|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
12-223 |
1.28e-66 |
|
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: 206.03 E-value: 1.28e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 12 RKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL 171
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1475409280 172 EAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDE 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-221 |
2.25e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 6 SLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVT 165
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1475409280 166 NNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-223 |
2.83e-13 |
|
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: 68.93 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsegkcaELEEELKTVTN 166
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1475409280 167 NLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
12-116 |
5.67e-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: 64.25 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 12 RKIRSLQEQADAAEERAGTLQRELDHERKLRETAEadvaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam12718 42 HKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKV 117
|
90 100
....*....|....*....|....*
gi 1475409280 92 KVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:pfam12718 118 QALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-223 |
2.00e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 87 sergmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196 328 -------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1475409280 167 NLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10-222 |
5.64e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 10 VRRKIRSLQEQADAAEE-----------RAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLE 78
Cdd:COG1196 198 LERQLEPLERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 79 EAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELE 158
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1475409280 159 EELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-223 |
1.15e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 8 EAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 88 ERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNN 167
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1475409280 168 LKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-224 |
3.75e-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: 59.69 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 23 AAEERAGTLQR--ELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQK 100
Cdd:TIGR02168 665 SAKTNSSILERrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 101 DEEKMEIQEIQLKEAKHIAEDADRKYE-------EVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEA 173
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1475409280 174 QAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDKF 224
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-210 |
6.34e-10 |
|
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: 58.93 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 4 SSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKT 163
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1475409280 164 VTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSV 210
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-215 |
1.23e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 87 SERGmkviESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196 391 ALRA----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1475409280 167 NLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEK 215
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-221 |
2.53e-09 |
|
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: 56.70 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 1 MAGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 81 EKAADESErgmKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 160
Cdd:COG4942 96 RAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1475409280 161 LKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-222 |
5.85e-09 |
|
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: 56.23 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 4 SSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQ-LVEEELDRAQERLATALQKLEEAEK 82
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLER 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 83 AADESERGMKVIESRAQKDEEkmEIQEIQLKeakhiAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELK 162
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEA--EIDKLLAE-----IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 163 TVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-224 |
9.53e-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: 55.45 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 5 SSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 85 DESErgmkvieSRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTV 164
Cdd:TIGR02168 326 EELE-------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 165 TNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAefAERSVTKLEKSIDDLEDKF 224
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEEL 456
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-224 |
9.80e-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: 55.45 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADAAEeRAGTLQRELDHERKL-----RETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAE-RYKELKAELRELELAllvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 82 KAADESERGMKVI--------------ESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERA 147
Cdd:TIGR02168 274 LEVSELEEEIEELqkelyalaneisrlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1475409280 148 ELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDKF 224
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-223 |
2.92e-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: 53.92 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 2 AGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 82 KAADESERGMKVIESR-----AQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAE 156
Cdd:TIGR02169 751 QEIENVKSELKELEARieeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1475409280 157 LEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-177 |
9.22e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRET---------AEADVASLNRRIQLVEEELDRAQE---RLATAL 74
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDAssdDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 75 QKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLViiesDLERAEERAELSEGKC 154
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVEREL 767
|
170 180
....*....|....*....|....
gi 1475409280 155 AE-LEEELKTVTNNLKSLEAQAEK 177
Cdd:COG4913 768 REnLEERIDALRARLNRAEEELER 791
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-221 |
1.92e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLqEQADAAEERAGTLQRELDHERKLRETAEADVASlnRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4913 244 LEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 87 SERgmkviesraqkdeekmeiQEIQLKEAKhiaedADRKYEEVARklviIESDLERAEERAELSEGKCAELEEELK---- 162
Cdd:COG4913 321 LRE------------------ELDELEAQI-----RGNGGDRLEQ----LEREIERLERELEERERRRARLEALLAalgl 373
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1475409280 163 TVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-204 |
2.16e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 11 RRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 90
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGkcAELEEELKTvtnnlks 170
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAA------- 757
|
170 180 190
....*....|....*....|....*....|....
gi 1475409280 171 lEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE 204
Cdd:COG4913 758 -ALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-206 |
2.38e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADA-----AEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATA-LQKLEEA 80
Cdd:COG4913 264 YAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 81 EKAADESERGMKVIESRAQKDEEKmeIQEIQLkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 160
Cdd:COG4913 344 EREIERLERELEERERRRARLEAL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1475409280 161 LKTVTNNLKSLEAQAEKYSQkedRYEEEIKVLSDKLKEAETRAEFA 206
Cdd:COG4913 421 LRELEAEIASLERRKSNIPA---RLLALRDALAEALGLDEAELPFV 463
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-222 |
3.24e-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: 50.84 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 4 SSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELdrAQERLATALQKLEEAEKA 83
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL--HKLEEALNDLEARLSHSR 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKT 163
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1475409280 164 VTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-221 |
3.85e-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: 50.84 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 4 SSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEEL-----DRAQERLATALQKLE 78
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELS 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 79 EAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELE 158
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1475409280 159 EELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-222 |
4.75e-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: 50.44 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 4 SSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELeeELKT 163
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKE 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1475409280 164 VTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-222 |
9.58e-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: 49.28 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 87 SERGMKviESRAQKDEEKMEIQEIQLKEA---KHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEElkt 163
Cdd:TIGR02168 913 LRRELE--ELREKLAQLELRLEGLEVRIDnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV--- 987
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1475409280 164 vtnNLKSLEAqaekYSQKEDRYEEEIKVLSDklkeaetraefAERSVTKLEKSIDDLED 222
Cdd:TIGR02168 988 ---NLAAIEE----YEELKERYDFLTAQKED-----------LTEAKETLEEAIEEIDR 1028
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
8-198 |
2.43e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 8 EAVRRKIRSLQEQADAAEERAGTLQRELdheRKLREtaEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAAL---EEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 88 ERGMKVIESRAQKDEEKMEIQEIQLKEAkhiaeDADRKYEEVARKL-----VIIESDLERAEERAELSEgkcaELEEELK 162
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQLA-----ELEAELAELSARYtpnhpDVIALRAQIAALRAQLQQ----EAQRILA 316
|
170 180 190
....*....|....*....|....*....|....*.
gi 1475409280 163 TVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKE 198
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-223 |
2.47e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 8 EAVRRKIRSLQEQADAAEE-RAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAdRKYEEVARKLVIIESD-LERAEERAELSEG--------KCAEL 157
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA-RKADELKKAEEKKKADeAKKAEEKKKADEAkkkaeeakKADEA 1320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1475409280 158 EEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-202 |
3.69e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 12 RKIRSLQEQADAAEERAGTLQRELDHERKLRETAE-----------ADVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARErlaeleylraaLRLWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 81 EKAADESERgmKVIESRAQKDEEKMEiqeiQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 160
Cdd:COG4913 315 EARLDALRE--ELDELEAQIRGNGGD----RLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1475409280 161 LKTVTNNLKSLEAQAEKY----SQKEDRYEEEIKVLSDKLKEAETR 202
Cdd:COG4913 389 AAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAEIASLERR 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
5-204 |
5.61e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 5 SSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 85 DESERGMKVIE------------SRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG 152
Cdd:COG3883 96 YRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1475409280 153 KCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE 204
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
13-229 |
7.00e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.84 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 13 KIRSLQEQADAAEERAGTLQRELDHERKLRET-AEADVASLNRRIQLVEEELDRAQERLATALQKLEE--AEKAADESE- 88
Cdd:PRK05771 44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISEleNEIKELEQEi 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 89 -------------------RGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA---RKLVIIESDLERAE-E 145
Cdd:PRK05771 124 erlepwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVvlkELSDEVEEELKKLGfE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 146 RAELSEGKC-----AELEEELKTVTNNLKSLEAQAEKYSQKedrYEEEIKVLSDKL----KEAETRAEFA---------- 206
Cdd:PRK05771 204 RLELEEEGTpseliREIKEELEEIEKERESLLEELKELAKK---YLEELLALYEYLeielERAEALSKFLktdktfaieg 280
|
250 260
....*....|....*....|....*.
gi 1475409280 207 ---ERSVTKLEKSIDDLEDKFLCFTS 229
Cdd:PRK05771 281 wvpEDRVKKLKELIDKATGGSAYVEF 306
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-222 |
1.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 2 AGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRI---------------------QLVE 60
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdapvdlgnaedflEELR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 61 EELDRAQERLATALQKLEEAEKAADESER----------GMKVIES----RAQKDEEKMEIQEIQLKEAKHIAEDADRKY 126
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEAEAlleagkcpecGQPVEGSphveTIEEDRERVEELEAELEDLEEEVEEVEERL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 127 EEvARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFA 206
Cdd:PRK02224 499 ER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577
|
250
....*....|....*.
gi 1475409280 207 ERSVTKLEKSIDDLED 222
Cdd:PRK02224 578 NSKLAELKERIESLER 593
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-179 |
1.29e-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: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 4 SSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 84 ADESERGMKVIESRAQK-----DEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELE 158
Cdd:TIGR02168 402 IERLEARLERLEDRRERlqqeiEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180
....*....|....*....|.
gi 1475409280 159 EELKTVTNNLKSLEAQAEKYS 179
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-223 |
2.41e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 33 RELDHERKLRE------TAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKME 106
Cdd:COG4913 590 HEKDDRRRIRSryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 107 IQEiqLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEkysQKEDRYE 186
Cdd:COG4913 670 IAE--LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---AAEDLAR 744
|
170 180 190
....*....|....*....|....*....|....*..
gi 1475409280 187 EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG4913 745 LELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
46-222 |
4.39e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 46 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI-ESRAQKDEEKMEIQEI--QLKEAKHIAEDA 122
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIeDLRETIAETEREREELaeEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 123 DRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETR 202
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
170 180
....*....|....*....|
gi 1475409280 203 AEFAERSVTKLEKSIDDLED 222
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEE 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
5-204 |
4.68e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 5 SSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 85 DESE------------RGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG 152
Cdd:COG3883 103 SYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1475409280 153 KCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAE 204
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-222 |
4.81e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 8 EAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 88 ERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNN 167
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1475409280 168 LKSLEAQAEKYSQ--------------KEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:PRK02224 435 LRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-216 |
5.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 9 AVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEAD----VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKlviiesdlERAEERAELSEGKCAELE--EELK 162
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA--------DEAKKKAEEDKKKADELKkaAAAK 1417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1475409280 163 TVTNNLKSLEAQAEKYSQKEDRYEEEIKvlSDKLKEAETRAEFAERSVTKLEKS 216
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEEA 1469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-221 |
9.36e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 11 RRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADrkyEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKS 170
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELA---ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1475409280 171 LEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
11-193 |
1.29e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 11 RRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEEL-----DRAQERLATALQKLE--EAEKA 83
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEaeLAELS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 84 ADESERGMKVIESRAQKDEEKMEIQEiqlkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAEL---SEGKCAELEEE 160
Cdd:COG3206 284 ARYTPNHPDVIALRAQIAALRAQLQQ----EAQRILASLEAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLERE 359
|
170 180 190
....*....|....*....|....*....|...
gi 1475409280 161 LKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLS 193
Cdd:COG3206 360 VEVARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2-85 |
1.31e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 2 AGSSSLEAVRRKIRSL----QEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIqlveEELDRAQERLATALQKL 77
Cdd:PRK09039 88 ASLSAAEAERSRLQALlaelAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI----AALRRQLAALEAALDAS 163
|
....*...
gi 1475409280 78 EEAEKAAD 85
Cdd:PRK09039 164 EKRDRESQ 171
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
33-201 |
1.54e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.30 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 33 RELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDE---------E 103
Cdd:pfam05262 192 KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPkpadtsspkE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 104 KMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLER-AEERAELSEGKCAELEEELKTVTNNLKSL--EAQAEKYSQ 180
Cdd:pfam05262 272 DKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQKTkpQVEAQPTSL 351
|
170 180
....*....|....*....|.
gi 1475409280 181 KEDRYEEEIKVLSDKLKEAET 201
Cdd:pfam05262 352 NEDAIDSSNPVYGLKVVDPIT 372
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
7-220 |
1.73e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVR---RKIRSLQEQADAAEERAGTLQRELD-HERKLRETAEADVASLNrriqlvEEELDRAQERLATA---LQKLEE 79
Cdd:COG0497 157 LEEYReayRAWRALKKELEELRADEAERARELDlLRFQLEELEAAALQPGE------EEELEEERRRLSNAeklREALQE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 80 AEKAADESERG--------MKVIESRAQKDEEKMEIQEiQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEER----- 146
Cdd:COG0497 231 ALEALSGGEGGaldllgqaLRALERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFDPERLEEVEERlallr 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 147 ----------AELSEgKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKlkeaetRAEFAERSVTKLEKS 216
Cdd:COG0497 310 rlarkygvtvEELLA-YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAA------RKKAAKKLEKAVTAE 382
|
....
gi 1475409280 217 IDDL 220
Cdd:COG0497 383 LADL 386
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-215 |
1.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 19 EQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRA 98
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 99 QKDEEKMEIQEIQLKEAKHI--AEDADRKYEEVARKlviiESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAE 176
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKK----AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1475409280 177 KYSQ-KEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEK 215
Cdd:PTZ00121 1717 KAEElKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-225 |
2.43e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 59 VEEELDRAQERLATalqkLEEAEKAADESERGMKVIESRAQKDEEkmeIQEIQLKEAKHIAEDADRKYEEVARKLVIIES 138
Cdd:COG4913 223 TFEAADALVEHFDD----LERAHEALEDAREQIELLEPIRELAER---YAAARERLAELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 139 DLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQ-AEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSI 217
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
....*...
gi 1475409280 218 DDLEDKFL 225
Cdd:COG4913 376 PASAEEFA 383
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
55-224 |
3.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 55 RIQLVEEELDRAQERLATALQKLEEAEKAAdESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLV 134
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 135 IIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDrYEEEIKVLSDKLKE-AETRAEFAERSVTKL 213
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREAlAELNDERRERLAEKR 633
|
170
....*....|.
gi 1475409280 214 EKsIDDLEDKF 224
Cdd:PRK02224 634 ER-KRELEAEF 643
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
7-205 |
4.04e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQAD--AAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3206 191 LEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 85 DESERGMKVIESRAQKDEEKMEIQEIQLKeakhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTV 164
Cdd:COG3206 271 QLAELEAELAELSARYTPNHPDVIALRAQ----IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1475409280 165 TNNLKSLEAQAEKYSQKEDRYEEeikvLSDKLKEAETRAEF 205
Cdd:COG3206 347 PELEAELRRLEREVEVARELYES----LLQRLEEARLAEAL 383
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
13-200 |
5.09e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 13 KIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEE-----ELDRAQERLATALQKLEEAEKAAD-- 85
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEkkkaeEAKKAEEDKNMALRKAEEAKKAEEar 1593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 86 --------ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKlviiESDLERAEERAELSEGKCAEL 157
Cdd:PTZ00121 1594 ieevmklyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK----AEELKKAEEENKIKAAEEAKK 1669
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1475409280 158 EEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSD-KLKEAE 200
Cdd:PTZ00121 1670 AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElKKKEAE 1713
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-200 |
5.67e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 11 RRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVtNNLKS 170
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-EQLKK 1640
|
170 180 190
....*....|....*....|....*....|
gi 1475409280 171 LEAQAEKYSQKEDRYEEEIKVLSDKLKEAE 200
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
12-222 |
5.71e-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: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 12 RKIRSLQEQADAAEERAG--------------TLQRELDHERKLR------------------ETAEADVASLNRRIQLV 59
Cdd:TIGR02169 170 RKKEKALEELEEVEENIErldliidekrqqleRLRREREKAERYQallkekreyegyellkekEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 60 EEELDRAQERLATALQKLEEAEKAADE-SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIES 138
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 139 DLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSID 218
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
....
gi 1475409280 219 DLED 222
Cdd:TIGR02169 410 RLQE 413
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
8-197 |
7.04e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 8 EAVRRKIRSLQEqADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEEL---DRAQERLATALQKLEEAEKAA 84
Cdd:PRK10929 48 EALQSALNWLEE-RKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMstdALEQEILQVSSQLLEKSRQAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 85 DESERGMKVIESRAQKDEEKMEIQEiQLKEAKH-------------IAEDADRKYEEVARKLVIIESDL---------ER 142
Cdd:PRK10929 127 QEQDRAREISDSLSQLPQQQTEARR-QLNEIERrlqtlgtpntplaQAQLTALQAESAALKALVDELELaqlsannrqEL 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 143 AEERAELSEGKCAELEEELKTVTNNLKSLEAQ-AEKYSQKEDRYEEEI----KVLSDKLK 197
Cdd:PRK10929 206 ARLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgdlpKSIVAQFK 265
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
40-222 |
7.64e-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: 40.13 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 40 KLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKhia 119
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 120 EDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEA 199
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180
....*....|....*....|...
gi 1475409280 200 ETRAEFAERSVTKLEKSIDDLED 222
Cdd:COG4942 177 EALLAELEEERAALEALKAERQK 199
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
41-223 |
1.24e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 41 LRETAEADVASLNRRIQLVEEELDRAQERLATALQKLE---EAEKAADESERGMKVIESRAQKDEEKMEIQeIQLKEAKH 117
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrQKNGLVDLSEEAKLLLQQLSELESQLAEAR-AELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 118 IAEDADRKYEEVARKLVIIESDLERAEERAELSEGKcAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLsdkLK 197
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE-AELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI---LA 316
|
170 180
....*....|....*....|....*.
gi 1475409280 198 EAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEAR 342
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-224 |
1.35e-03 |
|
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: 39.65 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 66 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQE-----------IQLKEAKHIAEDADRKYEEVARKLV 134
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAelrelelallvLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 135 IIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLE 214
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170
....*....|
gi 1475409280 215 KSIDDLEDKF 224
Cdd:TIGR02168 337 EELAELEEKL 346
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-223 |
1.38e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 47 ADVASLNRRIQLVEEELDRAQERLATA----------LQKLE-EAEKA---------ADESERGMKVIESRAQKDEEKME 106
Cdd:COG1196 165 AGISKYKERKEEAERKLEATEENLERLedilgelerqLEPLErQAEKAeryrelkeeLKELEAELLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 107 IQEIQLKEAKhiAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYE 186
Cdd:COG1196 245 EAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190
....*....|....*....|....*....|....*..
gi 1475409280 187 EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
14-219 |
1.80e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 14 IRSLQEQADAAEERAGTLQRELDHERKLREtaeadvaSLNRRIQLVEEELDRAQERLA-TALQKLEEAEKAADESERGMK 92
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKE-------ELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELR 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 93 VIESRAQKDEEKMEIQEIQ--LKEAKHIAEDADRKYEEVARKL-----VIIESDLERAeERAELSEGKCAELEEE---LK 162
Cdd:PRK00409 595 QLQKGGYASVKAHELIEARkrLNKANEKKEKKKKKQKEKQEELkvgdeVKYLSLGQKG-EVLSIPDDKEAIVQAGimkMK 673
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1475409280 163 TVTNNLKSLEAQAEKYSQKedryeeeIKVLSDKLKEAET----RAEFAERSVTKLEKSIDD 219
Cdd:PRK00409 674 VPLSDLEKIQKPKKKKKKK-------PKTVKPKPRTVSLeldlRGMRYEEALERLDKYLDD 727
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
54-202 |
1.91e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 54 RRIQLVEEELDRAQERLATALQKLEEaekaadesergmkVIESRaqkdEEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 133
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKLNE-------------LIASL----EELERELEQKAEEAEALLKEAEKLKEELEEKK 557
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 134 VIIESDLERAEERAELS-EGKCAELEEELKTVTNNLKSLEaQAEKYSQKEDRYEEEIKVLSDKLKEAETR 202
Cdd:PRK00409 558 EKLQEEEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-224 |
2.01e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 19 EQADAAEERAGTLQ--RELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEE----AEKAADESERGMK 92
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKK 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 93 VIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEElktvtnnlKSLE 172
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK--------KIAH 1761
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1475409280 173 AQAEKYSQKEDRYEEEIKVLSDKLKEAEtraefaERSVTKLEKSIDDLEDKF 224
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEED------EKRRMEVDKKIKDIFDNF 1807
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-221 |
2.05e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 17 LQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIqlveEELDRAQERLATALQKLEEAEKAADESERGMKVIES 96
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 97 RAQKDEEKMEIQEIQLKEAKHIAEDADRK------YEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKS 170
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1475409280 171 LEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
108-203 |
3.02e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 38.78 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 108 QEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEE 187
Cdd:PRK11448 140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 1475409280 188 EIKVLSDK---LKEAETRA 203
Cdd:PRK11448 220 EITDQAAKrleLSEEETRI 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-173 |
3.03e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 8 EAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 88 ERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAE-DADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEeQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....*..
gi 1475409280 167 NLKSLEA 173
Cdd:COG1196 775 EIEALGP 781
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
61-183 |
3.06e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 38.60 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 61 EELDRAQERLATALQKLEEAEKAAD---ESERGMK-VIESRAQKDEEKMEIQEIQLKE----AKHIAEDADRK--YEEVA 130
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREHLEKEVEkklESKSGNKnKMEAKAQANSQKDEIFALINKEanrdARAIAYTQNLKgiKRELS 689
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1475409280 131 RKLVIIESDLER-AEERAELSEGKCAEL---EEELKTVTNNLKSLEAQAEKYSQKED 183
Cdd:pfam18971 690 DKLEKISKDLKDfSKSFDEFKNGKNKDFskaEETLKALKGSVKDLGINPEWISKVEN 746
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
9-222 |
3.29e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.34 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 9 AVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESE 88
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 89 RGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNL 168
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1475409280 169 KSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-188 |
4.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADAAEEragtLQRELDHERKLRETAEADVASLNRRIQLVEEELdraqeRLATALQKLEEAEKAADE 86
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVArklVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180
....*....|....*....|..
gi 1475409280 167 NLKSLEAQAEKYSQKEDRYEEE 188
Cdd:COG4717 221 ELEELEEELEQLENELEAAALE 242
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
19-198 |
4.05e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 38.07 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 19 EQADAAE-ERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQ----KLEEAEKAADeSERGMKV 93
Cdd:NF033838 216 KKAEATRlEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPatpdKKENDAKSSD-SSVGEET 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 94 IESRAQKDEEKMEIQEIQLKEAKHIAEDAD----RKYEEVARK---LVIIESDLERAEERAEL--SEGKCAELEEELKTV 164
Cdd:NF033838 295 LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKeedrRNYPTNTYKtleLEIAESDVKVKEAELELvkEEAKEPRNEEKIKQA 374
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1475409280 165 TNNLKSLEAQA---EKYSQKEDRYEEEIK---VLSDKLKE 198
Cdd:NF033838 375 KAKVESKKAEAtrlEKIKTDRKKAEEEAKrkaAEEDKVKE 414
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
73-193 |
4.25e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 37.84 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 73 ALQKLEEAEKAADEsergmKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEE----RAE 148
Cdd:PRK12704 29 AEAKIKEAEEEAKR-----ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldrKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1475409280 149 LSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLS 193
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
52-193 |
5.30e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 37.88 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 52 LNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkviESRAQKDEEKMEIQEiQLKEAKHIAEDADRKYEEVAR 131
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEE-----KKEKLQEEEDKLLEE-AEKEAQQAIKEAKKEADEIIK 591
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1475409280 132 KLviiesdleRAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYE--EEIKVLS 193
Cdd:PRK00409 592 EL--------RQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKvgDEVKYLS 647
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-210 |
5.44e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 37.81 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 2 AGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERK---LRETAEADVASLNRrIQLVEEELDRAQE--RLATALQK 76
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADE-LKKAAAAKKKADEakKKAEEKKK 1432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 77 LEEAEKAADESERG---------MKVIESRAQKDEEKMEIQEIQLK-EAKHIAEDADRKYEEVARKLVIIESDLERAEER 146
Cdd:PTZ00121 1433 ADEAKKKAEEAKKAdeakkkaeeAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1475409280 147 AELSEGKCAELEEELKTVTNNLKSLEAQA--EKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSV 210
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
46-202 |
5.51e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.21 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 46 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEiqeiQLKEAKHIaEDADRK 125
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG----NVRNNKEY-EALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1475409280 126 YEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKysqKEDRYEEEIKVLSDKLKEAETR 202
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAEREELAAK 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
6-206 |
5.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.57 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 6 SLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAelSEGKCAELEEELKTVT 165
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE--AEQALDELLKEANRNA 196
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1475409280 166 NNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFA 206
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
7-93 |
6.13e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 37.53 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRET---AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:COG2433 422 VERLEAEVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLERELEEERERIEELKRKLERLKEL 501
|
90
....*....|
gi 1475409280 84 ADESERGMKV 93
Cdd:COG2433 502 WKLEHSGELV 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-215 |
6.24e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.44 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 33 RELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAdesergmkviesRAQKDEEKMEIQEIQL 112
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL------------QLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 113 KEAKHIAEDADRKYEEVARKlviiESDLERAEERAELSEGKCAELEEELKTVT-NNLKSLEAQAEKYSQKEDRYEEEIKV 191
Cdd:COG4717 142 AELPERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEE 217
|
170 180
....*....|....*....|....
gi 1475409280 192 LSDKLKEAETRAEFAERSVTKLEK 215
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAAL 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
11-116 |
7.98e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 37.24 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 11 RRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELdRAQERLATALQKLEEAEKAADESERG 90
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQEDLEELTERLEEQEEV 369
|
90 100
....*....|....*....|....*.
gi 1475409280 91 MKVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:COG3096 370 VEEAAEQLAEAEARLEAAEEEVDSLK 395
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-140 |
8.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 37.20 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 2 AGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELdheRKLRETAEADvaslnrriqlvEEELDRAQERLATALQKLEEAE 81
Cdd:COG4913 335 NGGDRLEQLEREIERLERELEERERRRARLEALL---AALGLPLPAS-----------AEEFAALRAEAAALLEALEEEL 400
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1475409280 82 KAADESERGMKVIESRAQKDEEKMEiQEIQLKEAKH--IAEDADRKYEEVARKLVIIESDL 140
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELE-AEIASLERRKsnIPARLLALRDALAEALGLDEAEL 460
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
5-214 |
8.46e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.33 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 5 SSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAqERLATALQKLEEAEKAA 84
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEI 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 85 DE------------SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG 152
Cdd:PRK02224 609 ERlrekrealaelnDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1475409280 153 KCAELE---EELKTVTNNLKSLEAQAEKYSQKEDRYeeeikvlsdklkeAETRAEFAERSVTKLE 214
Cdd:PRK02224 689 ELEELEelrERREALENRVEALEALYDEAEELESMY-------------GDLRAELRQRNVETLE 740
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
7-223 |
8.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 37.43 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRR--KIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVAslnRRIqlveEELDRAQE-RLATALQKLEEAEK- 82
Cdd:PTZ00121 1130 AEEARKaeDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA---KKA----EAARKAEEvRKAEELRKAEDARKa 1202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 83 -AADESERGMKVIESRAQKDEEKMEIQEiQLKEAKHIAEDAdRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEL 161
Cdd:PTZ00121 1203 eAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA 1280
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1475409280 162 KTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLK--EAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
44-223 |
9.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 36.73 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 44 TAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEA----KHIA 119
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 120 EDADRKYEEVARKLVIIES-DLERAEERAELsegkcaeLEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKE 198
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSeSFSDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180
....*....|....*....|....*
gi 1475409280 199 AETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAE 190
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
7-177 |
9.72e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 36.44 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 7 LEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAekaadE 86
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAelsEGKCAELEEELKTVTN 166
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEA 163
|
170
....*....|.
gi 1475409280 167 NLKSLEAQAEK 177
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
71-225 |
9.85e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 36.80 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409280 71 ATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELS 150
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1475409280 151 EGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDKFL 225
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
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