|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-356 |
2.91e-15 |
|
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: 79.33 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 71 LSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasltnkhSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQ 150
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 151 R------NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHIN 224
Cdd:TIGR02168 741 EveqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 225 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 304
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 575771882 305 GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAgqflrakEQEVCRLQEQL 356
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGL-------EVRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
90-388 |
1.49e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 90 TLSEKMQELDK----LRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEA 165
Cdd:COG1196 217 ELKEELKELEAelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 166 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVL 245
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 246 RTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKE 325
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575771882 326 EMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE-KLITWLNKELNENQ 388
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-388 |
3.45e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 149 HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQT 228
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 229 KVAVLEQEI------KDKDQLVL-RTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 301
Cdd:TIGR02168 317 QLEELEAQLeeleskLDELAEELaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 302 TLMGKLK-LKNTVTI---QQEKLLAEKEEMLQK-ERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 376
Cdd:TIGR02168 397 SLNNEIErLEARLERledRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250
....*....|..
gi 575771882 377 ITWLNKELNENQ 388
Cdd:TIGR02168 477 LDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
73-376 |
4.59e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 73 LTRsLDDVTRQLHITQETL---SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL- 148
Cdd:TIGR02168 188 LDR-LEDILNELERQLKSLerqAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELe 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 149 -----HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHI 223
Cdd:TIGR02168 267 ekleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 224 NQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ------KVA-LEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKL 296
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQletlrsKVAqLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 297 Q-----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEE------ 365
Cdd:TIGR02168 427 LkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfse 506
|
330
....*....|..
gi 575771882 366 -SKQLLKNNEKL 376
Cdd:TIGR02168 507 gVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
142-396 |
2.85e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 142 KKELETL-HQRNIHQLQSRLSELEAANKELTERKykgdSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKE 220
Cdd:COG1196 219 KEELKELeAELLLLKLRELEAELEELEAELEELE----AELEELEAELAELEAELEELRLELEELELEL-------EEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 221 KHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEEngeknqiQLGKLEATIKSLSAELLKANEIIKKLQGDL 300
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 301 KTLMGKLKLKNTVTIQ-QEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITW 379
Cdd:COG1196 361 AEAEEALLEAEAELAEaEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250
....*....|....*..
gi 575771882 380 LNKELNENQLVRKQDTL 396
Cdd:COG1196 441 EEALEEAAEEEAELEEE 457
|
|
| HD_SAS6_N |
cd10142 |
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; ... |
1-50 |
3.85e-11 |
|
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; Spindle assembly abnormal protein 6 (SAS6) is a central scaffolding component of the centrioles that ensures their 9-fold symmetry. It is required for centrosome biogenesis and duplication, and is required for both mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. It is also required for the recruitment of microcephaly protein STIL to the procentriole and for STIL-mediated centriole amplification. SAS6 is comprised of an N-terminal globular head domain, a centrally located coiled-coil domain, and a disordered C-terminus. These monomers homodimerize symmetrically, through two dimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These homodimers can self-assemble into a 9-fold symmetric cartwheel structure comprised of nine SAS6 homodimers associated via their head domains; the dimerized coiled-coil domains being the spokes, the central hub being the head domains. This model corresponds to the N-terminal head domain of SAS6, which is structurally related to other XRCC4-superfamily members, XRCC4, PAXX, XLF and CCDC61.
Pssm-ID: 408998 Cd Length: 137 Bit Score: 61.03 E-value: 3.85e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 575771882 1 MQEHAKETPRFLLQLLSSAtllENSPVLLNVVETNPFKHLIHLSLKLLPG 50
Cdd:cd10142 91 IKEESKEPPKFLLVLVISS---DKGRATLEIVETNPFKHLTHLSLKFLPG 137
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
154-393 |
1.10e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 154 HQLQSRLSELEAankELTERKYkgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVL 233
Cdd:COG1196 216 RELKEELKELEA---ELLLLKL------RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 234 EQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTV 313
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 314 TIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 393
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
77-386 |
1.32e-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: 64.32 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 77 LDDVTRQLHITQETLSEKMQELDKLRSEwashtasltnkhsqELTAEKEKALQTQVQCQQQHEQQKKELEtlHQRNIHQL 156
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRRE--------------REKAERYQALLKEKREYEGYELLKEKEA--LERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 157 QSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEvlslrrENCTLDTECHEKEKHINQLQTKVAVLEQE 236
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 237 IKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKlknTVTIQ 316
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 317 QEKLLAEKEEM------LQKERKESQDAGQFLRAK-----------EQEVCRLQEQLETTVQKLEESKQLLKNNEKLITW 379
Cdd:TIGR02169 394 LEKLKREINELkreldrLQEELQRLSEELADLNAAiagieakinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
....*..
gi 575771882 380 LNKELNE 386
Cdd:TIGR02169 474 LKEEYDR 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
67-339 |
2.54e-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: 63.54 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 67 KEEKLSLTRSLDDVTRQLHITQETLSEKM-------QELDKLRSEWASHTASLTNKHSQ-ELTAEKEKALQTQVQCQQQH 138
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYALANEISRLEQQkQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 139 EQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHE 218
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 219 KEKHINQLQTKVAVLEQEIKDKDQLVLRTKeaFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQG 298
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 575771882 299 DLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAG 339
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-332 |
4.16e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 67 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQtqvqcqqqheqqkKELE 146
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL-------------EERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 147 TLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKEKHINQL 226
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-------AEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 227 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK 306
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260
....*....|....*....|....*.
gi 575771882 307 LKLKNTVTIQQEKLLAEKEEMLQKER 332
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-393 |
5.27e-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: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 168 KELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKEKHINQLQTKVAVLEQEIKDKDQLVLRT 247
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL-------EELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 248 KEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAEllkaneiIKKLQGDLKTlmgklkLKNTVTIQQEKLLAEKEEM 327
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-------IEQLKEELKA------LREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771882 328 LQKERKESQDAGQfLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 393
Cdd:TIGR02168 820 ANLRERLESLERR-IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
142-392 |
2.45e-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: 60.47 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 142 KKELETLHQR------NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTE 215
Cdd:TIGR02169 687 KRELSSLQSElrrienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 216 CHEKEKHINQLQTKVAVLEQEIKDkdqlvlrtkEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKK 295
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 296 LQGDLKTLMGKlklKNTVTIQQEKLLAEKEEMLQKERKesqdagqfLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEK 375
Cdd:TIGR02169 838 LQEQRIDLKEQ---IKSIEKEIENLNGKKEELEEELEE--------LEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250
....*....|....*..
gi 575771882 376 LITWLNKELNENQLVRK 392
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
150-393 |
4.59e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 150 QRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTK 229
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 230 VAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM----- 304
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLealra 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 305 --GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNK 382
Cdd:COG1196 395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250
....*....|.
gi 575771882 383 ELNENQLVRKQ 393
Cdd:COG1196 475 LEAALAELLEE 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
155-384 |
2.29e-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: 56.31 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 155 QLQSRLSELEAANKELTERKYKgdstVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 234
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKE----LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 235 QEIKDKDQLvlrtkeafdtIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 314
Cdd:COG4942 97 AELEAQKEE----------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 315 IQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKEL 384
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
213-461 |
4.49e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 213 DTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELlkaNEI 292
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 293 IKKLQ---------------GDLKTLMGKLKLKNTVTIQQEKLLAE---KEEMLQKERKESQDAGQFLRAKEQEVCRLQE 354
Cdd:COG3883 92 ARALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 355 QLETTVQKLEESKQLLKNNEK-LITWLNKELNENQLVRKQDTLGTSATPHSTSNSTIRSGLSPNLNVVDRLNYPSCGIGY 433
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAaAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|....*...
gi 575771882 434 PVSSALTFQNAFPHVVAAKNTSHPISGP 461
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAGAGAAAA 279
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
155-368 |
7.00e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 155 QLQSRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQ--RAKQEVLSLRRENCTLDTEchekekhINQLQTKVAV 232
Cdd:COG3206 165 NLELRREEARKALEFLEEQ-------LPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQ-------LSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 233 LEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI--QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-- 308
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqe 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771882 309 -------LKNTVTI--QQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQ 368
Cdd:COG3206 311 aqrilasLEAELEAlqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
183-384 |
1.52e-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: 54.69 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 183 ELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDK-------DQLVLRTKEAFDTIQ 255
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlsslEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 256 EQKVALEENGEKNQIQLGKLEAT-----IKSLSAELLKANEIIKKLQGDLKTLMGKLklkntvtiqqeKLLAEKEEMLQK 330
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKL-----------NRLTLEKEYLEK 833
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 575771882 331 ERKESQDAGQFLRAKEQEVCRLQEQLETtvqKLEESKQLLKNNEKLITWLNKEL 384
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNG---KKEELEEELEELEAALRDLESRL 884
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-396 |
4.85e-07 |
|
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: 52.72 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 63 LKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNkhsqeLTAEKEKALQTQVQCQQQHEQQK 142
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-----LKDEQNKIKKQLSEKQKELEQNN 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 143 KELETLhQRNIHQLQSRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECH 217
Cdd:TIGR04523 281 KKIKEL-EKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 218 EKEKHINQLQTKVAVLEQEIKDKDQ----LVLRTKEAFDTIQEQKVA---LEENGEKNQIQLGKLEATIKSLSAELLKAN 290
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQeiknLESQINDLESKIQNQEKLnqqKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 291 EIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQ---LETTVQKLEESK 367
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKI 519
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 575771882 368 QLLKNN-----------EKLITWLNKELNENQLVRKQDTL 396
Cdd:TIGR04523 520 SSLKEKieklesekkekESKISDLEDELNKDDFELKKENL 559
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
166-325 |
4.99e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 166 ANKELTERKYKGDSTVRELKAKL-AGVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLV 244
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAeAIKKEALLEAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 245 LRTKEAFDTIQEQKVALEEngeknqiQLGKLEATIKSLSAELLKANEIIKKLQGD------LKTLMGKLKLKNTVTIQQE 318
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKEI 178
|
....*..
gi 575771882 319 KLLAEKE 325
Cdd:PRK12704 179 EEEAKEE 185
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
178-349 |
6.62e-07 |
|
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: 50.69 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 178 DSTVRELKAKLAGVEEELQRAKQEVLSLRrenctldTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 257
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALE-------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 258 K--VALeengeknQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKEEMLQKERKES 335
Cdd:COG1579 89 KeyEAL-------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA-------ELEAELEEKKAELDEELAEL 154
|
170
....*....|....
gi 575771882 336 QDAGQFLRAKEQEV 349
Cdd:COG1579 155 EAELEELEAEREEL 168
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
85-394 |
6.66e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 85 HITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLhQRNIHQLQSRLSELE 164
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL-KKAIEELKKAKGKCP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 165 AANKELTERKYKGdsTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTkvavLEQEIKDKDQLv 244
Cdd:PRK03918 440 VCGRELTEEHRKE--LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL----AEQLKELEEKL- 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 245 lrtkEAFDtIQEQKVALEENgEKNQIQLGKLEATIKSLSAELLKANEIIKKL----------QGDLKTLMGKLKLKNTVT 314
Cdd:PRK03918 513 ----KKYN-LEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLaelekkldelEEELAELLKELEELGFES 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 315 IQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 394
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE 666
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
156-376 |
7.32e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.82 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 156 LQSRLSELEAANKELterkykgdstVRELKAKLAGVEEELQRAKqevlslrRENCTLDTECHEKEKHINQLQTKVAVLEQ 235
Cdd:pfam07888 32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYK-------RDREQWERQRRELESRVAELKEELRQSRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 236 EIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 315
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575771882 316 QQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 376
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
59-300 |
2.78e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 59 LAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEK---MQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQ 135
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELekrLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 136 QQHEQQKKELETLHQR------NIHQLQSRLSELEAANKELTERK------YKGDSTVRE-LKAKLAGVEEELQRAKQEV 202
Cdd:TIGR02169 308 RSIAEKERELEDAEERlakleaEIDKLLAEIEELEREIEEERKRRdklteeYAELKEELEdLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 203 LSLRREnctLDTECHEKEKHIN----------QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQL 272
Cdd:TIGR02169 388 KDYREK---LEKLKREINELKReldrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
250 260
....*....|....*....|....*...
gi 575771882 273 GKLEATIKSLSAELLKANEIIKKLQGDL 300
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-358 |
3.52e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 96 QELDKLRSEWASHTASLtnkhsQELTAEKEKALQTQVQCQQQHEQQKKELETL-HQRNIHQLQSRLSELEAANKELterk 174
Cdd:COG4913 617 AELAELEEELAEAEERL-----EALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDDL---- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 175 ykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIkdKDQLVLRTKEAFDTI 254
Cdd:COG4913 688 -------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 255 QEQKV------ALEENGEKNQIQLGKLEATI---------------KSLSAELLKANEIIKKLQgdlktlmgklklkntv 313
Cdd:COG4913 759 LGDAVerelreNLEERIDALRARLNRAEEELeramrafnrewpaetADLDADLESLPEYLALLD---------------- 822
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 575771882 314 TIQQEKLLAEKEEMLQ-KERKESQDAGQFLRAKEQEVCRLQEQLET 358
Cdd:COG4913 823 RLEEDGLPEYEERFKElLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
123-291 |
3.89e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 123 EKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEAANKELT--ERKYKGDSTVRELKAKLAGVEEELQRAKQ 200
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 201 EVLSLRRenctLDTECHEKEKHINQLQTKVAVLEQEIK-DKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATI 279
Cdd:COG4717 154 RLEELRE----LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|..
gi 575771882 280 KSLSAELLKANE 291
Cdd:COG4717 230 EQLENELEAAAL 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-377 |
4.04e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 66 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasLTNKHSQELTAEKEKAlqtqvqcqqQHEQQKKEL 145
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEE-------IEELEKELESLEGSKR---------KLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 146 EtlhqRNIHQLQSRLSELEAANKELTERKYKGDSTVR------ELKAKLAGVEEELQRAKQEVLSLRRENctldTECHEK 219
Cdd:PRK03918 265 E----ERIEELKKEIEELEEKVKELKELKEKAEEYIKlsefyeEYLDELREIEKRLSRLEEEINGIEERI----KELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 220 EKHINQLQTKvavlEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI-QLGKLEATIKSLSAELLKANEIIKKLQG 298
Cdd:PRK03918 337 EERLEELKKK----LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771882 299 DLKTLMGKLKLKNTVTIQQEKllAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLI 377
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
76-386 |
5.74e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 76 SLDDVTRQLHITQETlsEKMQELDKLRSEWASHTASLTNKHSQELTAEKekALQTQVQCQQQHEQQKKELETLHQrNIHQ 155
Cdd:PRK02224 188 SLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARE--TRDEADEVLEEHEERREELETLEA-EIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 156 LQSRLSELEAANKELTERKYKGDSTVRELKAKLAGV--EEELQRAKQEVLSLRRE--------------NCTLDTECHEK 219
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEAVEARREeledrdeelrdrleECRVAAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 220 E-----KHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQ-------IQLGKLEATIKSLSAELL 287
Cdd:PRK02224 343 EaeslrEDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 288 KANEIIKKLQGDLKTLMGKLKLKNTV--------------------TI-----QQEKLLAEKEEM--LQKERKESQDAGQ 340
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALleagkcpecgqpvegsphveTIeedreRVEELEAELEDLeeEVEEVEERLERAE 502
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 575771882 341 FLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 386
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
142-391 |
8.93e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 142 KKELETLHQRNIHQLQSRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLslrrenctldtec 216
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEAldklrSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIK------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 217 hEKEKHINQLQTKVAVLEQEIKDKDQLvlrtkEAFDTiqeqKVALEENGEKNQIQLGKLEATIKS-LSAELLKANEIIKK 295
Cdd:PRK05771 104 -ELEEEISELENEIKELEQEIERLEPW-----GNFDL----DLSLLLGFKYVSVFVGTVPEDKLEeLKLESDVENVEYIS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 296 lqgdlktlmgKLKLKNTVTIQQEKLLAEK-EEMLQK---ERKESQDAG---QFLRAKEQEVCRLQEQLETTVQKLEESKQ 368
Cdd:PRK05771 174 ----------TDKGYVYVVVVVLKELSDEvEEELKKlgfERLELEEEGtpsELIREIKEELEEIEKERESLLEELKELAK 243
|
250 260
....*....|....*....|...
gi 575771882 369 llKNNEKLITWlnKELNENQLVR 391
Cdd:PRK05771 244 --KYLEELLAL--YEYLEIELER 262
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
155-398 |
1.00e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 155 QLQSRLSELEAANKELterkykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 234
Cdd:COG4372 32 QLRKALFELDKLQEEL-----------EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 235 QEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 314
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 315 IQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 394
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
....
gi 575771882 395 TLGT 398
Cdd:COG4372 261 EELE 264
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
223-393 |
1.44e-05 |
|
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: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 223 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 302
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 303 LMGKLKlKNTVTIQQ------EKLLAEKEEMLQKER---------KESQDAGQFLRAKEQEVCRLQEQLETTVQKLEesk 367
Cdd:COG4942 102 QKEELA-ELLRALYRlgrqppLALLLSPEDFLDAVRrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE--- 177
|
170 180
....*....|....*....|....*.
gi 575771882 368 QLLKNNEKLITWLNKELNENQLVRKQ 393
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLAR 203
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
143-382 |
1.98e-05 |
|
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: 47.48 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 143 KELETLHQRNIHQLQSRLSELEAANKELTERKYKGD---STVRELKAKLAGVEEELQRAKQEvlslrrenctLDTECHEK 219
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHE----------LESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 220 EKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGD 299
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 300 LKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESK-QLLKNNEKLIT 378
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaQLAKKEEELQA 247
|
....
gi 575771882 379 WLNK 382
Cdd:pfam01576 248 ALAR 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
72-307 |
2.74e-05 |
|
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: 46.68 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 72 SLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLtnkhsqeltAEKEKALQTQVQCQQQHEQQKKELETLHQR 151
Cdd:COG4942 59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 152 NIHQLQSRLSELEAANKELTERkykgdstVRELKAKLagveEELQRAKQEvlslrrenctLDTECHEKEKHINQLQTKVA 231
Cdd:COG4942 130 DFLDAVRRLQYLKYLAPARREQ-------AEELRADL----AELAALRAE----------LEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771882 232 VLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKnqiqlgkLEATIKSLSAELLKANEiiKKLQGDLKTLMGKL 307
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEE-------LEALIARLEAEAAAAAE--RTPAAGFAALKGKL 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
142-367 |
3.25e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 142 KKELETLHQRNiHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQR----------AKQEVLSLRRENCT 211
Cdd:PRK03918 178 IERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleelkeeieeLEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 212 LDTECHEKEKHINQLQTKVAVLEQ------EIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAE 285
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 286 LLKANEIIKKLQG----------------DLKTLMGKL-KLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQE 348
Cdd:PRK03918 337 EERLEELKKKLKElekrleeleerhelyeEAKAKKEELeRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
250
....*....|....*....
gi 575771882 349 VCRLQEQLETTVQKLEESK 367
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAK 435
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
117-388 |
5.58e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.12 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 117 SQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKaklagVEEELQ 196
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK-----LNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 197 RAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE-QEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKL 275
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 276 EATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ----QEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCR 351
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEleklQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270
....*....|....*....|....*....|....*..
gi 575771882 352 LQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 388
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
92-390 |
8.62e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 92 SEKMQELDKlRSEWASHTASLTNKHSQELTAE--KEKA--LQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAAN 167
Cdd:PTZ00121 1456 AKKAEEAKK-KAEEAKKADEAKKKAEEAKKADeaKKKAeeAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 168 KELTERKYKGDSTVREL-KAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR 246
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 247 TKEAfdTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEE 326
Cdd:PTZ00121 1615 AEEA--KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771882 327 MLQKERKESQDAGQfLRAKEQEVCRLQEQL----ETTVQKLEESKQLLKNNEKLITWLNKELNENQLV 390
Cdd:PTZ00121 1693 ALKKEAEEAKKAEE-LKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
142-332 |
9.85e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 9.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 142 KKELETLHQRNIHQLQSRLSELEAANKELTERKykgdSTVRELKAKLAGVEEELQRAKQEVLSLRRE---------NCTL 212
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREEleklekllqLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 213 DTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEE----NGEKNQIQLGKLEATIKSLSAELLK 288
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElleqLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 575771882 289 ANEIIKKLQGDLKTLMGKLKlkntvTIQQEKLLAEKEEMLQKER 332
Cdd:COG4717 211 LEEELEEAQEELEELEEELE-----QLENELEAAALEERLKEAR 249
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
67-262 |
1.14e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 67 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKAlqtqvQCQQQHEQQKKELE 146
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-----ELAAQLEELEEAEE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 147 TLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQL 226
Cdd:COG1196 411 ALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
170 180 190
....*....|....*....|....*....|....*.
gi 575771882 227 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALE 262
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-393 |
1.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 121 TAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRE----LKAKLAGVEEELQ 196
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKEL-AEQLKELEEKLKKYNLEELEKKAEEYEKLKEklikLKGEIKSLKKELE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 197 RAKQevlsLRRENCTLDTECHEKEKHINQLQTKVAVLEQE-IKDKDQLVLRTKEAFDTIQEQKVALEEngeknqiqLGKL 275
Cdd:PRK03918 550 KLEE----LKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLELKDAEKE--------LERE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 276 EATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtVTIQQEKLLAEKEEMLQKERKESQdagqfLRAKEQEVCRLQEQ 355
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELE-KKYSEEEYEELREEYLELSRELAG-----LRAELEELEKRREE 691
|
250 260 270
....*....|....*....|....*....|....*...
gi 575771882 356 LETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 393
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
110-368 |
1.22e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 110 ASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELetlhQRNIHQLQSRLSELEAANKELTERkykgdstVRELKAKLA 189
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARR-------IRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 190 GVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTkvavleQEIKDKDQLVLRTKEAFDTIQEQKV------ALEE 263
Cdd:COG4942 80 ALEAELAELEKEIAELRAE---LEAQKEELAELLRALYR------LGRQPPLALLLSPEDFLDAVRRLQYlkylapARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 264 NGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtiqqEKLLAEKEEMLQKERKESQDAGQFLR 343
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAAL--------------EALKAERQKLLARLEKELAELAAELA 216
|
250 260
....*....|....*....|....*
gi 575771882 344 AKEQEVCRLQEQLETTVQKLEESKQ 368
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
72-272 |
1.29e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 72 SLTRSLDDVTRQLHITQETLSEKMQELDKLRSE----WASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELET 147
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 148 LHQ--------RNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVL-SLRRENCTLDTECHE 218
Cdd:COG3206 252 GPDalpellqsPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 575771882 219 KEKHINQLQTKVAVL---EQEIKDKDQLVLRTKEAFDTIQE--QKVALEENGEKNQIQL 272
Cdd:COG3206 332 LQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
88-339 |
1.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 88 QETLSEKMQELDKLRSEwashtASLTNKHSQELTAEKEKALqtqvqcqqqheqqkKELETLhQRNIHQLQSRLSELEAAN 167
Cdd:COG4942 19 ADAAAEAEAELEQLQQE-----IAELEKELAALKKEEKALL--------------KQLAAL-ERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 168 KELTERkykgdstVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE----KHINQLQTKVAVLEQEIKDKDQL 243
Cdd:COG4942 79 AALEAE-------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 244 VLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAE 323
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|....*.
gi 575771882 324 KEEMLQKERKESQDAG 339
Cdd:COG4942 232 LEAEAAAAAERTPAAG 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
92-366 |
1.42e-04 |
|
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: 44.72 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 92 SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQK------KELETLHQRNIHQLQSRLSELEA 165
Cdd:pfam15921 252 SESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqeqaRNQNSMYMRQLSDLESTVSQLRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 166 ankELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTEChekEKHINQLQTKVAVLEQEIKDKDQLVL 245
Cdd:pfam15921 332 ---ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL---QKLLADLHKREKELSLEKEQNKRLWD 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 246 RTKEAFDTIQEQKVALEEngekNQIQLGKLEATIKSLSAEllkaneiikkLQGDLKTLMGKLKLKNTVTIQQEKLLAEKE 325
Cdd:pfam15921 406 RDTGNSITIDHLRRELDD----RNMEVQRLEALLKAMKSE----------CQGQMERQMAAIQGKNESLEKVSSLTAQLE 471
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 575771882 326 ---EMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEES 366
Cdd:pfam15921 472 stkEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT 515
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
144-239 |
2.06e-04 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 42.65 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 144 ELETlHQRNIHQLQSRLSEL----EAANKELTERKyKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEK 219
Cdd:pfam05266 79 ELEK-HGFDVKAPQSRINKLlslkDRQTKLLEELK-KLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAA 156
|
90 100
....*....|....*....|
gi 575771882 220 EKHINQLQTKVAVLEQEIKD 239
Cdd:pfam05266 157 DKEIARLKSEAEKLEQEIQD 176
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
68-375 |
2.46e-04 |
|
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: 44.01 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 68 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLR----SEWASHTASLTN---KHSQELTAEKEKaLQTQVQCQQQHEQ 140
Cdd:pfam01576 299 EELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleEETRSHEAQLQEmrqKHTQALEELTEQ-LEQAKRNKANLEK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 141 QKKELETLHQrnihQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE 220
Cdd:pfam01576 378 AKQALESENA----ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 221 KHINQLQTKVAVLEQEIKDKDQLV---LRTKEAFDT----IQEQKVALEENGEKNQIQLGKLEATIKSLSAELLkanEII 293
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLqeeTRQKLNLSTrlrqLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS---DMK 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 294 KKLQGDLKTLMGKLKLKntvtiqqEKLLAEKEEMLQKERKESQDAGQFLRAKEqevcRLQEQLETTVQKLEESKQLLKNN 373
Cdd:pfam01576 531 KKLEEDAGTLEALEEGK-------KRLQRELEALTQQLEEKAAAYDKLEKTKN----RLQQELDDLLVDLDHQRQLVSNL 599
|
..
gi 575771882 374 EK 375
Cdd:pfam01576 600 EK 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
157-365 |
3.05e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 157 QSRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQRAKQevlslRRENCTLDTECHEKEKHINQLQTKVAVLEQE 236
Cdd:COG4913 609 RAKLAALEAELAELEEE-------LAEAEERLEALEAELDALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 237 IKDkdqlVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntVTIQ 316
Cdd:COG4913 677 LER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---------EDLA 743
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 575771882 317 QEKLLAEKEEMLQKERKEsQDAGQFLRAKEQEVCRLQEQLETTVQKLEE 365
Cdd:COG4913 744 RLELRALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELER 791
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
74-272 |
5.41e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 74 TRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLtNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLhQRNI 153
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-EKEIENLNGKKEELEEELEELEAALRDLESRLGDL-KKER 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 154 HQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELqrakQEVLSLRREnctlDTECHEKEKHINQLQTKVAVL 233
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL----SEIEDPKGE----DEEIPEEELSLEDVQAELQRV 963
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 575771882 234 EQEIKDKDQLVLR-------TKEAFDTIQEQKVALEEngEKNQIQL 272
Cdd:TIGR02169 964 EEEIRALEPVNMLaiqeyeeVLKRLDELKEKRAKLEE--ERKAILE 1007
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
54-384 |
6.00e-04 |
|
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: 42.70 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 54 EIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKA------ 127
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykqei 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 128 --LQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQrakqevlSL 205
Cdd:TIGR04523 387 knLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK-------NL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 206 RRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAE 285
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 286 LLKANEIIKKLQGDLK-TLMGKLKLKNTVTIQQ-----EKLLA---EKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQL 356
Cdd:TIGR04523 540 ISDLEDELNKDDFELKkENLEKEIDEKNKEIEElkqtqKSLKKkqeEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
330 340
....*....|....*....|....*...
gi 575771882 357 ETTVQKLEESKQLLKNNEKLITWLNKEL 384
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
63-364 |
6.63e-04 |
|
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: 42.80 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 63 LKCSKEEKLSLTRSLDDVTRQLHITQETLSE-------KMQELDKLRSEwashtasltNKHSQELTAEKEKALQTQVQCQ 135
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlKLQELQHLKNE---------GDHLRNVQTECEALKLQMAEKD 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 136 QQHEQQKKELETL------HQRNIHQLQSRLSELEaanKELTER----------KYKGDSTVRELKAKLAGVEEE---LQ 196
Cdd:pfam15921 562 KVIEILRQQIENMtqlvgqHGRTAGAMQVEKAQLE---KEINDRrlelqefkilKDKKDAKIRELEARVSDLELEkvkLV 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 197 RAKQE----VLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDK--------DQLVLRTKEAFDTIQEQKVALEEN 264
Cdd:pfam15921 639 NAGSErlraVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKseemetttNKLKMQLKSAQSELEQTRNTLKSM 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 265 ------------GEKNQI-----QLGKLEATIKSLSAELLKAN-------EIIKKLQGDLKTLM---GKLKLKNTVTIQQ 317
Cdd:pfam15921 719 egsdghamkvamGMQKQItakrgQIDALQSKIQFLEEAMTNANkekhflkEEKNKLSQELSTVAtekNKMAGELEVLRSQ 798
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 575771882 318 EKLLAEK----EEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLE 364
Cdd:pfam15921 799 ERRLKEKvanmEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
163-383 |
8.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 163 LEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRenctLDTECHEKEKHINQLQTKVAVLEQEIKDKDQ 242
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 243 LvlrtKEAFDTIQEQKvALEENGEKNQIQLGKLEA---TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQek 319
Cdd:COG4717 124 L----LQLLPLYQELE-ALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD-- 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575771882 320 lLAEKEEMLQKERKEsqdagqflrakeqevcrLQEQLETTVQKLEESKQLLKNNEKLITWLNKE 383
Cdd:COG4717 197 -LAEELEELQQRLAE-----------------LEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
254-386 |
1.06e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 254 IQEQKVALEENGEKNQIQLGKLEAtiKSLSAE-LLKANEIIKKLQGDLKTlmgKLKLKNTVTIQQEKLLAEKEEMLqKER 332
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEA--EAIKKEaLLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENL-DRK 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 575771882 333 KESqdagqfLRAKEQEvcrLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 386
Cdd:PRK12704 102 LEL------LEKREEE---LEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
178-398 |
1.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 178 DSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 257
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 258 KVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-LKNTVTIQQEKLLAEKEEMLQKERKESQ 336
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEsLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575771882 337 DAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQDTLGT 398
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
89-394 |
1.89e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 89 ETLSEKMQELDKLRSEWASHTASLTNKHS-QELTAEKEKALQTQVQCQQQHEQQKKELETlHQRNIHQLQSRLSELEAAN 167
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTvQQVNQEKQEKQHELDTVVSKIELNRKLIQD-QQEQIQHLKSKTNELKSEK 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 168 KELTERKYKGDSTVRELKAKLAGVEE---ELQRAKQEVLSLRRencTLDTECHEKEKHINQLQTKVAVLEQEIKDK---- 240
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSlirEIKDAKEQDSPLET---FLEKDQQEKEELISSKETSNKKAQDKVNDIkekv 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 241 DQLVLRTKEAFDTIQEQKvaleengeknQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtvtiQQEKL 320
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDGK----------DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK----IQERW 1016
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771882 321 LaEKEEMLQKERKESQDAGQFLRAKEQEVCRLQ-EQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 394
Cdd:TIGR00606 1017 L-QDNLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKE 1090
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
149-388 |
2.02e-03 |
|
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: 40.88 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 149 HQRNI--HQLQSRLSELEAAN-KELTERKYKGDSTVRELKAKLAGVEEELQR-----AKQEVLSLRRENCTLDTECHEKE 220
Cdd:pfam17380 280 HQKAVseRQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 221 KHINQL-QTKVAVLEQEIKDKDQLVL-------RTKEAFDTIQEQKVALEENGEKNQIQLGKLEatikSLSAELLKANEI 292
Cdd:pfam17380 360 RELERIrQEEIAMEISRMRELERLQMerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 293 -IKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQdagqflraKEQEVCRLQEQLETTV--QKLEESKQL 369
Cdd:pfam17380 436 eVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--------KEKRDRKRAEEQRRKIleKELEERKQA 507
|
250
....*....|....*....
gi 575771882 370 LKNNEKLITWLNKELNENQ 388
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQ 526
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
143-308 |
2.18e-03 |
|
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: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 143 KELETLHQRnIHQLQSRLSELEAANKELteRKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKH 222
Cdd:COG4913 255 EPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 223 INQ--------LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQ----LGKLEATIKSLSAELLKAN 290
Cdd:COG4913 332 IRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAE 411
|
170
....*....|....*...
gi 575771882 291 EIIKKLQGDLKTLMGKLK 308
Cdd:COG4913 412 AALRDLRRELRELEAEIA 429
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
66-357 |
2.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 66 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASL--TNKHSQELTAEKEKALQTQVQCQQQHEQQKK 143
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELeqLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 144 ELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE--K 221
Cdd:COG4372 109 EAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 222 HINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 301
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 575771882 302 TLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLE 357
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
125-267 |
2.24e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 125 EKALQTQVQCQQQHEQQKKELETLH-QRNIHQLQSRLSELEAANKELteRKYkgdstVRELKAKLAGVEEELQRAKQEVL 203
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHeERELTEEEEEIRRLEEQVERL--EAE-----VEELEAELEEKDERIERLERELS 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771882 204 SLRREnctLDTEcHEKEKHINQLQTKVAVLEQEIKDKDQlvlRTKEAFDTIQEQK--VALEENGEK 267
Cdd:COG2433 452 EARSE---ERRE-IRKDREISRLDREIERLERELEEERE---RIEELKRKLERLKelWKLEHSGEL 510
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
223-395 |
2.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 223 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKN---------QIQLGKLEATIKSL---SAELLKAN 290
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLdasSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 291 EIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEvcRLQEQLETTVQKlEESKQLL 370
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD-AVERELR 768
|
170 180
....*....|....*....|....*..
gi 575771882 371 KNNEKLITWLNKELN--ENQLVRKQDT 395
Cdd:COG4913 769 ENLEERIDALRARLNraEEELERAMRA 795
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
54-388 |
2.93e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 54 EIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQEL-DKLRSEWASHTASLTNKHSQELTAEKEKALQTQV 132
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 133 QCQQQHEQQKKELETLHQR-NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCT 211
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERiNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 212 LDTeCHEKEKHINQlQTKVAVLEQEIKDkdqlvlrtkeafdtiqeQKVALEENGEKNQIQLGKLEATIKSLSAELlkanE 291
Cdd:TIGR00618 347 LQT-LHSQEIHIRD-AHEVATSIREISC-----------------QQHTLTQHIHTLQQQKTTLTQKLQSLCKEL----D 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 292 IIKKLQGDLKTLMGKLKlkntvTIQQEKLLAEKEEMLQKERKE-----SQDAGQFLRAKEQEVCRLQEQLETTVQKLEES 366
Cdd:TIGR00618 404 ILQREQATIDTRTSAFR-----DLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478
|
330 340
....*....|....*....|..
gi 575771882 367 KQLLKNNEKLITWLNKELNENQ 388
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQ 500
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
82-328 |
3.57e-03 |
|
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: 40.21 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 82 RQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL--HQRNIHQLQSR 159
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaaDQEQLPSWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 160 LSELEAANKELT------ERKYKG--DSTVRELKAKLAGVEEELQRAKQE-VLSLRRENCTLDTECHEKEKHINQLQTKV 230
Cdd:pfam12128 356 LENLEERLKALTgkhqdvTAKYNRrrSKIKEQNNRDIAGIKDKLAKIREArDRQLAVAEDDLQALESELREQLEAGKLEF 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 231 AVLEQEIKDK-DQLVLRTKEAfdTIQEQkvaLEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 309
Cdd:pfam12128 436 NEEEYRLKSRlGELKLRLNQA--TATPE---LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
250
....*....|....*....
gi 575771882 310 KNTVTIQQEKLLAEKEEML 328
Cdd:pfam12128 511 ASRRLEERQSALDELELQL 529
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
68-378 |
4.66e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 39.72 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 68 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELE- 146
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 147 --------------TLHQRNIHQLQSRLSELEAANKELTERKYKgdstVRELKAKLAGVE---EELQRAKQEVLSLRREN 209
Cdd:pfam05557 128 qstnseleelqerlDLLKAKASEAEQLRQNLEKQQSSLAEAEQR----IKELEFEIQSQEqdsEIVKNSKSELARIPELE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 210 CTLDtECHEKEKHINQLQTKVAVLEQEIKDkdqlvLRTK-EAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLK 288
Cdd:pfam05557 204 KELE-RLREHNKHLNENIENKLLLKEEVED-----LKRKlEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 289 ----ANEIIKKLQGDLkTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLE 364
Cdd:pfam05557 278 pedlSRRIEQLQQREI-VLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERD 356
|
330
....*....|....
gi 575771882 365 ESKQLLKNNEKLIT 378
Cdd:pfam05557 357 GYRAILESYDKELT 370
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
189-375 |
5.60e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 189 AGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKN 268
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 269 QIQLGKLE-ATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQ 347
Cdd:pfam02463 242 LQELLRDEqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180
....*....|....*....|....*...
gi 575771882 348 EVCRLQEQLETTVQKLEESKQLLKNNEK 375
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
75-382 |
5.96e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 75 RSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLT--NKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQrN 152
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE-D 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 153 IHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEV--LSLRRENctLDTECHEKEKHINQLQTKV 230
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFgdAPVDLGN--AEDFLEELREERDELRERE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 231 AVLEQEIKDKDQLVLRTKEAF------------------DTIQEQKVALEENGEknqiQLGKLEATIKSLSAELLKANEI 292
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLeagkcpecgqpvegsphvETIEEDRERVEELEA----ELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 293 iKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKN 372
Cdd:PRK02224 505 -VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
330
....*....|
gi 575771882 373 NEKLITWLNK 382
Cdd:PRK02224 584 LKERIESLER 593
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
88-370 |
6.96e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.42 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 88 QETLSEKMQELDKLRSEWASHTASLTNKHS-----QELTAEKEKALqtqvqcqqqheqqkkelETLHQRNIHQLQSRLSE 162
Cdd:pfam10174 407 QEQLRDKDKQLAGLKERVKSLQTDSSNTDTalttlEEALSEKERII-----------------ERLKEQREREDRERLEE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 163 LEAANKELterkykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLqtkvavlEQEIKDKDQ 242
Cdd:pfam10174 470 LESLKKEN-----------KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-------EIAVEQKKE 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 243 LVLRTKEAFDTIQEQKVALEENGEKNQiqlgkleaTIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLA 322
Cdd:pfam10174 532 ECSKLENQLKKAHNAEEAVRTNPEIND--------RIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA 603
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771882 323 EKEEMLQKERKESQDAGQFLRAKEQEV--------------------CRLQEQLETTVQKLEESKQLL 370
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEMkkkgaqlleearrrednladNSQQLQLEELMGALEKTRQEL 671
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
96-237 |
7.69e-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: 38.37 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 96 QELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQK-----------KELETLhQRNIHQLQSRLSELE 164
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvrnnKEYEAL-QKEIESLKRRISDLE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771882 165 AANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEvlslrrenctLDTECHEKEKHINQLQTKVAVLEQEI 237
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAE----------LDEELAELEAELEELEAEREELAAKI 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
142-393 |
8.51e-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: 38.85 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 142 KKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLR----------RENCT 211
Cdd:TIGR04523 136 NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllsnlkkkiQKNKS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 212 LDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAEL----- 286
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlks 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 287 -------LKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETT 359
Cdd:TIGR04523 296 eisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
|
250 260 270
....*....|....*....|....*....|....
gi 575771882 360 VQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 393
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
172-386 |
8.92e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 172 ERKYKGDSTV-RELKAKLAGVEEELQRaKQEVLSLRRENctlDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR---T 247
Cdd:PRK03918 161 ENAYKNLGEViKEIKRRIERLEKFIKR-TENIEELIKEK---EKELEEVLREINEISSELPELREELEKLEKEVKEleeL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 248 KEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKklqgDLKTLMGKLKlkntvtiQQEKLLAEKEEM 327
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK----ELKELKEKAE-------EYIKLSEFYEEY 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 575771882 328 LQKERKESQDAGQFlrakEQEVCRLQEQLEttvqKLEESKQLLKNNEKLITWLNKELNE 386
Cdd:PRK03918 306 LDELREIEKRLSRL----EEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEE 356
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
89-381 |
9.14e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 89 ETLSEKMQELDKLRSEWAS---HTASLTNKHsqeltaEKEKALQTQVQCQQQHEQQKKELETLhqrnIHQLQSRLSELEA 165
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDleeEVEEVEERL------ERAEDLVEAEDRIERLEERREDLEEL----IAERRETIEEKRE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 166 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTEchekekhINQLQTKVAVLEqEIKDKDQLVL 245
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER-------IESLERIRTLLA-AIADAEDEIE 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 246 RTKEAFDTIQEQ----KVALEENGEKNQIQLGKL-EATIKSLSAELLKANEIIKKLQGDLKTLMGKL-KLKNTVTIQQEK 319
Cdd:PRK02224 610 RLREKREALAELnderRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEIGAVENE 689
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771882 320 LlaEKEEMLQKERKESQDAGQFLRAKEQEVcrlqEQLETTVQKLE-ESKQllKNNEKLITWLN 381
Cdd:PRK02224 690 L--EELEELRERREALENRVEALEALYDEA----EELESMYGDLRaELRQ--RNVETLERMLN 744
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
265-388 |
9.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771882 265 GEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTV---------TIQQEKLLAEKEEMLQKERKES 335
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeidVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 575771882 336 QDagqfLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 388
Cdd:COG4913 685 DD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| |
