|
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 |
3.67e-79 |
|
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: 242.24 E-value: 3.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 160 AEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADK 239
Cdd:pfam00261 34 AEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 240 KYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAE 319
Cdd:pfam00261 114 KYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAE 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068700094 320 FAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELS 361
Cdd:pfam00261 194 FAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-355 |
1.22e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
166-231 |
5.70e-13 |
|
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: 65.40 E-value: 5.70e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700094 166 ALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAK 231
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-360 |
8.09e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 8.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 360
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-355 |
1.97e-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: 68.54 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 146 KNELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILET 225
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 226 QLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELrvvgnnlKSLEVSEEKAAQREDNFEEQIK 305
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-------ESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068700094 306 ELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-360 |
1.82e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 150 HNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMeddrvgiLETQLAQ 229
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE-------LEEKLEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 230 AKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKEL-- 307
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlk 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700094 308 ---THRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 360
Cdd:TIGR02168 429 kleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-355 |
1.98e-11 |
|
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: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-360 |
1.99e-11 |
|
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: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 360
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-360 |
3.20e-11 |
|
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: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 360
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-360 |
4.73e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELR-------VVGNNLKSLEVSEEKAAQREDNFEEQIKELT 308
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllneeaaNLRERLESLERRIAATERRLEDLEEQIEELS 851
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2068700094 309 HRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 360
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-355 |
1.59e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-349 |
1.69e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
170 180 190
....*....|....*....|....*....|....
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSI 349
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
156-362 |
5.45e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAA-----LNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQA 230
Cdd:TIGR02168 221 ELRELELALLVlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 231 KHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHR 310
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2068700094 311 MREAEARAEFAERSVQKLQKEVDRLEDELvnekekyKSITDELDQTFSELSG 362
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARL-------ERLEDRRERLQQEIEE 425
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-360 |
1.12e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALnrRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG1196 221 ELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 360
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-363 |
2.78e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESER-------ARKCLENRANME-----DDRVGIL 223
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidvasaEREIAELEAELErldasSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 224 ETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVgnnlKSLEVSEEKAAQREDNFEEQ 303
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE----LRALLEERFAAALGDAVERE 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068700094 304 IKELTHRmreaearaefaerSVQKLQKEVDRLEDELVNE----KEKYKSITDELDQTFSELSGY 363
Cdd:COG4913 767 LRENLEE-------------RIDALRARLNRAEEELERAmrafNREWPAETADLDADLESLPEY 817
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
155-310 |
3.76e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERArkclenRANMEDDRVGILETQLAQAKHIA 234
Cdd:COG4913 281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ------IRGNGGDRLEQLEREIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 235 EEADKKYEEVARKLAMVE----ADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHR 310
Cdd:COG4913 355 EERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
154-356 |
1.12e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 154 NVQLKRAEGEVAA--LNRRIQLLEEDLERSEERLNtattKLAEASQAADeserarkcLENRANMEDDRVGILETQLAQAK 231
Cdd:COG3206 165 NLELRREEARKALefLEEQLPELRKELEEAEAALE----EFRQKNGLVD--------LSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 232 HIAEEADKKYEEVARKLAM---------------------VEADLERAEERAETGES--KIVELEEELRVVGNNLK---- 284
Cdd:COG3206 233 AELAEAEARLAALRAQLGSgpdalpellqspviqqlraqlAELEAELAELSARYTPNhpDVIALRAQIAALRAQLQqeaq 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700094 285 ----SLEVSEEKAAQREDNFEEQIKELTHRMreaearaefaeRSVQKLQKEVDRLEDELVNEKEKYKSITDELDQT 356
Cdd:COG3206 313 rilaSLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-355 |
5.21e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLE------EDLERSEERLNT-----ATTKLAEASQAADESERARKCLENRANMEDDRVGILE 224
Cdd:COG4913 236 DLERAHEALEDAREQIELLEpirelaERYAAARERLAEleylrAALRLWFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 225 TQLAQAKHIAEEADKKYEEV-ARKLAMVEADLERAEERAETGESKIVELEEELRVVGnnlkslevseEKAAQREDNFEEQ 303
Cdd:COG4913 316 ARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALG----------LPLPASAEEFAAL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2068700094 304 IKELTHRmreaearAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:COG4913 386 RAEAAAL-------LEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
138-345 |
7.97e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 7.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 138 TMMKF--SIIKNELHNIMNvQLKRAEGEVAALN-RRIQLLEEDL---ERSEERLNTATTKLAEASQAADESERARKCLEN 211
Cdd:COG4717 38 TLLAFirAMLLERLEKEAD-ELFKPQGRKPELNlKELKELEEELkeaEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 212 RANMEDDRVGILET--QLAQAKHIAEEADKKYEEVARKLAmveaDLERAEERAETGESKIVELEEELRvvgnnlKSLEVS 289
Cdd:COG4717 117 ELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELE------ELLEQL 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700094 290 EEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEK 345
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-361 |
8.35e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 175 EEDLERSEERLNTATTKLAE-ASQA---ADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAM 250
Cdd:COG1196 178 ERKLEATEENLERLEDILGElERQLeplERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 251 VEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQK 330
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190
....*....|....*....|....*....|.
gi 2068700094 331 EVDRLEDELVNEKEKYKSITDELDQTFSELS 361
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-339 |
8.56e-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: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEV-------------------------ARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSE 290
Cdd:COG4942 101 AQKEELAELlralyrlgrqpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2068700094 291 EKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-345 |
3.37e-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: 52.38 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 157 LKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKclENRANMEDDRVGILETQLAQAKHIAEE 236
Cdd:TIGR02169 711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK--ELEARIEELEEDLHKLEEALNDLEARL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 237 ADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELrvvgnnlKSLEVSEEKAAQREDNFEEQIKELTHRMREAEA 316
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK-------EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180
....*....|....*....|....*....
gi 2068700094 317 RAEFAERSVQKLQKEVDRLEDELVNEKEK 345
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKE 890
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
156-277 |
1.48e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASqaadeSERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIE 120
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELR 277
Cdd:COG1579 121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
223-360 |
1.71e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 223 LETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNN--LKSLEVSEEKAAQREDNF 300
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQKEIESLKRRISDL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 301 EEQIKELTHRMREAEARaefaersVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 360
Cdd:COG1579 109 EDEILELMERIEELEEE-------LAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
153-363 |
1.93e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 153 MNVQLKraeGEVAALNRRIQLLEEDLERSEERLNTaTTKLAEASQAADESERARKCL---ENRANMEDDRVGILETQLAQ 229
Cdd:PHA02562 168 MDKLNK---DKIRELNQQIQTLDMKIDHIQQQIKT-YNKNIEEQRKKNGENIARKQNkydELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 230 AKHIAEEADkkYEEVARKLAMVEADLERAEERA--------------------ETGESKIVELEEELRVVGNNLKSLEVS 289
Cdd:PHA02562 244 LNLVMDIED--PSAALNKLNTAAAKIKSKIEQFqkvikmyekggvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTA 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2068700094 290 EEKAAQREDNFEEQ---IKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY 363
Cdd:PHA02562 322 IDELEEIMDEFNEQskkLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
155-361 |
2.48e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 155 VQLKRAEGEVAALNRRIQLLEEDLER-SEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHI 233
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 234 AEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELR----------------------VVGNNLKSLEVSEE 291
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelkdyrekleklkreineLKRELDRLQEELQR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700094 292 KAAQRED------NFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELS 361
Cdd:TIGR02169 418 LSEELADlnaaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
158-356 |
2.98e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 158 KRAEGEVAALNRRIQL--LEEDLERSEERLNTATTKLAEASQAADEserarkclenranmeddrvgiLETQLAQAKHIAE 235
Cdd:TIGR02168 664 GSAKTNSSILERRREIeeLEEKIEELEEKIAELEKALAELRKELEE---------------------LEEELEQLRKELE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRvvgnnlkSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE-------ELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQT 356
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
229-352 |
9.57e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 229 QAKHIAEEADKKYEEVaRKLAMVEADLERAEERAEtgeskiveLEEELRVVGNNLKSLEvseEKAAQREDNFEEQIKELT 308
Cdd:PRK12704 39 EAKRILEEAKKEAEAI-KKEALLEAKEEIHKLRNE--------FEKELRERRNELQKLE---KRLLQKEENLDRKLELLE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2068700094 309 HR---MREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDE 352
Cdd:PRK12704 107 KReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
157-307 |
1.53e-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: 46.97 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 157 LKRAEGEVAALNRRIQLLE-------EDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQ 229
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEeqieelsEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700094 230 AKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEE-ELRVVGNNLKSLEVSEEKAAQREDNFEEQIKEL 307
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
170-339 |
2.69e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 170 RIQLLEEDLERSEERLNTATTKLAEASQAAdESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLA 249
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 250 MVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNfEEQIKELTHRMREAEARAEFAERSVQKLQ 329
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADA-EDEIERLREKREALAELNDERRERLAEKR 633
|
170
....*....|
gi 2068700094 330 KEVDRLEDEL 339
Cdd:PRK02224 634 ERKRELEAEF 643
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
152-278 |
2.85e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 152 IMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAE--ASQAADESERAR-----KCLENRANMEDDRVGILE 224
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANlrASLSAAEAERSRlqallAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068700094 225 TQLAQAKHIAEEADKKYE----EVA---RKLAMVEADLERAEERAETGESKIVELEEELRV 278
Cdd:PRK09039 123 QELDSEKQVSARALAQVEllnqQIAalrRQLAALEAALDASEKRDRESQAKIADLGRRLNV 183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
155-309 |
3.26e-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: 45.82 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIA 234
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 235 EEADKK------------YEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEkaaqREDNFEE 302
Cdd:TIGR02168 431 EEAELKelqaeleeleeeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE----NLEGFSE 506
|
....*..
gi 2068700094 303 QIKELTH 309
Cdd:TIGR02168 507 GVKALLK 513
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
156-310 |
4.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADE-----SERARKCLENRANMED------------- 217
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelGERARALYRSGGSVSYldvllgsesfsdf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 218 -DRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQR 296
Cdd:COG3883 118 lDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
|
170
....*....|....
gi 2068700094 297 EDNFEEQIKELTHR 310
Cdd:COG3883 198 LAELEAELAAAEAA 211
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
155-307 |
4.52e-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: 44.15 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKhia 234
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR--- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2068700094 235 eeADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVS-EEKAAQREDNFEEQIKEL 307
Cdd:COG1579 87 --NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAElEEKKAELDEELAELEAEL 158
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
164-354 |
6.79e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 164 VAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLEN-RANMEDDRVGILET---------QLAQAKHI 233
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETlEAEIEDLRETIAETerereelaeEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 234 AEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMRE 313
Cdd:PRK02224 288 LEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2068700094 314 AEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELD 354
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG 408
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
166-277 |
1.17e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 42.25 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 166 ALNRRIQLLEEDLERSEERLNTATTKLAEA----SQAADESERARKCLENRAnmeddrVGILETQLAQAKhiaeeadkky 241
Cdd:PRK07352 47 ILEERREAILQALKEAEERLRQAAQALAEAqqklAQAQQEAERIRADAKARA------EAIRAEIEKQAI---------- 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2068700094 242 EEVARKLAMVEADLERAEERA------ETGESKIVELEEELR 277
Cdd:PRK07352 111 EDMARLKQTAAADLSAEQERViaqlrrEAAELAIAKAESQLP 152
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-307 |
1.52e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 145 IKNELHNIMNVQLKRAEGEVAALNRRIQLLEE-------------DLERSEERLNTATTKLAEASQAADESERARKCLEN 211
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPfyneylelkdaekELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 212 RANMeddrvgiLETQLAQAKHiaEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSeE 291
Cdd:PRK03918 648 ELEE-------LEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL-E 717
|
170
....*....|....*.
gi 2068700094 292 KAAQREDNFEEQIKEL 307
Cdd:PRK03918 718 KALERVEELREKVKKY 733
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
188-361 |
1.55e-04 |
|
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: 43.21 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 188 ATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGES 267
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 268 KIVELEEELRVVGNNLKSLEVSEEKAAQRE--------DNFEEQIKELtHRMREAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180
....*....|....*....|..
gi 2068700094 340 VNEKEKYKSITDELDQTFSELS 361
Cdd:COG4942 170 EAERAELEALLAELEEERAALE 191
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
154-355 |
1.95e-04 |
|
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: 43.40 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 154 NVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADES--------------ERARKCLEN-------- 211
Cdd:COG3096 360 TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqalEKARALCGLpdltpena 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 212 ---------RANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEAdlERAEERAEtgesKIVELEEELRVVGNN 282
Cdd:COG3096 440 edylaafraKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER--SQAWQTAR----ELLRRYRSQQALAQR 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2068700094 283 LKSL--EVSE-EKAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:COG3096 514 LQQLraQLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
156-339 |
1.96e-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: 43.52 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLaqakhiae 235
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK-------- 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 eadkkyEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRM---- 311
Cdd:TIGR02169 864 ------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELseie 937
|
170 180 190
....*....|....*....|....*....|
gi 2068700094 312 --REAEARAEFAERSVQKLQKEVDRLEDEL 339
Cdd:TIGR02169 938 dpKGEDEEIPEEELSLEDVQAELQRVEEEI 967
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-330 |
2.84e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 145 IKNELHNiMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDD------ 218
Cdd:PRK03918 236 LKEEIEE-LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElreiek 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 219 RVGILETQLAQAKHIAEEADKK---YEEVARKLAMVEADLERAEERAETGE---SKIVELEE-ELRVVGNNLKSLEVSEE 291
Cdd:PRK03918 315 RLSRLEEEINGIEERIKELEEKeerLEELKKKLKELEKRLEELEERHELYEeakAKKEELERlKKRLTGLTPEKLEKELE 394
|
170 180 190
....*....|....*....|....*....|....*....
gi 2068700094 292 KAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQK 330
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
139-306 |
4.26e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 139 MMKFSIIKNELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTattklaeasqaaDESERARKCLE------NR 212
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ------------QEEERKRKKLElekekrDR 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 213 ANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEER--AETGESKIVELEEELRVVGNNLK-SLEVS 289
Cdd:pfam17380 487 KRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRreAEEERRKQQEMEERRRIQEQMRKaTEERS 566
|
170
....*....|....*..
gi 2068700094 290 EEKAAQREDNFEEQIKE 306
Cdd:pfam17380 567 RLEAMEREREMMRQIVE 583
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
146-338 |
4.76e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 146 KNELHNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEE-RLNTATTKLAEASQAADESERARKCLENRANMEDDRVgile 224
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK---- 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 225 tqlaqakhiAEEADKKYEEVARKLAMVEADLERAEERAEtgesKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQI 304
Cdd:PTZ00121 1690 ---------AAEALKKEAEEAKKAEELKKKEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
170 180 190
....*....|....*....|....*....|....
gi 2068700094 305 KELTHRMREAEARAEFAERSVQKLQKEVDRLEDE 338
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-360 |
4.88e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 172 QLLEEDLERSEERLNTATTKLAE-ASQAADESERARKCLENRanmeddrvgilETQLAQAKHIAEEADKKYEEVARKLAM 250
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPElNLKELKELEEELKEAEEK-----------EEEYAELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 251 VEADLERAE--ERAETGESKIVELEEELRVVGNNLKSLE--VSEEKAAQRE-DNFEEQIKELTHRMREAEARAEFAERS- 324
Cdd:COG4717 114 LREELEKLEklLQLLPLYQELEALEAELAELPERLEELEerLEELRELEEElEELEAELAELQEELEELLEQLSLATEEe 193
|
170 180 190
....*....|....*....|....*....|....*.
gi 2068700094 325 VQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 360
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
156-353 |
5.48e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAE 235
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAE 315
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190
....*....|....*....|....*....|....*...
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDEL 353
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
167-311 |
6.00e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 167 LNRRIQLLEEDLERSEERLNTATTKLAEASQAADES-ERARKCLENRANMEDDRVGILETQLAQAKhiaEEADKKYEeva 245
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELlLRERNQQRQEARREREELQREEERLVQKE---EQLDARAE--- 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700094 246 rKLAMVEADLERAEERAETGESKIVELEEELR---VVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRM 311
Cdd:PRK12705 99 -KLDNLENQLEEREKALSARELELEELEKQLDnelYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKI 166
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
155-360 |
7.39e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 155 VQLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIA 234
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 235 EEADKKYEEVARKLAMVEADLERAEERAETGES----------------------------KIVELEEELRVVGNNLKSL 286
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieedreRVEELEAELEDLEEEVEEV 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 287 EVSEE------KAAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSEL 360
Cdd:PRK02224 495 EERLEraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
163-354 |
8.17e-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: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 163 EVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADkkyE 242
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA---E 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 243 EVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAE 322
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
170 180 190
....*....|....*....|....*....|....*....
gi 2068700094 323 RSVQKLQKEVDRL-------EDELVNEKEKYKSITDELD 354
Cdd:COG1196 767 RELERLEREIEALgpvnllaIEEYEELEERYDFLSEQRE 805
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
167-353 |
1.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 167 LNRRIQLLEEDLERSE---ERLNTATTKLAEASQAADESERARKCLEnranmedDRVGILETQLAQAKHIAEEadkkYEE 243
Cdd:PRK03918 174 IKRRIERLEKFIKRTEnieELIKEKEKELEEVLREINEISSELPELR-------EELEKLEKEVKELEELKEE----IEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 244 VARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQRE--DNFEEQIKELTHRMREAEARAEFA 321
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIklSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190
....*....|....*....|....*....|..
gi 2068700094 322 ERSVQKLQKEVDRLEDELVNEKEKYKSITDEL 353
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-355 |
1.37e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNR------RIQLLEE---DLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQ 226
Cdd:PRK03918 430 ELKKAKGKCPVCGRelteehRKELLEEytaELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 227 LAQAKHIAEEADKK---YEEVARKLAMVEADLERAEERAETG---ESKIVELEEELRVVGNNLKSLEVS-EEKAAQREDN 299
Cdd:PRK03918 510 EKLKKYNLEELEKKaeeYEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKElEELGFESVEE 589
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2068700094 300 FEEQIKELTH------RMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:PRK03918 590 LEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
156-308 |
1.49e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLL----------------EEDLERSEERLNTATtKLAEASQAA----DESE--------RARK 207
Cdd:COG0497 173 ELEELRADEAERARELDLLrfqleeleaaalqpgeEEELEEERRRLSNAE-KLREALQEAlealSGGEggaldllgQALR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 208 CLENRANMeDDRVGILETQLAQAKHIAEEAdkkYEEVARKLAMVEAD---LERAEER------------------AETGE 266
Cdd:COG0497 252 ALERLAEY-DPSLAELAERLESALIELEEA---ASELRRYLDSLEFDperLEEVEERlallrrlarkygvtveelLAYAE 327
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068700094 267 skivELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELT 308
Cdd:COG0497 328 ----ELRAELAELENSDERLEELEAELAEAEAELLEAAEKLS 365
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-362 |
1.64e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADEserarkclenranmeddrvgiLETQLAQAKHIAE 235
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE---------------------LEAEAEEKREAAA 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGEsKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRmrEAE 315
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER--KRE 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2068700094 316 ARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSG 362
Cdd:PRK02224 639 LEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGA 685
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
161-355 |
2.17e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 161 EGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLEnranmedDRVGILETQLAQAKHIAEEADKK 240
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA-------EKLSKLQSELESVSSLLNEAEGK 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 241 YEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEF 320
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
|
170 180 190
....*....|....*....|....*....|....*
gi 2068700094 321 AERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDK 570
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
167-355 |
2.22e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 167 LNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVAR 246
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 247 KLAMVEADLERAEER--AETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEFAERS 324
Cdd:TIGR04523 539 KISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
170 180 190
....*....|....*....|....*....|.
gi 2068700094 325 VQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
247-356 |
2.42e-03 |
|
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: 38.05 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 247 KLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHrmreAEARAEFAERSVQ 326
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKE----KAEESEKLKTNNE 76
|
90 100 110
....*....|....*....|....*....|
gi 2068700094 327 KLQKEVDRLEDELVNEKEKYKSITDELDQT 356
Cdd:pfam12718 77 NLTRKIQLLEEELEESDKRLKETTEKLRET 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
176-359 |
2.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 176 EDLERSEERLNTATTKLAEASQAadesERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADL 255
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 256 ERAEERAEtgesKIVELEEELRVVGNNLKSLEVSEEKAAQrEDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRL 335
Cdd:PTZ00121 1643 AEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
170 180
....*....|....*....|....
gi 2068700094 336 EDELVNEKEKYKSITDELDQTFSE 359
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
134-335 |
2.74e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.63 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 134 FSSNTMMKFSIIKNELHNIMNVQLKRaEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRA 213
Cdd:pfam05667 308 FTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 214 NMEDDRVGILETqlaqakhiAEEADKKYEevarklAMVEADLERAEERAETGESKIVELEEELRvvgnNLKSLEVSEEKA 293
Cdd:pfam05667 387 KVKKKTLDLLPD--------AEENIAKLQ------ALVDASAQRLVELAGQWEKHRVPLIEEYR----ALKEAKSNKEDE 448
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2068700094 294 AQREdnfEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRL 335
Cdd:pfam05667 449 SQRK---LEEIKELREKIKEVAEEAKQKEELYKQLVAEYERL 487
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
243-361 |
2.77e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 39.74 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 243 EVARKLAMVEADLERAEERAETGESK----IVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARA 318
Cdd:COG1193 490 EIARRLGLPEEIIERARELLGEESIDveklIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKA 569
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2068700094 319 EFAERS-VQKLQKEVDRLEDELVN---EKEKYKSITDELDQTFSELS 361
Cdd:COG1193 570 REEAEEiLREARKEAEELIRELREaqaEEEELKEARKKLEELKQELE 616
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
154-347 |
3.61e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 154 NVQLKRAEGEVAALNRRIqllEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDdrvgiLETQLAQAKHI 233
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARI---EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ-----LKKKEAEEKKK 1648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 234 AEEADKKYEEVARKlamvEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMRE 313
Cdd:PTZ00121 1649 AEELKKAEEENKIK----AAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
170 180 190
....*....|....*....|....*....|....
gi 2068700094 314 AEARAEFAERSVQKLQKEVDRLEDELVNEKEKYK 347
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK 1758
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-353 |
3.96e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 141 KFSIIKNELHNIMNVqLKRAEGEVAALNRRIqlleEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRV 220
Cdd:PRK03918 201 ELEEVLREINEISSE-LPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 221 GILETQLAQAKHIAEEAD------KKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAA 294
Cdd:PRK03918 276 EELEEKVKELKELKEKAEeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068700094 295 QREDNFE--EQIKELTHRMreAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDEL 353
Cdd:PRK03918 356 ELEERHElyEEAKAKKEEL--ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARI 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
159-307 |
4.72e-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: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 159 RAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEAD 238
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2068700094 239 KKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKEL 307
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-353 |
5.80e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 145 IKNELHNIMNVQLKRAEGEVAALNRRIQLLEED---LERSEERLNTATTKLAEASQAADESERARKCLENR-ANMEDDRV 220
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESV 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 221 GILETQLAQAkhiaEEADKKYEEvarkLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSL--EVSEEKAAQRED 298
Cdd:PRK03918 588 EELEERLKEL----EPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELrkELEELEKKYSEE 659
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2068700094 299 NFEEqIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDEL 353
Cdd:PRK03918 660 EYEE-LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
150-361 |
6.08e-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: 38.25 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 150 HNIMNVQLKRAEGEVAALNRRIQLLEEDLERSEERLNTAT---TKLAEASQAAD----ESERARKCLENRANMEDD--RV 220
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVrekTSLSASVASLEkqllELTRVNELLKAKFSEDGTqkKM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 221 GILETQLAQAKHiaeEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELrvvgnnlksleVSEEKAAQREDNF 300
Cdd:pfam15905 155 SSLSMELMKLRN---KLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKL-----------VSTEKEKIEEKSE 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068700094 301 EEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELS 361
Cdd:pfam15905 221 TEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLN 281
|
|
| HrpB7 |
pfam09486 |
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ... |
157-275 |
7.28e-03 |
|
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes which are found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia.
Pssm-ID: 370523 [Multi-domain] Cd Length: 157 Bit Score: 36.65 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 157 LKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEAS-QAADESERARKCLEnranmedDRVGILETQLAQAKHIAE 235
Cdd:pfam09486 31 LAQAEAALAAAQAQAEQARDRVRAHEERLDDLTTGGSPFSaADYLACRAYRDVLE-------GRVGAAEAALAAARQALD 103
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2068700094 236 EADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEE 275
Cdd:pfam09486 104 AAEDAVAATRRKIARNDAQLDVCRERIARLRRAAERARED 143
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
156-355 |
7.39e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 38.49 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 156 QLKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEA----------SQAADESERARKCLENRANMEDDRVGILET 225
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdvtimERFQMELKDVERKIAQQAAKLQGSDLDRTV 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 226 QlaQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIK 305
Cdd:TIGR00606 825 Q--QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR 902
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2068700094 306 ELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQ 355
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
157-307 |
7.42e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 38.12 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 157 LKRAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADEserarkcLENRANMEDDRVGILETQLAQAKHIAEE 236
Cdd:pfam19220 155 LQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAE-------LETQLDATRARLRALEGQLAAEQAERER 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2068700094 237 ADKKYEEVARKLAMVEA----DLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKEL 307
Cdd:pfam19220 228 AEAQLEEAVEAHRAERAslrmKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL 302
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-325 |
7.56e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.51 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 161 EGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERARKCLENRANMEDDRVGILETQLAQAKHIAEEADKK 240
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 241 YEEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKAAQREDNFEEQIKELTHRMREAEARAEF 320
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARA 501
|
....*
gi 2068700094 321 AERSV 325
Cdd:TIGR02169 502 SEERV 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
218-362 |
9.73e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.97 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2068700094 218 DRVGILETQLAQAKHIAEEADKKYEEVARKLAMVEADLERAEERAETGESKI--VELEEELRVVGNNLKSLEVSE---EK 292
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSddlAA 689
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2068700094 293 AAQREDNFEEQIKELTHRMREAEARAEFAERSVQKLQKEVDRLEDELVN-EKEKYKSITDELDQTFSELSG 362
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALG 760
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