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Conserved domains on  [gi|922581955|ref|NP_001300455|]
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Tropomyosin [Caenorhabditis elegans]

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 ...
 16-191 4.22e-51

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: 164.43  E-value: 4.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   16 KIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAG 95
Cdd:pfam00261  60 AEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   96 ENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKER 175
Cdd:pfam00261 140 ESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEK 219

                         170
                  ....*....|....*.
gi 922581955  176 YKTISEELDSTFQELS 191
Cdd:pfam00261 220 YKAISEELDQTLAELN 235
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 16-191 4.22e-51

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: 164.43  E-value: 4.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   16 KIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAG 95
Cdd:pfam00261  60 AEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   96 ENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKER 175
Cdd:pfam00261 140 ESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEK 219

                         170
                  ....*....|....*.
gi 922581955  176 YKTISEELDSTFQELS 191
Cdd:pfam00261 220 YKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 9-190 6.81e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   9 ERAEERLKIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERA 88
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  89 EERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDE 168
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        170       180
                 ....*....|....*....|..
gi 922581955 169 LVHEKERYKTISEELDSTFQEL 190
Cdd:COG1196  458 EEALLELLAELLEEAALLEAAL 479
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-185 1.16e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955    31 ESERVRKVMENRSLQDEERANtVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVG 110
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581955   111 NNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDS 185
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
46 PHA02562
endonuclease subunit; Provisional
 93-193 6.61e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 6.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  93 EAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTV---SSRLKEAETRAEFAERSVQKLQKEVDRLEDEL 169
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374

                         90       100
                 ....*....|....*....|....
gi 922581955 170 VHEKERYKTISEELDSTFQELSGY 193
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSEL 398
 
Name Accession Description Interval E-value
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 16-191 4.22e-51

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: 164.43  E-value: 4.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   16 KIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAG 95
Cdd:pfam00261  60 AEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   96 ENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKER 175
Cdd:pfam00261 140 ESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEK 219

                         170
                  ....*....|....*.
gi 922581955  176 YKTISEELDSTFQELS 191
Cdd:pfam00261 220 YKAISEELDQTLAELN 235
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 9-190 6.81e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   9 ERAEERLKIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERA 88
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  89 EERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDE 168
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        170       180
                 ....*....|....*....|..
gi 922581955 169 LVHEKERYKTISEELDSTFQEL 190
Cdd:COG1196  458 EEALLELLAELLEEAALLEAAL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 18-175 2.71e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  18 ATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGEN 97
Cdd:COG1196  237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581955  98 KIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKER 175
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-185 1.16e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955    31 ESERVRKVMENRSLQDEERANtVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVG 110
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581955   111 NNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDS 185
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-190 1.89e-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: 47.36  E-value: 1.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955    20 EKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKI 99
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   100 VELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELvhEKERYKTI 179
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKEL 438

                          170
                   ....*....|.
gi 922581955   180 SEELDSTFQEL 190
Cdd:TIGR02168  439 QAELEELEEEL 449
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 42-191 6.97e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  42 RSLQDEERANTVEA---QLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEV 118
Cdd:COG1196  216 RELKEELKELEAELlllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581955 119 SEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQELS 191
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-190 8.48e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 8.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  10 RAEERLKIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAE 89
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  90 ERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDEL 169
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                        170       180
                 ....*....|....*....|.
gi 922581955 170 VHEKERYKTISEELDSTFQEL 190
Cdd:COG1196  438 EEEEEALEEAAEEEAELEEEE 458
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-192 1.27e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  10 RAEERLKIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAE 89
Cdd:COG1196  327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  90 ERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDEL 169
Cdd:COG1196  407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486

                        170       180
                 ....*....|....*....|...
gi 922581955 170 VHEKERYKTISEELDSTFQELSG 192
Cdd:COG1196  487 AEAAARLLLLLEAEADYEGFLEG 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 18-190 1.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  18 ATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGEN 97
Cdd:COG1196  272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  98 KIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYK 177
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431

                        170
                 ....*....|...
gi 922581955 178 TISEELDSTFQEL 190
Cdd:COG1196  432 ELEEEEEEEEEAL 444
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 36-190 2.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  36 RKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKS 115
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581955 116 LEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQEL 190
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-183 3.77e-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: 43.51  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955    20 EKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKI 99
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   100 VELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTI 179
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398


                   ....
gi 922581955   180 SEEL 183
Cdd:TIGR02168  399 NNEI 402
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 53-186 8.30e-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: 42.35  E-value: 8.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955    53 VEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEE 132
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 922581955   133 QIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDST 186
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
33-169 2.63e-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: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   33 ERVRKVMENRSLQDEERANTVEAQLKEAQLL-AEEADRKYDEVARKLAMVEA-----DLERAEERAEAGENKIVELEEEL 106
Cdd:COG4913   225 EAADALVEHFDDLERAHEALEDAREQIELLEpIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAEL 304

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922581955  107 RVVGNNLKSLEVSEEKALQREDSYEEQIRTVS-SRLKEAETRAEFAERSVQKLQKEVDRLEDEL 169
Cdd:COG4913   305 ARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALL 368
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
73-191 2.82e-04

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 40.90  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  73 EVARKLAMVEADLERAEERAEAGENK----IVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRA 148
Cdd:COG1193  490 EIARRLGLPEEIIERARELLGEESIDveklIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKA 569

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 922581955 149 EF-AERSVQKLQKEVDRLEDEL---VHEKERYKTISEELDSTFQELS 191
Cdd:COG1193  570 REeAEEILREARKEAEELIRELreaQAEEEELKEARKKLEELKQELE 616
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-183 4.00e-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: 4.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955     1 MTLLEEELERAEERLKIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAM 80
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955    81 VEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKAlqredsyEEQIRTVSSRLKEAETRAEFAERSVQKLQK 160
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-------ESELEALLNERASLEEALALLRSELEELSE 901

                          170       180
                   ....*....|....*....|...
gi 922581955   161 EVDRLEDELVHEKERYKTISEEL 183
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKL 924
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 11-190 5.32e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 5.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  11 AEERLKIATEKLEEATHNVDESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEE 90
Cdd:COG1196  258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  91 RAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELV 170
Cdd:COG1196  338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417

                        170       180
                 ....*....|....*....|
gi 922581955 171 HEKERYKTISEELDSTFQEL 190
Cdd:COG1196  418 RLEEELEELEEALAELEEEE 437
46 PHA02562
endonuclease subunit; Provisional
 93-193 6.61e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 6.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  93 EAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTV---SSRLKEAETRAEFAERSVQKLQKEVDRLEDEL 169
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLlelKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374

                         90       100
                 ....*....|....*....|....
gi 922581955 170 VHEKERYKTISEELDSTFQELSGY 193
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSEL 398
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 31-184 1.08e-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: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  31 ESERVRKVMENRSLQDEERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVG 110
Cdd:COG1196  645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955 111 NNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRL-------EDELVHEKERYKTISEEL 183
Cdd:COG1196  725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaIEEYEELEERYDFLSEQR 804


                 .
gi 922581955 184 D 184
Cdd:COG1196  805 E 805
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 88-177 1.17e-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: 38.98  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  88 AEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLED 167
Cdd:COG4942   18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                         90
                 ....*....|
gi 922581955 168 ELVHEKERYK 177
Cdd:COG4942   98 ELEAQKEELA 107
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 47-190 1.38e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955    47 EERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEA-GENKIVELEEELRVVGNNLKSLEVSEEKALQ 125
Cdd:TIGR02169  236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKER 315

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922581955   126 REDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTI---SEELDSTFQEL 190
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraeLEEVDKEFAET 383
PRK12704 PRK12704
phosphodiesterase; Provisional
 49-182 1.41e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  49 RANTVEAQLKEAQLLAE---EADRKYDEVARKLAMVEADLERAEERAEagenkiveLEEELRVVGNNLKSLEvseEKALQ 125
Cdd:PRK12704  25 RKKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLEAKEEIHKLRNE--------FEKELRERRNELQKLE---KRLLQ 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955 126 REDSYEEQIRTVSSR---LKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEE 182
Cdd:PRK12704  94 KEENLDRKLELLEKReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
29-190 2.71e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 37.97  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   29 VDESERVRKVMENRSLQDEERAntvEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRV 108
Cdd:COG4913   258 RELAERYAAARERLAELEYLRA---ALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  109 VGNnlkslevseekalQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQ 188
Cdd:COG4913   335 NGG-------------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401


                  ..
gi 922581955  189 EL 190
Cdd:COG4913   402 AL 403
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 30-193 2.99e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 37.60  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  30 DESERVRKVMENRSlQDEERANTVEAQLKEAQLLAEEADR-KYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRV 108
Cdd:PRK05771  40 LSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKKKvSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKE 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955 109 VGNNLKSLE------------------------VSEEKA----LQREDSYEEQIRT---------VSSRLKEAETRAEFA 151
Cdd:PRK05771 119 LEQEIERLEpwgnfdldlslllgfkyvsvfvgtVPEDKLeelkLESDVENVEYISTdkgyvyvvvVVLKELSDEVEEELK 198

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 922581955 152 ERSVQKLQKEVDRLEDELVHE-KERYKTISEELDSTFQELSGY 193
Cdd:PRK05771 199 KLGFERLELEEEGTPSELIREiKEELEEIEKERESLLEELKEL 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 47-190 4.05e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 36.83  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  47 EERANTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNlkslevSEEKALQR 126
Cdd:COG1579   23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN------KEYEALQK 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581955 127 E-DSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEELDSTFQEL 190
Cdd:COG1579   97 EiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 30-162 5.13e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.11  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  30 DESERVRKVMEnrSLQDEERanTVEAQLKEAQLLAEEADRKYDEVARKLAMVEADLERAEERAEAGENKIV-ELEEELRV 108
Cdd:PRK00409 513 EDKEKLNELIA--SLEELER--ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIkEAKKEADE 588

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 922581955 109 VGNNLKSLEVSEEKALQREDSYEEQirtvsSRLKEAETRAEFAERSVQKLQKEV 162
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHELIEAR-----KRLNKANEKKEKKKKKQKEKQEEL 637
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 81-190 6.38e-03

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 36.96  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   81 VEADLERAEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKAlqredsyEEQIRTVSSRLKEAETRAEFAERSVQKLQK 160
Cdd:pfam05911 700 LEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLA-------ETQLKCMAESYEDLETRLTELEAELNELRQ 772

                          90       100       110
                  ....*....|....*....|....*....|
gi 922581955  161 EVDRLEDELVHEKERYktisEELDSTFQEL 190
Cdd:pfam05911 773 KFEALEVELEEEKNCH----EELEAKCLEL 798
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
44-193 7.66e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 36.43  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   44 LQDEERANTVEAQLKEAQLLAEEADRKYD--------EVARKLAMVEADLERAEERAEAGENKIVELEEELRVVGNNLKS 115
Cdd:COG4913   570 LRRHPRAITRAGQVKGNGTRHEKDDRRRIrsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA 649

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955  116 LEVSEE--------KALQRE-DSYEEQIRTV---SSRLKEAETRAEFAERSVQKLQKEVDRLEDELVHEKERYKTISEEL 183
Cdd:COG4913   650 LQRLAEyswdeidvASAEREiAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729

                         170
                  ....*....|
gi 922581955  184 DSTFQELSGY 193
Cdd:COG4913   730 DELQDRLEAA 739
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
20-189 7.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 36.43  E-value: 7.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   20 EKLEEATHNVDESERVRKVMENRSLQDEERANTVE--AQLKEAQLLAEEADRKYDEVARKLAMVEAD----------LER 87
Cdd:COG4913   617 AELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASsddlaaleeqLEE 696

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581955   88 AEERAEAGENKIVELEEELRVVGNNLKSLEVSEEKALQREDSYEEQIRTVSSRLKEAETRAEFAERSVQKLQKevdRLED 167
Cdd:COG4913   697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE---NLEE 773

                         170       180
                  ....*....|....*....|..
gi 922581955  168 ELVHEKERYKTISEELDSTFQE 189
Cdd:COG4913   774 RIDALRARLNRAEEELERAMRA 795
 
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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