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Conserved domains on  [gi|1057867570|ref|NP_001317273|]
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tropomyosin alpha-1 chain isoform Tpm1.9cy [Homo sapiens]

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 ...
 12-246 6.59e-63

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: 196.79  E-value: 6.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  12 RKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057867570 172 MAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 246
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 ...
 12-246 6.59e-63

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: 196.79  E-value: 6.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  12 RKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057867570 172 MAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-247 4.78e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   6 SLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMD 165
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570 166 QTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLEL 245
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514


                  ..
gi 1057867570 246 NN 247
Cdd:COG1196   515 LL 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-230 4.26e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 4.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    5 SSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIM 164
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057867570  165 DQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 230
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
PTZ00121 PTZ00121
MAEBL; Provisional
 8-229 2.92e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    8 EAVRRKIRSLQEQADAAEE-RAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:PTZ00121  1162 DARKAEEARKAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD-----RKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQL 161
Cdd:PTZ00121  1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkadelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057867570  162 RIMDQTLKALMAAEDKYSQKEDRYE---EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKE 229
Cdd:PTZ00121  1322 KKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 12-246 6.59e-63

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: 196.79  E-value: 6.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  12 RKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261   1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL 171
Cdd:pfam00261  81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1057867570 172 MAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 6-247 4.78e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 4.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   6 SLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196   275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMD 165
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570 166 QTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLEL 245
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514


                  ..
gi 1057867570 246 NN 247
Cdd:COG1196   515 LL 516
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-246 4.50e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 4.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:COG1196   328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570 167 TLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 246
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-230 4.26e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 4.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    5 SSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIM 164
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057867570  165 DQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 230
Cdd:TIGR02168  851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-232 9.26e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 9.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196   227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:COG1196   307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057867570 167 TLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENL 232
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 12-116 1.34e-10

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 57.70  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  12 RKIRSLQEQADAAEERAGTLQRELDHERKLRETAEadvaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam12718  42 HKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKV 117

                          90       100
                  ....*....|....*....|....*
gi 1057867570  92 KVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:pfam12718 118 QALEQERDEWEKKYEELEEKYKEAK 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 7-246 1.66e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196   255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570 167 TLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELN 246
Cdd:COG1196   415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 31-247 1.76e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  31 LQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEI 110
Cdd:COG1196   237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570 111 QLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIK 190
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1057867570 191 VLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNN 247
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-240 2.80e-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: 53.91  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   24 AEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEE 103
Cdd:TIGR02168  279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  104 KMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALM-----AAEDKY 178
Cdd:TIGR02168  359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAELKEL 438

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057867570  179 SQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQ 240
Cdd:TIGR02168  439 QAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-233 8.49e-08

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 52.07  E-value: 8.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   1 MAGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  81 EKAADESErgmKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQ 160
Cdd:COG4942    96 RAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057867570 161 LRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLS 233
Cdd:COG4942   173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-225 2.20e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 2.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    4 SSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168  725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRI 163
Cdd:TIGR02168  805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057867570  164 MDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVA 225
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-225 3.41e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 3.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:TIGR02168  843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  167 TLKALMAAEDKYSQKEDRYEEEIKVL-SDKLKEAETRAEFAERSVTKLEKSIDDLEEKVA 225
Cdd:TIGR02168  923 KLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-230 5.63e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 5.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    2 AGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   82 KAADESERGMKVIESRAQKDEEKmeIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQL 161
Cdd:TIGR02169  751 QEIENVKSELKELEARIEELEED--LHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057867570  162 RIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 230
Cdd:TIGR02169  829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-210 1.13e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    4 SSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02169  300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRI 163
Cdd:TIGR02169  380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1057867570  164 MDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSV 210
Cdd:TIGR02169  460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-230 1.13e-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: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    7 LEAVRRKIRSLQEQADAAEeRAGTLQRELDherklretaEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  195 LNELERQLKSLERQAEKAE-RYKELKAELR---------ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   87 SErgMKVIESRAQKDEEKMEIQEIQlkeakhiaedadRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:TIGR02168  265 LE--EKLEELRLEVSELEEEIEELQ------------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057867570  167 TLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 230
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-162 3.02e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 3.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRET---------AEADVASLNRRIQLVEEELDRAQE---RLATAL 74
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDAssdDLAALE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   75 QKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLViiesDLERAEERAELSEGQV 154
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVEREL 767


                   ....*....
gi 1057867570  155 R-QLEEQLR 162
Cdd:COG4913    768 ReNLEERID 776
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 21-240 4.24e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.07  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  21 ADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQK 100
Cdd:COG4942    15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570 101 DEEKMEIQEIQLKEakhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQ 180
Cdd:COG4942    95 LRAELEAQKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570 181 KEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQ 240
Cdd:COG4942   172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
11-204 6.42e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 6.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   11 RRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 90
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsEGQVRQLEEQLrimdqtlkA 170
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF--------A 756

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1057867570  171 LMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAE 204
Cdd:COG4913    757 AALGDAVERELRENLEERIDALRARLNRAEEELE 790
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-221 2.48e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    7 LEAVRRKIRSLqEQADAAEERAGTLQRELDHERKLRETAEADVASlnRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4913    244 LEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDA 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   87 SERgmkviesraqkdeekmeiQEIQLKEAkhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLrimDQ 166
Cdd:COG4913    321 LRE------------------ELDELEAQ--IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL---PA 377

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1057867570  167 TLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG4913    378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
PTZ00121 PTZ00121
MAEBL; Provisional
 8-229 2.92e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 2.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    8 EAVRRKIRSLQEQADAAEE-RAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:PTZ00121  1162 DARKAEEARKAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD-----RKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQL 161
Cdd:PTZ00121  1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARkadelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057867570  162 RIMDQTLKALMAAEDKYSQKEDRYE---EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKE 229
Cdd:PTZ00121  1322 KKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
PTZ00121 PTZ00121
MAEBL; Provisional
 11-237 3.56e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 3.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   11 RRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121  1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQtLKA 170
Cdd:PTZ00121  1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-LKK 1640

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057867570  171 LMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQM 237
Cdd:PTZ00121  1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 7-222 3.70e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 3.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   87 SERGMKviESRAQKDEEKMEIQEIQLKEA---KHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEqlri 163
Cdd:TIGR02168  913 LRRELE--ELREKLAQLELRLEGLEVRIDnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP---- 986

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1057867570  164 mdqtlkALMAAEDKYSQKEDRYEEEIKVLSDklkeaetraefAERSVTKLEKSIDDLEE 222
Cdd:TIGR02168  987 ------VNLAAIEEYEELKERYDFLTAQKED-----------LTEAKETLEEAIEEIDR 1028
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
12-202 4.34e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 4.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   12 RKIRSLQEQADAAEERAGTLQRELDHERKLRETAE-----------ADVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEPIRELAERYAAARErlaeleylraaLRLWFAQRRLELLEAELEELRAELARLEAELERL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   81 EKAADESErgmkviESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG----QVRQ 156
Cdd:COG4913    315 EARLDALR------EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaaLRAE 388

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1057867570  157 LEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETR 202
Cdd:COG4913    389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
PTZ00121 PTZ00121
MAEBL; Provisional
 9-229 4.79e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 4.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    9 AVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEAD----VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:PTZ00121  1266 ARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKlviiesdlERAEERAELSEGQVRQLEEQLRIM 164
Cdd:PTZ00121  1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA--------DEAKKKAEEDKKKADELKKAAAAK 1417

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057867570  165 DQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLE--KSIDDLEEKVAHAKE 229
Cdd:PTZ00121  1418 KKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKK 1484
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
7-206 4.97e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 4.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    7 LEAVRRKIRSLQEQADA-----AEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATA-LQKLEEA 80
Cdd:COG4913    264 YAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQL 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   81 EKAADESERGMKVIESRAQKDEEKmeIQEIQLkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQ 160
Cdd:COG4913    344 EREIERLERELEERERRRARLEAL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1057867570  161 LRIMDQTLKALMAAEDKYSQkedRYEEEIKVLSDKLKEAETRAEFA 206
Cdd:COG4913    421 LRELEAEIASLERRKSNIPA---RLLALRDALAEALGLDEAELPFV 463
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4-157 6.39e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 6.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    4 SSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAE------------ADVASLNRRIQLVEEELDRAQERLA 71
Cdd:COG4913    630 EERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEleaelerldassDDLAALEEQLEELEAELEELEEELD 709

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   72 TALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLviiESDLERAEERAELSE 151
Cdd:COG4913    710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL---EERIDALRARLNRAE 786


                   ....*.
gi 1057867570  152 GQVRQL 157
Cdd:COG4913    787 EELERA 792
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
44-230 2.14e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 2.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   44 TAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEiqLKEAKHIAEDAD 123
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE--LEAELERLDASS 684

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  124 RKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLrimDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRA 203
Cdd:COG4913    685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761

                          170       180
                   ....*....|....*....|....*..
gi 1057867570  204 EFAERSVTKLEKSIDDLEEKVAHAKEE 230
Cdd:COG4913    762 AVERELRENLEERIDALRARLNRAEEE 788
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
7-205 3.11e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   7 LEAVRRKIRSLQEQAD--AAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3206   191 LEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  85 DESERGMKVIESRAQKDEEKMEIQEIQLKeakhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIM 164
Cdd:COG3206   271 QLAELEAELAELSARYTPNHPDVIALRAQ----IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1057867570 165 DQTLKALMAAEDKYSQKEDRYEEeikvLSDKLKEAETRAEF 205
Cdd:COG3206   347 PELEAELRRLEREVEVARELYES----LLQRLEEARLAEAL 383
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 47-247 3.40e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  47 ADVASLNRRIQLVEEELDRAQERlatalqkLEEAEKAADESERGMKVIESRAQKDEE----KMEIQEIQLKEAKHIAEDA 122
Cdd:COG1196   165 AGISKYKERKEEAERKLEATEEN-------LERLEDILGELERQLEPLERQAEKAERyrelKEELKELEAELLLLKLREL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570 123 DRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETR 202
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1057867570 203 AEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQTLLELNN 247
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
PTZ00121 PTZ00121
MAEBL; Provisional
 19-230 3.71e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   19 EQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRA 98
Cdd:PTZ00121  1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   99 QKDEE---KMEIQEIQLKEAKHIAEDADRKYEEVARK---LVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKALM 172
Cdd:PTZ00121  1647 KKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAeedEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1057867570  173 AAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 230
Cdd:PTZ00121  1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
PRK09039 PRK09039
peptidoglycan -binding protein;
2-85 8.20e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   2 AGSSSLEAVRRKIRSL----QEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIqlveEELDRAQERLATALQKL 77
Cdd:PRK09039   88 ASLSAAEAERSRLQALlaelAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI----AALRRQLAALEAALDAS 163


                  ....*...
gi 1057867570  78 EEAEKAAD 85
Cdd:PRK09039  164 EKRDRESQ 171
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 66-230 8.68e-04

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: 40.43  E-value: 8.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   66 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEiQLKEAKHIA-----EDADRKYEEVARKLVIIESDL 140
Cdd:TIGR02168  177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKA-ELRELELALlvlrlEELREELEELQEELKEAEEEL 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  141 ERAEERAELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDL 220
Cdd:TIGR02168  256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL 335

                          170
                   ....*....|
gi 1057867570  221 EEKVAHAKEE 230
Cdd:TIGR02168  336 AEELAELEEK 345
PTZ00121 PTZ00121
MAEBL; Provisional
 7-229 1.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    7 LEAVRRKirslqEQADAAEERAGTLQRELDHErKLRETAEADVASLNRRIQLVEEEldraQERLATALQKLEEAEKA--A 84
Cdd:PTZ00121  1226 AEAVKKA-----EEAKKDAEEAKKAEEERNNE-EIRKFEEARMAHFARRQAAIKAE----EARKADELKKAEEKKKAdeA 1295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   85 DESERGMKVIESRaQKDEEKMEIQEIQLK--EAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLR 162
Cdd:PTZ00121  1296 KKAEEKKKADEAK-KKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057867570  163 IMDQTLKAL--MAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLE--KSIDDLEEKVAHAKE 229
Cdd:PTZ00121  1375 EAKKKADAAkkKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEEAKK 1445
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 12-230 1.23e-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: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   12 RKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA----EKAADES 87
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaiERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   88 ERGMKVIESRAQKDEEKMEIQEIQLKE-AKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQ 166
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057867570  167 TLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 230
Cdd:TIGR02169  330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
14-167 1.41e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  14 IRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 93
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057867570  94 IESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQT 167
Cdd:COG4372   106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
6-230 1.74e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   6 SLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSE--GQVRQLEEQLRI 163
Cdd:COG4372   119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldELLKEANRNAEK 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057867570 164 MDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEE 230
Cdd:COG4372   199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
PTZ00121 PTZ00121
MAEBL; Provisional
 19-222 1.99e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 1.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   19 EQADAAEERAGTLQ--RELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEE----AEKAADESERGMK 92
Cdd:PTZ00121  1610 EEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKK 1689

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   93 VIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQlEEQLRIMDQTLKALM 172
Cdd:PTZ00121  1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE-EEKKKIAHLKKEEEK 1768

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1057867570  173 AAEDKYSQKEDRYEEEIKvlsdklKEAETRAEFAERSVTKLEKSIDDLEE 222
Cdd:PTZ00121  1769 KAEEIRKEKEAVIEEELD------EEDEKRRMEVDKKIKDIFDNFANIIE 1812
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-229 2.01e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   8 EAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEEL--------------DRAQERLATA 73
Cdd:PRK02224  275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeecrvaaqahneeaESLREDADDL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  74 LQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQ 153
Cdd:PRK02224  355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057867570 154 VRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKE 229
Cdd:PRK02224  435 LRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR 510
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
8-229 2.28e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   8 EAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:PRK02224  345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  88 ERGMKVIESRAQKDEEKMEIQEIQLKEAKhiAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRImdQT 167
Cdd:PRK02224  425 REREAELEATLRTARERVEEAEALLEAGK--CPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERL--ER 500

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057867570 168 LKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKE 229
Cdd:PRK02224  501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
PTZ00121 PTZ00121
MAEBL; Provisional
 13-235 2.62e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   13 KIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEE-----ELDRAQERLATALQKLEEAEKAAD-- 85
Cdd:PTZ00121  1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEkkkaeEAKKAEEDKNMALRKAEEAKKAEEar 1593

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   86 --------ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARK----------LVIIESDLERAEERA 147
Cdd:PTZ00121  1594 ieevmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKaeelkkaeeeNKIKAAEEAKKAEED 1673

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  148 ELSEGQVRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHA 227
Cdd:PTZ00121  1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753


                   ....*...
gi 1057867570  228 KEENLSMH 235
Cdd:PTZ00121  1754 EEKKKIAH 1761
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
7-244 3.14e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.30  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   7 LEAVRRKIRSLQEQADAAEERAGTLQRELdherklretaeadvASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG2433   408 LTEEEEEIRRLEEQVERLEAEVEELEAEL--------------EEKDERIERLERELSEARSEERREIRKDREISRLDRE 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  87 SERgmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDaDRKYEEVARKLV--IIESDLERAEERAELSEGQVRQLEEQL--- 161
Cdd:COG2433   474 IER----LERELEEERERIEELKRKLERLKELWKL-EHSGELVPVKVVekFTKEAIRRLEEEYGLKEGDVVYLRDASgag 548

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570 162 -----RIMDQTLKALMAAEDKYSQ-KEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEEnlSMH 235
Cdd:COG2433   549 rstaeLLAEAGPRAVIVPGELSEAaDEVLFEEGIPVLPAEDVTIQEVDDLAVVDEEELEAAIEDWEERAEERRRE--KKA 626


                  ....*....
gi 1057867570 236 QMLDQTLLE 244
Cdd:COG2433   627 EMLERLISE 635
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 17-240 3.45e-03

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: 38.39  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   17 LQEQADAAEERAGtlQRELDHERKlrETAEADVASLNRRIQLVEEELDRAQER---LATALQKLEEAEKAADESERGMKV 93
Cdd:COG3096    363 LEEQEEVVEEAAE--QLAEAEARL--EAAEEEVDSLKSQLADYQQALDVQQTRaiqYQQAVQALEKARALCGLPDLTPEN 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   94 IESRAQKDEEKMEIQEIQLKEAKH---IAEDADRKYEEVARKLVIIESDLERAE--ERAELSEGQVRQLEEQLRIMDQTL 168
Cdd:COG3096    439 AEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQQALAQRLQQLR 518

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057867570  169 KALMAAEDKYSQKEdRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEKVAHAKEENLSMHQMLDQ 240
Cdd:COG3096    519 AQLAELEQRLRQQQ-NAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 11-223 3.95e-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: 3.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   11 RRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:pfam02463  243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE----ERAELSEGQVRQLEEQLRIMDQ 166
Cdd:pfam02463  323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLakkkLESERLSSAAKLKEEELELKSE 402

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1057867570  167 TLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEK 223
Cdd:pfam02463  403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 33-160 4.78e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 37.67  E-value: 4.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  33 RELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIql 112
Cdd:pfam05262 192 KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSP-- 269

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1057867570 113 KEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQ 160
Cdd:pfam05262 270 KEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEK 317
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-223 5.24e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  17 LQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIqlveEELDRAQERLATALQKLEEAEKAADESERGMKVIES 96
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  97 RAQKDEEKMEIQEIQLKEAKHIAEDADRK------YEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKA 170
Cdd:PRK03918  267 RIEELKKEIEELEEKVKELKELKEKAEEYiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1057867570 171 LMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEK 223
Cdd:PRK03918  347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA 399
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 5-204 5.69e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.50  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   5 SSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3883    16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  85 DESERGMKVIE------------SRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG 152
Cdd:COG3883    96 YRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1057867570 153 QVRQLEEQLRIMDQTLKALMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAE 204
Cdd:COG3883   176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
PTZ00121 PTZ00121
MAEBL; Provisional
 19-231 7.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   19 EQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE---SERGMKVIE 95
Cdd:PTZ00121  1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAkkkADEAKKAEE 1520

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   96 SR----AQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGQVRQLEEQLRIMDQTLKAL 171
Cdd:PTZ00121  1521 AKkadeAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  172 MAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEEkVAHAKEEN 231
Cdd:PTZ00121  1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEEN 1659
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
61-230 7.08e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.59  E-value: 7.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   61 EELDRAQERLATALQKLEEAEKAADESERgmkviesrAQKDEEKMEIQEIQLKEAKHiaEDADRKYEEVARKLVIIESDL 140
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEPIRELAER--------YAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELRAEL 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570  141 ERAEERAELSEGQVRQLEEQLRimdqTLKALMAAEDkySQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDL 220
Cdd:COG4913    305 ARLEAELERLEARLDALREELD----ELEAQIRGNG--GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378

                          170
                   ....*....|
gi 1057867570  221 EEKVAHAKEE 230
Cdd:COG4913    379 AEEFAALRAE 388
PTZ00121 PTZ00121
MAEBL; Provisional
 2-210 7.36e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570    2 AGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERK---LRETAEADVASLNRrIQLVEEELDRAQE--RLATALQK 76
Cdd:PTZ00121  1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADE-LKKAAAAKKKADEakKKAEEKKK 1432

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057867570   77 LEEAEKAADESERG---------MKVIESRAQKDEEKMEIQEIQLK-EAKHIAEDADRKYEEVARKLVIIESDLERAEER 146
Cdd:PTZ00121  1433 ADEAKKKAEEAKKAdeakkkaeeAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1057867570  147 AELSEGQVRQLEEQLRIMDQTLKA--LMAAEDKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSV 210
Cdd:PTZ00121  1513 DEAKKAEEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
 
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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