|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2-333 |
1.14e-30 |
|
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: 122.59 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 2 SEKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESR 81
Cdd:pfam01576 403 SEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETR 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 82 MKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVrSEEVEELKRKMNAKIQELESEA 161
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT-LEALEEGKKRLQRELEALTQQL 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 162 ESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRL 241
Cdd:pfam01576 562 EEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 242 KAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLE 321
Cdd:pfam01576 642 ARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVN 721
|
330
....*....|..
gi 21998636 322 MSQIRQEIDRRL 333
Cdd:pfam01576 722 MQALKAQFERDL 733
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
43-335 |
5.96e-17 |
|
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: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 43 ELQRQLEEAESQLSQLNKikQQLSAQLEEARHSLEDESRMKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQ 122
Cdd:COG1196 217 ELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 123 GELQQLRSRgggggdvrSEEVEELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERK 202
Cdd:COG1196 295 AELARLEQD--------IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 203 QNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHE 282
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 21998636 283 IDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
10-331 |
6.96e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.78 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 10 ESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSL-------EDESRM 82
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaevEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 83 KAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSrgggggdvRSEEVEELKRKMNAKIQELESEAE 162
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--------ELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 163 SAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEwqkkyadSQAELENAQRDARGQSTEIFRLK 242
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 243 AQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRL-EMEKEELQAALEEAESALEQEEAKVQRAQLE 321
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
330
....*....|
gi 21998636 322 MSQIRQEIDR 331
Cdd:TIGR02168 974 LKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-331 |
1.58e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 22 EATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNK---IKQQLSA--------QLEEARHSLEDESRMKAKLNGEV 90
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykeLKAELRElelallvlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 91 RNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRgggggdvrSEEVEELKRKMNAKIQELESEAESAKSKCGQ 170
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE--------ISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 171 LEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHE 250
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 251 QMEGLRRENKNLSDEIHDLTEQLGEGgrSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEID 330
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
.
gi 21998636 331 R 331
Cdd:TIGR02168 486 Q 486
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-335 |
5.27e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRM 82
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 83 KAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSrgggggdvRSEEVEELKRKMNAKIQELESEAE 162
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE--------ALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 163 SAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLK 242
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 243 AQLEEVHEQMEGLRRE------NKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQ 316
Cdd:COG1196 470 EEAALLEAALAELLEElaeaaaRLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
330
....*....|....*....
gi 21998636 317 RAQLEMSQIRQEIDRRLAE 335
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKA 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-335 |
1.65e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 45 QRQLEEAESQLSQLNKIKQQLSAQLE----EAR-----HSLEDESR-MKAKLNG-EVRNLTSDLDSLRETLEEEQSAKGD 113
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEplerQAEkaeryRELKEELKeLEAELLLlKLRELEAELEELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 114 LQAQLQKLQGELQQLRSRgGGGGDVRSEEVEELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERAN 193
Cdd:COG1196 258 LEAELAELEAELEELRLE-LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 194 GLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQL 273
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21998636 274 GEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
3-330 |
3.07e-12 |
|
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: 67.51 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRM 82
Cdd:pfam01576 207 EKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 83 KAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQELESEAE 162
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 163 SAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLK 242
Cdd:pfam01576 367 QAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVS 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 243 AQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEM 322
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQL 526
|
....*...
gi 21998636 323 SQIRQEID 330
Cdd:pfam01576 527 SDMKKKLE 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-335 |
7.11e-12 |
|
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: 66.63 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 32 STKARSSQEVSELQRQLEEAESQLSQLNkikQQLSAQLEEARHSLEDESRMKAKLNGEVRNLTSDLDSLRETLEEEQSAK 111
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKR---QQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 112 GDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRK-------MNAKIQELESEAESAKSKCGQLEKTKARLQGELED 184
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 185 LMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSD 264
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR 406
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21998636 265 EIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-323 |
8.21e-12 |
|
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: 66.24 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 7 KALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKL 86
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 87 NGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELqqlrsrggggGDVRSEEVEELKRKMNAKIQELESEAESAKS 166
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL----------SHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 167 KCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLE 246
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21998636 247 EVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEElqaaleeaESALEQEEAKVQRAQLEMS 323
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE--------ELSLEDVQAELQRVEEEIR 968
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
30-254 |
1.04e-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: 62.09 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 30 QASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLNGEVRNLTSDLDSLRETLEEEQS 109
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 110 AKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRK---MNAKIQELESEAESAKSKCGQLEKTKARLQGELEDLM 186
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21998636 187 VDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEG 254
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-307 |
1.17e-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: 62.78 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNE-QASTKARSSQEVSELQRQLEEAESQLSQLNkikqqlsAQLEEARHSLEDESR 81
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLE-------RSIAEKERELEDAEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 82 MKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRgggggdvrSEEVEELKRKMNAKIQELESEA 161
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE--------LEEVDKEFAETRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 162 ESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRL 241
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21998636 242 KAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNR-------RRLEMEKEELQAALEEAESA 307
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGN 547
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-290 |
1.76e-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: 62.38 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 19 KLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLNGEVR------- 91
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerla 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 92 NLTSDLDSLRETLEEEQSAKGDLQA-------QLQKLQGELQQLRSRGggggdvrsEEVEELKRKMNAKIQELESEAESA 164
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEelaeleeKLEELKEELESLEAEL--------EELEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 165 KSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKK-----YADSQAELENAQRDARGQSTEIF 239
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 21998636 240 RLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEG---GRSVHEIDKNRRRL 290
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLegfSEGVKALLKNQSGL 518
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2-228 |
1.76e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 2 SEKTVKALESQLQEVSVKLDEATRNLNE---------QASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEA 72
Cdd:COG3206 173 ARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 73 RHSLEDESRmkaklNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRsrgggggdvrseevEELKRKMNA 152
Cdd:COG3206 253 PDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR--------------AQLQQEAQR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21998636 153 KIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQ 228
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-265 |
2.40e-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: 58.53 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRM 82
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 83 KAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSrgggggdvRSEEVEELKRKMNAKIQELESEAE 162
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS--------KVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 163 sakskcgQLEKTKARLQGELEDLMVDVERANglASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLK 242
Cdd:TIGR02168 411 -------RLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260
....*....|....*....|...
gi 21998636 243 AQLEEVHEQMEGLRRENKNLSDE 265
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-233 |
4.18e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRM 82
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 83 KAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRG---GGGGDVRSEEVEELKRKMnakiqeLES 159
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLerlEDRRERLQQEIEELLKKL------EEA 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21998636 160 EAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARG 233
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
40-335 |
5.69e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 40 EVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLNGEVRNLTsdldslretlEEEQSAkgdLQAQLQ 119
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG----------EEEQLR---VKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 120 KLQGELQQLRSRgggggdvrSEEVEELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQL 199
Cdd:TIGR02169 298 ELEAEIASLERS--------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 200 ERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLgeggrs 279
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK------ 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 21998636 280 vHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:TIGR02169 444 -EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
39-275 |
1.39e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 39 QEVSELQRQLEEAESQLSQLNKIkQQLSAQLEEARHSLEDESRMKAKLNG-----EVRNLTSDLDSLRETLEEEQSAKGD 113
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPI-RELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 114 LQAQLQKLQGELQQLR-SRGGGGGDvrseeveelkrkmnaKIQELESEAESAKSKCGQLEKTKARLQGELEDLmvdvera 192
Cdd:COG4913 314 LEARLDALREELDELEaQIRGNGGD---------------RLEQLEREIERLERELEERERRRARLEALLAAL------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 193 nGLASQLERKQnnFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQ 272
Cdd:COG4913 372 -GLPLPASAEE--FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
...
gi 21998636 273 LGE 275
Cdd:COG4913 449 LAE 451
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-324 |
4.40e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRM 82
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 83 KAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGggggdvrsEEVEELKRKMNAKIQELESEAE 162
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI--------ESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 163 SAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQsteifrLK 242
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE------YS 950
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 243 AQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEM 322
Cdd:TIGR02168 951 LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREA 1030
|
..
gi 21998636 323 SQ 324
Cdd:TIGR02168 1031 RE 1032
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
108-335 |
5.63e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 108 QSAKGDLQAQLQKLQGELQQLRSRgggggdvrSEEVEELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQGELEDLMv 187
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKE--------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 188 dvERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIH 267
Cdd:COG4942 90 --KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21998636 268 DLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-334 |
3.73e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 7 KALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKL 86
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 87 NGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGG--GGGDVRSEEVEELKRKMNAKIQELESEAESA 164
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEaeEALLERLERLEEELEELEEALAELEEEEEEE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 165 KSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELenAQRDARGQSTEIFRLKAQ 244
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE--ADYEGFLEGVKAALLLAG 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 245 LEEVHEQMEGLRRENKNLSDEIHDLteqlgEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQ 324
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAA-----LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
330
....*....|
gi 21998636 325 IRQEIDRRLA 334
Cdd:COG1196 594 RGAIGAAVDL 603
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-335 |
3.88e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 99 SLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNaKIQELESEAESAKSKCGQLEKTKARL 178
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK-EIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 179 QGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQaeLENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRE 258
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21998636 259 NKNLSDEIHDLTEQlgeggrsVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:TIGR02169 828 KEYLEKEIQELQEQ-------RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
54-328 |
3.91e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 54 QLSQLNKIKQQLSAQLEEARHSLEDESRmkaKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGEL-------- 125
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIE---ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLhkrekels 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 126 --QQLRSRGGGGGDVRSEEVEELKRKM---NAKIQELESEAESAKSKC-GQLEKTKARLQGELEDLmvdvERANGLASQL 199
Cdd:pfam15921 395 leKEQNKRLWDRDTGNSITIDHLRRELddrNMEVQRLEALLKAMKSECqGQMERQMAAIQGKNESL----EKVSSLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 200 ERKQNNFNR----------TLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSD----- 264
Cdd:pfam15921 471 ESTKEMLRKvveeltakkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtec 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 265 -------------------EIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQI 325
Cdd:pfam15921 551 ealklqmaekdkvieilrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
...
gi 21998636 326 RQE 328
Cdd:pfam15921 631 ELE 633
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-167 |
1.47e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 1 NSEKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDes 80
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE-- 898
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 81 rmkakLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQELESE 160
Cdd:TIGR02168 899 -----LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
....*..
gi 21998636 161 AESAKSK 167
Cdd:TIGR02168 974 LKRLENK 980
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-258 |
1.76e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 6 VKALESQLQEVSVKLDEATRNLNEQA----STKARSSQEVSELQRQLEEAesqlsqLNKIKQqLSAQLEEarhsledesr 81
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYNknieEQRKKNGENIARKQNKYDEL------VEEAKT-IKAEIEE---------- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 82 mkakLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSrgGGGGDVRSEEVEELKRKMnakiqelESEA 161
Cdd:PHA02562 239 ----LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRI-------TKIK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 162 ESAKSKCGQLEKTKARlQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRL 241
Cdd:PHA02562 306 DKLKELQHSLEKLDTA-IDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKL 384
|
250
....*....|....*..
gi 21998636 242 KAQLEEVHEQMEGLRRE 258
Cdd:PHA02562 385 QDELDKIVKTKSELVKE 401
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
16-335 |
1.85e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.52 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 16 VSVKLDEATRNLNEQASTKARSSQEVSELQRQ-----LEEAESQLSQLNKIKQQlsaQLEEARHSLEDESRMKAKLNGEV 90
Cdd:PLN02939 100 ASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEdlvgmIQNAEKNILLLNQARLQ---ALEDLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 91 RNLtSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMnakiQELESEAESAKSKCGQ 170
Cdd:PLN02939 177 MRL-SETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEN----MLLKDDIQFLKAELIE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 171 LEKTKARLqgeledlmvdveranglaSQLERKQNNFNRTLAEWQKKYADSQAE---LENAQRDARGQSTEifRLKAQLEE 247
Cdd:PLN02939 252 VAETEERV------------------FKLEKERSLLDASLRELESKFIVAQEDvskLSPLQYDCWWEKVE--NLQDLLDR 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 248 VHEQMEG---LRRENKNLSDEIHDLTEQLGEGG---RSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLE 321
Cdd:PLN02939 312 ATNQVEKaalVLDQNQDLRDKVDKLEASLKEANvskFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDT 391
|
330
....*....|....
gi 21998636 322 MSQIRQEIDRRLAE 335
Cdd:PLN02939 392 LSKLKEESKKRSLE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-132 |
1.99e-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: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNE-QASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESR 81
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 21998636 82 MKAKLNGEVRNLTSDLDSLRETLEEEQ----SAKGDLQAQLQKLQGELQQLRSRG 132
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALaeaeAALRDLRRELRELEAEIASLERRK 435
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
19-227 |
3.73e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 19 KLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLS------------AQLEEARHSLEDESRMKAKL 86
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdeidvasaereiAELEAELERLDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 87 NGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQELESEAEsaks 166
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE---- 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21998636 167 kcgqlekTKARLQGELEDLmvdVERANGLASQLERKQNNFNRtlaEWQKKYADSQAELENA 227
Cdd:COG4913 767 -------LRENLEERIDAL---RARLNRAEEELERAMRAFNR---EWPAETADLDADLESL 814
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
3-192 |
6.63e-06 |
|
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: 47.45 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQL-NKIKQQLSAQLEEARH------- 74
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQkEELAELLRALYRLGRQpplalll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 75 ---SLEDESRMKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSrgggggdvRSEEVEELKRKMN 151
Cdd:COG4942 127 speDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE--------ERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21998636 152 AKIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERA 192
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
39-331 |
1.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 39 QEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEdesrmkaklngEVRNLTSDLDSLRETLEEEQSAKGDLQAQL 118
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-----------ELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 119 QKLQGELQQLRSRGGGG------GDVRSEEVEELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERA 192
Cdd:PRK02224 282 RDLRERLEELEEERDDLlaeaglDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 193 NGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQ 272
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 21998636 273 LGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDR 331
Cdd:PRK02224 442 VEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
12-272 |
1.11e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 12 QLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQL----SQLNKIKQQLSA------QLEEARHSLEdesr 81
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVdelkSQLADYQQALDVqqtraiQYQQAVQALE---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 82 mKAKLNGEVRNLTsdLDSLRETLEEeqsakgdLQAQLQKLQGELQQLRSRGGGGGDVRS--EEVEELKRKMNAKIqELES 159
Cdd:PRK04863 425 -RAKQLCGLPDLT--ADNAEDWLEE-------FQAKEQEATEELLSLEQKLSVAQAAHSqfEQAYQLVRKIAGEV-SRSE 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 160 EAESAKSKCGQLEKTKAR------LQGELEDLmvdveranglaSQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARG 233
Cdd:PRK04863 494 AWDVARELLRRLREQRHLaeqlqqLRMRLSEL-----------EQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
250 260 270
....*....|....*....|....*....|....*....
gi 21998636 234 QSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQ 272
Cdd:PRK04863 563 LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
20-335 |
1.97e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 20 LDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLS------AQLEEARHSLEDESRMKAKLNGEVRNL 93
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKelekrlEELEERHELYEEAKAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 94 TS-DLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGG------------------GGDVRSEEVEELKRKMNAKI 154
Cdd:PRK03918 382 TGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaieelkkakgkcpvcGRELTEEHRKELLEEYTAEL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 155 QELESEAESAKSKCGQLEKTKARLQGELEDlMVDVERANGLASQLERKQNNFNRTLAEWQKKYADsqaELENAQRDARGQ 234
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEELEKKAE---EYEKLKEKLIKL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 235 STEIFRLKAQLEEVHE---QMEGLRRENKNLSDEIHDLTEQLGEGG-RSVHEIDKNRRRLEMEKEELqAALEEAESALEQ 310
Cdd:PRK03918 538 KGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEY-LELKDAEKELER 616
|
330 340
....*....|....*....|....*
gi 21998636 311 EEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKR 641
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
102-306 |
3.33e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 102 ETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQGE 181
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 182 LEDLM------VDVERANGLAS-----------QLERKQNNFNRTLAEW--------------QKKYADSQAEL------ 224
Cdd:PRK05771 123 IERLEpwgnfdLDLSLLLGFKYvsvfvgtvpedKLEELKLESDVENVEYistdkgyvyvvvvvLKELSDEVEEElkklgf 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 225 ENAQRDARGQSTEIFR-LKAQLEEVHEQMEGLRRENKNLSDEIHDLTeqlgeggRSVHEIdknrrrLEMEKEELQAALEE 303
Cdd:PRK05771 203 ERLELEEEGTPSELIReIKEELEEIEKERESLLEELKELAKKYLEEL-------LALYEY------LEIELERAEALSKF 269
|
...
gi 21998636 304 AES 306
Cdd:PRK05771 270 LKT 272
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
49-331 |
4.48e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 49 EEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLNGEVRNLTsdlDSLRETLEEEQSAKG----DLQAQLQKLQGE 124
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEK---DKKNKALAERKDSANerlnSLEAQLKQLDKK 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 125 LQ--------QLRSRGGGGGDVRSEEVEELKRKMNAKIQELESEAESAKSKCGQLEK--------------TKARLQGEL 182
Cdd:pfam12128 698 HQawleeqkeQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETwykrdlaslgvdpdVIAKLKREI 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 183 EDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQsteifrLKAQLEEVHEQMEGLRRENKNL 262
Cdd:pfam12128 778 RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQ------LARLIADTKLRRAKLEMERKAS 851
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21998636 263 SDEIHDLTEQLgEGGRSVHEiDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRaqlEMSQIRQEIDR 331
Cdd:pfam12128 852 EKQQVRLSENL-RGLRCEMS-KLATLKEDANSEQAQGSIGERLAQLEDLKLKRDY---LSESVKKYVEH 915
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-334 |
4.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 152 AKIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNnfnrtLAEWQKKYADSQAELENAQRDa 231
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAELERLDAS- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 232 rgqSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQE 311
Cdd:COG4913 684 ---SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180
....*....|....*....|...
gi 21998636 312 EAKVQRAQLEMSQIRQEIDRRLA 334
Cdd:COG4913 761 DAVERELRENLEERIDALRARLN 783
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1-105 |
5.86e-05 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 44.33 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 1 NSEKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLS-AQLEEARHSLEDE 79
Cdd:TIGR04320 251 NPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAqNNLATAQAALANA 330
|
90 100
....*....|....*....|....*.
gi 21998636 80 SRMKAKLNGEVRNLTSDLDSLRETLE 105
Cdd:TIGR04320 331 EARLAKAKEALANLNADLAKKQAALD 356
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
8-308 |
6.77e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.83 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 8 ALESQLQEVS--VKLDEATRN-LNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQ-LSAQLEEARHSLEDESRMK 83
Cdd:NF012221 1539 ESSQQADAVSkhAKQDDAAQNaLADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNaLETNGQAQRDAILEESRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 84 AKlngEVRNLTSDLDSLREtlEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQELESEAes 163
Cdd:NF012221 1619 TK---ELTTLAQGLDALDS--QATYAGESGDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAV-- 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 164 AKSKCG--QLEKTKARLQGELEDLMVDVE--RANGLASQLERKQnnfnrtlAEWQKKYADSQAEL--ENAQRDARGQSTe 237
Cdd:NF012221 1692 AKSEAGvaQGEQNQANAEQDIDDAKADAEkrKDDALAKQNEAQQ-------AESDANAAANDAQSrgEQDASAAENKAN- 1763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 238 ifrlKAQLEEVHEQMEGLRRENKN------LSDEIHDLtEQLGEGGRSVHEIDK---NRRRLEMEKEELQAALEEAESAL 308
Cdd:NF012221 1764 ----QAQADAKGAKQDESDKPNRQgaagsgLSGKAYSV-EGVAEPGSHINPDSPaaaDGRFSEGLTEQEQEALEGATNAV 1838
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-328 |
7.30e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 4 KTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQqlsaQLEEARHSLEDESRMK 83
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 84 AKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQgELQQLRSrgggggdvRSEEVEELKRKMNAKIQELESEAES 163
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAE--------EYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 164 akskcgqLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRtLAEWQKKYADSQAELENAQR-DARGQSTEIFRLK 242
Cdd:PRK03918 319 -------LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE-LEERHELYEEAKAKKEELERlKKRLTGLTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 243 AQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRL-----EMEKEELQAALEEAESALEQEEAKVQR 317
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKELLEEYTAELKRIEKELKE 470
|
330
....*....|.
gi 21998636 318 AQLEMSQIRQE 328
Cdd:PRK03918 471 IEEKERKLRKE 481
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
44-254 |
7.93e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 44 LQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDesrMKAKLNgeVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQG 123
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEE---FRQKNG--LVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 124 ELQQLRSRGGGGGDVRSEEVE-ELKRKMNAKIQELESEAESAKSKCG-----------QLEKTKARLQGELEDLMVDVER 191
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQsPVIQQLRAQLAELEAELAELSARYTpnhpdvialraQIAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21998636 192 ANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEG 254
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
155-335 |
8.29e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 155 QELEsEAESAKSKcGQLEKTKArLQGELeDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYAdsqAELENAQRDARGQ 234
Cdd:PRK10929 30 QELE-QAKAAKTP-AQAEIVEA-LQSAL-NWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLN---NERDEPRSVPPNM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 235 ST-----EIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDknrRRLEMEKEELqAALEEAESALE 309
Cdd:PRK10929 103 STdaleqEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIE---RRLQTLGTPN-TPLAQAQLTAL 178
|
170 180 190
....*....|....*....|....*....|...
gi 21998636 310 QEEAKVQRA---QLEMSQI----RQEIDRRLAE 335
Cdd:PRK10929 179 QAESAALKAlvdELELAQLsannRQELARLRSE 211
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
48-235 |
8.93e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.69 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 48 LEEAESQLSQLNKIKQQlsAQLEEARHSLED-ESRMKAKLNG--EVRNLTSDLDSLRETlEEEQSAKGDLQAQLQKLQGE 124
Cdd:COG3524 160 LAESEELVNQLSERARE--DAVRFAEEEVERaEERLRDAREAllAFRNRNGILDPEATA-EALLQLIATLEGQLAELEAE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 125 LQQLRSRggggGDVRSEEVEELKRKMNAKIQELESEAESAKSKCGqlEKTKARLQGELEDLMVDVERAnglasqlerkqn 204
Cdd:COG3524 237 LAALRSY----LSPNSPQVRQLRRRIAALEKQIAAERARLTGASG--GDSLASLLAEYERLELEREFA------------ 298
|
170 180 190
....*....|....*....|....*....|.
gi 21998636 205 nfnrtlaewQKKYADSQAELENAQRDARGQS 235
Cdd:COG3524 299 ---------EKAYTSALAALEQARIEAARQQ 320
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-331 |
2.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 141 EEVEELKRKMNA--KIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERAngLASQLERKQNNFNRTLAEWQKKYA 218
Cdd:COG4913 242 EALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA--ELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 219 DSQAELENAQRDARGQSTE-IFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEEL 297
Cdd:COG4913 320 ALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190
....*....|....*....|....*....|....
gi 21998636 298 QAALEEAESALEQEEAKVQRAQlemSQIRQEIDR 331
Cdd:COG4913 400 LEALEEALAEAEAALRDLRREL---RELEAEIAS 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-335 |
2.15e-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: 43.12 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 1 NSEKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKikQQLSAQLEEARHSLEDES 80
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 81 RMKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQL--------------------RSRGGGGGDVRS 140
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLerlqenlegfsegvkallknQSGLSGILGVLS 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 141 E--EVEE-----------------LKRKMNAKIQELESEAESAKSKCGQLEKTKAR---LQGELEDLMVDVERANGLASQ 198
Cdd:TIGR02168 527 EliSVDEgyeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgteIQGNDREILKNIEGFLGVAKD 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 199 LERKQNNFNRTLAEWQKKYADSQaELENAQRDAR--GQSTEIFRLKAQL-----------EEVHEQMEGLRRENKNLSDE 265
Cdd:TIGR02168 607 LVKFDPKLRKALSYLLGGVLVVD-DLDNALELAKklRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEK 685
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 266 IHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-185 |
2.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALEsQLQEVSVKLDEATRNLNEQASTKA-----RSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLE 77
Cdd:COG4913 248 REQIELLE-PIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 78 DESRMKAKLNGEvrnltsDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLrsrgGGGGDVRSEEVEELKRKMNAKIQEL 157
Cdd:COG4913 327 ELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALLAAL----GLPLPASAEEFAALRAEAAALLEAL 396
|
170 180
....*....|....*....|....*...
gi 21998636 158 ESEAESAKSKCGQLEKTKARLQGELEDL 185
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELREL 424
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
12-331 |
2.74e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 12 QLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQ--------------LNKIKQQLSAQLEEARHSLE 77
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaeaglddadaeaVEARREELEDRDEELRDRLE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 78 DESRMKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSrgggggdvRSEEVEELKRKMNAKIQEL 157
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE--------EIEELEEEIEELRERFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 158 ESEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLER--------------KQNNFNRTLAEWQKKYADSQAE 223
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVEELEAE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 224 LENAQRDARGQSTEIFRLKaQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEE 303
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
330 340
....*....|....*....|....*...
gi 21998636 304 AESALEQEEAKVQRAQLEMSQIRQEIDR 331
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
6-275 |
3.67e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 6 VKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAK 85
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 86 LNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRgggGGDVRSEEVEELKRKMNAKIQELESEAESAK 165
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE---LAALEQELQALSEAEAEQALDELLKEANRNA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 166 SKcgQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQL 245
Cdd:COG4372 197 EK--EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270
....*....|....*....|....*....|
gi 21998636 246 EEVHEQMEGLRRENKNLSDEIHDLTEQLGE 275
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNL 304
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
20-310 |
3.74e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 20 LDEATRNLNEQASTKARSSQEVSELQRQLEEAESQL----SQLNKIKQQLSA------QLEEARHSLEdesrmkaklngE 89
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslkSQLADYQQALDVqqtraiQYQQAVQALE-----------K 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 90 VRNLTSDLDSLRETLEEEQSAkgdLQAQLQKLQGELQQLRSRGGGGGDVRS--EEVEELKRKMNAKI---------QELE 158
Cdd:COG3096 425 ARALCGLPDLTPENAEDYLAA---FRAKEQQATEEVLELEQKLSVADAARRqfEKAYELVCKIAGEVersqawqtaRELL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 159 SEAESAKSKCGQLEKTKARLqGELEDLMVDVERANGLASQLERKQN-------NFNRTLAEWQKKYADSQAELENAQRDA 231
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQL-AELEQRLRQQQNAERLLEEFCQRIGqqldaaeELEELLAELEAQLEELEEQAAEAVEQR 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 232 RGqsteifrLKAQLEEVHEQMEGLRRENKN---LSDEIHDLTEQLGEGGRSVHEID-------KNRRRLEMEKEELQAAL 301
Cdd:COG3096 581 SE-------LRQQLEQLRARIKELAARAPAwlaAQDALERLREQSGEALADSQEVTaamqqllEREREATVERDELAARK 653
|
....*....
gi 21998636 302 EEAESALEQ 310
Cdd:COG3096 654 QALESQIER 662
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-317 |
3.99e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 42 SELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKA--KLNGEVRNLTSDLDSLR-ETLEEEQSAKGDLQAQL 118
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 119 QKLQGELQQLRsrgggggdvrseevEELKRkmnakIQELESEAESAKSKCGQLEKTKARLQGELEDL-MVDVERANGLAS 197
Cdd:PRK03918 535 IKLKGEIKSLK--------------KELEK-----LEELKKKLAELEKKLDELEEELAELLKELEELgFESVEELEERLK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 198 QLERKQNNFN------RTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVH-----EQMEGLRRENKNLSDEI 266
Cdd:PRK03918 596 ELEPFYNEYLelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkkyseEEYEELREEYLELSREL 675
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 21998636 267 HDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESaLEQEEAKVQR 317
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-335 |
4.22e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 1 NSEKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDES 80
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 81 RMKAKLNGEVRNLTSDLDSLRETLEEEQSAKGD--LQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQELE 158
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDD 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 159 SEAESAKSKCGQ----------LEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQ 228
Cdd:COG1196 557 EVAAAAIEYLKAakagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 229 RDARGQSTEIFRLKAQLEEVH-----------EQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEEL 297
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSaggsltggsrrELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
330 340 350
....*....|....*....|....*....|....*...
gi 21998636 298 QAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-193 |
4.43e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 1 NSEKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQ-------LNKIKQQLSAQLEEAR 73
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienLNGKKEELEEELEELE 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 74 HSLEDESRMKAKLNGEVRNLTSDL-------DSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEE---- 142
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLrelerkiEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsle 954
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21998636 143 -VEELKRKMNAKIQELES-------EAESAKSKCGQLEKTKARLQGELEDLMVDVERAN 193
Cdd:TIGR02169 955 dVQAELQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1-335 |
4.92e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 1 NSEKTVKALESQLQEVSVKLDEATRNLNE---QASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLE 77
Cdd:pfam17380 241 ESFNLAEDVTTMTPEYTVRYNGQTMTENEflnQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 78 DESRMKAKLNgevRNLTSDLDSLRETLEEEQSAKgdlQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQEL 157
Cdd:pfam17380 321 AEKARQAEMD---RQAAIYAEQERMAMERERELE---RIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 158 ESEAESA-KSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENaqrdARGQST 236
Cdd:pfam17380 395 RQELEAArKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER----LRQQEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 237 EIFRLKAQLEEVHEQMEGLRRENKNLsdeihdLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQ 316
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQRRKI------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK 544
|
330
....*....|....*....
gi 21998636 317 RAQLEMSQIRQEIDRRLAE 335
Cdd:pfam17380 545 QQEMEERRRIQEQMRKATE 563
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
91-324 |
5.97e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 91 RNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSR-GGGGGDVRSEEVEELKRKMNAKIQELESEAESAKSKCG 169
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 170 QLEKTKARLQGELEDLMvdverANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIF-RLKAQLEEV 248
Cdd:COG3206 244 ALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqEAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21998636 249 HEQMEGLRRENKNLSDEIHDLTEQLgeggrsvheidKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQ 324
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
101-333 |
6.92e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 101 RETLEEEQSAKGDLQAQLQKLQgELQQLRSRgggggdVRSEEVEELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQG 180
Cdd:COG4913 251 IELLEPIRELAERYAAARERLA-ELEYLRAA------LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 181 ELEDLmvdveranglasqLERKQNNFNRTLAEWQKkyadsqaELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENK 260
Cdd:COG4913 324 ELDEL-------------EAQIRGNGGDRLEQLER-------EIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21998636 261 NLSDEIHDLTEQLGEggrSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRL 333
Cdd:COG4913 384 ALRAEAAALLEALEE---ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAL 453
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1-131 |
9.25e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 1 NSEKTVKALESQLQEVSVKLDEATRNLNeQASTKARS-SQEVSELQRQLEEAESQLSQlnkIKQQLSAQ------LEEAR 73
Cdd:PRK10929 99 PPNMSTDALEQEILQVSSQLLEKSRQAQ-QEQDRAREiSDSLSQLPQQQTEARRQLNE---IERRLQTLgtpntpLAQAQ 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21998636 74 H-SLEDES-RMKAKLNG-EVRNLTS----DLDSLRETLEEEQSAkgDLQAQLQKLQGELQQLRSR 131
Cdd:PRK10929 175 LtALQAESaALKALVDElELAQLSAnnrqELARLRSELAKKRSQ--QLDAYLQALRNQLNSQRQR 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-335 |
9.39e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 156 ELESEAESAKSKCGQLEKTKArLQGELEDLMVDVERANGLASQLERKQNnfnrtlaewQKKYADSQAELENAQRDARGQS 235
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRE-LAERYAAARERLAELEYLRAALRLWFA---------QRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 236 TEIFRLKAQLEEVHEQMEGLRRE-NKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAK 314
Cdd:COG4913 309 AELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180
....*....|....*....|.
gi 21998636 315 VQRAQLEMSQIRQEIDRRLAE 335
Cdd:COG4913 389 AAALLEALEEELEALEEALAE 409
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-331 |
9.85e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLE-----EARHSLE 77
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLllleaEADYEGF 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 78 DESRMKAKLNGEVRNLTSDLDSLRETLEEEQSA---------KGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKR 148
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 149 KMNAKIQELESEAESA--KSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELEN 226
Cdd:COG1196 587 ALAAALARGAIGAAVDlvASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 227 AQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAES 306
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
330 340
....*....|....*....|....*
gi 21998636 307 ALEQEEAKVQRAQLEMSQIRQEIDR 331
Cdd:COG1196 747 LLEEEALEELPEPPDLEELERELER 771
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
105-328 |
1.11e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 40.75 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 105 EEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVE---ELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQGE 181
Cdd:TIGR00927 690 KGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEgeiETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 182 LEDLMVDVERAnglaSQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKN 261
Cdd:TIGR00927 770 TEAEGKEDEDE----GEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQGEA 845
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21998636 262 LSDEIHDLTEQLGEGGRSVHEidknrrrlEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQE 328
Cdd:TIGR00927 846 KQDEKGVDGGGGSDGGDSEEE--------EEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQK 904
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
153-322 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 153 KIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAqRDAR 232
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 233 gqsteifrlkaQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEE 312
Cdd:COG1579 90 -----------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|
gi 21998636 313 AKVQRAQLEM 322
Cdd:COG1579 159 EELEAEREEL 168
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
6-332 |
1.29e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 6 VKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAK 85
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 86 LNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQELESEAESAK 165
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 166 SKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQL 245
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 246 EEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQI 325
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
....*..
gi 21998636 326 RQEIDRR 332
Cdd:COG4372 346 LLVGLLD 352
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-310 |
1.35e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 2 SEKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEE---AESQLSQLNKIKQQLSAQLEEARHSLED 78
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEakkAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 79 ESRMKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKlQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQELE 158
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 159 -SEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARgQSTE 237
Cdd:PTZ00121 1625 lKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-EAKK 1703
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21998636 238 IFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNrrrlEMEKEELQAALEEAESALEQ 310
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKAEE 1772
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
40-329 |
1.38e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 40 EVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQ 119
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 120 KLQGELQQLRSRgggggDVRSE--EVEELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLAS 197
Cdd:TIGR04523 299 DLNNQKEQDWNK-----ELKSElkNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 198 QLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGG 277
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 21998636 278 RSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEI 329
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3-334 |
1.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNE-QASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESR 81
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEElLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 82 MKAKLNGEVR----NLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQEL 157
Cdd:COG4717 235 ELEAAALEERlkeaRLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 158 ESEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLE--RKQNNFNRTLAEWQKKYADSQAELENAQRDARGQS 235
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEelEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 236 TEIFRLKAQLEEVHEQMEGLRRENKNLSDEI--HDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEA 313
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
|
330 340
....*....|....*....|.
gi 21998636 314 KVQRAQLEmSQIRQEIDRRLA 334
Cdd:COG4717 475 LQELEELK-AELRELAEEWAA 494
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
14-134 |
1.61e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 14 QEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLsqlnkikQQLSAQLEEARhsleDESRMKAKLNGEVRNL 93
Cdd:COG2433 402 EHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI-------ERLERELSEAR----SEERREIRKDREISRL 470
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 21998636 94 TSDLDSLRETLEEEQSAKGDLQAQLQKLQgELQQLRSRGGG 134
Cdd:COG2433 471 DREIERLERELEEERERIEELKRKLERLK-ELWKLEHSGEL 510
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
19-196 |
1.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 19 KLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQL-NKIKQQLSAQLEEARHSLEDESRMKAKLNGEVRNLTSDL 97
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 98 DSLRETLEEEQSAKGDLQAQLQKLQGELQQLRsrgggggdvrsEEVEELKRKMNAKIQELESEAESAKSKCGQLEKTKAR 177
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEEL-----------EALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
170
....*....|....*....
gi 21998636 178 LQGELEDLMVDVERANGLA 196
Cdd:COG4913 438 IPARLLALRDALAEALGLD 456
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1-162 |
2.40e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 1 NSEKTVKALESQLQEVSVKLDEATRNLN---EQASTKAR---SSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARH 74
Cdd:PRK11281 77 RQKEETEQLKQQLAQAPAKLRQAQAELEalkDDNDEETRetlSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 75 SLEdesRMKAKLNG------EVRNLTSDLDSLRETLEEEQSAKgdLQAQLQKLQGELQQLRSRGGGGG---DVRSEEVEE 145
Cdd:PRK11281 157 QPE---RAQAALYAnsqrlqQIRNLLKGGKVGGKALRPSQRVL--LQAEQALLNAQNDLQRKSLEGNTqlqDLLQKQRDY 231
|
170
....*....|....*..
gi 21998636 146 LkrkmNAKIQELESEAE 162
Cdd:PRK11281 232 L----TARIQRLEHQLQ 244
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8-335 |
3.08e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 8 ALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLN 87
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 88 GEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRS--------------------EEVEELK 147
Cdd:PRK02224 398 ERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpecgqpvegsphvetiEEDRERV 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 148 RKMNAKIQELESEAESAKSKCGQLEKTKArLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENA 227
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 228 QRDARGQSTEIFR-------LKAQLEEVHEQMEGLRRENKNLS--DEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQ 298
Cdd:PRK02224 557 REAAAEAEEEAEEareevaeLNSKLAELKERIESLERIRTLLAaiADAEDEIERLREKREALAELNDERRERLAEKRERK 636
|
330 340 350
....*....|....*....|....*....|....*....
gi 21998636 299 AALEEA--ESALEQEEAKVQRAQLEMSQIRQEIDRRLAE 335
Cdd:PRK02224 637 RELEAEfdEARIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-326 |
3.11e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.33 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 1 NSEKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSEL----------QRQLEEAESQLSQLNKIKQQLSAQLE 70
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLknegdhlrnvQTECEALKLQMAEKDKVIEILRQQIE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 71 EARHSLEDESRMKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQG-----ELQQLRSRGGGGGDVRS----- 140
Cdd:pfam15921 573 NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEArvsdlELEKVKLVNAGSERLRAvkdik 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 141 -------EEVEELKRKMNAKIQELESEAESAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEW 213
Cdd:pfam15921 653 qerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 214 QKKYADSQAELENAQrdargqsTEIFRLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEME 293
Cdd:pfam15921 733 QKQITAKRGQIDALQ-------SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
330 340 350
....*....|....*....|....*....|...
gi 21998636 294 KEELQAALEEAESALEQEEAKVQRAQLEMSQIR 326
Cdd:pfam15921 806 VANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
14-205 |
3.12e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 39.28 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 14 QEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLNGEVRNL 93
Cdd:pfam15070 200 KELAKKLGQLQEELGELKETLELKSQEAQSLQEQRDQYLAHLQQYVAAYQQLASEKEELHKQYLLQTQLMDRLQHEEVQG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 94 TSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKMNAKIQELESEAESA---KSKCGQ 170
Cdd:pfam15070 280 KVAAEMARQELQETQERLEALTQQNQQLQAQLSLLANPGEGDGLESEEEEEEAPRPSLSIPEDFESREAMVaffNSALAQ 359
|
170 180 190
....*....|....*....|....*....|....*
gi 21998636 171 LEKTKARLQGELEDLMVDVERANGLASQLERKQNN 205
Cdd:pfam15070 360 AEEERAELRRQLKEQKRRCRRLAQQAAPAQEEPEH 394
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
42-333 |
3.48e-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: 39.39 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 42 SELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKL 121
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 122 QGELQQLRSRGGGGGDVRSEEVEElKRKMNAKIQELESEAESAKSKCGQLEKTKARLQ---GELEDLMVDVERANGLASQ 198
Cdd:pfam01576 102 QQHIQDLEEQLDEEEAARQKLQLE-KVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEeriSEFTSNLAEEEEKAKSLSK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 199 LERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEifrLKAQLEEVHEQMEGLRRENKNLSDEIHDLTEQLGEGGR 278
Cdd:pfam01576 181 LKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTD---LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 21998636 279 SVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQLEMSQIRQEIDRRL 333
Cdd:pfam01576 258 QKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTL 312
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3-329 |
3.76e-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: 39.23 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 3 EKTVKALESQLQEVSVKLDEATRNLNEQASTKARSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRM 82
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 83 KAKLNGEVRNLTSDLDSLRETLEEEQSAKGDLQAQLQKLQGELQQLRsrgggggdvrseeveelkrKMNAKIQELESEAE 162
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK-------------------KKIQKNKSLESQIS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 163 SAKSKCGQLEKTKARLQGELEDLMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRDARGQSTEIFRLK 242
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 243 AQLE-----EVHEQMEGLRRENKNLSDEIHDLTEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQR 317
Cdd:TIGR04523 302 NQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
330
....*....|..
gi 21998636 318 AQLEMSQIRQEI 329
Cdd:TIGR04523 382 YKQEIKNLESQI 393
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
14-275 |
3.81e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 14 QEVSVKLDEATRNLNEQASTKArSSQEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLNGEVRNL 93
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKL-VQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 94 TSDL------DSLRETLEEEQSAKGDL-----------------QAQLQKLQGELQQLRSRGGGGGDVRSEEVEELKRKM 150
Cdd:PRK11281 118 LSTLslrqleSRLAQTLDQLQNAQNDLaeynsqlvslqtqperaQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 151 NAKIQELEseaesakskcGQLEKTKARLQG--ELEDLM---VD--VERANGLASQLERKQNNFNrtlaewQKKYADSQ-- 221
Cdd:PRK11281 198 QAEQALLN----------AQNDLQRKSLEGntQLQDLLqkqRDylTARIQRLEHQLQLLQEAIN------SKRLTLSEkt 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 21998636 222 -AELENAQRDARGQSTEIfrLKAQLEevheqmeglrrENKNLSDEIHDLTEQLGE 275
Cdd:PRK11281 262 vQEAQSQDEAARIQANPL--VAQELE-----------INLQLSQRLLKATEKLNT 303
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
39-130 |
5.03e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 38.52 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 39 QEVSELQRQLEEAESQLSQLNKIKQQLS----AQLEEARHSLEDE-SRMKAKLNGEvRNLTSDLDSLRETLEEEQSAKGD 113
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASferlAELRDELAELEEElEALKARWEAE-KELIEEIQELKEELEQRYGKIPE 489
|
90
....*....|....*..
gi 21998636 114 LQAQLQKLQGELQQLRS 130
Cdd:COG0542 490 LEKELAELEEELAELAP 506
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
170-320 |
7.10e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 37.91 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 170 QLEKTKARLQGELEDL--------MVDVERANGLASQLerkqnnfnrtLAEWQKKYADSQAELENAQRDARGQSTEIFRL 241
Cdd:COG3524 185 EVERAEERLRDAREALlafrnrngILDPEATAEALLQL----------IATLEGQLAELEAELAALRSYLSPNSPQVRQL 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21998636 242 KAQLEEVHEQMEGLRREnknlsdeihdLTEqlGEGGRSVHEIDKNRRRLEMEKEELQAALEEAESALEQEEAKVQRAQL 320
Cdd:COG3524 255 RRRIAALEKQIAAERAR----------LTG--ASGGDSLASLLAEYERLELEREFAEKAYTSALAALEQARIEAARQQR 321
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
39-334 |
7.87e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.01 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 39 QEVSELQRQLEEAESQLSQLNKIKQQLSAQLEEARHSLEDESRMKAKLNG-EVRNLTSDLDSLRETLEEEQSAKGDLQAQ 117
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLlADETLADRLEELREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 118 ---LQKLQGELQQLRSRGGGGGDVRSE--EVEELKRKMNAKIQELE-----SEAESAKSKCGQLEKTKA---RLQGELED 184
Cdd:COG3096 916 gkaLAQLEPLVAVLQSDPEQFEQLQADylQAKEQQRRLKQQIFALSevvqrRPHFSYEDAVGLLGENSDlneKLRARLEQ 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 185 LMVDVERANGLASQLERKQNNFNRTLAEWQKKYADSQAELENAQRdargqsteifRLKAQLEEVHEQMEGLRRENKnlsD 264
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQ----------ELEELGVQADAEAEERARIRR---D 1062
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21998636 265 EIHdltEQLGEGGRSVHEIDKNRRRLEMEKEELQAALEEAEsaleqEEAKVQRAQLEMSQIRQEIDRRLA 334
Cdd:COG3096 1063 ELH---EELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAE-----RDYKQEREQVVQAKAGWCAVLRLA 1124
|
|
| |
