|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
12-246 |
3.65e-65 |
|
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: 202.18 E-value: 3.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 12 RKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 92 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTL 171
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393141 172 QASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSELN 246
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-230 |
2.12e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 6 SIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALD 165
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393141 166 QTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEE 230
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-245 |
2.73e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 12 RKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 92 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTL 171
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41393141 172 QASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSEL 245
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-247 |
4.97e-13 |
|
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: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQ 166
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 167 TLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSELN 246
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
.
gi 41393141 247 S 247
Cdd:COG1196 488 E 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-230 |
4.92e-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: 65.46 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 5 NSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 85 DESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRAL 164
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41393141 165 DQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEE 230
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-245 |
4.99e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQ-------LVEEELDRAQERLATALQKLEE 79
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqaeeyELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 80 AEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEE 159
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 160 ELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLD 239
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
....*.
gi 41393141 240 QTLSEL 245
Cdd:COG1196 474 LLEAAL 479
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-248 |
6.30e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQ 166
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 167 TLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSELN 246
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
..
gi 41393141 247 SF 248
Cdd:COG1196 502 DY 503
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
5-116 |
1.49e-11 |
|
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: 60.40 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 5 NSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEaevaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:pfam12718 35 QEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKA 110
|
90 100 110
....*....|....*....|....*....|..
gi 41393141 85 DESERGMKVIENRALKDEEKMELQEIQLKEAK 116
Cdd:pfam12718 111 EHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-248 |
1.10e-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: 58.14 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 3 GSNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNR---------------------------- 54
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqisalrkdlarleaeveqlee 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 55 RIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLV 134
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 135 IVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLE 214
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260 270
....*....|....*....|....*....|....
gi 41393141 215 KTIDDLEEKLRDAKEENIKIHATLDQTLSELNSF 248
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-245 |
2.14e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 20 QADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAL 99
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 100 KDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQASEEKYS 179
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41393141 180 QKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSEL 245
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-226 |
3.59e-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: 56.60 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 4 SNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 84 ADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRA 163
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41393141 164 LDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRD 226
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-230 |
1.43e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 1 MAGSNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 81 EKAADESErgmKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEE 160
Cdd:COG4942 96 RAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 161 LRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEE 230
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-234 |
3.39e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 11 KRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 91 MKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQtLKT 170
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-LKK 1640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41393141 171 LQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKI 234
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-210 |
5.46e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 6 SIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALD 165
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41393141 166 QTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSV 210
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
13-240 |
1.15e-07 |
|
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: 52.26 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 13 KIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAevaslnrRIQLVEEELDRAQERLA-----------------TALQ 75
Cdd:COG3096 348 KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEA-------RLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqQAVQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 76 KLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKH---IAEEADRKYEEVARKLVIVEGELERteerAELAES 152
Cdd:COG3096 421 ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsVADAARRQFEKAYELVCKIAGEVER----SQAWQT 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 153 HVKQMEE--ELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTD---KLKEAETRAEFAERSVAKLEKTIDDLEEKLRDA 227
Cdd:COG3096 497 ARELLRRyrSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfcqRIGQQLDAAEELEELLAELEAQLEELEEQAAEA 576
|
250
....*....|...
gi 41393141 228 KEENIKIHATLDQ 240
Cdd:COG3096 577 VEQRSELRQQLEQ 589
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-233 |
1.51e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 13 KIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEaekaadesergmk 92
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR------------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 93 vIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQ 172
Cdd:TIGR02168 300 -LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41393141 173 ASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIK 233
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-215 |
2.57e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 87 SERGmkviENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQ 166
Cdd:COG1196 391 ALRA----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 41393141 167 TLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEK 215
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-233 |
3.93e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 11 KRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESErg 90
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-- 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 91 mKVIENRALKDEEKMELQEIQLK-EAKHIAEEADRKYEEVARKlviveGELERTEERAELAESHVKQMEEELRALDQTLK 169
Cdd:PTZ00121 1392 -KADEAKKKAEEDKKKADELKKAaAAKKKADEAKKKAEEKKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41393141 170 TLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAeRSVAKLEKTIDDLEEKLRDAKEENIK 233
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA-KKAAEAKKKADEAKKAEEAKKADEAK 1528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-225 |
5.14e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 4 SNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 84 ADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAEShvKQMEEELRA 163
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKE 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41393141 164 LDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLR 225
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-204 |
5.76e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 11 KRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELD--RAQERLATALQKLEEAEKAADESE 88
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvaSAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 89 rgmkvienralkdeekmELQEiQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRA----- 163
Cdd:COG4913 689 -----------------ALEE-QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelral 750
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41393141 164 LDQTLKTLQAsEEKYSQKEDKYEEEIKILTDKLKEAETRAE 204
Cdd:COG4913 751 LEERFAAALG-DAVERELRENLEERIDALRARLNRAEEELE 790
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-229 |
7.11e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 8 DAVKRKIKVLQQQADEAEE-RAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEAdRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRAlDQ 166
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA-RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA-DE 1319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41393141 167 TLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKE 229
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
9-199 |
1.66e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 48.53 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 9 AVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEaEVASLNRRIQLVE--EELdraQERLATALQKLEEAEKAADE 86
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAALQPG-EEEELEEERRRLSnaEKL---REALQEALEALSGGEGGALD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 87 S-ERGMKVIENRALKDEEKMELQEiQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEER---------------AELA 150
Cdd:COG0497 245 LlGQALRALERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFDPERLEEVEERlallrrlarkygvtvEELL 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 41393141 151 ESHvKQMEEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEA 199
Cdd:COG0497 324 AYA-EELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-240 |
1.77e-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: 48.53 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 10 VKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESER 89
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 90 GMKviENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLK 169
Cdd:TIGR02169 759 ELK--ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41393141 170 TLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSV-------AKLEKTIDDLEEKLRDAKEENIKIHATLDQ 240
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrdlesrlGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-247 |
2.98e-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: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 12 RKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEaevaslnrRIQLVEEELDRAQERLAtaLQKLEEAEKAADESERGM 91
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPLERQAEKAE--------RYRELKEELKELEAELL--LLKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 92 KVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTL 171
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41393141 172 QASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSELNS 247
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-247 |
5.63e-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: 46.97 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 10 VKRKIKVLQQQAdeaeERAEILQRQVEEEKrareqaEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESEr 89
Cdd:TIGR02168 198 LERQLKSLERQA----EKAERYKELKAELR------ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELE- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 90 gmkvienralkdeEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLK 169
Cdd:TIGR02168 267 -------------EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41393141 170 TLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSELNS 247
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
17-230 |
9.34e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 17 LQQQADEAEERAEILQRQVEEEKRAREQAEAEVA---------SLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 88 ERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEAD--RKYEEVARKLVIVEGELERTEERAElaeshvKQMEEELRALD 165
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsARYTPNHPDVIALRAQIAALRAQLQ------QEAQRILASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393141 166 QTLKTLQASEEKYSQKEDKYEEEIKiltdKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEE 230
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLA----ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-192 |
9.66e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 9.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQ---QQADEAEERAEILQRQVEEEKRAR-EQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEK 82
Cdd:COG4913 244 LEDAREQIELLEpirELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 83 AADESERgmkVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKL-VIVEGELERTEERAELAESHVKQMEEEL 161
Cdd:COG4913 324 ELDELEA---QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALgLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|.
gi 41393141 162 RALDQTLKTLQASEEKYSQKEDKYEEEIKIL 192
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-222 |
1.19e-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: 46.20 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 87 SERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEER--------AELAESHVKQME 158
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlseeysltLEEAEALENKIE 964
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41393141 159 EELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEE 222
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-230 |
2.03e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 19 QQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRA 98
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 99 LKDEE---KMELQEIQLKEAKHIAEEADRKYEEVAR---KLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQ 172
Cdd:PTZ00121 1647 KKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKaeeDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 41393141 173 ASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEE 230
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-229 |
2.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 8 DAVKRKIKVLQQQADEAEERAEILQ-----RQVEEEKRAREQAEAEVASLNRRIQLVEE-----ELDRAQE-RLATALQK 76
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKkadeaKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkadELKKAEElKKAEEKKK 1565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 77 LEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKL--VIVEGELERTEERAELAESHV 154
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeeLKKAEEEKKKVEQLKKKEAEE 1645
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393141 155 KQMEEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKE 229
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
20-173 |
2.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 20 QADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATA-LQKLEEAEKAADESERGMKVIENRA 98
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRR 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393141 99 LKDEEKmeLQEIQLkEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQA 173
Cdd:COG4913 362 ARLEAL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-247 |
4.55e-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: 44.29 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 4 SNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQ-LVEEELDRAQERLATALQKLEEAEK 82
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 83 AADESERGMKVIENRALKDEEKMELQEIQLKE-AKHIAEEADRK------YEEVARKLVIVEGELERTEERAELAESHVK 155
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEElEREIEEERKRRdklteeYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 156 QMEEELRA-------LDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAK 228
Cdd:TIGR02169 389 DYREKLEKlkreineLKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250
....*....|....*....
gi 41393141 229 EENIKIHATLDQTLSELNS 247
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSK 487
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
11-193 |
4.86e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 11 KRKIKVLQQQAD----EAEERAEILQRQV-----EEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:PRK12704 30 EAKIKEAEEEAKrileEAKKEAEAIKKEAlleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 82 KAADESERgmkvienralKDEEKMELQEIQLKEAKHIAEEADRKYEEVArklvivegELERTEERAELaeshVKQMEEEL 161
Cdd:PRK12704 110 EELEKKEK----------ELEQKQQELEKKEEELEELIEEQLQELERIS--------GLTAEEAKEIL----LEKVEEEA 167
|
170 180 190
....*....|....*....|....*....|..
gi 41393141 162 RAldQTLKTLQASEEKYSQKEDKYEEEIKILT 193
Cdd:PRK12704 168 RH--EAAVLIKEIEEEAKEEADKKAKEILAQA 197
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-225 |
5.39e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 2 AGSNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRARE--QAEAEVASLNRRIQLVEEELDRAQE--RLATALQKL 77
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAAAKKKADEakKKAEEKKKA 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 78 EEAEKAADESERG---------MKVIENRALKDEEKMELQEIQLK-EAKHIAEEADRKYEEVARKLVIVEGELERTEERA 147
Cdd:PTZ00121 1434 DEAKKKAEEAKKAdeakkkaeeAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD 1513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 148 ELAESHVKQMEEELRALDQTLKT--LQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLR 225
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKAdeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-233 |
6.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 18 QQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERlatALQKLEEAEKAADESERGmkvieNR 97
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE---AKKKADEAKKAAEAKKKA-----DE 1514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 98 ALKDEEKMELQEIQLKEAKHIAEEAdRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQASEEK 177
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEA-KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 41393141 178 YSQKEDKYEEEIKILTDKLKEAETRAEFAERsVAKLEKTIDDLEEKLRDAKEENIK 233
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-LKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
18-222 |
1.90e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.24 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 18 QQQADEAEERAEILQRQVEEEKRARE--QAEAEVASLNRRIQLVEEELDRAQERLATALQKL-EEAEKAADESERGMKVI 94
Cdd:PRK05035 445 KKKAEEAKARFEARQARLEREKAAREarHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIvIKAGARPDNSAVIAARE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 95 ENRALKDEEKMELQEIQLKEAK----------------HIAEEADRKYEEVARKLVIVEGELERTEER-AELAESHVKQM 157
Cdd:PRK05035 525 ARKAQARARQAEKQAAAAADPKkaavaaaiarakakkaAQQAANAEAEEEVDPKKAAVAAAIARAKAKkAAQQAASAEPE 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393141 158 EEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEE 222
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEP 669
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
18-240 |
2.02e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 18 QQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLA-----------------TALQKLEEA 80
Cdd:PRK04863 347 QEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqaldvqqtraiqyqQAVQALERA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 81 EK---AADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERtEERAELAESHVKQM 157
Cdd:PRK04863 427 KQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSR-SEAWDVARELLRRL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 158 EEElRALDQTLKTLQASE---EKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKI 234
Cdd:PRK04863 506 REQ-RHLAEQLQQLRMRLselEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMAL 584
|
....*.
gi 41393141 235 HATLDQ 240
Cdd:PRK04863 585 RQQLEQ 590
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
14-234 |
2.23e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 14 IKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 93
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 94 IENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTL----- 168
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaeqal 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41393141 169 -KTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKI 234
Cdd:COG4372 186 dELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
7-133 |
2.98e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAR-EQAEAEVASLNRRIQLVEEELDRAQ---ERLATALQKLEEAEK 82
Cdd:COG1566 76 LDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAEiAAAEAQLAAAQAQLDLAQRELERYQalyKKGAVSQQELDEARA 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 41393141 83 AADESERGMKVIENRALKDEEKMELQEiQLKEAKHIAEEADRKYEEVARKL 133
Cdd:COG1566 156 ALDAAQAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNL 205
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
63-248 |
3.08e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 63 LDRAQERLATALQKL-----------EEAEKAADESERGMKVIEN----RALKDEEKM---ELQEIQLKEAKHIAEEADR 124
Cdd:PRK05771 14 LKSYKDEVLEALHELgvvhiedlkeeLSNERLRKLRSLLTKLSEAldklRSYLPKLNPlreEKKKVSVKSLEELIKDVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 125 KYEEVARKLVIVEGELERTEERAELAESHVKQMeEELRALDQTLKTLQAS---------------EEKYSQKEDKYEEEI 189
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENEIKELEQEIERL-EPWGNFDLDLSLLLGFkyvsvfvgtvpedklEELKLESDVENVEYI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41393141 190 K---------ILTDKLKEAETRAEFAERSVAKLE-KTIDDLEEKLRDAKEENIKIHATLDQTLSELNSF 248
Cdd:PRK05771 173 StdkgyvyvvVVVLKELSDEVEEELKKLGFERLElEEEGTPSELIREIKEELEEIEKERESLLEELKEL 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-248 |
3.34e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 55 RIQLVEEELDRAQERL---ATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKhiAEEADRKYEEVAR 131
Cdd:COG1196 190 RLEDILGELERQLEPLerqAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 132 KLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVA 211
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190
....*....|....*....|....*....|....*..
gi 41393141 212 KLEKTIDDLEEKLRDAKEENIKIHATLDQTLSELNSF 248
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
25-245 |
3.39e-04 |
|
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: 41.59 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 25 EERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEaekaadESERGMKVIENRALKDEEK 104
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 105 MELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAElaeshvkqmeeelrALDQTLKTLQASEEKYSQKEDK 184
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE--------------ELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41393141 185 YEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSEL 245
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-240 |
3.41e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 2 AGSNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEE-- 79
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEElr 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 80 ----------AEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHI--AEEADRKYEEVARKLVIVEGELERTEERA 147
Cdd:PRK02224 419 eerdelrereAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 148 ELAESHVKQmEEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDA 227
Cdd:PRK02224 499 ERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577
|
250
....*....|...
gi 41393141 228 KEENIKIHATLDQ 240
Cdd:PRK02224 578 NSKLAELKERIES 590
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
6-246 |
4.02e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 6 SIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 86 ESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAE--SHVKQMEEELRA 163
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 164 LDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLS 243
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
...
gi 41393141 244 ELN 246
Cdd:COG4372 279 EIA 281
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
7-211 |
4.12e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 87 SERGMKVIE------------NRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHV 154
Cdd:COG3883 98 SGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 41393141 155 KQMEEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVA 211
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
7-93 |
4.76e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQ---AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:COG2433 422 VERLEAEVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLERELEEERERIEELKRKLERLKEL 501
|
90
....*....|
gi 41393141 84 ADESERGMKV 93
Cdd:COG2433 502 WKLEHSGELV 511
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
11-234 |
5.10e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 11 KRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVE--------EELDRAQERLATALQKLEEAEK 82
Cdd:PRK05771 78 KVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldLSLLLGFKYVSVFVGTVPEDKL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 83 AADESERGMKVIENRAlKDEEKMELQEIQLKEAKHIAEEADRKYEevARKLVIVEG-----ELERTEERAELAESHVKQM 157
Cdd:PRK05771 158 EELKLESDVENVEYIS-TDKGYVYVVVVVLKELSDEVEEELKKLG--FERLELEEEgtpseLIREIKEELEEIEKERESL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 158 EEELRALDQTLKTLQ-ASEEKYSQKEDKYEEeikiltdKLKEAETRAEFA------ERSVAKLEKTIDDLEEKL-----R 225
Cdd:PRK05771 235 LEELKELAKKYLEELlALYEYLEIELERAEA-------LSKFLKTDKTFAiegwvpEDRVKKLKELIDKATGGSayvefV 307
|
....*....
gi 41393141 226 DAKEENIKI 234
Cdd:PRK05771 308 EPDEEEEEV 316
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
12-230 |
5.85e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 12 RKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEA----EKAADES 87
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaiERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 88 ERGMKVIENRALKDEEKMELQEIQLKE-AKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQ 166
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41393141 167 TLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEE 230
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-237 |
8.29e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 45 AEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEiqLKEAKHIAEEADR 124
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE--LEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 125 KYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQASEEKYSQKEDKYEEEikiLTDKLKEAETRAE 204
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA---LLEERFAAALGDA 762
|
170 180 190
....*....|....*....|....*....|...
gi 41393141 205 FAERSVAKLEKTIDDLEEKLRDAKEENIKIHAT 237
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-172 |
8.52e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQ---------AEAEVASLNRRIQLVEEELDRAQE---RLATAL 74
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDAssdDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 75 QKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIvegELERTEERAELAESHV 154
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVERELR 768
|
170
....*....|....*...
gi 41393141 155 KQMEEELRALDQTLKTLQ 172
Cdd:COG4913 769 ENLEERIDALRARLNRAE 786
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-234 |
8.91e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 1 MAGSNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 81 EKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEE--RAELAESHVKQME 158
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAEAEQALD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41393141 159 EELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKI 234
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
61-247 |
1.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 61 EELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQeiqLKEAKHIAEEADRKYEEVARKLVIVEGEL 140
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALR---LWFAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 141 ERTEERAELAESHVKQMEEELR--------ALDQTLKTLQASEEKYSQKEDKYEEEIKILtdKLKEAETRAEFAE----- 207
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAAL--GLPLPASAEEFAAlraea 389
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41393141 208 -RSVAKLEKTIDDLEEKLRDAKEENIKIHATLDQTLSELNS 247
Cdd:COG4913 390 aALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2-236 |
1.35e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 2 AGSNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 82 KAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEEL 161
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41393141 162 RALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKEENIKIHA 236
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
23-229 |
1.47e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 23 EAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEE-----------LDRAQERLATALQKLEEAEKA--ADESER 89
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEArmahfarrqaaIKAEEARKADELKKAEEKKKAdeAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 90 GMKVIENRAlKDEEKMELQEIQLK--EAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVK----QMEEELRA 163
Cdd:PTZ00121 1301 KKKADEAKK-KAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekKKEEAKKK 1379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41393141 164 LDQTLKtlQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLE--KTIDDLEEKLRDAKE 229
Cdd:PTZ00121 1380 ADAAKK--KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEEAKK 1445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-229 |
1.48e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 1 MAGSNSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 81 EKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEAdRKYEEVARKLVIVEGELERTEERAELAESHVKQME-- 158
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAA-RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEea 1242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41393141 159 ---EELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEEKLRDAKE 229
Cdd:PTZ00121 1243 kkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
|
| PLN03223 |
PLN03223 |
Polycystin cation channel protein; Provisional |
11-104 |
1.70e-03 |
|
Polycystin cation channel protein; Provisional
Pssm-ID: 215637 [Multi-domain] Cd Length: 1634 Bit Score: 39.54 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 11 KRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVE--EELDRAQERLATALQKLEEAEKAADESE 88
Cdd:PLN03223 1536 KGKKKETLATADEIDQAAHMLMDQVGQVPDDEDDDEDGDVLEKEVDQLQQslERLAEVQRELAEGQVKVIEGQKQMAERQ 1615
|
90
....*....|....*.
gi 41393141 89 RGMKVIENRALKDEEK 104
Cdd:PLN03223 1616 SRLSQLENKILGVLEK 1631
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
17-163 |
1.73e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 17 LQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQ-ERLATALQKLEEAEKAADESERGMKVIE 95
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRErEELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41393141 96 NRALKDEEKMELQEIQLKEAKH----IAEEADRKYEEVARKLVIVEGELERTEERAELaeshVKQMEEELRA 163
Cdd:PRK12705 105 NQLEEREKALSARELELEELEKqldnELYRVAGLTPEQARKLLLKLLDAELEEEKAQR----VKKIEEEADL 172
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
21-230 |
1.77e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 21 ADEAEERAEilqrQVEEEKRAREQAEAEVASLNRRIQLVEE------ELDRAQERLATALQKLEEAEKAADESERGMKVI 94
Cdd:PRK02224 467 VETIEEDRE----RVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 95 ENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAEShVKQMEEELRALDQTLKTLQAS 174
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKREALAEL 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 41393141 175 EEKYSQKEDKYEEEIKILTDKLKEAetRAEFAERSVAKLEKTIDDLEEKLRDAKEE 230
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEA--RIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| PHA03248 |
PHA03248 |
DNA packaging tegument protein UL25; Provisional |
22-111 |
3.54e-03 |
|
DNA packaging tegument protein UL25; Provisional
Pssm-ID: 223022 Cd Length: 583 Bit Score: 38.47 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 22 DEAEERAEILQRQVEEEKRAREQAEAEVASL----NRRIQLVEEELdraqERLATALQKLEEAEKAADES-----ERGMK 92
Cdd:PHA03248 49 ETAAARLALLEARNRAAAAALDNLAGQAATIpvevDRRLRPIERQL----EEVADALADLEEAAAAAEEAdaaadERKAA 124
|
90
....*....|....*....
gi 41393141 93 VIENRALKDEEKMELQEIQ 111
Cdd:PHA03248 125 AGDGDGRAAGEDDEAREVQ 143
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
73-204 |
3.93e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.22 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 73 ALQKLEEAEKAADEsergmkvienraLKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAES 152
Cdd:PRK12704 29 AEAKIKEAEEEAKR------------ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 41393141 153 hvkQMEEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETRAE 204
Cdd:PRK12704 97 ---NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE 145
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-229 |
6.72e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.71 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 14 IKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 93
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 94 IENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQA 173
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVE 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 41393141 174 SEEKYSQKEDKYEEEIKILTDKLKEAETRAEFAErSVAKLEKTIDDLEEKLRDAKE 229
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEE 523
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
46-230 |
7.02e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.33 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 46 EAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALK---DEEKMELQEIQLKEAKHIAEEA 122
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETiaeTEREREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 123 DRKYEEVARKLVIVEGELERTEERAELAESHVKQMEEELRALDQTLKTLQASEEKYSQKEDKYEEEIKILTDKLKEAETR 202
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
170 180
....*....|....*....|....*...
gi 41393141 203 AEFAERSVAKLEKTIDDLEEKLRDAKEE 230
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRER 399
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
7-219 |
7.18e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 37.50 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 7 IDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAEVASLNRRiqlVEEELDRAQERLATALQKLE-------- 78
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEE---LEEKKEKLQEEEDKLLEEAEkeaqqaik 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 79 EAEKAADESERGMKVIENRALKDEEKMELQEIQ--LKEAKHIAEEAdrKYEEVARKLVIVEGE---LERTEERAELAEsh 153
Cdd:PRK00409 581 EAKKEADEIIKELRQLQKGGYASVKAHELIEARkrLNKANEKKEKK--KKKQKEKQEELKVGDevkYLSLGQKGEVLS-- 656
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41393141 154 vKQMEEELRALDQTLK-TLQASEEKYSQKEDKYEEE-IKILTDKLKEAET----RAEFAERSVAKLEKTIDD 219
Cdd:PRK00409 657 -IPDDKEAIVQAGIMKmKVPLSDLEKIQKPKKKKKKkPKTVKPKPRTVSLeldlRGMRYEEALERLDKYLDD 727
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
5-216 |
7.92e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 37.20 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 5 NSIDAVKRKIKVLQQQADEAEERAEILQRQVEEEKRAREQAEAE------VASLNRRIQLVEEELDRAQERLATALQKL- 77
Cdd:PRK11281 73 DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLv 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 78 ------EEAEKAADESERGMKVIENR---------ALKDEEKMELQ-EIQLKEAKHiaeeadrkyeEVARKLVIVEGELE 141
Cdd:PRK11281 153 slqtqpERAQAALYANSQRLQQIRNLlkggkvggkALRPSQRVLLQaEQALLNAQN----------DLQRKSLEGNTQLQ 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41393141 142 RT-EERAELAESHVKQMEEELRALdQTL---KTLQASEEKYSQKEDKyEEEIKILTDKL--KEAETRAEFAERSVAKLEK 215
Cdd:PRK11281 223 DLlQKQRDYLTARIQRLEHQLQLL-QEAinsKRLTLSEKTVQEAQSQ-DEAARIQANPLvaQELEINLQLSQRLLKATEK 300
|
.
gi 41393141 216 T 216
Cdd:PRK11281 301 L 301
|
|
| |
