFAGGLldrvqEQLDDAKKISGKQlADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAK 1716

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  168 RKLVIIEGDLERTEERAELAESKCSELEEELKN------VTNNLKSLEAQAEKYSQKEDK 221
Cdd:NF012221  1717 ADAEKRKDDALAKQNEAQQAESDANAAANDAQSrgeqdaSAAENKANQAQADAKGAKQDE 1776
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 44-262 6.85e-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: 43.60  E-value: 6.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  44 LAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 123
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 124 SERGMKvienrALKDEEKMELQEIQLKEAKHIAEE--ADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNV 201
Cdd:COG4942    95 LRAELE-----AQKEELAELLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622825854 202 TNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLK 262
Cdd:COG4942   170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 25-225 8.54e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 8.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  25 QAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRA- 103
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERa 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 104 -----QERLATALQKLEEAEKAADESERgMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLE 178
Cdd:COG3883    93 ralyrSGGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1622825854 179 RTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEE 225
Cdd:COG3883   172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
PTZ00121 PTZ00121
MAEBL; Provisional
 3-260 9.01e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 9.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQE--KLELAEKKAA 80
Cdd:PTZ00121  1119 EAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAED 1198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   81 DAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEAd 160
Cdd:PTZ00121  1199 ARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA- 1277

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  161 RKYEEVARKLVIIEGDLERTEERAELAES---------KCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTD 231
Cdd:PTZ00121  1278 RKADELKKAEEKKKADEAKKAEEKKKADEakkkaeeakKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357

                          250       260
                   ....*....|....*....|....*....
gi 1622825854  232 KLKEAETRAEFAERSVAKLEKTIDDLEDK 260
Cdd:PTZ00121  1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
15-267 1.28e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  15 DKENALD--RAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAdaeaevaslnrR 92
Cdd:PRK02224  184 DQRGSLDqlKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----------E 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  93 IQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVI 172
Cdd:PRK02224  253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 173 IEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEK 252
Cdd:PRK02224  333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAED 412

                         250
                  ....*....|....*
gi 1622825854 253 TIDDLEDKLKCTKEE 267
Cdd:PRK02224  413 FLEELREERDELRER 427
PTZ00121 PTZ00121
MAEBL; Provisional
 15-225 1.31e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   15 DKENALDRAEQA-EAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKySEALKDAQEKLELAEKKAADAEAEVASLNRRI 93
Cdd:PTZ00121  1575 DKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   94 QLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVII 173
Cdd:PTZ00121  1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622825854  174 EGDLERTEERAELAESKCSelEEELKNVTNNLKSLEAQAEKYSQKEDKYEEE 225
Cdd:PTZ00121  1734 EAKKEAEEDKKKAEEAKKD--EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
3-130 1.38e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.92  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   3 EAIKKKMQMLKLDKENALDRAEQ-AEAEQKQAEERSKQLEDELAAMQ---KKLKGTEDELDKYSEALKDAQEKLELAEKK 78
Cdd:COG2433   380 EALEELIEKELPEEEPEAEREKEhEERELTEEEEEIRRLEEQVERLEaevEELEAELEEKDERIERLERELSEARSEERR 459

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622825854  79 AADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 130
Cdd:COG2433   460 EIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELV 511
PTZ00121 PTZ00121
MAEBL; Provisional
 3-260 2.34e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:PTZ00121  1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRK 162
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  163 YEEVARKlviiegdlERTEERAELAESKCSELE--EELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRA 240
Cdd:PTZ00121  1387 AEEKKKA--------DEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458

                          250       260
                   ....*....|....*....|
gi 1622825854  241 EFAERSVAKLEKTIDDLEDK 260
Cdd:PTZ00121  1459 AEEAKKKAEEAKKADEAKKK 1478
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
3-126 4.04e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 4.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERS----------------KQLEDELAAMQKKLkgteDELDKYSEALK 66
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREIAELEAEL----ERLDASSDDLA 688

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   67 DAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 126
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
67-261 4.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   67 DAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLAtALQKLEEaekaADESERGMKVIENRALkdeekmelqe 146
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAE----YSWDEIDVASAEREIA---------- 671

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  147 iQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEi 226
Cdd:COG4913    672 -ELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA- 749

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622825854  227 kiLTDKLKEAETRAEFAERSVAKLEKTIDDLEDKL 261
Cdd:COG4913    750 --LLEERFAAALGDAVERELRENLEERIDALRARL 782
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2-241 5.81e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   2 MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD 81
Cdd:COG4372    47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  82 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADR 161
Cdd:COG4372   127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 162 KYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:COG4372   207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 19-234 6.95e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.19  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   19 ALDRAEQAEAEQKQAEERSKQLE---DELAAMQKKLKgteDELDKYSEALKDAQEKLelaekkaadaeaEVASLNRRI-- 93
Cdd:PRK10929    49 ALQSALNWLEERKGSLERAKQYQqviDNFPKLSAELR---QQLNNERDEPRSVPPNM------------STDALEQEIlq 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   94 ---QLVEE------ELDRAQE---RLATALQKLEEAEKAADESERGMKVIENRALKDEEkmelqeiqlkeakhiAEEADR 161
Cdd:PRK10929   114 vssQLLEKsrqaqqEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTAL 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  162 KYEEVARKLVIIEGDLE------RTE---ERAELAESKCSELEEELKNVTNNLKSLEAQ-AEKYSQKEDKYEEEI----K 227
Cdd:PRK10929   179 QAESAALKALVDELELAqlsannRQElarLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgdlpK 258


                   ....*..
gi 1622825854  228 ILTDKLK 234
Cdd:PRK10929   259 SIVAQFK 265
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-243 7.63e-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: 7.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   21 DRAEQAEAEQKQAEERSKQLED--ELAAMQKKLKGTEDELDKYSEALKD--AQEKLELAEKKAADAEAEVASLNRRIQLV 96
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEPirELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   97 EEELDRAQERLATA--------LQKLEEAEKAADESERGMKVIENRALKDEEKmeLQEIQLkEAKHIAEEADRKYEEVAR 168
Cdd:COG4913    315 EARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEAL--LAALGL-PLPASAEEFAALRAEAAA 391

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825854  169 KLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKiltDKLKEAETRAEFA 243
Cdd:COG4913    392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA---EALGLDEAELPFV 463
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-117 7.70e-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: 7.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   21 DRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEEL 100
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771

                           90
                   ....*....|....*..
gi 1622825854  101 DRAQERLATALQKLEEA 117
Cdd:COG4913    772 EERIDALRARLNRAEEE 788
PTZ00121 PTZ00121
MAEBL; Provisional
 21-252 8.57e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 8.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   21 DRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTE---DELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVE 97
Cdd:PTZ00121  1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   98 -------EELDRAQERLATALQKLEEAEKAadesERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKL 170
Cdd:PTZ00121  1560 aeekkkaEEAKKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  171 VIIEGDLERTEERAEL---AESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSV 247
Cdd:PTZ00121  1636 EQLKKKEAEEKKKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK 1715


                   ....*
gi 1622825854  248 AKLEK 252
Cdd:PTZ00121  1716 KKAEE 1720
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-249 1.28e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   2 MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLelaekkaad 81
Cdd:COG4942    36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL--------- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  82 aeaevaslnrriqlvEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADR 161
Cdd:COG4942   107 ---------------AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 162 KYEEVARKLViiegdlERTEERAELAESKcSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:COG4942   172 ERAELEALLA------ELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244


                  ....*...
gi 1622825854 242 FAERSVAK 249
Cdd:COG4942   245 AAGFAALK 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 60-267 1.31e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   60 KYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQE------------------RLATALQKLEEAEKAA 121
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelelallvlRLEELREELEELQEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  122 DESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNV 201
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622825854  202 TNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEE 267
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
16-230 1.42e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  16 KENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLK---------GTEDELDKYSEALKDAQEKLELAEKKAADAEAEV 86
Cdd:COG3206   163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  87 ASLNRRIQLVEEEL-----DRAQERLATALQKLE--EAEKAADESERGMKVIENRALKDEEKMELQEiqlkEAKHIAEEA 159
Cdd:COG3206   243 AALRAQLGSGPDALpellqSPVIQQLRAQLAELEaeLAELSARYTPNHPDVIALRAQIAALRAQLQQ----EAQRILASL 318

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825854 160 DRKYEEVARKLVIIEGDLERTEERAEL---AESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILT 230
Cdd:COG3206   319 EAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVID 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
13-177 1.52e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   13 KLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEA---------------LKDAQEKLELAEK 77
Cdd:COG4913    280 ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrleqlereIERLERELEERER 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   78 KAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMElQEIQLKEAKH--I 155
Cdd:COG4913    360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnI 438

                          170       180
                   ....*....|....*....|..
gi 1622825854  156 AEEADRKYEEVARKLVIIEGDL 177
Cdd:COG4913    439 PARLLALRDALAEALGLDEAEL 460
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 24-284 1.57e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   24 EQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKyseALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRA 103
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREK---AERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  104 QERLAtalQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEakhiaeeadrKYEEVARKLVIIEGDLERTEER 183
Cdd:TIGR02169  250 EEELE---KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE----------KIGELEAEIASLERSIAEKERE 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  184 AELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKC 263
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396

                          250       260
                   ....*....|....*....|.
gi 1622825854  264 TKEEHLCTQRMLDQTLLDLNE 284
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQR 417
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 3-190 1.68e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  83 EAEVASLN------------RRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLK 150
Cdd:COG3883    99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622825854 151 EAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESK 190
Cdd:COG3883   179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
PTZ00121 PTZ00121
MAEBL; Provisional
 3-248 2.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKlkgTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:PTZ00121  1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK---KEEAKKKADAAKKKAEEKKKADEAKKKAE 1401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG---------MKVIENRALKDEEKMELQEIQLK--- 150
Cdd:PTZ00121  1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAdeakkkaeeAKKAEEAKKKAEEAKKADEAKKKaee 1481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  151 -----EAKHIAEEADRKYEEVARKlviiegdLERTEERAELAESKCSELEEELKNVTNNLKSLEAQA--EKYSQKEDKYE 223
Cdd:PTZ00121  1482 akkadEAKKKAEEAKKKADEAKKA-------AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKA 1554

                          250       260
                   ....*....|....*....|....*
gi 1622825854  224 EEIKILTDKLKEAETRAEFAERSVA 248
Cdd:PTZ00121  1555 EELKKAEEKKKAEEAKKAEEDKNMA 1579
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 141-267 2.42e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 141 KMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKED 220
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622825854 221 KYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEE 267
Cdd:COG1196   299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-134 2.56e-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: 2.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    2 MEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEE---------------RSKQLEDELAAMQKKLKGTEDELDKYSEALK 66
Cdd:COG4913    290 LELLEAELEELRAELARLEAELERLEARLDALREeldeleaqirgnggdRLEQLEREIERLERELEERERRRARLEALLA 369

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825854   67 DAQEKLELAEKKAADAEAEVAslnRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENR 134
Cdd:COG4913    370 ALGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
8-232 2.78e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   8 KMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVA 87
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  88 SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIEN---RALKDEEKMELQEIQLKEAKHIAEEADRKYE 164
Cdd:COG4372   119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaALEQELQALSEAEAEQALDELLKEANRNAEK 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825854 165 EVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDK 232
Cdd:COG4372   199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
19-261 2.88e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  19 ALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLE--------------LAEKKAADAEA 84
Cdd:PRK02224  235 TRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEeleeerddllaeagLDDADAEAVEA 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  85 EVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYE 164
Cdd:PRK02224  315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 165 EVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQ-------KEDKYEEEIKILTDKLKEAE 237
Cdd:PRK02224  395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcPECGQPVEGSPHVETIEEDR 474

                         250       260
                  ....*....|....*....|....
gi 1622825854 238 TRAEFAERSVAKLEKTIDDLEDKL 261
Cdd:PRK02224  475 ERVEELEAELEDLEEEVEEVEERL 498
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 14-259 2.93e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.14  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  14 LDKENALDRAEQAEAEQKQAEERSKQLEDeLAAMQKKLKGTEDELDKYS--EALKDAQEKLELAEKKAADAEAEVASLNR 91
Cdd:PRK05771   36 LKEELSNERLRKLRSLLTKLSEALDKLRS-YLPKLNPLREEKKKVSVKSleELIKDVEEELEKIEKEIKELEEEISELEN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  92 RIQLVEEELDRAQerlatALQKLEEAEKAADESERgMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKY-------- 163
Cdd:PRK05771  115 EIKELEQEIERLE-----PWGNFDLDLSLLLGFKY-VSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvlke 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854 164 -----EEVARKLVIIEGDLERTEERAELAeskcSELEEELKNVTNNLKSLEAQAEKYSQKEDK----YEEEIKILTDK-- 232
Cdd:PRK05771  189 lsdevEEELKKLGFERLELEEEGTPSELI----REIKEELEEIEKERESLLEELKELAKKYLEellaLYEYLEIELERae 264

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1622825854 233 --LKEAETRAEFA------ERSVAKLEKTIDDLED 259
Cdd:PRK05771  265 alSKFLKTDKTFAiegwvpEDRVKKLKELIDKATG 299
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
98-268 3.05e-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: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   98 EELDRAQERLATALQKLE----------EAEKAADESERGMKVIE-NRALKDEEKMELQEIQLKEAKHIAEEADRKYEEV 166
Cdd:COG4913    235 DDLERAHEALEDAREQIEllepirelaeRYAAARERLAELEYLRAaLRLWFAQRRLELLEAELEELRAELARLEAELERL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  167 ARKLVIIEGDLERTEE--------RAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDkyeEEIKILTDKLKEAET 238
Cdd:COG4913    315 EARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLP---ASAEEFAALRAEAAA 391

                          170       180       190
                   ....*....|....*....|....*....|
gi 1622825854  239 RAEFAERSVAKLEKTIDDLEDKLKCTKEEH 268
Cdd:COG4913    392 LLEALEEELEALEEALAEAEAALRDLRREL 421
PTZ00121 PTZ00121
MAEBL; Provisional
 13-267 3.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   13 KLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTE----DELDKYSEALK----DAQEKLELAEKKAADAEA 84
Cdd:PTZ00121  1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEAKkkadEAKKAAEAKKKADEAKKA 1518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   85 EVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYE 164
Cdd:PTZ00121  1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  165 EVARKLVIIEGDLERTEERAELAESKCSELEEELKNVtNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAE 244
Cdd:PTZ00121  1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677

                          250       260
                   ....*....|....*....|...
gi 1622825854  245 RSVAKLEKTIDDLEDKLKCTKEE 267
Cdd:PTZ00121  1678 EEAKKAEEDEKKAAEALKKEAEE 1700
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-241 3.16e-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: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   48 QKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELD--RAQERLATALQKLEEAEKAADESE 125
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  126 rgmkvienralkdeekmELQEiQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTN-- 203
Cdd:COG4913    689 -----------------ALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRal 750

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1622825854  204 --NLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAE 241
Cdd:COG4913    751 leERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
133-284 3.94e-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: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  133 NRALKDEEKMELQEIQ--LKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAEL--AESKCSELEEELKNVTNN---L 205
Cdd:COG4913    608 NRAKLAALEAELAELEeeLAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAELERLDASsddL 687

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825854  206 KSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDklKCTKEEHLCTQRMLDQTLLDLNE 284
Cdd:COG4913    688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED--LARLELRALLEERFAAALGDAVE 764
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 3-267 5.51e-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: 38.41  E-value: 5.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    3 EAIKKKMQMLKLDKENALDRAEQaEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:pfam02463  706 QREKEELKKLKLEAEELLADRVQ-EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   83 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRK 162
Cdd:pfam02463  785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  163 YEEVARKLVIIEGDLERTEERAELaESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEF 242
Cdd:pfam02463  865 KEELLQELLLKEEELEEQKLKDEL-ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE 943

                          250       260
                   ....*....|....*....|....*
gi 1622825854  243 AERSVAKLEKTIDDLEDKLKCTKEE 267
Cdd:pfam02463  944 EADEKEKEENNKEEEEERNKRLLLA 968
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 28-129 6.05e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 38.14  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  28 AEQKQAEERSKQLEDELAAMQK-KLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVAslnrRIQLVEEELDRAQER 106
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKeQDEASFERLAELRDELAELEEELEALKARWEAEKELIE----EIQELKEELEQRYGK 486

                          90       100
                  ....*....|....*....|...
gi 1622825854 107 LATALQKLEEAEKAADESERGMK 129
Cdd:COG0542   487 IPELEKELAELEEELAELAPLLR 509
PRK12704 PRK12704
phosphodiesterase; Provisional
 1-166 6.98e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   1 MMEAIKKKMQMLKldKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLElaekkaa 80
Cdd:PRK12704   43 ILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELE------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  81 daeAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMkVIENraLKDEEKMELQEIQLKEAKHIAEEAD 160
Cdd:PRK12704  114 ---KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEI-LLEK--VEEEARHEAAVLIKEIEEEAKEEAD 187


                  ....*.
gi 1622825854 161 RKYEEV 166
Cdd:PRK12704  188 KKAKEI 193
mukB PRK04863
chromosome partition protein MukB;
16-277 7.26e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.01  E-value: 7.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   16 KENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELaekkaadAEAEVASLNRRIQL 95
Cdd:PRK04863   315 ELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEE-------ADEQQEENEARAEA 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   96 VEEELDRAQERLA-----------------TALQKLEEAEK---AADESERGMKVIENRALKDEEKMELQEIQLKEAKHI 155
Cdd:PRK04863   388 AEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSV 467

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  156 AEEADRKYEEVARKLVIIEGDLERtEERAELAESKCSELEEElKNVTNNLKSLEAQ---AEKYSQKEDKYEEEIKILTDK 232
Cdd:PRK04863   468 AQAAHSQFEQAYQLVRKIAGEVSR-SEAWDVARELLRRLREQ-RHLAEQLQQLRMRlseLEQRLRQQQRAERLLAEFCKR 545

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1622825854  233 LKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQRMLDQ 277
Cdd:PRK04863   546 LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
PTZ00121 PTZ00121
MAEBL; Provisional
 3-267 7.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 7.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854    3 EAIKKKMQMLKLDKENALDRAEQAEaEQKQAEERSKQLEDELAAMQK--KLKGTEDELDKYSEALKDAQEKLELAEKKAA 80
Cdd:PTZ00121  1537 DEAKKAEEKKKADELKKAEELKKAE-EKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   81 DAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAadESERGMKVIENRALKDEEKMELQEI-QLKEAKHIAEEA 159
Cdd:PTZ00121  1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAkKAEEDEKKAAEA 1693

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854  160 DRKYEEVARKLVIIEGDLERTEERAElaesKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETR 239
Cdd:PTZ00121  1694 LKKEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769

                          250       260
                   ....*....|....*....|....*...
gi 1622825854  240 AEFAERSVAKLEKTIDDLEDKLKCTKEE 267
Cdd:PTZ00121  1770 AEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
PRK12705 PRK12705
hypothetical protein; Provisional
 3-126 9.22e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 37.38  E-value: 9.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825854   3 EAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADA 82
Cdd:PRK12705   52 AALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNE 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622825854  83 EAEVASLNRRI--QLVEEELDRAQERLATALQKLEEaEKAADESER 126
Cdd:PRK12705  132 LYRVAGLTPEQarKLLLKLLDAELEEEKAQRVKKIE-EEADLEAER 176
 
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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