|
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 |
2.40e-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: 205.65 E-value: 2.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 92 KVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL 171
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568961235 172 EAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDE 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
6-221 |
2.01e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 6 SLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVT 165
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568961235 166 NNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-223 |
7.22e-14 |
|
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: 70.86 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsegkcaELEEELKTVTN 166
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSE 852
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568961235 167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 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 |
9.15e-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: 63.86 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEadvaSLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGM 91
Cdd:pfam12718 42 HKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNE----NLTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKV 117
|
90 100
....*....|....*....|....*
gi 568961235 92 KVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:pfam12718 118 QALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-223 |
2.64e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568961235 167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-223 |
3.37e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 sergmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196 328 -------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568961235 167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10-222 |
5.91e-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: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 10 VRRKIRSLQEQADAAEE-----------RAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLE 78
Cdd:COG1196 198 LERQLEPLERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 79 EAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELE 158
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961235 159 EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-223 |
1.39e-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: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 8 EAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 88 ERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNN 167
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568961235 168 LKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-210 |
6.46e-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: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKT 163
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568961235 164 VTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSV 210
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-215 |
1.85e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 SERGmkviESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196 391 ALRA----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568961235 167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEK 215
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-221 |
1.90e-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: 57.08 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 1 MAGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA 80
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 81 EKAADESErgmKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 160
Cdd:COG4942 96 RAELEAQK---EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568961235 161 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
32-224 |
1.92e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 32 QRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQ 111
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 112 LKEAKHIAEDADRKYE-------EVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDK 184
Cdd:TIGR02168 756 LTELEAEIEELEERLEeaeeelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568961235 185 YEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDKF 224
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-223 |
5.05e-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: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 2 AGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 82 KAADESERGMKVIESR-----AQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAE 156
Cdd:TIGR02169 751 QEIENVKSELKELEARieeleEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568961235 157 LEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-224 |
1.86e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEEragsLQRELDQERKLR--------ETAEADVASLNRRIQLVEEELDRAQERLATALQKLE 78
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAER----YKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 79 EAEKAADESERGMKVI--------------ESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAE 144
Cdd:TIGR02168 271 ELRLEVSELEEEIEELqkelyalaneisrlEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 145 ERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDKF 224
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-224 |
2.08e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 6 SLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 86 ESERGMKVIESRAQKDEEKMEIQ-------EIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELE 158
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961235 159 EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAefAERSVTKLEKSIDDLEDKF 224
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEEL 456
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-177 |
4.04e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRET---------AEADVASLNRRIQLVEEELDRAQE---RLATAL 74
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDAssdDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 75 QKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLViiesDLERAEERAELSEGKC 154
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVEREL 767
|
170 180
....*....|....*....|....
gi 568961235 155 AE-LEEELKTVTNNLKSLEAQAEK 177
Cdd:COG4913 768 REnLEERIDALRARLNRAEEELER 791
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-204 |
6.10e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQerLATALQKLEEAEKAADESERG 90
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS--AEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGkcAELEEELKTvtnnlks 170
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAA------- 757
|
170 180 190
....*....|....*....|....*....|....
gi 568961235 171 lEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 204
Cdd:COG4913 758 -ALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-221 |
1.08e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLqEQADAAEERAGSLQRELDQERKLRETAEADVASlnRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:COG4913 244 LEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 SERgmkviesraqkdeekmeiQEIQLKEAkhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEelkTVTN 166
Cdd:COG4913 321 LRE------------------ELDELEAQ--IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL---PLPA 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568961235 167 NLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-221 |
1.28e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEEL-----DRAQERLATALQKLE 78
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELS 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 79 EAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELE 158
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961235 159 EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7-206 |
2.59e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADA-----AEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATA-LQKLEEA 80
Cdd:COG4913 264 YAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 81 EKAADESERGMKVIESRAQKDEEKmeIQEIQLkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEE 160
Cdd:COG4913 344 EREIERLERELEERERRRARLEAL--LAALGL-PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568961235 161 LKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLSDKLKEAETRAEFA 206
Cdd:COG4913 421 LRELEAEIASLERRKSNIPA---RLLALRDALAEALGLDEAELPFV 463
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-215 |
3.15e-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: 50.83 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 4 SSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 84 ADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAE------------LSE 151
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEellkkleeaelkELQ 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961235 152 GKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEK 215
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-176 |
4.38e-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: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 SERGMKviESRAQKDEEKMEIQEIQLKEA---KHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAEL------ 157
Cdd:TIGR02168 913 LRRELE--ELREKLAQLELRLEGLEVRIDnlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnla 990
|
170 180
....*....|....*....|
gi 568961235 158 -EEELKTVTNNLKSLEAQAE 176
Cdd:TIGR02168 991 aIEEYEELKERYDFLTAQKE 1010
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
5-204 |
9.35e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 5 SSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 85 DESERGMKVIE------------SRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG 152
Cdd:COG3883 96 YRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568961235 153 KCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 204
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
8-198 |
1.08e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 8 EAVRRKIRSLQEQADAAEERAGSLQRELDQ-ERKLRE-TAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAkhiaeDADRKYEEVARKL-----VIIESDLERAEERAELSEgkcaELEEE 160
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLA-----ELEAELAELSARYtpnhpDVIALRAQIAALRAQLQQ----EAQRI 314
|
170 180 190
....*....|....*....|....*....|....*...
gi 568961235 161 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKE 198
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAE 352
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-223 |
1.63e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 8 EAVRRKIRSLQEQADAAEE-RAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADE 86
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAdRKYEEVARKLVIIESD-LERAEERAELSEG--------KCAEL 157
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA-RKADELKKAEEKKKADeAKKAEEKKKADEAkkkaeeakKADEA 1320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961235 158 EEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
33-223 |
7.70e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 33 RELDQERKLRE------TAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKME 106
Cdd:COG4913 590 HEKDDRRRIRSryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 107 IQEiqLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYE 186
Cdd:COG4913 670 IAE--LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190
....*....|....*....|....*....|....*..
gi 568961235 187 EEikvLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG4913 748 RA---LLEERFAAALGDAVERELRENLEERIDALRAR 781
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
13-233 |
1.30e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 13 KIRSLQEQADAAEERAGSLQRELDQERKLRET-AEADVASLNRRIQLVEEELDRAQERLATALQKLEE--AEKAADESE- 88
Cdd:PRK05771 44 RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISEleNEIKELEQEi 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 89 -------------------RGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVA---RKLVIIESDLERAE-E 145
Cdd:PRK05771 124 erlepwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVvlkELSDEVEEELKKLGfE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 146 RAELSEGKC-----AELEEELKTVTNNLKSLEAQAEKYSQkedKYEEEIKVLSDKL----KEAETRAEFA---------- 206
Cdd:PRK05771 204 RLELEEEGTpseliREIKEELEEIEKERESLLEELKELAK---KYLEELLALYEYLeielERAEALSKFLktdktfaieg 280
|
250 260 270
....*....|....*....|....*....|..
gi 568961235 207 ---ERSVTKLEKSIDDLEDKFLC--FTPPKTP 233
Cdd:PRK05771 281 wvpEDRVKKLKELIDKATGGSAYveFVEPDEE 312
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-216 |
1.37e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 9 AVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEAD----VASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADeakkKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKlviiesdlERAEERAELSEGKCAELE--EELK 162
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA--------DEAKKKAEEDKKKADELKkaAAAK 1417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568961235 163 TVTNNLKSLEAQAEKYSQKEDKYEEEIKvlSDKLKEAETRAEFAERSVTKLEKS 216
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKAEEAKKKAEEA 1469
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-222 |
1.95e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 8 EAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRI---------------------QLVEEELDRA 66
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdapvdlgnaedflEELREERDEL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 67 QERLATALQKLEEAEKAADESER----------GMKVIES----RAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEvARK 132
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEAlleagkcpecGQPVEGSphveTIEEDRERVEELEAELEDLEEEVEEVEERLER-AED 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 133 LVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTK 212
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
250
....*....|
gi 568961235 213 LEKSIDDLED 222
Cdd:PRK02224 584 LKERIESLER 593
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-222 |
2.29e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 8 EAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 88 ERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNN 167
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961235 168 LKSLEAQAEKYSQ--------------KEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:PRK02224 435 LRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
11-193 |
3.08e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEEL-----DRAQERLATALQKLE--EAEKA 83
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEaeLAELS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 84 ADESERGMKVIESRAQKDEEKMEIQEiqlkEAKHIAEDADRKYEEVARKLVIIESDLERAEERAEL---SEGKCAELEEE 160
Cdd:COG3206 284 ARYTPNHPDVIALRAQIAALRAQLQQ----EAQRILASLEAELEALQAREASLQAQLAQLEARLAElpeLEAELRRLERE 359
|
170 180 190
....*....|....*....|....*....|...
gi 568961235 161 LKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLS 193
Cdd:COG3206 360 VEVARELYESLLQRLEEARLAEALTVGNVRVID 392
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
46-222 |
4.55e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 46 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVI-ESRAQKDEEKMEIQEI--QLKEAKHIAEDA 122
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIeDLRETIAETEREREELaeEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 123 DRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETR 202
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
170 180
....*....|....*....|
gi 568961235 203 AEFAERSVTKLEKSIDDLED 222
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEE 391
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2-85 |
4.73e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 2 AGSSSLEAVRRKIRSL----QEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIqlveEELDRAQERLATALQKL 77
Cdd:PRK09039 88 ASLSAAEAERSRLQALlaelAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI----AALRRQLAALEAALDAS 163
|
....*...
gi 568961235 78 EEAEKAAD 85
Cdd:PRK09039 164 EKRDRESQ 171
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
11-221 |
6.89e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADrkyEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKS 170
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELA---ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568961235 171 LEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
7-220 |
1.31e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVR---RKIRSLQEQADAAEERAGSLQRELDQ-ERKLRETAEADVASLNrriqlvEEELDRAQERLATA---LQKLEE 79
Cdd:COG0497 157 LEEYReayRAWRALKKELEELRADEAERARELDLlRFQLEELEAAALQPGE------EEELEEERRRLSNAeklREALQE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 80 AEKAADESERG--------MKVIESRAQKDEEKMEIQEiQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEER----- 146
Cdd:COG0497 231 ALEALSGGEGGaldllgqaLRALERLAEYDPSLAELAE-RLESALIELEEAASELRRYLDSLEFDPERLEEVEERlallr 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 147 ----------AELSEgKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKlkeaetRAEFAERSVTKLEKS 216
Cdd:COG0497 310 rlarkygvtvEELLA-YAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAA------RKKAAKKLEKAVTAE 382
|
....
gi 568961235 217 IDDL 220
Cdd:COG0497 383 LADL 386
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
33-201 |
1.52e-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: 42.68 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 33 RELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDE---------E 103
Cdd:pfam05262 192 KGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPkpadtsspkE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 104 KMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLER-AEERAELSEGKCAELEEELKTVTNNLKSL--EAQAEKYSQ 180
Cdd:pfam05262 272 DKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQKTkpQVEAQPTSL 351
|
170 180
....*....|....*....|.
gi 568961235 181 KEDKYEEEIKVLSDKLKEAET 201
Cdd:pfam05262 352 NEDAIDSSNPVYGLKVVDPIT 372
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
7-205 |
1.53e-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: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQAD--AAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:COG3206 191 LEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 85 DESERGMKVIESRAQKDEEKMEIQEIQLKeakhIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTV 164
Cdd:COG3206 271 QLAELEAELAELSARYTPNHPDVIALRAQ----IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568961235 165 TNNLKSLEAQAEKYSQKEDKYEEeikvLSDKLKEAETRAEF 205
Cdd:COG3206 347 PELEAELRRLEREVEVARELYES----LLQRLEEARLAEAL 383
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-200 |
1.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERG 90
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 91 MKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVtNNLKS 170
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-EQLKK 1640
|
170 180 190
....*....|....*....|....*....|
gi 568961235 171 LEAQAEKYSQKEDKYEEEIKVLSDKLKEAE 200
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-222 |
1.90e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 15 RSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEElDRAQERLATALQKLEEAEKAadesERGMKVI 94
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA-KKAEEDKNMALRKAEEAKKA----EEARIEE 1596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 95 ESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAElsegKCAELEEELKTVTNNLKSLEAQ 174
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEE 1672
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568961235 175 AEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
14-219 |
2.52e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 14 IRSLQEQADAAEERAGSLQRELDQERKLREtaeadvaSLNRRIQLVEEELDRAQERLA-TALQKLEEAEKAADESERGMK 92
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKE-------ELEEKKEKLQEEEDKLLEEAEkEAQQAIKEAKKEADEIIKELR 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 93 VIESRAQKDEEKMEIQEIQ--LKEAKHIAEDADRKYEEVARKL-----VIIESDLERAeERAELSEGKCAELEEELKTVT 165
Cdd:PRK00409 595 QLQKGGYASVKAHELIEARkrLNKANEKKEKKKKKQKEKQEELkvgdeVKYLSLGQKG-EVLSIPDDKEAIVQAGIMKMK 673
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568961235 166 NNLKSLeaqaEKYSQKEDKYEEEIKVLSDKLKEAET----RAEFAERSVTKLEKSIDD 219
Cdd:PRK00409 674 VPLSDL----EKIQKPKKKKKKKPKTVKPKPRTVSLeldlRGMRYEEALERLDKYLDD 727
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
55-224 |
3.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 55 RIQLVEEELDRAQERLATALQKLEEAEKAAdESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLV 134
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 135 IIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDkYEEEIKVLSDKLKE-AETRAEFAERSVTKL 213
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD-AEDEIERLREKREAlAELNDERRERLAEKR 633
|
170
....*....|.
gi 568961235 214 EKsIDDLEDKF 224
Cdd:PRK02224 634 ER-KRELEAEF 643
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-225 |
5.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 59 VEEELDRAQERLATalqkLEEAEKAADESERGMKVIESRAQKDEEkmeIQEIQLKEAKHIAEDADRKYEEVARKLVIIES 138
Cdd:COG4913 223 TFEAADALVEHFDD----LERAHEALEDAREQIELLEPIRELAER---YAAARERLAELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 139 DLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSI 217
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
....*...
gi 568961235 218 DDLEDKFL 225
Cdd:COG4913 376 PASAEEFA 383
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
7-92 |
5.89e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQ--------EQADAAEERAGSLQRELDQERKLRETAEADVAS---LNRRIQLVEEELDRAQERLATALQ 75
Cdd:COG0542 413 LDELERRLEQLEiekealkkEQDEASFERLAELRDELAELEEELEALKARWEAekeLIEEIQELKEELEQRYGKIPELEK 492
|
90
....*....|....*..
gi 568961235 76 KLEEAEKAADESERGMK 92
Cdd:COG0542 493 ELAELEEELAELAPLLR 509
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
24-239 |
6.30e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 24 AEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkviESRAQKDEE 103
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA-----EIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 104 KMEIQEIQ-----------LKEAKHIAEDADRkyeeVARKLVIIESD---LERAEERAELSEGKCAELEEELKTVTNNLK 169
Cdd:COG3883 89 GERARALYrsggsvsyldvLLGSESFSDFLDR----LSALSKIADADadlLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 170 SLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDKFLCFTPPKTPSSSWMS 239
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAA 234
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-207 |
7.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 33 RELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQL 112
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 113 KEakhiaedadRKYEEVARKLVIIESDLERAEER-AELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKV 191
Cdd:COG4717 154 RL---------EELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170
....*....|....*.
gi 568961235 192 LSDKLKEAETRAEFAE 207
Cdd:COG4717 225 LEEELEQLENELEAAA 240
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
108-203 |
1.18e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.93 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 108 QEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEE 187
Cdd:PRK11448 140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 568961235 188 EIKVLSDK---LKEAETRA 203
Cdd:PRK11448 220 EITDQAAKrleLSEEETRI 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
19-190 |
1.22e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 19 EQADAAEERAGSLQ--RELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEE----AEKAADESERGMK 92
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKK 1689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 93 VIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAelEEELKTVTNNLKSLE 172
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD--EEEKKKIAHLKKEEE 1767
|
170
....*....|....*....
gi 568961235 173 AQAEKY-SQKEDKYEEEIK 190
Cdd:PTZ00121 1768 KKAEEIrKEKEAVIEEELD 1786
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
14-197 |
1.23e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.04 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 14 IRSLQEQADAAEERAGSLQR--------------------ELDQERKLRETAEADVAS--LNRRI-----QLVEE----- 61
Cdd:PRK10929 47 VEALQSALNWLEERKGSLERakqyqqvidnfpklsaelrqQLNNERDEPRSVPPNMSTdaLEQEIlqvssQLLEKsrqaq 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 62 -ELDRAQE---RLATALQKLEEAEKAADESERGMKVIESRAQKDEEkmeiqeiqlkeakhiAEDADRKYEEVARKLVIIE 137
Cdd:PRK10929 127 qEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQ---------------AQLTALQAESAALKALVDE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961235 138 SDL---------ERAEERAELSEGKCAELEEELKTVTNNLKSLEAQ-AEKYSQKEDKYEEEI----KVLSDKLK 197
Cdd:PRK10929 192 LELaqlsannrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQReAERALESTELLAEQSgdlpKSIVAQFK 265
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
54-202 |
1.46e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 54 RRIQLVEEELDRAQERLATALQKLEEaekaadesergmkVIESRaqkdEEKMEIQEIQLKEAKHIAEDADRKYEEVARKL 133
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKLNE-------------LIASL----EELERELEQKAEEAEALLKEAEKLKEELEEKK 557
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 134 VIIESDLERAEERAELS-EGKCAELEEELKTVTNNLKSLEaQAEKYSQKEDKYEEEIKVLSDKLKEAETR 202
Cdd:PRK00409 558 EKLQEEEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
9-222 |
1.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 9 AVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESE 88
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 89 RGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNL 168
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568961235 169 KSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
6-206 |
1.51e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 6 SLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAAD 85
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 86 ESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAelSEGKCAELEEELKTVT 165
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE--AEQALDELLKEANRNA 196
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568961235 166 NNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFA 206
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
11-116 |
1.65e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELdRAQERLATALQKLEEAEKAADESERG 90
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQADLEELEERLEEQNEV 370
|
90 100
....*....|....*....|....*.
gi 568961235 91 MKVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:PRK04863 371 VEEADEQQEENEARAEAAEEEVDELK 396
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
73-193 |
1.70e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 73 ALQKLEEAEKAADEsergmKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEE----RAE 148
Cdd:PRK12704 29 AEAKIKEAEEEAKR-----ILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldrKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 568961235 149 LSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLS 193
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
17-221 |
1.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 17 LQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIqlveEELDRAQERLATALQKLEEAEKAADESERGMKVIES 96
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 97 RAQKDEEKMEIQEIQLKEAKHIAEDADRK------YEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKS 170
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568961235 171 LEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-224 |
2.52e-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: 38.88 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 66 AQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQE-----------IQLKEAKHIAEDADRKYEEVARKLV 134
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAelrelelallvLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 135 IIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLE 214
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170
....*....|
gi 568961235 215 KSIDDLEDKF 224
Cdd:TIGR02168 337 EELAELEEKL 346
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
7-93 |
2.69e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 38.69 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRET---AEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:COG2433 422 VERLEAEVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLERELEEERERIEELKRKLERLKEL 501
|
90
....*....|
gi 568961235 84 ADESERGMKV 93
Cdd:COG2433 502 WKLEHSGELV 511
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
7-85 |
2.70e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 38.29 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKlRETAEADVASLNR---RIQLVEEELDRAQERLATALQKLEEAEKA 83
Cdd:COG3524 237 LAALRSYLSPNSPQVRQLRRRIAALEKQIAAERA-RLTGASGGDSLASllaEYERLELEREFAEKAYTSALAALEQARIE 315
|
..
gi 568961235 84 AD 85
Cdd:COG3524 316 AA 317
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-188 |
2.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEEragsLQRELDQERKLRETAEADVASLNRRIQLVEEELdraqeRLATALQKLEEAEKAADE 86
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVArklVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180
....*....|....*....|..
gi 568961235 167 NLKSLEAQAEKYSQKEDKYEEE 188
Cdd:COG4717 221 ELEELEEELEQLENELEAAALE 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
41-223 |
2.73e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 38.84 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 41 LRETAEADVASLNRRIQLVEEELDRAQERLATALQKLE---EAEKAADESERGMKVIESRAQKDEEKMEIQeIQLKEAKH 117
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrQKNGLVDLSEEAKLLLQQLSELESQLAEAR-AELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 118 IAEDADRKYEEVARKLVIIESDLERAEERAELSEGKcAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLsdkLK 197
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE-AELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI---LA 316
|
170 180
....*....|....*....|....*.
gi 568961235 198 EAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEAR 342
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
7-223 |
2.90e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRR--KIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVAslnRRIqlveEELDRAQE-RLATALQKLEEAEK- 82
Cdd:PTZ00121 1130 AEEARKaeDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDA---KKA----EAARKAEEvRKAEELRKAEDARKa 1202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 83 -AADESERGMKVIESRAQKDEEKMEIQEiQLKEAKHIAEDAdRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEEL 161
Cdd:PTZ00121 1203 eAARKAEEERKAEEARKAEDAKKAEAVK-KAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA 1280
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961235 162 KTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLK--EAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
52-193 |
2.99e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 38.65 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 52 LNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERgmkviESRAQKDEEKMEIQEiQLKEAKHIAEDADRKYEEVAR 131
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEE-----KKEKLQEEEDKLLEE-AEKEAQQAIKEAKKEADEIIK 591
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568961235 132 KLviiesdleRAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYE--EEIKVLS 193
Cdd:PRK00409 592 EL--------RQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKvgDEVKYLS 647
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-173 |
3.28e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.38 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 8 EAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADES 87
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 88 ERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAE-DADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTN 166
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEeQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....*..
gi 568961235 167 NLKSLEA 173
Cdd:COG1196 775 EIEALGP 781
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-210 |
3.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 2 AGSSSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERK---LRETAEADVASLNRrIQLVEEELDRAQE--RLATALQK 76
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADE-LKKAAAAKKKADEakKKAEEKKK 1432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 77 LEEAEKAADESERG---------MKVIESRAQKDEEKMEIQEIQLK-EAKHIAEDADRKYEEVARKLVIIESDLERAEER 146
Cdd:PTZ00121 1433 ADEAKKKAEEAKKAdeakkkaeeAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568961235 147 AELSEGKCAELEEELKTVTNNLKSLEAQA--EKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSV 210
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
14-219 |
3.44e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.34 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 14 IRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKV 93
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 94 IESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEA 173
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568961235 174 QAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDD 219
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-216 |
3.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.58 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 18 QEQADAAEERAGSLQRELDQERKLRETAEADVASlnrriqlVEEELDRAQE-RLATALQKLEEAEKAADESERGMKVIES 96
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-------KADELKKAEElKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 97 RAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKlviiESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAE 176
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK----AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568961235 177 KYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKS 216
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
12-204 |
3.66e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 38.51 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 12 RKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEA----EKAADES 87
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQkeaiERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 88 ERGMKVIESRAQKDEEKMEIQEIQLKE-AKHIAEDADRKYEEVARKLVIIESDLERAE-------ERAELSEGKCAELEE 159
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLErsiaekeRELEDAEERLAKLEA 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 568961235 160 ELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAE 204
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-223 |
3.69e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.38 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 47 ADVASLNRRIQLVEEELDRAQERLATA----------LQKLE-EAEKA---------ADESERGMKVIESRAQKDEEKME 106
Cdd:COG1196 165 AGISKYKERKEEAERKLEATEENLERLedilgelerqLEPLErQAEKAeryrelkeeLKELEAELLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 107 IQEIQLKEAKhiAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYE 186
Cdd:COG1196 245 EAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190
....*....|....*....|....*....|....*..
gi 568961235 187 EEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDK 223
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
13-198 |
3.97e-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: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 13 KIRSLQEQADAAEERAGSLQR------ELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQ----KLEEAEK 82
Cdd:NF033838 205 KIKQAKAKVESKKAEATRLEKiktdreKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPatpdKKENDAK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 83 AADeSERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDAD----RKYEEVARK---LVIIESDLERAEERAEL--SEGK 153
Cdd:NF033838 285 SSD-SSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKeedrRNYPTNTYKtleLEIAESDVKVKEAELELvkEEAK 363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568961235 154 CAELEEELKTVTNNLKSLEAQA---EKYSQKEDKYEEEIK---VLSDKLKE 198
Cdd:NF033838 364 EPRNEEKIKQAKAKVESKKAEAtrlEKIKTDRKKAEEEAKrkaAEEDKVKE 414
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
61-183 |
4.14e-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: 38.21 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 61 EELDRAQERLATALQKLEEAEKAAD---ESERGMK-VIESRAQKDEEKMEIQEIQLKE----AKHIAEDADRK--YEEVA 130
Cdd:pfam18971 610 DEVKKAQKDLEKSLRKREHLEKEVEkklESKSGNKnKMEAKAQANSQKDEIFALINKEanrdARAIAYTQNLKgiKRELS 689
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 568961235 131 RKLVIIESDLER-AEERAELSEGKCAEL---EEELKTVTNNLKSLEAQAEKYSQKED 183
Cdd:pfam18971 690 DKLEKISKDLKDfSKSFDEFKNGKNKDFskaEETLKALKGSVKDLGINPEWISKVEN 746
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
7-202 |
4.19e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.40 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLretaeaDVASLNRRIQLVEEELDRAQErlatALQKLEEAEKAADE 86
Cdd:PRK04863 853 LADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLL------ADETLADRVEEIREQLDEAEE----AKRFVQQHGNALAQ 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 SERGMKVIesraQKDEEKMEIQEIQLKEAKHIAEDADRKY----EEVARKLVIIESD-LERAEERAELSE---GKCAELE 158
Cdd:PRK04863 923 LEPIVSVL----QSDPEQFEQLKQDYQQAQQTQRDAKQQAfaltEVVQRRAHFSYEDaAEMLAKNSDLNEklrQRLEQAE 998
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 568961235 159 EELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETR 202
Cdd:PRK04863 999 QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQE 1042
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
11-116 |
4.55e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.01 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELdRAQERLATALQKLEEAEKAADESERG 90
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQEDLEELTERLEEQEEV 369
|
90 100
....*....|....*....|....*.
gi 568961235 91 MKVIESRAQKDEEKMEIQEIQLKEAK 116
Cdd:COG3096 370 VEEAAEQLAEAEARLEAAEEEVDSLK 395
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
7-177 |
4.98e-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: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 7 LEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAekaadE 86
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-----R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 87 SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAelsEGKCAELEEELKTVTN 166
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEA 163
|
170
....*....|.
gi 568961235 167 NLKSLEAQAEK 177
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
46-198 |
6.21e-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: 36.83 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 46 EADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEiqeiQLKEAKHIaEDADRK 125
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG----NVRNNKEY-EALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961235 126 YEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKE 198
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-223 |
6.39e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 37.81 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 11 RRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASlnrriqlVEEELDRAQERLATALQKLEEAEKAADESERg 90
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA-------AADEAEAAEEKAEAAEKKKEEAKKKADAAKK- 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 91 mkviesraqKDEEKMEIQEiqlkeAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKS 170
Cdd:PTZ00121 1386 ---------KAEEKKKADE-----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568961235 171 LEAQAEKYSQKEDKYEEEIKVLSDKLKEAETR-AEFAERSVTKLEKSIDDLEDK 223
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkADEAKKKAEEAKKKADEAKKA 1505
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
11-185 |
6.78e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 37.45 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 11 RRKIRSLQEQAD----AAEERAGSLQREL-----DQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAE 81
Cdd:PRK12704 30 EAKIKEAEEEAKrileEAKKEAEAIKKEAlleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 82 KAadesergmkvIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARklviiesdLERAEERAELSEgkcaELEEEL 161
Cdd:PRK12704 110 EE----------LEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--------LTAEEAKEILLE----KVEEEA 167
|
170 180
....*....|....*....|....*
gi 568961235 162 KTVTNNL-KSLEAQAEKYSQKEDKY 185
Cdd:PRK12704 168 RHEAAVLiKEIEEEAKEEADKKAKE 192
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
5-214 |
7.14e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.33 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 5 SSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAqERLATALQKLEEAEKAA 84
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEI 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 85 DE------------SERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEG 152
Cdd:PRK02224 609 ERlrekrealaelnDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961235 153 KCAELE---EELKTVTNNLKSLEAQAEKYSQKEDKYeeeikvlsdklkeAETRAEFAERSVTKLE 214
Cdd:PRK02224 689 ELEELEelrERREALENRVEALEALYDEAEELESMY-------------GDLRAELRQRNVETLE 740
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
5-225 |
7.44e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 37.31 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 5 SSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 85 DESERGMKVIESRAQKDEEKMEIQEIQLKE------------AKHIAEDADRKYEEVARKLVIIESDLERAEERAELS-- 150
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELlekeierlketiIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvl 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961235 151 EGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDKFL 225
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
71-225 |
7.52e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.19 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 71 ATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELS 150
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961235 151 EGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDKFL 225
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
32-221 |
7.56e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 37.35 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 32 QRELDQERK--LRETAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAqkdeekmEIQE 109
Cdd:pfam13166 262 GQPLPAERKaaLEAHFDDEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEA-------EVLN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 110 IQLKEAKHIAED------ADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAqaEKYSQKED 183
Cdd:pfam13166 335 SQLDGLRRALEAkrkdpfKSIELDSVDAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRLHLV--EEFKSEID 412
|
170 180 190
....*....|....*....|....*....|....*...
gi 568961235 184 KYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLE 221
Cdd:pfam13166 413 EYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELE 450
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
101-221 |
7.85e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 37.21 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 101 DEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLEraeeraelSEGKCAELEEELKtvtnnLKSLEAQAEKYSQ 180
Cdd:PRK05771 27 ELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLP--------KLNPLREEKKKVS-----VKSLEELIKDVEE 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568961235 181 KEDKYEEEIKVLSDKLKEAETRaefaersVTKLEKSIDDLE 221
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENE-------IKELEQEIERLE 127
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
47-221 |
8.23e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 37.35 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 47 ADVASLNRRIQLVEEELDRAQERLATALQKLEEAEkaaDESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKY 126
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKR---QQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 127 EEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSL-EAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEF 205
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170
....*....|....*.
gi 568961235 206 AERSVTKLEKSIDDLE 221
Cdd:TIGR02169 320 AEERLAKLEAEIDKLL 335
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
5-222 |
8.69e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.33 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 5 SSLEAVRRKIRSLQEQADAAEERAGSLQRELDQERKLRETAEAdvasLNRRIQLVEEELDRAQERLATALQKLEEAEKAA 84
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961235 85 DESERGMKVIESRAQKDEEKMEIQEIQLKEAKHiAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTV 164
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKE-RIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568961235 165 TNNLKSLEAQ-----AEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLED 222
Cdd:PRK02224 633 RERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| |
