|
Name |
Accession |
Description |
Interval |
E-value |
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
48-282 |
8.68e-69 |
|
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: 220.67 E-value: 8.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 48 KKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERAR 127
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 128 KILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSL 207
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553377 208 EVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLIVEKERYCMIGDSLDEAFVDLI 282
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQTLAELN 235
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
7-152 |
2.13e-26 |
|
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: 104.31 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 7 KMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESeva 86
Cdd:pfam12718 1 KMNSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNEN--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553377 87 aLNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEAR 152
Cdd:pfam12718 78 -LTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKEAK 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
21-266 |
7.11e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.30 E-value: 7.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 21 RALVCEQEARDANTRA---EKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEE 97
Cdd:COG1196 216 RELKEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 98 DLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLE 177
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 178 RAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
....*....
gi 45553377 258 DDLIVEKER 266
Cdd:COG1196 456 EEEEALLEL 464
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-267 |
3.62e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 7 KMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVA 86
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 87 ALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVA 166
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 167 RKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSV 246
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260
....*....|....*....|.
gi 45553377 247 QKLQKEVDRLEDDLIVEKERY 267
Cdd:COG1196 473 ALLEAALAELLEELAEAAARL 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-260 |
3.85e-16 |
|
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: 82.03 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKN-------KALQNAESEVAALNRRIQLLEED 98
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisalrKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 99 LERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLER 178
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 179 AEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLED 258
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
..
gi 45553377 259 DL 260
Cdd:TIGR02168 916 EL 917
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-252 |
2.12e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:TIGR02168 219 KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 115 EASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELE 194
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45553377 195 EELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKE 252
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-277 |
3.75e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 115 EASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELE 194
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 195 EELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRL-----KEAEARAEFAERSVQKLQKEVDRLEDDLIVEKERYCM 269
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaelKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
....*...
gi 45553377 270 IGDSLDEA 277
Cdd:TIGR02168 473 AEQALDAA 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-260 |
7.36e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 82 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADEserarkiLENRALADEERMDALENQLKEARFLAEEADKK 161
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------LNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 162 YDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEF 241
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
250
....*....|....*....
gi 45553377 242 AERSVQKLQKEVDRLEDDL 260
Cdd:TIGR02168 927 LELRLEGLEVRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-226 |
7.54e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 82 ESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKK 161
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553377 162 YDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIK 226
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-260 |
1.04e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 106 LGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVE-------ADLER 178
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLElqiaslnNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 179 AEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKAnqREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLED 258
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQA--ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
..
gi 45553377 259 DL 260
Cdd:TIGR02168 483 EL 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-260 |
1.62e-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: 63.93 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 7 KMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVA 86
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 87 ALNRRIQLLEEDLERSEERLGSATAKLS---------------------EASQAADESERARKILENRALADE-----ER 140
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARLShsripeiqaelskleeevsriEARLREIEQKLNRLTLEKEYLEKEiqelqEQ 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 141 MDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEE 220
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 45553377 221 YKNQIKTLNTRLKEAEARAEF------AERSVQKLQKEVDRLEDDL 260
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEI 967
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
22-233 |
4.67e-10 |
|
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: 61.32 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 22 ALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLER 101
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 102 SEERLGSATAKLSE----------ASQAADESERARKILENRALADEERMDALENQLKEARF-LAEEADKKYDEVARKLA 170
Cdd:COG4942 88 LEKEIAELRAELEAqkeelaellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARReQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553377 171 MVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLK 233
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
18-193 |
7.88e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 18 ALERALV-CEQEARDANTRAEKAEEEARQLQKKIQT---------VENELDQTQEALTlvtgKLEEKNKALQNAESEVAA 87
Cdd:COG4913 614 ALEAELAeLEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIA----ELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 88 LNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVAR 167
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
170 180
....*....|....*....|....*.
gi 45553377 168 KLamvEADLERAEERAEQGENKIVEL 193
Cdd:COG4913 770 NL---EERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-226 |
1.04e-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: 61.23 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 3 AIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAE 82
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 83 SEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALadEERMDALENQLKEARFLAEEADKKY 162
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE--ELLKKLEEAELKELQAELEELEEEL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553377 163 DEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIK 226
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-233 |
1.17e-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: 61.23 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 106 LGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQ 185
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45553377 186 GENKIVELEEELRVVGN-NLKSLEVSEEKANQREEEYKNQIKTLNTRLK 233
Cdd:TIGR02168 934 LEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-261 |
1.63e-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: 60.84 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 47 QKKIQTvENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEE----DLERSEERLGSATAKLSEASQAADE 122
Cdd:TIGR02168 172 ERRKET-ERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAElrelELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 123 SERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGN 202
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45553377 203 NLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLI 261
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-252 |
5.54e-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: 57.85 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 106 LgsatAKLSEASQAADESERARKILENRALADEERMDALENQLKEARflaeeadkkydevARKLAMVEADLERAEERAEQ 185
Cdd:COG4942 106 L----AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR-------------REQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553377 186 GENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKE 252
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-267 |
9.52e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 50 IQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQaadeseRARKI 129
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA------EVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 130 LENRALADEERMDaLENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEV 209
Cdd:TIGR02168 746 EERIAQLSKELTE-LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45553377 210 SEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLIVEKERY 267
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-257 |
3.06e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEK-AEEEARQLQKKIQTVENELDQTQealtlvtGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEE 104
Cdd:TIGR02169 271 EQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLE-------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 105 RLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAE 184
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553377 185 QGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLE 257
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
32-226 |
5.32e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 32 ANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATA 111
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 112 KLSEASQAADESERarkILENRALADE-ERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKI 190
Cdd:COG3883 94 ALYRSGGSVSYLDV---LLGSESFSDFlDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 45553377 191 VELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIK 226
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
54-267 |
3.52e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 54 ENELDQTQEALTLVTGKLEEKNKALQN--AESEVAalnRRIQLLEEDLERSEERLgsATAKLSEASQAADESERARKILE 131
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPleRQAEKA---ERYRELKEELKELEAEL--LLLKLRELEAELEELEAELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 132 NRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSE 211
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45553377 212 EKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLIVEKERY 267
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
51-267 |
4.69e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 51 QTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEedlerSEERLGSATAKLSEASQAADESERARKIL 130
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 131 ENraladeeRMDALENQLKEARFLAEE--ADKKYDEVARKLAMVEAdlERAEERAEQGEN--KIVELEEELRVVGNNLK- 205
Cdd:COG3206 239 EA-------RLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEA--ELAELSARYTPNhpDVIALRAQIAALRAQLQq 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553377 206 -------SLEVSEEKANQREEEYKNQIKTLNTRLKeaearaefaerSVQKLQKEVDRLEDDLIVEKERY 267
Cdd:COG3206 310 eaqrilaSLEAELEALQAREASLQAQLAQLEARLA-----------ELPELEAELRRLEREVEVARELY 367
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
26-221 |
6.92e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQ---------TQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLE 96
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 97 EDLERSEERLGSATAK--LSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEadkkydEVARKLAMVEA 174
Cdd:COG3206 247 AQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ------EAQRILASLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45553377 175 DLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEY 221
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY 367
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
26-221 |
8.36e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLE---RS 102
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraRA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 103 EERLGSATAKLSEASQAADESERARKI--LENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAE 180
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDFLDRLsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45553377 181 ERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEY 221
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
27-204 |
8.41e-07 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 51.61 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 27 QEARDANTRAEKAEEEARQLQKKIQTVE---NELdqtqEALTLVTG---KLEEKNKALQNAESEVAALNRRIQLLEEDLE 100
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRfqlEEL----EAAALQPGeeeELEEERRRLSNAEKLREALQEALEALSGGEG 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 101 RSEERLGSATAKLSEASQAADESERARKILEN---------RAL--------ADEERMDALENQLKEARFLAeeadKKY- 162
Cdd:COG0497 241 GALDLLGQALRALERLAEYDPSLAELAERLESalieleeaaSELrryldsleFDPERLEEVEERLALLRRLA----RKYg 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45553377 163 ---DEVARKLAMVEADLER---AEERAEQGENKIVELEEELRVVGNNL 204
Cdd:COG0497 317 vtvEELLAYAEELRAELAElenSDERLEELEAELAEAEAELLEAAEKL 364
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
26-152 |
1.20e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEE--KNKALQNAESEVAALNRRIQLLEEDLERSE 103
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEALQKEIESLKRRISDLEDEILELM 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 45553377 104 ERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEAR 152
Cdd:COG1579 117 ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-233 |
1.64e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 1 MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQealtlvtGKLEEKNKALQN 80
Cdd:TIGR02169 289 QLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER-------KRRDKLTEEYAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 81 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARF----LAE 156
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkineLEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 157 EADKKYDEVA---RKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLK 233
Cdd:TIGR02169 442 EKEDKALEIKkqeWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
9-255 |
1.99e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 9 QAMKVDKDGALERALVCEQEARDantraekAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAAL 88
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEE-------LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 89 NRRIQLLEEDLERSEERLGSATAKLSEASQAadeserarkILENRALADEERMDALENQLKEARFL--AEEADKKYDEVA 166
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARER---------VEEAEALLEAGKCPECGQPVEGSPHVetIEEDRERVEELE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 167 RKLAMVEADLERAEERAEQGEnKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSV 246
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
....*....
gi 45553377 247 QKLQKEVDR 255
Cdd:PRK02224 561 AEAEEEAEE 569
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
42-192 |
2.57e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 42 EARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSA-TAKLSEASQAA 120
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEALQKE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553377 121 DES-ERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVE 192
Cdd:COG1579 98 IESlKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-174 |
2.79e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAE--------SEVAALNRRIQLLEE 97
Cdd:COG4913 273 ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 98 DLERSEERLGSATAKLSEASQAADESE----RARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVE 173
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
.
gi 45553377 174 A 174
Cdd:COG4913 433 R 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
47-265 |
4.36e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 47 QKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEE--DLERSEERLGSATAKLSEASQAADESE 124
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeiDVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 125 RARKILENRaladEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVE-------LEEEL 197
Cdd:COG4913 689 ALEEQLEEL----EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEerfaaalGDAVE 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553377 198 RVVGNNL-KSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLIVEKE 265
Cdd:COG4913 765 RELRENLeERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYE 833
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2-187 |
6.78e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 82 ESEVAALN------------RRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLK 149
Cdd:COG3883 99 GGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 45553377 150 EARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGE 187
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
78-260 |
1.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 78 LQNAESEVAALNRRIQLLEEdLERSEERLGSATAKLSEASQAAD-----ESERARKILENRALADEERMDALENQLKEAR 152
Cdd:COG4913 237 LERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 153 FLAEEADKKYDEV--------ARKLAMVEADLERAEERAEQGENKIVELEEELRVVGnnlKSLEVSEEKANQREEEYKNQ 224
Cdd:COG4913 316 ARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAAL 392
|
170 180 190
....*....|....*....|....*....|....*.
gi 45553377 225 IKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDL 260
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
35-233 |
1.74e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS 114
Cdd:PRK02224 224 RYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 115 EASQAADESERARKILENRALADEERMD-------ALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGE 187
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLEecrvaaqAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRR 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45553377 188 NKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLK 233
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-199 |
2.08e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 27 QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAEsevaaLNRRIQLLEEDLERSEERL 106
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP-----LYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 107 GSATAKLSEASQAADESERARKILENralADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQG 186
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170
....*....|...
gi 45553377 187 ENKIVELEEELRV 199
Cdd:COG4717 226 EEELEQLENELEA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
27-231 |
2.77e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 27 QEARDAN-TRAEKAEEEARQLQKKIQTVENELD-------QTQEALTLvtgkLEEKNKALQNAESEVAALNRRIQLLEED 98
Cdd:PRK04863 375 DEQQEENeARAEAAEEEVDELKSQLADYQQALDvqqtraiQYQQAVQA----LERAKQLCGLPDLTADNAEDWLEEFQAK 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 99 LERSEERLGSATAKLSEASQAADESERARKILenRALADE-ERMDA------LENQLKEARFLAEEADK---KYDEVARK 168
Cdd:PRK04863 451 EQEATEELLSLEQKLSVAQAAHSQFEQAYQLV--RKIAGEvSRSEAwdvareLLRRLREQRHLAEQLQQlrmRLSELEQR 528
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45553377 169 LAM---VEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTR 231
Cdd:PRK04863 529 LRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
27-277 |
3.79e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 27 QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERL 106
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 107 GSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQG 186
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 187 ENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLIVEKER 266
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
250
....*....|.
gi 45553377 267 YCMIGDSLDEA 277
Cdd:COG4372 278 LEIAALELEAL 288
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-277 |
6.17e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 1 MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQN 80
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 81 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARF------- 153
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAArllllle 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 154 LAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRL- 232
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLp 578
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 45553377 233 --KEAEARAEFAERSVQKLQKEVDRLEDDLIVEKERYCMIGDSLDEA 277
Cdd:COG1196 579 ldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-260 |
8.77e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 28 EARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLG 107
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 108 SATAKLSEA--------------------------------------------------------------SQAADESER 125
Cdd:PRK02224 430 ELEATLRTArerveeaealleagkcpecgqpvegsphvetieedrerveeleaeledleeeveeveerlerAEDLVEAED 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 126 ARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLK 205
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 45553377 206 SLEVSEEKANQReEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDL 260
Cdd:PRK02224 590 SLERIRTLLAAI-ADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF 643
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
53-277 |
1.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 53 VENELDQTQEALTLVTGKLEEK-----NKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLS---EASQAADESE 124
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKeekdlHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEeheERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 125 RARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNL 204
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45553377 205 KSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLIVEKERYCMIGDSLDEA 277
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2-224 |
1.20e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 2 DAIKKKMQAMKVDKDGALERALVCE--QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTlvtgKLEEKNKALQ 79
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLVQQdlEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELE----ALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 80 NAESEVAALNRRIQLLEE---DLERSEERLGSATAKLSEASQAadeSERARKILENRAladeERMDALENQLKEARflAE 156
Cdd:PRK11281 115 RETLSTLSLRQLESRLAQtldQLQNAQNDLAEYNSQLVSLQTQ---PERAQAALYANS----QRLQQIRNLLKGGK--VG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 157 EADKKYDEVAR---KLAMVEA--DLERAE-------------ERAEQGEnKIVELEEELRVVGN--NLKSLEVSEEKANQ 216
Cdd:PRK11281 186 GKALRPSQRVLlqaEQALLNAqnDLQRKSlegntqlqdllqkQRDYLTA-RIQRLEHQLQLLQEaiNSKRLTLSEKTVQE 264
|
....*...
gi 45553377 217 REEEYKNQ 224
Cdd:PRK11281 265 AQSQDEAA 272
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
41-199 |
1.32e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 41 EEARQLQKkiqtvenELDQTQE---ALTLVTGKLEEKNKALQNAEsevaalnRRIQLLeedlerseerlGSATAKLSEAS 117
Cdd:PRK10929 120 EKSRQAQQ-------EQDRAREisdSLSQLPQQQTEARRQLNEIE-------RRLQTL-----------GTPNTPLAQAQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 118 QAADESERARKilenRALADEERMDALE--NQLKEARFLAEEADKKYDEVARKLAMV----------EAD--LERAEERA 183
Cdd:PRK10929 175 LTALQAESAAL----KALVDELELAQLSanNRQELARLRSELAKKRSQQLDAYLQALrnqlnsqrqrEAEraLESTELLA 250
|
170
....*....|....*.
gi 45553377 184 EQGENKIVELEEELRV 199
Cdd:PRK10929 251 EQSGDLPKSIVAQFKI 266
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
27-228 |
1.53e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 27 QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEaltlVTGKLEEKNKALQNAESEVAALNRRIQLL----EEDLERS 102
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELgfesVEELEER 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 103 EERLGSATAKLSEASQAADESERarkilenralaDEERMDALENQLKEARFLAEEADKKYDEVARKLAmvEADLERAEER 182
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELER-----------EEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEEE 660
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45553377 183 AEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTL 228
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
5-218 |
1.55e-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: 44.22 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 5 KKKMQAMKVDKDGALERAL----VCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQN 80
Cdd:pfam05262 180 KKVVEALREDNEKGVNFRRdmtdLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 81 AESEVaalnrRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKilenrALADEERmdalenqlKEARFLAEEADK 160
Cdd:pfam05262 260 LPKPA-----DTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKD-----HKAFDLK--------QESKASEKEAED 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45553377 161 KYDEVARKLAMVEADLERAEeraEQGENKIVELEEELRVVGNNLKSLEVSEEKANQRE 218
Cdd:pfam05262 322 KELEAQKKREPVAEDLQKTK---PQVEAQPTSLNEDAIDSSNPVYGLKVVDPITNLSE 376
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-261 |
1.60e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 66 LVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALE 145
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 146 NQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQI 225
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190
....*....|....*....|....*....|....*.
gi 45553377 226 KTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLI 261
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
19-196 |
1.66e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 19 LERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTlvtgkleEKNKALQNAESEVAALNRRIQLLEED 98
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAELKER 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 99 LERseerLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARklamveADLER 178
Cdd:PRK02224 588 IES----LERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAR------EDKER 657
|
170
....*....|....*...
gi 45553377 179 AEERAEQGENKIVELEEE 196
Cdd:PRK02224 658 AEEYLEQVEEKLDELREE 675
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-265 |
2.19e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 1 MDAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQN 80
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 81 AESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILE--NRALADEERMDALENQLKEARFLAEEA 158
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEqeLQALSEAEAEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 159 DKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEAR 238
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260
....*....|....*....|....*..
gi 45553377 239 AEFAERSVQKLQKEVDRLEDDLIVEKE 265
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAA 306
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
85-267 |
2.24e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 85 VAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERAR------------------KILENRALADEERMDALEN 146
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekaeryqallkekreyegYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 147 QLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQ-GENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQI 225
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45553377 226 KTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLIVEKERY 267
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-222 |
2.69e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 3 AIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEarqlQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAE 82
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA----KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 83 SEVAALNRRIQLL---EEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDA--LENQLKEARFLAEE 157
Cdd:PTZ00121 1655 AEEENKIKAAEEAkkaEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAeeLKKAEEENKIKAEE 1734
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553377 158 ADKKYDEVARKLAMVEADlERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYK 222
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-260 |
6.41e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 45 QLQKKIQTVENELDQTQEALTLVTGKLEEKN--------------------------------KALQNAESEVAALNRRI 92
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqlerlrrerekaeryqallkekreyegyellKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 93 QLLEEDLERSEERLGSATAKLSEASQAADE-SERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAM 171
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 172 VEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQK 251
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
....*....
gi 45553377 252 EVDRLEDDL 260
Cdd:TIGR02169 407 ELDRLQEEL 415
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
26-260 |
8.65e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRriqlLEEDLERSEER 105
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNR----YESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 106 LGSATAKLSEASQAadeSERARKILENRALADEERMD---ALENQLKEARFLAEEAD---KKYDEVARKLAMVEADLERA 179
Cdd:PRK01156 265 LSMELEKNNYYKEL---EERHMKIINDPVYKNRNYINdyfKYKNDIENKKQILSNIDaeiNKYHAIIKKLSVLQKDYNDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 180 EERAEQGENkIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDD 259
Cdd:PRK01156 342 IKKKSRYDD-LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
.
gi 45553377 260 L 260
Cdd:PRK01156 421 I 421
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-265 |
9.23e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 106 LGSATAKLSEASQAADESERARKILENRALADEERmdaLENQLKEarflAEEADKKYDEvarkLAMVEADLERAEERAEQ 185
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGFESVEE---LEERLKE----LEPFYNEYLE----LKDAEKELEREEKELKK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 186 GENKIVELEEELRVVGNNLKSL--EVSEEKANQREEEYKNqIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLIVE 263
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELrkELEELEKKYSEEEYEE-LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
..
gi 45553377 264 KE 265
Cdd:PRK03918 703 LE 704
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2-205 |
9.71e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 2 DAIKKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNA 81
Cdd:pfam19220 149 QAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 82 ES-----------EVAALNRRIQLLEEDLERSEERLGSATAKLSE-------ASQAADESERARKILENRALADEERMDA 143
Cdd:pfam19220 229 EAqleeaveahraERASLRMKLEALTARAAATEQLLAEARNQLRDrdeairaAERRLKEASIERDTLERRLAGLEADLER 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45553377 144 LENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLK 205
Cdd:pfam19220 309 RTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALE 370
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
37-175 |
9.95e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 42.05 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 37 EKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRI--------QLLEEDLERSE----E 104
Cdd:pfam07111 513 EQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELtqqqeiygQALQEKVAEVEtrlrE 592
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45553377 105 RLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARflAEEADKkydeVARKLAMVEAD 175
Cdd:pfam07111 593 QLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEAR--KEEGQR----LARRVQELERD 657
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
6-189 |
1.34e-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: 41.59 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 6 KKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEV 85
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 86 AALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRaLADEERMDALENQLKEARFLAEEADKKYDEV 165
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL-QRVEEEIRALEPVNMLAIQEYEEVLKRLDEL 991
|
170 180
....*....|....*....|....
gi 45553377 166 ARKLAMVEADLERAEERAEQGENK 189
Cdd:TIGR02169 992 KEKRAKLEEERKAILERIEEYEKK 1015
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
90-250 |
1.36e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 90 RRIQLLEEDLERSEERLGSATAKLSEASQAADESERArkilenraladeermdaLENQLKEARFLAEEADKKYDEVARKL 169
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKLNELIASLEELERE-----------------LEQKAEEAEALLKEAEKLKEELEEKK 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 170 AMVEADLERAEERAEQGENKIV-ELEEELRVVGNNLKSLEvSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQK 248
Cdd:PRK00409 558 EKLQEEEDKLLEEAEKEAQQAIkEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
..
gi 45553377 249 LQ 250
Cdd:PRK00409 637 LK 638
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
42-228 |
1.40e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 42 EARQLQKKIQTVENELDQTQ----EALTLVTGKLEEKNKALQNAE------SEVAALNR--RIQLLEEDLERSEERLGSA 109
Cdd:PRK10929 24 DEKQITQELEQAKAAKTPAQaeivEALQSALNWLEERKGSLERAKqyqqviDNFPKLSAelRQQLNNERDEPRSVPPNMS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 110 TAKLS------------EASQAADESERARKILE------------NRALAD-EERMDALENQ---LKEARFLAEEADKk 161
Cdd:PRK10929 104 TDALEqeilqvssqlleKSRQAQQEQDRAREISDslsqlpqqqteaRRQLNEiERRLQTLGTPntpLAQAQLTALQAES- 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45553377 162 ydeVARKLAMVEADL---------ERAEERAEQGENKIVELEEELRVVGNNLKSLEVSE-EKANQREEEYKNQIKTL 228
Cdd:PRK10929 183 ---AALKALVDELELaqlsannrqELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREaERALESTELLAEQSGDL 256
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
26-286 |
1.42e-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: 41.54 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEER 105
Cdd:TIGR04523 348 KKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 106 LGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQ 185
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 186 GENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKeaearAEFAERSVQKLQKEVDRLEDD---LIV 262
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTqksLKK 582
|
250 260
....*....|....*....|....
gi 45553377 263 EKERYCMIGDSLDEAFVDLIKGLE 286
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
45-233 |
1.44e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.36 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 45 QLQKKIQTVENELDQTQEAL-TLVTGKLEEKNKALQNA--------ESEVAALN---RRIQLLEEDLERSEERLGSATAK 112
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLeELDLDEAEEKNEEIQERidqlydilEREVKARKyveKNSDTLPDFLEHAKEQNKELKEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 113 LSEASQ----AADESERARKIlenraladEERMDALENQLKEARFLAEEADKKYDEVarklamveadleraEERAEQGEN 188
Cdd:PRK04778 333 IDRVKQsytlNESELESVRQL--------EKQLESLEKQYDEITERIAEQEIAYSEL--------------QEELEEILK 390
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45553377 189 KIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLK 233
Cdd:PRK04778 391 QLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLE 435
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
18-138 |
1.45e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 18 ALERALVCEQEARDANTRAEKAEEEArqLQKKIQTVENELDQTQEALTlvtGKLEEKNKALQNAESEVAALNRRIQLLEE 97
Cdd:PRK09039 70 SLERQGNQDLQDSVANLRASLSAAEA--ERSRLQALLAELAGAGAAAE---GRAGELAQELDSEKQVSARALAQVELLNQ 144
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 45553377 98 DLERSEERLGSATAKLsEASQAADEsERARKILE-----NRALADE 138
Cdd:PRK09039 145 QIAALRRQLAALEAAL-DASEKRDR-ESQAKIADlgrrlNVALAQR 188
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
5-257 |
1.52e-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: 41.16 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 5 KKKMQAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESE 84
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 85 VAA-------LNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEE 157
Cdd:TIGR04523 449 DSVkeliiknLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 158 ADKKYDEVARKLAMVEADLERAEER--AEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEA 235
Cdd:TIGR04523 529 LESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
250 260
....*....|....*....|..
gi 45553377 236 EARAEFAERSVQKLQKEVDRLE 257
Cdd:TIGR04523 609 EKKISSLEKELEKAKKENEKLS 630
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
70-266 |
1.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 70 KLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAAdeserarkilenRALADEERMDALENQLK 149
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL------------QLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 150 EARFLAEEADKKYDEVARKlamvEADLERAEERAEQGENKIVELEEELRVVG-NNLKSLEVSEEKANQREEEYKNQIKTL 228
Cdd:COG4717 143 ELPERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190
....*....|....*....|....*....|....*...
gi 45553377 229 NTRLkeaearaefaersvQKLQKEVDRLEDDLIVEKER 266
Cdd:COG4717 219 QEEL--------------EELEEELEQLENELEAAALE 242
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
77-232 |
1.66e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 77 ALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSE--ASQAADESERARkilenraladeermdaLENQLKEARFL 154
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANlrASLSAAEAERSR----------------LQALLAELAGA 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45553377 155 AEEADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNnlkSLEVSEEkanqREEEYKNQIKTLNTRL 232
Cdd:PRK09039 111 GAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEA---ALDASEK----RDRESQAKIADLGRRL 181
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
14-222 |
1.86e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 14 DKDGALERALVCEQEardantraekaeeearqlqkkIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQ 93
Cdd:PRK04863 280 ERRVHLEEALELRRE---------------------LYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 94 L------LEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQL---------KEARFLA-EE 157
Cdd:PRK04863 339 LvqtalrQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyqqaldvQQTRAIQyQQ 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45553377 158 ADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKsleVSEEKANQREEEYK 222
Cdd:PRK04863 419 AVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS---VAQAAHSQFEQAYQ 480
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
78-226 |
1.99e-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: 39.91 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 78 LQNAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARflaee 157
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR----- 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45553377 158 ADKKYDEVARKLAMVEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIK 226
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
35-255 |
2.04e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 35 RAEKAEEEARQLQKKIQTVENELDQTQEALTLVT-GK-----LEEKNKALQNAESEVAALNRRIQL---LEEDLERSEER 105
Cdd:PLN02939 157 DLEKILTEKEALQGKINILEMRLSETDARIKLAAqEKihveiLEEQLEKLRNELLIRGATEGLCVHslsKELDVLKEENM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 106 LGSATAKL--SEASQAADESERARKILENRALadeerMDALENQLkEARFLAEEAD------KKYDEVARKLAMVEADLE 177
Cdd:PLN02939 237 LLKDDIQFlkAELIEVAETEERVFKLEKERSL-----LDASLREL-ESKFIVAQEDvsklspLQYDCWWEKVENLQDLLD 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 178 RAEERAEQG----------ENKIVELEEELR---VVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAER 244
Cdd:PLN02939 311 RATNQVEKAalvldqnqdlRDKVDKLEASLKeanVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQD 390
|
250
....*....|.
gi 45553377 245 SVQKLQKEVDR 255
Cdd:PLN02939 391 TLSKLKEESKK 401
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
21-224 |
2.68e-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: 40.71 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 21 RALVCEQEARdANTRAEKAEEEARQLQKKIQTVENELD----------QTQEALTLVTGKLEEKNKALQNAESEVAALNR 90
Cdd:COG3096 370 VEEAAEQLAE-AEARLEAAEEEVDSLKSQLADYQQALDvqqtraiqyqQAVQALEKARALCGLPDLTPENAEDYLAAFRA 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 91 RIQLLEEDLERSEERLGSATAKLSEASQA-------ADESER------ARKIL----ENRALAdeERMDALENQLKE--- 150
Cdd:COG3096 449 KEQQATEEVLELEQKLSVADAARRQFEKAyelvckiAGEVERsqawqtARELLrryrSQQALA--QRLQQLRAQLAEleq 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 151 -------ARFLAEEADKKYDEVARKLAMVEADLERAEERAEqgenkivELEEELRVVGNNLKSLEVSEEKANQREEEYKN 223
Cdd:COG3096 527 rlrqqqnAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE-------ELEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
.
gi 45553377 224 Q 224
Cdd:COG3096 600 R 600
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
26-227 |
2.97e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAE------EEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEE-- 97
Cdd:PHA02562 206 EQRKKNGENIARKQNkydelvEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKgg 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 98 -------DLERSEERLGSATAKLSEASQAADESERARKILenraladEERMDALENQLKEARflaeeadkkydEVARKLA 170
Cdd:PHA02562 286 vcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL-------EEIMDEFNEQSKKLL-----------ELKNKIS 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45553377 171 MVEADLERAEERAEQGENKIVELE-------EELRVVGNNLKslEVSEEKANQREEEYKNQIKT 227
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQaefvdnaEELAKLQDELD--KIVKTKSELVKEKYHRGIVT 409
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-225 |
3.24e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 27 QEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERL 106
Cdd:pfam01576 728 QFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQM 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 107 GSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAEQG 186
Cdd:pfam01576 808 KDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRL 887
|
170 180 190
....*....|....*....|....*....|....*....
gi 45553377 187 ENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQI 225
Cdd:pfam01576 888 EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTEL 926
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
38-223 |
3.88e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 38 KAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERL----GSATAKL 113
Cdd:PRK01156 378 KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlnGQSVCPV 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 114 SEASQAADESERARKILENRALADEERMDALENQLkearflaeeadKKYDEVARKLAMVEADLERAE-ERAEQGENKIVE 192
Cdd:PRK01156 458 CGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEV-----------KDIDEKIVDLKKRKEYLESEEiNKSINEYNKIES 526
|
170 180 190
....*....|....*....|....*....|.
gi 45553377 193 LEEELRVVGNNLKSLEVSEEKANQREEEYKN 223
Cdd:PRK01156 527 ARADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
27-265 |
4.03e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 27 QEARDANTRAEKAEE--EARQLQKKIQTVENELDQTQEaltlvtgKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEE 104
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKK-------AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 105 RLGSATAKLSEASQAAD--ESERARKILENRalADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEER 182
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEElkKAEEKKKAEEAK--KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 183 AEQGENKIVELEEELRVVGNNLKSLEVSEEKANQ-REEEYKNQIKTlnTRLKEAEARAEFAERSVQKLQKEVDRLEDDLI 261
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKA--AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
....
gi 45553377 262 VEKE 265
Cdd:PTZ00121 1696 KEAE 1699
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
9-260 |
4.99e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 9 QAMKVDKDGALERALVCEQEARDANTRAEKAEEEARQ--LQKKIQTVENELDQTQEALTLvTGK-------LEEKNKALQ 79
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSAREsdLEQDYQAASDHLNLVQTALRQ-QEKieryqedLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 80 NAESEVAALNRRIQLLEEDLERSEERLGSATAKLSEASQAADES--------------ERARKILENRALADE------E 139
Cdd:COG3096 365 EQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqalEKARALCGLPDLTPEnaedylA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 140 RMDALENQLKEARF-------LAEEADKKYDEVARKLAMVEADLERaeERAEQGENKIVELEEELRVVGNNLKSLEVSEE 212
Cdd:COG3096 445 AFRAKEQQATEEVLeleqklsVADAARRQFEKAYELVCKIAGEVER--SQAWQTARELLRRYRSQQALAQRLQQLRAQLA 522
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 45553377 213 KANQREEEYKN---QIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDL 260
Cdd:COG3096 523 ELEQRLRQQQNaerLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
88-263 |
6.66e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 38.92 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 88 LNRRIQLLEEDLERSEERLGSATAKLSEASQAADES-ERARKILENRALADEERMDALENQLKEArflAEEADKKYDeva 166
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELlLRERNQQRQEARREREELQREEERLVQK---EEQLDARAE--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 167 rKLAMVEADLERAEERAEQGENKIVELEEELRvvgnnlkslEVSEEKANQREEEYKNQI-KTLNTRLKEAEARAEFAERs 245
Cdd:PRK12705 99 -KLDNLENQLEEREKALSARELELEELEKQLD---------NELYRVAGLTPEQARKLLlKLLDAELEEEKAQRVKKIE- 167
|
170
....*....|....*...
gi 45553377 246 vQKLQKEVDRLEDDLIVE 263
Cdd:PRK12705 168 -EEADLEAERKAQNILAQ 184
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-233 |
6.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 108 SATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAE--EADKKYDEVARKLamveADLERAEERAEQ 185
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEysWDEIDVASAEREI----AELEAELERLDA 682
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 45553377 186 GENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLK 233
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
14-260 |
7.88e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 14 DKDGALE--RALVCEQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEKNKALQnaesEVAALNRR 91
Cdd:PRK02224 184 DQRGSLDqlKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE----ELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 92 IQLLEEDLERSEERLGSATAKLSEASQAADESERARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAM 171
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 172 VEADLERAEERAEQGENKIVELEEELRVVGNNLKSLEVSEEKANQREEEYKNQIKTLNTRLKEAEARAEFAERSVQKLQK 251
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
....*....
gi 45553377 252 EVDRLEDDL 260
Cdd:PRK02224 420 ERDELRERE 428
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
106-232 |
8.15e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.61 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 106 LGSATAKLSEASQAADESERARKILEN-RALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLERAEERAE 184
Cdd:PRK12704 20 IGYFVRKKIAEAKIKEAEEEAKRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 45553377 185 QGENKIVELEEELRvvgNNLKSLEVSEEKANQREEEYKNQIKTLNTRL 232
Cdd:PRK12704 100 RKLELLEKREEELE---KKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
26-122 |
8.40e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTGKLEEK-NKALQNAESEVAALNRRIQLLE--EDLERS 102
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQLQkgGYASVK 605
|
90 100
....*....|....*....|
gi 45553377 103 EERLGSATAKLSEASQAADE 122
Cdd:PRK00409 606 AHELIEARKRLNKANEKKEK 625
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
26-265 |
8.55e-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: 39.17 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 26 EQEARDANTRAEKAEEEARQLQKKIQTVENELDQTQEALTLVTG------------------KLEEKNKALQNAESEVAA 87
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladrleELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 88 LNRRIQLLE----------EDLERSEERLGSATAKLSEASQAADE-------------SERARKILENRALAD--EERMD 142
Cdd:COG3096 915 HGKALAQLEplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFAlsevvqrrphfsyEDAVGLLGENSDLNEklRARLE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 143 ALENQLKEARFLAEEADKKYDEVARklamVEADLERAEERAEQgenKIVELEEELRVVGnnLKSLEVSEEKANQREEEYK 222
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQ----VLASLKSSRDAKQQ---TLQELEQELEELG--VQADAEAEERARIRRDELH 1065
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 45553377 223 NQIKTLNTRLKEAEARAEFAERSVQKLQKEVDRLEDDLIVEKE 265
Cdd:COG3096 1066 EELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
35-136 |
9.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45553377 35 RAEKAEEEARQLQKKIQTVENELDQTQEAL-TLVTGKLEEKNKALQNAESEVAALNRRIQLLEEDLERSEERLGSATAKL 113
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
90 100
....*....|....*....|...
gi 45553377 114 SEASQAADESERARKILENRALA 136
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLL 252
|
|
| |
