|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
160-361 |
1.39e-81 |
|
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: 248.40 E-value: 1.39e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 160 AEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADR 239
Cdd:pfam00261 34 AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 240 KYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAE 319
Cdd:pfam00261 114 KYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAE 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068700074 320 FAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQTFTEMS 361
Cdd:pfam00261 194 FAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
166-231 |
9.27e-16 |
|
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: 73.49 E-value: 9.27e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700074 166 ALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEAR 231
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-355 |
2.29e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068700074 316 ARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQ 355
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-359 |
1.90e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2068700074 316 ARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQTFTE 359
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-348 |
1.56e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190
....*....|....*....|....*....|...
gi 2068700074 316 ARAEFAERSVQKLQKEVDRLEDELVIQKERYKS 348
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-355 |
2.15e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068700074 316 ARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQ 355
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-340 |
1.15e-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: 66.23 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 154 NVQLKRAEGEVAALNRRIQLLEEDLERS-------EERLNTATTKLAEASQAADESERMRKVLEnrslsdeERMDALENQ 226
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELrlevselEEEIEELQKELYALANEISRLEQQKQILR-------ERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 227 LKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKT 306
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190
....*....|....*....|....*....|....
gi 2068700074 307 LANKLKAAEARAEFAERSVQKLQKEVDRLEDELV 340
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-361 |
2.18e-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: 65.46 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMD-------ALENQLK 228
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskeltELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 229 EARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLA 308
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2068700074 309 NKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQTFTEMS 361
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-355 |
1.35e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEdLERSEERLNTATTKLAEASQAAD-----ESERMRKVLENRSLSDEERMDALENQLKEA 230
Cdd:COG4913 236 DLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 231 RFLAEEADRKYDEV--------ARKLAMVEADLERAEERAETGESKIVELEEELRVVGnnLKSLEVSEEKANQREEAyKE 302
Cdd:COG4913 315 EARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEALLAALG--LPLPASAEEFAALRAEA-AA 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2068700074 303 QIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQ 355
Cdd:COG4913 392 LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-339 |
1.40e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALnrRIQLLEEDLERSEERLNTATTKLAEASQAADEsermrkvlenrslsDEERMDALENQLKEARFLAE 235
Cdd:COG1196 221 ELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAE--------------LEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180
....*....|....*....|....
gi 2068700074 316 ARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEEL 388
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-362 |
6.86e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALnrRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:TIGR02168 221 ELRELELALLVL--RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068700074 316 ARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQTFTEMSG 362
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-360 |
8.49e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 150 HNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLenrslsdEERMDALENQLKE 229
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-------AEELAELEEKLEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 230 ARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLA- 308
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLk 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700074 309 ----NKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQTFTEM 360
Cdd:TIGR02168 429 kleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-345 |
1.69e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 146 KNELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALEN 225
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 226 QLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIV---------------------ELEEELRVVGNNLK 284
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsedieslaaeieeleelieELESELEALLNERA 883
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068700074 285 SLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKER 345
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
154-356 |
3.89e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.10 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 154 NVQLKRAEGEVAA--LNRRIQLLEEDLERSEERLNtattKLAEASQAADesermrkvLENRSLSDEERMDALENQLKEAR 231
Cdd:COG3206 165 NLELRREEARKALefLEEQLPELRKELEEAEAALE----EFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 232 FLAEEADRKYDEVARKLAM---------------------VEADLERAEERAETGES--KIVELEEELRVVGNNLK---- 284
Cdd:COG3206 233 AELAEAEARLAALRAQLGSgpdalpellqspviqqlraqlAELEAELAELSARYTPNhpDVIALRAQIAALRAQLQqeaq 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700074 285 ----SLEVSEEKANQREEAYKEQIKTLANKLKaaearaefaerSVQKLQKEVDRLEDELVIQKERYKSITDELDQT 356
Cdd:COG3206 313 rilaSLEAELEALQAREASLQAQLAQLEARLA-----------ELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-345 |
8.90e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELrvvgnnlkslEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL----------EEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190
....*....|....*....|....*....|
gi 2068700074 316 ARAEFAERSVQKLQKEVDRLEDELVIQKER 345
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-339 |
2.00e-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: 55.54 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEAR-FLA 234
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 235 EEADRKY-----------------DEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQRE 297
Cdd:COG4942 108 ELLRALYrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068700074 298 EAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-354 |
2.36e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 169 RRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALEnqlkearfLAEEADRKYDEVAR-- 246
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--------AEREIAELEAELERld 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 247 ----KLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAY-----KEQIKTLANKLKAAEAR 317
Cdd:COG4913 682 assdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarLELRALLEERFAAALGD 761
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068700074 318 AEFAE------RSVQKLQKEVDRLEDELVIQ----KERYKSITDELD 354
Cdd:COG4913 762 AVERElrenleERIDALRARLNRAEEELERAmrafNREWPAETADLD 808
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-348 |
2.89e-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: 54.77 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE-SERMRKVLenRSLSDEERMDALENQLKEARFLA 234
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAqKEELAELL--RALYRLGRQPPLALLLSPEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 235 EEADRKYDEvarklAMVEADLERAEE---RAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:COG4942 134 AVRRLQYLK-----YLAPARREQAEElraDLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 2068700074 312 KAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKS 348
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-339 |
3.43e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRK-------YDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLA 308
Cdd:TIGR02168 870 ELESEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
|
170 180 190
....*....|....*....|....*....|..
gi 2068700074 309 N-KLKAAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:TIGR02168 950 SlTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-272 |
6.10e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA 758
|
90 100 110
....*....|....*....|....*....|....*..
gi 2068700074 236 EADRKYDEVARKLamvEADLERAEERAETGESKIVEL 272
Cdd:COG4913 759 LGDAVERELRENL---EERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-345 |
7.37e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 157 LKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARflAEE 236
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 237 ADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELrvvgnnlKSLEVSEEKANQREEAYKEQIKTLANKLKAAEA 316
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK-------EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190
....*....|....*....|....*....|
gi 2068700074 317 RAEFAERSVQKLQKEVDRLEDELV-IQKER 345
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGdLKKER 891
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-311 |
7.69e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAAD--ESERMRKVLENRSLSDEERMDALENQLKEARfl 233
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELR-- 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700074 234 aeEADRKYDEVARKLAMVEADLERAEER-AETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:COG4717 160 --ELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-339 |
3.10e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 138 TMMKF--SIIKNELHNIMNvQLKRAEGEVAALN-RRIQLLEEDLERSEERlntaTTKLAEASQAADESERMRKVLENRSL 214
Cdd:COG4717 38 TLLAFirAMLLERLEKEAD-ELFKPQGRKPELNlKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 215 SDEERMDALENQLKearflAEEADRKYDEVARKLAMVEADLERAEERAETgeskIVELEEELRVVGNNLKSLEVS-EEKA 293
Cdd:COG4717 113 ELREELEKLEKLLQ-----LLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEElEELL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2068700074 294 NQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
145-339 |
3.98e-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: 51.99 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 145 IKNELHNImNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALE 224
Cdd:TIGR02169 292 VKEKIGEL-EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 225 NQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQI 304
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
170 180 190
....*....|....*....|....*....|....*
gi 2068700074 305 KTLANKLKAAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-310 |
5.89e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 147 NELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERL-----------NTATTKLAEASQAADESERMRKVLENRSLS 215
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 216 DEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQ 295
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
170
....*....|....*
gi 2068700074 296 REEAYKEQIKTLANK 310
Cdd:COG4942 228 LIARLEAEAAAAAER 242
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
132-363 |
6.95e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 132 SIFSS-NTMMKfSIIK--NELHNIMNVQLKRAEGEVAALNRRIQLLEE-DLERSEERLNTATTKLAEASQAADESERMRK 207
Cdd:PHA02562 163 SVLSEmDKLNK-DKIRelNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkNGENIARKQNKYDELVEEAKTIKAEIEELTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 208 VLENRSLSDEERMDALeNQLKEARFLAEEadrKYDEVARKLAMVE---------ADLERAEERAETGESKIVELEEELRv 278
Cdd:PHA02562 242 ELLNLVMDIEDPSAAL-NKLNTAAAKIKS---KIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLE- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 279 vgnnlkSLEVSEEKANQREEAYKEQIKT---LANKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQ 355
Cdd:PHA02562 317 ------KLDTAIDELEEIMDEFNEQSKKlleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
....*...
gi 2068700074 356 TFTEMSGY 363
Cdd:PHA02562 391 IVKTKSEL 398
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
164-359 |
1.38e-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: 50.45 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 164 VAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMR-KVLENRSLSDEER----------MDALENQLKEARF 232
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREReKAERYQALLKEKReyegyellkeKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 233 LAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVEL-EEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2068700074 312 KAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQTFTE 359
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
152-339 |
2.01e-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: 49.68 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 152 IMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEAR 231
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 232 FLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
170 180 190
....*....|....*....|....*....|....
gi 2068700074 312 K------AAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:TIGR02169 934 SeiedpkGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-312 |
4.73e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 145 IKNELHNIMNVQLKRAEGEVAALNRRIQLLEE------DLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEE 218
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 219 RMDALENQLKEARFlaEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSeEKANQREE 298
Cdd:PRK03918 648 ELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVE 724
|
170
....*....|....
gi 2068700074 299 AYKEQIKTLANKLK 312
Cdd:PRK03918 725 ELREKVKKYKALLK 738
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-339 |
5.02e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 170 RIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSdEERMDALENQLKEARFLAEEADRKYDEVARKLA 249
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL-EELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 250 MVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEaYKEQIKTLANKLKAAEARAEFAERSVQKLQ 329
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKR 633
|
170
....*....|
gi 2068700074 330 KEVDRLEDEL 339
Cdd:PRK02224 634 ERKRELEAEF 643
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-356 |
5.50e-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: 48.51 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 214 LSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKA 293
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068700074 294 NQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQT 356
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-361 |
6.59e-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: 47.45 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 188 ATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGES 267
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 268 KIVELEEELRVVGNNLKSLEVSEEKANQRE---------------------EAYKEQIKTLANKLKAAEARAEFAERSVQ 326
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2068700074 327 KLQKEVDRLEDELVIQKERYKSITDELDQTFTEMS 361
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-305 |
7.08e-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: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLE---------RSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEermdALENQ 226
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLEtlrskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK----LEEAE 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700074 227 LKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIK 305
Cdd:TIGR02168 435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
179-355 |
7.25e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 179 ERSEERLNTATTKLAEASQAADESERMRKVLEN--------RSLSDEER----------MDALENQLKEARFLAEEADRK 240
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERQLEPLERqaekaeryRELKEELKeleaellllkLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 241 YDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEF 320
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190
....*....|....*....|....*....|....*
gi 2068700074 321 AERSVQKLQKEVDRLEDELVIQKERYKSITDELDQ 355
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
155-312 |
7.75e-06 |
|
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: 46.46 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARfla 234
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR--- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700074 235 eeADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLK 312
Cdd:COG1579 87 --NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
156-354 |
8.80e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068700074 316 ARAEFAERSVQKLQKEVDRLEDELVIQKER---YKSITDELD 354
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLK 517
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
156-339 |
1.13e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDlerseerLNTATTKLAEASQAADESERMRKVL-ENRSLSDEERMDALENQLKEARFLA 234
Cdd:pfam10174 409 QLRDKDKQLAGLKERVKSLQTD-------SSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 235 EEADRKYDEVARKLAMVEADLERAEERAETG---ESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKtLANKL 311
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGlkkDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPE-INDRI 560
|
170 180
....*....|....*....|....*...
gi 2068700074 312 KAAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:pfam10174 561 RLLEQEVARYKEESGKAQAEVERLLGIL 588
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
156-311 |
2.04e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.22 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLL----------------EEDLERSEERLNTATtKLAEASQAA----DESE--------RMRK 207
Cdd:COG0497 173 ELEELRADEAERARELDLLrfqleeleaaalqpgeEEELEEERRRLSNAE-KLREALQEAlealSGGEggaldllgQALR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 208 VLENRSlSDEERMDALENQLKEARFLAEEAdrkYDEVARKLAMVEAD---LERAEER------------------AETGE 266
Cdd:COG0497 252 ALERLA-EYDPSLAELAERLESALIELEEA---ASELRRYLDSLEFDperLEEVEERlallrrlarkygvtveelLAYAE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068700074 267 skivELEEELrvvgNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:COG0497 328 ----ELRAEL----AELENSDERLEELEAELAEAEAELLEAAEKL 364
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
164-355 |
2.11e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 164 VAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDE 243
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 244 VARKLAMVEADLER-------------------------AEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREE 298
Cdd:COG4942 95 LRAELEAQKEELAEllralyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068700074 299 AYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQ 355
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
167-353 |
2.56e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 167 LNRRIQLLEEDLERSE---ERLNTATTKLAEASQAADE-SERMRKVlenrslsdEERMDALENQLKEARFLAEEadrkYD 242
Cdd:PRK03918 174 IKRRIERLEKFIKRTEnieELIKEKEKELEEVLREINEiSSELPEL--------REELEKLEKEVKELEELKEE----IE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 243 EVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREE--AYKEQIKTLANKLKAAEARAEF 320
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190
....*....|....*....|....*....|...
gi 2068700074 321 AERSVQKLQKEVDRLEDELVIQKERYKSITDEL 353
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-355 |
3.26e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNR------RIQLLEE---DLERSEERLNTATTKLAEASQAADESE----RMRKVLENRSLSDEERmdA 222
Cdd:PRK03918 430 ELKKAKGKCPVCGRelteehRKELLEEytaELKRIEKELKEIEEKERKLRKELRELEkvlkKESELIKLKELAEQLK--E 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 223 LENQLKEARF-LAEEADRKYDEVARKLAMVEADLERAEERAETG----------ESKIVELEEELRVVGNNL-----KSL 286
Cdd:PRK03918 508 LEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelkkklaelEKKLDELEEELAELLKELeelgfESV 587
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700074 287 EVSEEKANQREEAYKEQIKtlankLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQ 355
Cdd:PRK03918 588 EELEERLKELEPFYNEYLE-----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-354 |
3.82e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERM----RKVLENRSLSDEERmDALENQLKEAR 231
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiEDLRETIAETERER-EELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 232 FLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA 365
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2068700074 312 KAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELD 354
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-354 |
5.74e-05 |
|
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: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 163 EVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARflaEEADRKYD 242
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE---AELEELAE 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 243 EVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAE 322
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
170 180 190
....*....|....*....|....*....|....*....
gi 2068700074 323 RSVQKLQKEVDRL-------EDELVIQKERYKSITDELD 354
Cdd:COG1196 767 RELERLEREIEALgpvnllaIEEYEELEERYDFLSEQRE 805
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
156-353 |
6.96e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190
....*....|....*....|....*....|....*...
gi 2068700074 316 ARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDEL 353
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
222-359 |
8.04e-05 |
|
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: 43.37 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 222 ALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEV-SEEKANQRE-EA 299
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqLGNVRNNKEyEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 300 YKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQTFTE 359
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
155-278 |
9.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRslsdEERMDALENQLK-EARFL 233
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL----QEELEELLEQLSlATEEE 193
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2068700074 234 AEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRV 278
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
224-352 |
1.16e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 224 ENQLKEARFLAE---EADRKYDEVARKLAMVEADLERAEERAEtgeskiveLEEELRVVGNNLKSLEvseEKANQREEAY 300
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAEAIKKEALLEAKEEIHKLRNE--------FEKELRERRNELQKLE---KRLLQKEENL 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2068700074 301 KEQIKTLA---NKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDE 352
Cdd:PRK12704 99 DRKLELLEkreEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-355 |
1.68e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 172 QLLEEDLERSEERLNTATTKLAE-ASQAADESERMRKVLENRslsdEERMDALENQLKEARFLAEEADRKYDEVARKLAM 250
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPElNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 251 VEADLERAEERAEtgeskIVELEEELRVVGNNLKSLEVSEEKANQREEAY---KEQIKTLANKLKAAEARAEFAERS-VQ 326
Cdd:COG4717 121 LEKLLQLLPLYQE-----LEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEeLQ 195
|
170 180
....*....|....*....|....*....
gi 2068700074 327 KLQKEVDRLEDELVIQKERYKSITDELDQ 355
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEE 224
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
166-277 |
1.71e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 41.86 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 166 ALNRRIQLLEEDLERSEERLNTATTKLAEA----SQAADESERMRKVLENRSlsdeermdalenqlKEARflAEEADRKY 241
Cdd:PRK07352 47 ILEERREAILQALKEAEERLRQAAQALAEAqqklAQAQQEAERIRADAKARA--------------EAIR--AEIEKQAI 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2068700074 242 DEVARKLAMVEADLERAEERA------ETGESKIVELEEELR 277
Cdd:PRK07352 111 EDMARLKQTAAADLSAEQERViaqlrrEAAELAIAKAESQLP 152
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
156-324 |
1.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE-----SERMRK-------------VLENRSLSDE 217
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelGERARAlyrsggsvsyldvLLGSESFSDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 218 -ERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQR 296
Cdd:COG3883 118 lDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
|
170 180
....*....|....*....|....*...
gi 2068700074 297 EEAYKEQIKTLANKLKAAEARAEFAERS 324
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-307 |
2.64e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 159 RAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEAD 238
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068700074 239 RKYDEVARKLAM----VEADLERAEERAEtgeskivELEEELRVVGN-NLKSLEVSEEkANQREEAYKEQIKTL 307
Cdd:COG1196 742 LEEEELLEEEALeelpEPPDLEELERELE-------RLEREIEALGPvNLLAIEEYEE-LEERYDFLSEQREDL 807
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
155-266 |
5.45e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLA 234
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
90 100 110
....*....|....*....|....*....|..
gi 2068700074 235 EEADRKYDEVARKLAMVEADLERAEERAETGE 266
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAE 446
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-310 |
5.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEErmdaLENQLKEARFLAE 235
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ----LEELLGELEELLE 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700074 236 EADrkYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNnlkslEVSEEKANQREEAYKEQIKTLANK 310
Cdd:COG4717 424 ALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEE 491
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
174-302 |
6.05e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 174 LEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDAL-ENQLKEARFLAEEADRKYDEVARKLamve 252
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLlEEAEKEAQQAIKEAKKEADEIIKEL---- 593
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2068700074 253 adleRAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKE 302
Cdd:PRK00409 594 ----RQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-353 |
7.46e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 141 KFSIIKNELHNIMNVqLKRAEGEVAALNRRIqlleEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERM 220
Cdd:PRK03918 201 ELEEVLREINEISSE-LPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 221 DALENQLKEARFLAEEADRK------YDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAN 294
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700074 295 QREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDEL 353
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-355 |
1.22e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRiqLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:PTZ00121 1198 DARKAEAARKAEEER--KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 236 EAdRKYDEVARKLAMVEAD-LERAEERAETGESKIVELE----EELRVVGNNLK----SLEVSEEKANQREEAYKEQIKT 306
Cdd:PTZ00121 1276 EA-RKADELKKAEEKKKADeAKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKkkadAAKKKAEEAKKAAEAAKAEAEA 1354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700074 307 LANKLKAAEARAEFAERSVQKLQKEVDRLE---------DELVIQKERYKSITDELDQ 355
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaeekkkaDEAKKKAEEDKKKADELKK 1412
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
200-312 |
1.28e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 200 DESERMRKVLEnrSLSDEERmdALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAE-TGESKIVELEEELRV 278
Cdd:PRK00409 513 EDKEKLNELIA--SLEELER--ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....
gi 2068700074 279 VGNNLKSLEvSEEKANQREEAYKEQIKTLANKLK 312
Cdd:PRK00409 589 IIKELRQLQ-KGGYASVKAHELIEARKRLNKANE 621
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
145-312 |
1.56e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 145 IKNELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERS-------EERLNTATTKLAEASQAADE-SERMRKVLENRSLSD 216
Cdd:PRK04778 265 IDENLALLEELDLDEAEEKNEEIQERIDQLYDILEREvkarkyvEKNSDTLPDFLEHAKEQNKElKEEIDRVKQSYTLNE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 217 EE--RMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELrvvgnnlKSLEVSEEKAN 294
Cdd:PRK04778 345 SEleSVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEML-------QGLRKDELEAR 417
|
170
....*....|....*...
gi 2068700074 295 QREEAYKEQIKTLANKLK 312
Cdd:PRK04778 418 EKLERYRNKLHEIKRYLE 435
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-361 |
1.67e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 145 IKNELHNIMNvQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAAD--ESERMRKVLENRSLsdEERMDA 222
Cdd:TIGR04523 319 QEKKLEEIQN-QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEklKKENQSYKQEIKNL--ESQIND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 223 LENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKE 302
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700074 303 QIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQTFTEMS 361
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
152-278 |
1.81e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 152 IMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAE--ASQAADESERMR-----KVLENRSLSDEERMDALE 224
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANlrASLSAAEAERSRlqallAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068700074 225 NQLKEARFLAEEADRKYD----EVA---RKLAMVEADLERAEERAETGESKIVELEEELRV 278
Cdd:PRK09039 123 QELDSEKQVSARALAQVEllnqQIAalrRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
163-301 |
2.33e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 163 EVAALNRRIQLLEEDLERSEERLNTATT--------------------KLAEASQAADESERMRKVLENRSLSDEERMDA 222
Cdd:PRK04863 315 ELAELNEAESDLEQDYQAASDHLNLVQTalrqqekieryqadleeleeRLEEQNEVVEEADEQQEENEARAEAAEEEVDE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 223 LENQL---------KEARFLA-EEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKsleVSEEK 292
Cdd:PRK04863 395 LKSQLadyqqaldvQQTRAIQyQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS---VAQAA 471
|
....*....
gi 2068700074 293 ANQREEAYK 301
Cdd:PRK04863 472 HSQFEQAYQ 480
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-301 |
2.50e-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: 39.94 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 163 EVAALNRRIQLLEEDLERSEERLN--------------------TATTKLAEASQAADESERMRKVLENRSLSDEERMDA 222
Cdd:COG3096 314 ELEELSARESDLEQDYQAASDHLNlvqtalrqqekieryqedleELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 223 LENQL---------KEARFLA-EEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRvvgNNLKSLEVSEEK 292
Cdd:COG3096 394 LKSQLadyqqaldvQQTRAIQyQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVL---ELEQKLSVADAA 470
|
....*....
gi 2068700074 293 ANQREEAYK 301
Cdd:COG3096 471 RRQFEKAYE 479
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
150-361 |
2.74e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.41 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 150 HNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTAT---TKLAeASQAADESERMRKVLENRSL-------SDEER 219
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVrekTSLS-ASVASLEKQLLELTRVNELLkakfsedGTQKK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 220 MDALENQLKEARflaEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVvgnnLKSLEVSEEKANQREEA 299
Cdd:pfam15905 154 MSSLSMELMKLR---NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVS----TEKEKIEEKSETEKLLE 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068700074 300 YKEQIKTLANKLKAAEARaefaersVQKLQKEVDRLEDELVIQKERYKSITDELDQTFTEMS 361
Cdd:pfam15905 227 YITELSCVSEQVEKYKLD-------IAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLN 281
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
243-355 |
2.82e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 39.74 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 243 EVARKLAMVEADLERAEERAETGESK----IVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTL-ANKLKAAEAR 317
Cdd:COG1193 490 EIARRLGLPEEIIERARELLGEESIDveklIEELERERRELEEEREEAERLREELEKLREELEEKLEELeEEKEEILEKA 569
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2068700074 318 AEFAERSVQKLQKEVDRLEDEL---VIQKERYKSITDELDQ 355
Cdd:COG1193 570 REEAEEILREARKEAEELIRELreaQAEEEELKEARKKLEE 610
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
162-274 |
3.17e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 162 GEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQA------ADESERMRK-------------VLENRSLSDEERMDA 222
Cdd:COG2433 366 DEVKARVIRGLSIEEALEELIEKELPEEEPEAEREKEheerelTEEEEEIRRleeqverleaeveELEAELEEKDERIER 445
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2068700074 223 LENQLKEARFLAEEADRKYDEVA---RKLAMVEADLERAEERAETGESKIVELEE 274
Cdd:COG2433 446 LERELSEARSEERREIRKDREISrldREIERLERELEEERERIEELKRKLERLKE 500
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
174-278 |
3.42e-03 |
|
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein chain release factor RF1 is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439986 [Multi-domain] Cd Length: 356 Bit Score: 38.83 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 174 LEEDLERSEERLNTATTKLAEASQAADeSERMRKVL-ENRSLSD----EERMDALENQLKEAR-FLAEEADrkyDEVArk 247
Cdd:COG0216 2 MLDKLEALEERYEELEALLSDPEVISD-QKRFRKLSkEYAELEPiveaYREYKKLLEDIEEAKeLLEEESD---PEMR-- 75
|
90 100 110
....*....|....*....|....*....|.
gi 2068700074 248 lAMVEADLERAEERAEtgeskivELEEELRV 278
Cdd:COG0216 76 -EMAKEELEELEARLE-------ELEEELKI 98
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
158-339 |
3.89e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 158 KRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESErmrkvleNRSLSDEERMDALENQLKEARFLAEEA 237
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE-------GKNIKLSKDVSSLESQLQDTQELLQEE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 238 DRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEAR 317
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
170 180
....*....|....*....|..
gi 2068700074 318 AEFAERSVQKLQKEVDRLEDEL 339
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQEL 582
|
|
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
147-247 |
4.33e-03 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 38.79 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 147 NELHNI---MNVQLKRAEGEVAALNRRIQLLEEDLERSEErlntattklaeasqAADESERMRKVLEnRSLSD-EERMDA 222
Cdd:pfam02181 265 SELSHVkkaAKVNLEQLEKDVKQLERGLKKLERELELSAL--------------DEHPDDKFREVLK-EFLKSaEEKLDK 329
|
90 100
....*....|....*....|....*
gi 2068700074 223 LENQLKEARFLAEEADRKYDEVARK 247
Cdd:pfam02181 330 LESLLREALELFKELVEYFGEDPKE 354
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
217-339 |
4.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 217 EERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKI--VELEEELRVVGNNLKSLEVSE---E 291
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSddlA 688
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2068700074 292 KANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
167-312 |
5.64e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 38.54 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 167 LNRRIQLLEEDLERSEERLNTATTKLAEASQAADES-ERMRKVLENRSLSDEERMDALENQL-KEARFLAEEADrkydev 244
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELlLRERNQQRQEARREREELQREEERLvQKEEQLDARAE------ 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700074 245 arKLAMVEADLERAEERAETGESKIVELEEELRvvgnnlkslEVSEEKANQREEAYKEQI-KTLANKLK 312
Cdd:PRK12705 99 --KLDNLENQLEEREKALSARELELEELEKQLD---------NELYRVAGLTPEQARKLLlKLLDAELE 156
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
154-355 |
6.55e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 154 NVQLKRAE----GEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALE----- 224
Cdd:PTZ00121 1577 NMALRKAEeakkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkae 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 225 --NQLKEARFL-AEEADRKYDEVARKLAMVEADLERAEERAETGESKIVEL----EEELRVVGNNLKSLEVSEEKANQRE 297
Cdd:PTZ00121 1657 eeNKIKAAEEAkKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkkeAEEKKKAEELKKAEEENKIKAEEAK 1736
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700074 298 EAYKEQiKTLANKLKaaeaRAEFAERSVQKLQKEVDRLEDElvIQKERYKSITDELDQ 355
Cdd:PTZ00121 1737 KEAEED-KKKAEEAK----KDEEEKKKIAHLKKEEEKKAEE--IRKEKEAVIEEELDE 1787
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
161-336 |
6.76e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 38.34 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 161 EGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADEsermrkvlenrsLSDEERMDALENQLKEARFLAEEADRK 240
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE------------LSEEKDALLAQRAAHEARIRELEEDIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 241 ydEVARKLAMVEADLERAEERAETG--------------ESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKT 306
Cdd:pfam07888 140 --TLTQRVLERETELERMKERAKKAgaqrkeeeaerkqlQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
170 180 190
....*....|....*....|....*....|
gi 2068700074 307 LANKLKAAEARAEFAERSVQKLQKEVDRLE 336
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQERLN 247
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
156-359 |
6.95e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 38.41 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLEN---RSLSDEERMDALENQLKEARf 232
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAyltQKREAQEEQLKKQQLLKQLR- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 233 lAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQiktlanklk 312
Cdd:TIGR00618 267 -ARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ--------- 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068700074 313 aaEARAEFAERSVQKLQKEvdrlEDELVIQKERYKSITDELDQTFTE 359
Cdd:TIGR00618 337 --QSSIEEQRRLLQTLHSQ----EIHIRDAHEVATSIREISCQQHTL 377
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-349 |
7.79e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 176 EDLERSEERLNTATTKLAEASQAADE---SERMRKVLENRSLSD----EERMDALENQLKEARFLAEEADRKYDEVARKL 248
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADElkkAEELKKAEEKKKAEEakkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 249 AMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAyKEQIKTLANKLKAAEARAEFAERSVQKL 328
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
170 180
....*....|....*....|.
gi 2068700074 329 QKEVDRLEDELVIQKERYKSI 349
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKA 1704
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
156-280 |
8.52e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.14 E-value: 8.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNR--------RIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRslsdEERMDALENQL 227
Cdd:COG0542 419 RLEQLEIEKEALKKeqdeasfeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQR----YGKIPELEKEL 494
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 228 KEARFLAEEADRKY------DEVARKLA---------MVEADLEraeeraetgesKIVELEEEL--RVVG 280
Cdd:COG0542 495 AELEEELAELAPLLreevteEDIAEVVSrwtgipvgkLLEGERE-----------KLLNLEEELheRVIG 553
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-359 |
8.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.20 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 176 EDLERSEERLNTATTKLAEASQAADE---SERMRKVLENRSLSDEERMDAlENQLKEARFLAEEadRKYDEVaRKLAMVE 252
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEvrkAEELRKAEDARKAEAARKAEE-ERKAEEARKAEDA--KKAEAV-KKAEEAK 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 253 ADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERsvqKLQKEV 332
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEA---KKKAEE 1313
|
170 180
....*....|....*....|....*..
gi 2068700074 333 DRLEDELVIQKERYKSITDELDQTFTE 359
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEE 1340
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
156-355 |
8.71e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 38.10 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLEnrSLSDEERMDA----------LEN 225
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQM--ELKDVERKIAqqaaklqgsdLDR 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 226 QLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIK 305
Cdd:TIGR00606 823 TVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR 902
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068700074 306 TLANKLKAAEARAEFAERSVQKLQKEVDRLEDELVIQKERYKSITDELDQ 355
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
159-302 |
8.87e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 159 RAEGEVAALNRRIQLLEEDLERseerLNTATTKLAEASQAADESERMRKVLENRS-LSDE---------ERMDALENQLK 228
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIES----LERIRTLLAAIADAEDEIERLREKREALAeLNDErrerlaekrERKRELEAEFD 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700074 229 EARFLAEEADR-------------------KYDEVARKLAMVEADLERAEeraetgeskivELEEELRVVGNNLKSLEVS 289
Cdd:PRK02224 645 EARIEEAREDKeraeeyleqveekldelreERDDLQAEIGAVENELEELE-----------ELRERREALENRVEALEAL 713
|
170
....*....|...
gi 2068700074 290 EEKANQREEAYKE 302
Cdd:PRK02224 714 YDEAEELESMYGD 726
|
|
| |
