|
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 |
2.04e-78 |
|
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: 240.32 E-value: 2.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 160 AEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADR 239
Cdd:pfam00261 34 AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 240 KYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAE 319
Cdd:pfam00261 114 KYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAE 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068700071 320 FAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 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 |
1.63e-15 |
|
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: 72.72 E-value: 1.63e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700071 166 ALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEAR 231
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-361 |
9.60e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 9.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2068700071 316 ARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-361 |
2.45e-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: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2068700071 316 ARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-361 |
2.29e-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: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRvvgnNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2068700071 316 ARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-362 |
2.74e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALnrRIQLLEEDLERSEERLNTATTKLAEASQAADEsermrkvlenrslsDEERMDALENQLKEARFLAE 235
Cdd:COG1196 221 ELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAE--------------LEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068700071 316 ARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQN 362
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-361 |
4.06e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLA 234
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 235 EEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAA 314
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068700071 315 EARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-361 |
4.07e-12 |
|
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: 67.77 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 154 NVQLKRAEGEVAALNRRIQLLEEDLERS-------EERLNTATTKLAEASQAADESERMRKVLEnrslsdeERMDALENQ 226
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELrlevselEEEIEELQKELYALANEISRLEQQKQILR-------ERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 227 LKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKT 306
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700071 307 LANKLKAAEARAEFAERSVQKLQKEVDRLEDDLV-AEKDKSRMLQADMEATLQDIQ 361
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQ 453
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-351 |
4.14e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190
....*....|....*....|....*....|....*.
gi 2068700071 316 ARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQA 351
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-363 |
8.09e-12 |
|
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: 66.62 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMD-------ALENQLK 228
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAqlskeltELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 229 EARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLA 308
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068700071 309 NKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQNM 363
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-363 |
1.19e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2068700071 316 ARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQNM 363
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-336 |
7.67e-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: 57.37 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 146 KNELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALEN 225
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 226 QLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIV---------------------ELEEELRVVGNNLK 284
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEelsedieslaaeieeleelieELESELEALLNERA 883
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2068700071 285 SLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLE 336
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-312 |
1.48e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 169 RRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDE-ERMDALENQLKEARflaeeadRKYDEVARK 247
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLE-------RELEERERR 360
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700071 248 LAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEE----KANQREEAYKEQIKTLANKLK 312
Cdd:COG4913 361 RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELEAEIA 429
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-362 |
1.68e-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: 56.22 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 150 HNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKV-------LENRSLSDEERMDA 222
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElaeelaeLEEKLEELKEELES 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 223 LENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSL-----EVSEEKANQRE 297
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeieELLKKLEEAEL 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700071 298 EAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEAtLQDIQN 362
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-LERLQE 499
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-362 |
5.64e-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: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEedlerseeRLNTATTKLAEASQAADESERMRKVLenRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG4913 236 DLERAHEALEDAREQIELLE--------PIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRKYDEVARKLAMVEADLERAEE-RAETGESKIVELEEELRvvgnnlkSLEVSEEKANQREEAYKEQIKTLAnklkaa 314
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAqIRGNGGDRLEQLEREIE-------RLERELEERERRRARLEALLAALG------ 372
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2068700071 315 eARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQN 362
Cdd:COG4913 373 -LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-337 |
7.41e-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: 53.61 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEAR-FLA 234
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKeELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 235 EEADRKY-----------------DEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQRE 297
Cdd:COG4942 108 ELLRALYrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068700071 298 EAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLED 337
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-272 |
8.23e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA 758
|
90 100 110
....*....|....*....|....*....|....*..
gi 2068700071 236 EADRKYDEVARKLamvEADLERAEERAETGESKIVEL 272
Cdd:COG4913 759 LGDAVERELRENL---EERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-339 |
1.04e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRK-------YDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLA 308
Cdd:TIGR02168 870 ELESEleallneRASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
|
170 180 190
....*....|....*....|....*....|..
gi 2068700071 309 N-KLKAAEARAEFAERSVQKLQKEVDRLEDDL 339
Cdd:TIGR02168 950 SlTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-311 |
1.16e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAAD--ESERMRKVLENRSLSDEERMDALENQLKEARfl 233
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELR-- 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700071 234 aeEADRKYDEVARKLAMVEADLERAEER-AETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:COG4717 160 --ELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-361 |
1.17e-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: 52.84 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRKYDEVARKLAMVE-----------ADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQI 304
Cdd:COG4942 101 AQKEELAELLRALYRLGrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068700071 305 KTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-361 |
1.21e-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: 53.53 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 157 LKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARflAEE 236
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 237 ADRKYDEVARKLAMVEADLERAEERAEtgeskivELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEA 316
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLR-------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068700071 317 RAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-346 |
1.64e-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: 52.46 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE-SERMRKVLenRSLSDEERMDALENQLKEARFLA 234
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAqKEELAELL--RALYRLGRQPPLALLLSPEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 235 EEADRKYDEvarklAMVEADLERAEE---RAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:COG4942 134 AVRRLQYLK-----YLAPARREQAEElraDLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
170 180 190
....*....|....*....|....*....|....*
gi 2068700071 312 KAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKS 346
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-351 |
3.87e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 138 TMMKF--SIIKNELHNIMNvQLKRAEGEVAALN-RRIQLLEEDLERSEERlntaTTKLAEASQAADESERMRKVLENRSL 214
Cdd:COG4717 38 TLLAFirAMLLERLEKEAD-ELFKPQGRKPELNlKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 215 SDEERMDALENQLKearflAEEADRKYDEVARKLAMVEADLERAEERAETgeskIVELEEELRVVGNNLKSLEVS-EEKA 293
Cdd:COG4717 113 ELREELEKLEKLLQ-----LLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEElEELL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700071 294 NQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQA 351
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-340 |
5.93e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 169 RRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALEnqlkearfLAEEADRKYDEVAR-- 246
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--------AEREIAELEAELERld 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 247 ----KLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAY-----KEQIKTLANKLKAAEAR 317
Cdd:COG4913 682 assdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarLELRALLEERFAAALGD 761
|
170 180
....*....|....*....|....*....
gi 2068700071 318 AEFAE------RSVQKLQKEVDRLEDDLV 340
Cdd:COG4913 762 AVERElrenleERIDALRARLNRAEEELE 790
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-310 |
9.71e-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: 50.15 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 147 NELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERL-----------NTATTKLAEASQAADESERMRKVLENRSLS 215
Cdd:COG4942 68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaellralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 216 DEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQ 295
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
170
....*....|....*
gi 2068700071 296 REEAYKEQIKTLANK 310
Cdd:COG4942 228 LIARLEAEAAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
154-356 |
9.85e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 154 NVQLKRAEGEVAA--LNRRIQLLEEDLERSEERLNtattKLAEASQAADesermrkvLENRSLSDEERMDALENQLKEAR 231
Cdd:COG3206 165 NLELRREEARKALefLEEQLPELRKELEEAEAALE----EFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 232 FLAEEADRKYDEVARKLAM---------------------VEADLERAEERAETGES--KIVELEEELRVVGNNLK---- 284
Cdd:COG3206 233 AELAEAEARLAALRAQLGSgpdalpellqspviqqlraqlAELEAELAELSARYTPNhpDVIALRAQIAALRAQLQqeaq 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700071 285 ----SLEVSEEKANQREEAYKEQIKTLANKLKaaearaefaerSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEAT 356
Cdd:COG3206 313 rilaSLEAELEALQAREASLQAQLAQLEARLA-----------ELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
145-361 |
1.04e-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: 50.84 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 145 IKNELHNImNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALE 224
Cdd:TIGR02169 292 VKEKIGEL-EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 225 NQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQI 304
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2068700071 305 KTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLvaeKDKSRMLqADMEATLQDIQ 361
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL---SKLQREL-AEAEAQARASE 503
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-312 |
3.13e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 145 IKNELHNIMNVQLKRAEGEVAALNRRIQLLEE------DLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEE 218
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 219 RMDALENQLKEARFlaEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSeEKANQREE 298
Cdd:PRK03918 648 ELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL-EKALERVE 724
|
170
....*....|....
gi 2068700071 299 AYKEQIKTLANKLK 312
Cdd:PRK03918 725 ELREKVKKYKALLK 738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
152-341 |
3.20e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 152 IMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEAR 231
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 232 FLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
170 180 190
....*....|....*....|....*....|....*.
gi 2068700071 312 K------AAEARAEFAERSVQKLQKEVDRLEDDLVA 341
Cdd:TIGR02169 934 SeiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
164-361 |
3.77e-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: 48.91 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 164 VAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMR-KVLENRSLSDEER----------MDALENQLKEARF 232
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREReKAERYQALLKEKReyegyellkeKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 233 LAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVEL-EEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068700071 312 KAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-361 |
4.04e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 188 ATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGES 267
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 268 KIVELEEELRVVGNNLKSLEVSEEKANQRE---------------------EAYKEQIKTLANKLKAAEARAEFAERSVQ 326
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2068700071 327 KLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-362 |
6.61e-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: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 170 RIQLLEEDLERSEERLnTATTKLAEASQA--ADESERMRKVLENRSLSDEERMDALENQLKEARflaeeadRKYDEVARK 247
Cdd:TIGR02168 190 RLEDILNELERQLKSL-ERQAEKAERYKElkAELRELELALLVLRLEELREELEELQEELKEAE-------EELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 248 LAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQK 327
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190
....*....|....*....|....*....|....*...
gi 2068700071 328 LQKEVDRLE---DDLVAEKDKSRMLQADMEATLQDIQN 362
Cdd:TIGR02168 342 LEEKLEELKeelESLEAELEELEAELEELESRLEELEE 379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
217-361 |
6.70e-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: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 217 EERMDALENQ---LKEARFLAEEADR--------KYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKS 285
Cdd:COG1196 199 ERQLEPLERQaekAERYRELKEELKEleaellllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700071 286 LEVSEEKANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-305 |
9.05e-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: 47.74 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 148 ELHNIMNVQLKRAEGEVAALNRRIQLLEEDLE---------RSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEe 218
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLEtlrskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 219 rmdALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREE 298
Cdd:TIGR02168 430 ---LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
....*..
gi 2068700071 299 AYKEQIK 305
Cdd:TIGR02168 507 GVKALLK 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-339 |
1.08e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 170 RIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSdEERMDALENQLKEARFLAEEADRKYDEVARKLA 249
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL-EELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 250 MVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEaYKEQIKTLANKLKAAEARAEFAERSVQKLQ 329
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREALAELNDERRERLAEKR 633
|
170
....*....|
gi 2068700071 330 KEVDRLEDDL 339
Cdd:PRK02224 634 ERKRELEAEF 643
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
155-347 |
1.18e-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: 46.07 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARfla 234
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 235 eeadrkydeVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAA 314
Cdd:COG1579 87 ---------NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180 190
....*....|....*....|....*....|...
gi 2068700071 315 EARAEfaersvQKLQKEVDRLEDDLVAEKDKSR 347
Cdd:COG1579 158 LEELE------AEREELAAKIPPELLALYERIR 184
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-362 |
1.20e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERM----RKVLENRSLSDEERmDALENQLKEAR 231
Cdd:PRK02224 207 RLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLeaeiEDLRETIAETERER-EELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 232 FLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVV-------GNNLKSLEVSEEKANQREEAYKEQI 304
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrvaaqahNEEAESLREDADDLEERAEELREEA 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700071 305 KTLANKLKAAEARAEFAERSVQKLQKEVDRLE-----------------DDLVAEKDKSRMLQADMEATLQDIQN 362
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRerfgdapvdlgnaedflEELREERDELREREAELEATLRTARE 440
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
156-346 |
1.60e-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: 46.74 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDlerseerLNTATTKLAEASQAADESERMRKVL-ENRSLSDEERMDALENQLKEARFLA 234
Cdd:pfam10174 409 QLRDKDKQLAGLKERVKSLQTD-------SSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 235 EEADRKYDEVARKLAMVEADLERAEERAETG---ESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKtLANKL 311
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGlkkDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPE-INDRI 560
|
170 180 190
....*....|....*....|....*....|....*.
gi 2068700071 312 KAAEARAEFAERSVQKLQKEVDRLEDDLV-AEKDKS 346
Cdd:pfam10174 561 RLLEQEVARYKEESGKAQAEVERLLGILReVENEKN 596
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
164-363 |
3.12e-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: 45.53 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 164 VAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDE 243
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 244 VARKLAMVEADLER----AEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAE 319
Cdd:COG4942 95 LRAELEAQKEELAEllraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2068700071 320 FAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQNM 363
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
156-311 |
3.65e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLL----------------EEDLERSEERLNTATtKLAEASQAA----DESE--------RMRK 207
Cdd:COG0497 173 ELEELRADEAERARELDLLrfqleeleaaalqpgeEEELEEERRRLSNAE-KLREALQEAlealSGGEggaldllgQALR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 208 VLENRSlSDEERMDALENQLKEARFLAEEAdrkYDEVARKLAMVEAD---LERAEER------------------AETGE 266
Cdd:COG0497 252 ALERLA-EYDPSLAELAERLESALIELEEA---ASELRRYLDSLEFDperLEEVEERlallrrlarkygvtveelLAYAE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068700071 267 skivELEEELrvvgNNLKSLEVSEEKANQREEAYKEQIKTLANKL 311
Cdd:COG0497 328 ----ELRAEL----AELENSDERLEELEAELAEAEAELLEAAEKL 364
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
214-362 |
4.87e-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: 45.43 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 214 LSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKA 293
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700071 294 NQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQN 362
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-362 |
6.71e-05 |
|
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: 45.06 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 158 KRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENrslsDEERMDALENQLKEarfLAEEA 237
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK----EIEQLEQEEEKLKE---RLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 238 DRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELrvvgNNLKSlEVSEEKANQREEAYKEQIKTLanklKAAEAR 317
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL----NDLEA-RLSHSRIPEIQAELSKLEEEV----SRIEAR 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068700071 318 AEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQN 362
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-355 |
9.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNR------RIQLLEE---DLERSEERLNTATTKLAEASQAADESE----RMRKVLENRSLSDEERmdA 222
Cdd:PRK03918 430 ELKKAKGKCPVCGRelteehRKELLEEytaELKRIEKELKEIEEKERKLRKELRELEkvlkKESELIKLKELAEQLK--E 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 223 LENQLKEARF-LAEEADRKYDEVARKLAMVEADLERAEERAETG----------ESKIVELEEELRVVGNNL-----KSL 286
Cdd:PRK03918 508 LEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelkkklaelEKKLDELEEELAELLKELeelgfESV 587
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700071 287 EVSEEKANQREEAYKEQIKtlankLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEA 355
Cdd:PRK03918 588 EELEERLKELEPFYNEYLE-----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
159-275 |
9.54e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 159 RAEGEVAALNRRIQLLEEDLERseerLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEAD 238
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIES----LERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
90 100 110
....*....|....*....|....*....|....*..
gi 2068700071 239 RKYDEVARklamveADLERAEERAETGESKIVELEEE 275
Cdd:PRK02224 645 EARIEEAR------EDKERAEEYLEQVEEKLDELREE 675
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
153-307 |
1.08e-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: 44.28 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 153 MNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARF 232
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 233 --------LAEEADRKYDEVARKLAMVEADLERAEERaetgeskIVELEEELRVVGN-NLKSLEVSEEKaNQREEAYKEQ 303
Cdd:TIGR02168 937 ridnlqerLSEEYSLTLEEAEALENKIEDDEEEARRR-------LKRLENKIKELGPvNLAAIEEYEEL-KERYDFLTAQ 1008
|
....
gi 2068700071 304 IKTL 307
Cdd:TIGR02168 1009 KEDL 1012
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-337 |
1.90e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 145 IKNELHNIMNVQLKRAEGEVAALNRRIQLLEED---LERSEERLNTATTKLAEASQAADESERMRKVLENRSLS------ 215
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesv 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 216 --DEERMDALE------NQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVEL-----EEELRVVGNn 282
Cdd:PRK03918 588 eeLEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkysEEEYEELRE- 666
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 283 lKSLEVSEEKANQRE-----EAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLED 337
Cdd:PRK03918 667 -EYLELSRELAGLRAeleelEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
132-356 |
2.51e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 132 SIFSS-NTMMKfSIIK--NELHNIMNVQLKRAEGEVAALNRRIQLLEE-DLERSEERLNTATTKLAEASQAADESERMRK 207
Cdd:PHA02562 163 SVLSEmDKLNK-DKIRelNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkNGENIARKQNKYDELVEEAKTIKAEIEELTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 208 VLENRSLSDEERMDALeNQLKEARFLAEEadrKYDEVARKLAMVE---------ADLERAEERAETGESKIVELEEELRv 278
Cdd:PHA02562 242 ELLNLVMDIEDPSAAL-NKLNTAAAKIKS---KIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLE- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 279 vgnnlkSLEVSEEKANQREEAYKEQIKT---LANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEA 355
Cdd:PHA02562 317 ------KLDTAIDELEEIMDEFNEQSKKlleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
.
gi 2068700071 356 T 356
Cdd:PHA02562 391 I 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
156-347 |
2.87e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAE 315
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190
....*....|....*....|....*....|..
gi 2068700071 316 ARAEFAERSVQKLQKEVDRLEDDLVAEKDKSR 347
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
166-277 |
3.46e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.71 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 166 ALNRRIQLLEEDLERSEERLNTATTKLAEA----SQAADESERMRKVLENRSlsdeermdalenqlKEARflAEEADRKY 241
Cdd:PRK07352 47 ILEERREAILQALKEAEERLRQAAQALAEAqqklAQAQQEAERIRADAKARA--------------EAIR--AEIEKQAI 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2068700071 242 DEVARKLAMVEADLERAEERA------ETGESKIVELEEELR 277
Cdd:PRK07352 111 EDMARLKQTAAADLSAEQERViaqlrrEAAELAIAKAESQLP 152
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-307 |
3.93e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 159 RAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEAD 238
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068700071 239 RKYDEVARKLAM----VEADLERAEERAEtgeskivELEEELRVVGN-NLKSLEVSEEkANQREEAYKEQIKTL 307
Cdd:COG1196 742 LEEEELLEEEALeelpEPPDLEELERELE-------RLEREIEALGPvNLLAIEEYEE-LEERYDFLSEQREDL 807
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
167-355 |
4.31e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 167 LNRRIQLLEEDLERSE---ERLNTATTKLAEASQAADE-SERMRKVlenrslsdEERMDALENQLKEARFLAEEadrkYD 242
Cdd:PRK03918 174 IKRRIERLEKFIKRTEnieELIKEKEKELEEVLREINEiSSELPEL--------REELEKLEKEVKELEELKEE----IE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 243 EVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREE--AYKEQIKTLANKLKAAEARAEF 320
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190
....*....|....*....|....*....|....*
gi 2068700071 321 AERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEA 355
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEE 356
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
156-324 |
5.21e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE-----SERMRK-------------VLENRSLSDE 217
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelGERARAlyrsggsvsyldvLLGSESFSDF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 218 -ERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQR 296
Cdd:COG3883 118 lDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
|
170 180
....*....|....*....|....*...
gi 2068700071 297 EEAYKEQIKTLANKLKAAEARAEFAERS 324
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-336 |
5.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 141 KFSIIKNELHNIMNVqLKRAEGEVAALNRRIqlleEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERM 220
Cdd:PRK03918 201 ELEEVLREINEISSE-LPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 221 DALENQLKEARFLAEEADRK------YDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAN 294
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068700071 295 QREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLE 336
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
|
| 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 2068700071 174 LEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDAL-ENQLKEARFLAEEADRKYDEVARKLamve 252
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLlEEAEKEAQQAIKEAKKEADEIIKEL---- 593
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2068700071 253 adleRAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKE 302
Cdd:PRK00409 594 ----RQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
155-266 |
6.43e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLA 234
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
90 100 110
....*....|....*....|....*....|..
gi 2068700071 235 EEADRKYDEVARKLAMVEADLERAEERAETGE 266
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAE 446
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
158-354 |
7.54e-04 |
|
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: 41.70 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 158 KRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESErmrkvleNRSLSDEERMDALENQLKEARFLAEEA 237
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE-------GKNIKLSKDVSSLESQLQDTQELLQEE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 238 DRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEAR 317
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068700071 318 AEFAERSVQKLQKEVDRLE---DDLVAEKDKSRMLQADME 354
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQqelDDLLVDLDHQRQLVSNLE 600
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
163-350 |
1.28e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 163 EVAALNRRIQLLEEDLERSEERLNTATT--------------------KLAEASQAADESERMRKVLENRSLSDEERMDA 222
Cdd:PRK04863 315 ELAELNEAESDLEQDYQAASDHLNLVQTalrqqekieryqadleeleeRLEEQNEVVEEADEQQEENEARAEAAEEEVDE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 223 LENQL---------KEARFLA-EEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKsleVSEEK 292
Cdd:PRK04863 395 LKSQLadyqqaldvQQTRAIQyQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS---VAQAA 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700071 293 ANQREEAYK-----------EQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQ 350
Cdd:PRK04863 472 HSQFEQAYQlvrkiagevsrSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLA 540
|
|
| 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 2068700071 200 DESERMRKVLEnrSLSDEERmdALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAE-TGESKIVELEEELRV 278
Cdd:PRK00409 513 EDKEKLNELIA--SLEELER--ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADE 588
|
90 100 110
....*....|....*....|....*....|....
gi 2068700071 279 VGNNLKSLEvSEEKANQREEAYKEQIKTLANKLK 312
Cdd:PRK00409 589 IIKELRQLQ-KGGYASVKAHELIEARKRLNKANE 621
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-362 |
1.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 172 QLLEEDLERSEERLNTATTKLAE-ASQAADESERMRKVLENRslsdEERMDALENQLKEARFLAEEADRKYDEVARKLAM 250
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPElNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 251 VEADLERAEERAEtgeskIVELEEELRVVGNNLKSLEVSEEKANQREEAY---KEQIKTLANKLKAAEARAEFAERS-VQ 326
Cdd:COG4717 121 LEKLLQLLPLYQE-----LEALEAELAELPERLEELEERLEELRELEEELeelEAELAELQEELEELLEQLSLATEEeLQ 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 2068700071 327 KLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQN 362
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
145-312 |
1.79e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 145 IKNELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERS-------EERLNTATTKLAEASQAADE-SERMRKVLENRSLSD 216
Cdd:PRK04778 265 IDENLALLEELDLDEAEEKNEEIQERIDQLYDILEREvkarkyvEKNSDTLPDFLEHAKEQNKElKEEIDRVKQSYTLNE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 217 EE--RMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELrvvgnnlKSLEVSEEKAN 294
Cdd:PRK04778 345 SEleSVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEML-------QGLRKDELEAR 417
|
170
....*....|....*...
gi 2068700071 295 QREEAYKEQIKTLANKLK 312
Cdd:PRK04778 418 EKLERYRNKLHEIKRYLE 435
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
150-358 |
2.44e-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: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 150 HNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTAT---TKLAeASQAADESERMRKVLENRSL-------SDEER 219
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVrekTSLS-ASVASLEKQLLELTRVNELLkakfsedGTQKK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 220 MDALENQLKEARflaEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVvgnnLKSLEVSEEKANQREEA 299
Cdd:pfam15905 154 MSSLSMELMKLR---NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVS----TEKEKIEEKSETEKLLE 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700071 300 YKEQIKTLANKlkaaearaefaersVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQ 358
Cdd:pfam15905 227 YITELSCVSEQ--------------VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQ 271
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
152-278 |
2.77e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 152 IMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAE--ASQAADESERMR-----KVLENRSLSDEERMDALE 224
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANlrASLSAAEAERSRlqallAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068700071 225 NQLKEARFLAEEADRKYD----EVA---RKLAMVEADLERAEERAETGESKIVELEEELRV 278
Cdd:PRK09039 123 QELDSEKQVSARALAQVEllnqQIAalrRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
162-274 |
2.83e-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: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 162 GEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQA------ADESERMRK-------------VLENRSLSDEERMDA 222
Cdd:COG2433 366 DEVKARVIRGLSIEEALEELIEKELPEEEPEAEREKEheerelTEEEEEIRRleeqverleaeveELEAELEEKDERIER 445
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2068700071 223 LENQLKEARFLAEEADRKYDEVA---RKLAMVEADLERAEERAETGESKIVELEE 274
Cdd:COG2433 446 LERELSEARSEERREIRKDREISrldREIERLERELEEERERIEELKRKLERLKE 500
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-336 |
3.12e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 156 QLKRAEGEVAALNRRiqLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAE 235
Cdd:PTZ00121 1198 DARKAEAARKAEEER--KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 236 EAdRKYDEVARKLAMVEAD-LERAEERAETGESKIVELE----EELRVVGNNLK----SLEVSEEKANQREEAYKEQIKT 306
Cdd:PTZ00121 1276 EA-RKADELKKAEEKKKADeAKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKkkadAAKKKAEEAKKAAEAAKAEAEA 1354
|
170 180 190
....*....|....*....|....*....|
gi 2068700071 307 LANKLKAAEARAEFAERSVQKLQKEVDRLE 336
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
163-301 |
3.69e-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: 39.55 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 163 EVAALNRRIQLLEEDLERSEERLN--------------------TATTKLAEASQAADESERMRKVLENRSLSDEERMDA 222
Cdd:COG3096 314 ELEELSARESDLEQDYQAASDHLNlvqtalrqqekieryqedleELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 223 LENQL---------KEARFLA-EEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRvvgNNLKSLEVSEEK 292
Cdd:COG3096 394 LKSQLadyqqaldvQQTRAIQyQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVL---ELEQKLSVADAA 470
|
....*....
gi 2068700071 293 ANQREEAYK 301
Cdd:COG3096 471 RRQFEKAYE 479
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
174-278 |
3.74e-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: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 174 LEEDLERSEERLNTATTKLAEASQAADeSERMRKVL-ENRSLSD----EERMDALENQLKEAR-FLAEEADrkyDEVArk 247
Cdd:COG0216 2 MLDKLEALEERYEELEALLSDPEVISD-QKRFRKLSkEYAELEPiveaYREYKKLLEDIEEAKeLLEEESD---PEMR-- 75
|
90 100 110
....*....|....*....|....*....|.
gi 2068700071 248 lAMVEADLERAEERAEtgeskivELEEELRV 278
Cdd:COG0216 76 -EMAKEELEELEARLE-------ELEEELKI 98
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
146-362 |
3.90e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 146 KNELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEE-RLNTATTKLAEASQAADESERMRKVLENRSLSDEERMdale 224
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK---- 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 225 nqlkearflAEEADRKYDEVARKLAMVEADLERAEERAEtgesKIVELEEELRVVGNNLKSLEvsEEKANQREEAYKEQI 304
Cdd:PTZ00121 1690 ---------AAEALKKEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEA--EEDKKKAEEAKKDEE 1754
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700071 305 KTlaNKLKAAEARAEFAERSVQKLQKEVdrLEDDLVAEKDKSRMlqaDMEATLQDIQN 362
Cdd:PTZ00121 1755 EK--KKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRM---EVDKKIKDIFD 1805
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
217-360 |
4.02e-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: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 217 EERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKI--VELEEELRVVGNNLKSLEVSE---E 291
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSddlA 688
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 292 KANQREEAYKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLV-AEKDKSRMLQADMEATLQDI 360
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaAEDLARLELRALLEERFAAA 758
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-307 |
4.19e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 157 LKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARF---- 232
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkine 438
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2068700071 233 LAEEADRKYDEVA---RKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTL 307
Cdd:TIGR02169 439 LEEEKEDKALEIKkqeWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL 516
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
161-360 |
4.52e-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: 38.72 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 161 EGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADEsermrkvlenrsLSDEERMDALENQLKEARFLAEEADRK 240
Cdd:pfam07888 72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE------------LSEEKDALLAQRAAHEARIRELEEDIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 241 ydEVARKLAMVEADLERAEERAETgeskiveleeelrvVGNNLKSLEVSEEKANQREEAYKEQIKTLANKLKAAEARAEF 320
Cdd:pfam07888 140 --TLTQRVLERETELERMKERAKK--------------AGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQ 203
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068700071 321 AERSVQKLQKEVDRLEDDLVAEKDKsrmlQADMEATLQDI 360
Cdd:pfam07888 204 RDTQVLQLQDTITTLTQKLTTAHRK----EAENEALLEEL 239
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
243-362 |
4.55e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 38.97 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 243 EVARKLAMVEADLERAEERAETGESK----IVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTL-ANKLKAAEAR 317
Cdd:COG1193 490 EIARRLGLPEEIIERARELLGEESIDveklIEELERERRELEEEREEAERLREELEKLREELEEKLEELeEEKEEILEKA 569
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2068700071 318 AEFAERSVQKLQKEVDRLEDDL---VAEKDKSRMLQADMEATLQDIQN 362
Cdd:COG1193 570 REEAEEILREARKEAEELIRELreaQAEEEELKEARKKLEELKQELEE 617
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-339 |
4.56e-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: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 163 EVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARflaEEADRKYD 242
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE---AELEELAE 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 243 EVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQiktlankLKAAEARAEFAE 322
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL-------LEEEALEELPEP 759
|
170
....*....|....*..
gi 2068700071 323 RSVQKLQKEVDRLEDDL 339
Cdd:COG1196 760 PDLEELERELERLEREI 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-347 |
4.97e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 176 EDLERSEERLNTATTKLAEASQAADE---SERMRKVLENRSLSD----EERMDALENQLKEARFLAEEADRKYDEVARKL 248
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADElkkAEELKKAEEKKKAEEakkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 249 AMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAyKEQIKTLANKLKAAEARAEFAERSVQKL 328
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
170
....*....|....*....
gi 2068700071 329 QKEVDRLEDDLVAEKDKSR 347
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAK 1702
|
|
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
147-247 |
4.98e-03 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 38.41 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 147 NELHNI---MNVQLKRAEGEVAALNRRIQLLEEDLERSEErlntattklaeasqAADESERMRKVLEnRSLSD-EERMDA 222
Cdd:pfam02181 265 SELSHVkkaAKVNLEQLEKDVKQLERGLKKLERELELSAL--------------DEHPDDKFREVLK-EFLKSaEEKLDK 329
|
90 100
....*....|....*....|....*
gi 2068700071 223 LENQLKEARFLAEEADRKYDEVARK 247
Cdd:pfam02181 330 LESLLREALELFKELVEYFGEDPKE 354
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
167-312 |
6.05e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 38.54 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 167 LNRRIQLLEEDLERSEERLNTATTKLAEASQAADES-ERMRKVLENRSLSDEERMDALENQL-KEARFLAEEADrkydev 244
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELlLRERNQQRQEARREREELQREEERLvQKEEQLDARAE------ 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700071 245 arKLAMVEADLERAEERAETGESKIVELEEELRvvgnnlkslEVSEEKANQREEAYKEQI-KTLANKLK 312
Cdd:PRK12705 99 --KLDNLENQLEEREKALSARELELEELEKQLD---------NELYRVAGLTPEQARKLLlKLLDAELE 156
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-280 |
6.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 162 GEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESE----RMRKVLENRSLSDEERMDALENQLKEARFLAEEA 237
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2068700071 238 DRKYDEVARKLAMVE-------ADLE--RAEERAETGESkivelEEELRVVG 280
Cdd:COG4913 418 RRELRELEAEIASLErrksnipARLLalRDALAEALGLD-----EAELPFVG 464
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-362 |
6.83e-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: 38.46 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 145 IKNELHNIMNvQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAAD--ESERMRKVLENRSLsdEERMDA 222
Cdd:TIGR04523 319 QEKKLEEIQN-QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEklKKENQSYKQEIKNL--ESQIND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 223 LENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKE 302
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSR 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2068700071 303 QIKTLANKLKAAEARAEFAERSVQKLQKEVDRLE---DDLVAEKDKSRMLQADMEATLQDIQN 362
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKKLNEEKKELEekvKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
154-361 |
9.00e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.01 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 154 NVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADES--------------ERMRKVLENRSLSDE-- 217
Cdd:COG3096 360 TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqalEKARALCGLPDLTPEna 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700071 218 ----ERMDALENQLKEARF-------LAEEADRKYDEVARKLAMVEADLERaEERAETGESKIVELeEELRVVGNNLKSL 286
Cdd:COG3096 440 edylAAFRAKEQQATEEVLeleqklsVADAARRQFEKAYELVCKIAGEVER-SQAWQTARELLRRY-RSQQALAQRLQQL 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700071 287 EVS----EEKANQREEAyKEQIKTLANKLKAAEARAEFAERSVQKLQKEVDRLEDDLVAEKDKSRMLQADMEATLQDIQ 361
Cdd:COG3096 518 RAQlaelEQRLRQQQNA-ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
|
|
| |
