|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-283 |
1.01e-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: 80.49 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLEIL------ 75
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLeaeveq 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 76 HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT 155
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 156 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK 235
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462505358 236 lkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 283
Cdd:TIGR02168 905 -------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-315 |
6.32e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 15 RKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILhQQNIHQLQNRLSELEAAN 94
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 95 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRT 174
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 175 KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 254
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462505358 255 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNE-KLITWLNKELNENQ 315
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-315 |
2.72e-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: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 76 HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT 155
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 156 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEEN-------GEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK 228
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 229 TLMGKLK-LKNTVTI---QQEKLLAEKEEKLQK-EQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 303
Cdd:TIGR02168 397 SLNNEIErLEARLERledRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250
....*....|..
gi 2462505358 304 ITWLNKELNENQ 315
Cdd:TIGR02168 477 LDAAERELAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
69-321 |
5.59e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 69 KKDLEIL-HQQNIHQLQNRLSELEAANKDLTERKykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKE 147
Cdd:COG1196 219 KEELKELeAELLLLKLRELEAELEELEAELEELE----AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 148 KHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDL 227
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 228 KTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 307
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250
....*....|....
gi 2462505358 308 NKELNENQLVRKQD 321
Cdd:COG1196 455 EEEEEALLELLAEL 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-303 |
9.34e-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: 67.77 E-value: 9.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 7 ATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELT-----NEKEKALQAQVQYQQQHEQQKKDLEilhqQNIH 81
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEElrlevSELEEEIEELQKELYALANEISRLE----QQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEC-------HEKEKHVNQLQ 154
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrlEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 155 TKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLgkLEATIKSLSAELLKANEIIKKLQGDLKTLMGKL 234
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELERLEEAL 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505358 235 KlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQevckLQEQLEatvKKLEESKQLLKNNEKL 303
Cdd:TIGR02168 464 E-------ELREELEEAEQALDAAERELAQLQARLDSLER----LQENLE---GFSEGVKALLKNQSGL 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-313 |
1.66e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 4 LDDATKQLDFTRKTLAEKKQELDKL---RNEWASHTAALTNKHSQELT---NEKEKALQAQVQYQQQHEQQKKDLEILHQ 77
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLrreREKAERYQALLKEKREYEGYellKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 78 QnIHQLQNRLSELEAANKDLTER-KYKGDSTIRELKAKLSGVEEELQRT-------KQEVLSLRRENSTLDVECHEKEKH 149
Cdd:TIGR02169 259 E-ISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLersiaekERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 150 VNQLQTKvavLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLeatiKSLSAELLKANEIIKKLQGDLKT 229
Cdd:TIGR02169 338 IEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----KDYREKLEKLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 230 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNK 309
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
....
gi 2462505358 310 ELNE 313
Cdd:TIGR02169 491 ELAE 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-304 |
1.69e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 2 QSLDDATKQLDFTRKTLAEKKQELDKLrnewashtaaltNKHSQELTNEKEKALqaqvqyqqqheqqKKDLEILHQQnIH 81
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEEL------------NKKIKDLGEEEQLRV-------------KEKIGELEAE-IA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLE 161
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 162 QEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 241
Cdd:TIGR02169 385 DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462505358 242 IQQEKLLAEKEEKLQKEQKELQDVGQSLrikeqevcklqEQLEATVKKLEESKQLLKNNEKLI 304
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVL 516
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-313 |
1.86e-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: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 125 TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA 204
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 205 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 284
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180
....*....|....*....|....*....
gi 2462505358 285 ATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4-263 |
3.74e-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: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 4 LDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQaqvqyqqqheqqkkdleilhQQNIHQL 83
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL--------------------EERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 84 QNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQE 163
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 164 IKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 243
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260
....*....|....*....|
gi 2462505358 244 QEKLLAEKEEKLQKEQKELQ 263
Cdd:COG1196 475 LEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-294 |
8.37e-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: 61.62 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 69 KKDLEILHQ------QNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVE 142
Cdd:TIGR02169 687 KRELSSLQSelrrieNRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 143 CHEKEKHVNQLQTKVAVLEQEIKDkdqlvlrtkEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKK 222
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462505358 223 LQGDLKTLMGKlklKNTVTIQQEKL---LAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK 294
Cdd:TIGR02169 838 LQEQRIDLKEQ---IKSIEKEIENLngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
82-295 |
1.24e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 82 QLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQE--VLSLRRENSTLdvechekEKHVNQLQTKVAV 159
Cdd:COG3206 165 NLELRREEARKALEFLEEQ-------LPELRKELEEAEAALEEFRQKngLVDLSEEAKLL-------LQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 160 LEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQV--QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-- 235
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqe 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505358 236 -------LKNTVTI--QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQ 295
Cdd:COG3206 311 aqrilasLEAELEAlqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
106-311 |
2.32e-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: 55.93 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 106 STIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQK 185
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 186 VVLEENGEK---NQVQLGKLEATIKSLSAE----LLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKE 258
Cdd:COG4942 100 EAQKEELAEllrALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462505358 259 QKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 311
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
77-297 |
3.35e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 77 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 156
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 157 VAVLEQEIKdkdqlvlrtkEAFDTIQEqkvvLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 236
Cdd:TIGR02168 770 LEEAEEELA----------EAEAEIEE----LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462505358 237 K---NTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLL 297
Cdd:TIGR02168 836 TerrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
77-311 |
5.49e-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: 54.77 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 77 QQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 156
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 157 VAVLEQEIKDKDQLvlrtkeafdtIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 236
Cdd:COG4942 92 IAELRAELEAQKEE----------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462505358 237 KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 311
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
105-344 |
1.04e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 105 DSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDK-DQLVLRTKEAFdtiqe 183
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERrEELGERARALY----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 184 qkvvleengeKNQVQLGKLEATIKSLS-AELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKEL 262
Cdd:COG3883 97 ----------RSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELK-------ADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 263 QDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDVLGPSTTPPAHSSSNTIRSGI 342
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
..
gi 2462505358 343 SP 344
Cdd:COG3883 240 AA 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
108-311 |
1.51e-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: 54.30 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 108 IRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDK-------DQLVLRTKEAFDT 180
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlsslEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 181 IQEQKVVLEENGEKNQVQLGKLEAT-----IKSLSAELLKANEIIKKLQGDLKTLMGKLklkntvtiqqeKLLAEKEEKL 255
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKL-----------NRLTLEKEYL 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505358 256 QKEQKELQDVGQSLRIKEQEVCKLQEQLEAtvkKLEESKQLLKNNEKLITWLNKEL 311
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNG---KKEELEEELEELEAALRDLESRL 884
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
82-305 |
2.10e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQR---TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVA 158
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 159 VLEQEIKDKDQLVLRTKE------AFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMG 232
Cdd:PRK03918 270 ELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKK 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462505358 233 KLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLIT 305
Cdd:PRK03918 346 KLK-------ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
105-308 |
4.72e-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: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 105 DSTIRELKAKLSGVEEELQRTKQEVLSLRREnstldveCHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 184
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 185 KVVleengEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtiqqEKLLAEKEEKLQKEQKELQD 264
Cdd:COG1579 89 KEY-----EALQKEIESLKRRISDLEDEILELMERIEELEEELAEL--------------EAELAELEAELEEKKAELDE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462505358 265 VGQSLRIKEQEvckLQEQLEATVKKLEEskQLLKNNEKLITWLN 308
Cdd:COG1579 150 ELAELEAELEE---LEAEREELAAKIPP--ELLALYERIRKRKN 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
20-321 |
6.98e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 20 EKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDleilhqqnIHQLQNRLSELEAA------ 93
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE--------IKELKKAIEELKKAkgkcpv 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 94 -NKDLTERKYKGdsTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT--KVAVLEQEIKDKDQL 170
Cdd:PRK03918 441 cGRELTEEHRKE--LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNLE 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 171 VLRTKEafdtiqeqkvvleENGEKNQVQLGKLEATIKSLSAELLKANEIIKKL----------QGDLKTLMGKLKLKNTV 240
Cdd:PRK03918 519 ELEKKA-------------EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLaelekkldelEEELAELLKELEELGFE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 241 TIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 320
Cdd:PRK03918 586 SVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR 665
|
.
gi 2462505358 321 D 321
Cdd:PRK03918 666 E 666
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
83-303 |
8.77e-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: 51.43 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 83 LQNRLSELEAANKDLterkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLdvechekEKHVNQLQTKVAVLEQ 162
Cdd:pfam07888 32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYKRDREQWERQRREL-------ESRVAELKEELRQSRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 163 EIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 242
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462505358 243 QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 303
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
119-320 |
1.13e-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: 51.22 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 119 EEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDkdqlvlrtkeafdtIQEQKVVLEENGEKNQVQ 198
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE--------------IEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 199 LGKLEATIKSLSAELLKANEIIKKLqgdlktlmgklklkntvtiqqEKLLAEKEEKLQKEQKELQDVGQSLRikeqevck 278
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKEL---------------------EARIEELEEDLHKLEEALNDLEARLS-------- 789
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462505358 279 lQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 320
Cdd:TIGR02169 790 -HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
18-231 |
2.16e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 18 LAEKKQELDKLRNEWASHTAALtnkhsQELTNEKEKALQAQVQYQQQHEQQKKDLEIL-HQQNIHQLQNRLSELEAANKD 96
Cdd:COG4913 612 LAALEAELAELEEELAEAEERL-----EALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 97 LterkykgdstiRELKAKLSGVEEELQRTKQEvlslrrenstldvechekekhVNQLQTKVAVLEQEIKDKDQLVLRTKE 176
Cdd:COG4913 687 L-----------AALEEQLEELEAELEELEEE---------------------LDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505358 177 AFDTIQE-QKVVLEENGEK--NQVQLGKLEATI-KSLSAELLKANEIIKKLQGDLKTLM 231
Cdd:COG4913 735 RLEAAEDlARLELRALLEErfAAALGDAVERELrENLEERIDALRARLNRAEEELERAM 793
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
154-302 |
7.44e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 154 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK----- 228
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 229 ---------------------TLMGKLKLKNTVTIQQEKLLAE---KEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 284
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170
....*....|....*...
gi 2462505358 285 ATVKKLEESKQLLKNNEK 302
Cdd:COG3883 175 AQQAEQEALLAQLSAEEA 192
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
80-316 |
8.08e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 80 IHQLQNRLSELEAANKDL---TERKYKGDSTIRELKAKLSGVEEELQRTKQEV-LSLRRENSTLDV---ECHEKEKHVNQ 152
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeAGLDDADAEAVEARREELEDRDEELRDRLEECrVAAQAHNEEAESlreDADDLEERAEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 153 LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG 232
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 233 KLKlkntvtiQQEKLLA---------------------EKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVK--- 288
Cdd:PRK02224 441 RVE-------EAEALLEagkcpecgqpvegsphvetieEDRERVEELEAELED----LEEEVEEVEERLERAEDLVEaed 509
|
250 260
....*....|....*....|....*...
gi 2462505358 289 KLEESKQLLKNNEKLITWLNKELNENQL 316
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRE 537
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2-302 |
8.15e-06 |
|
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: 48.48 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEilhqqnih 81
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLE-------- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENStldvechEKEKHVNQLQTKVAVLE 161
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ-------SYKQEIKNLESQINDLE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 162 QEIKDKDQlvlrtkeafdtiqeQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 241
Cdd:TIGR04523 398 SKIQNQEK--------------LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462505358 242 IQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQ---LEATVKKLEESKQLLKNNEK 302
Cdd:TIGR04523 464 ESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEKIE 527
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-213 |
1.04e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKdleilhQQNIH 81
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA------EAELA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLE 161
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462505358 162 QEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAEL 213
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
72-315 |
1.14e-05 |
|
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: 48.19 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 72 LEILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEElqrtkqevlsLRRENSTLDVECHEKEKHVN 151
Cdd:pfam15921 258 IELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ----------ARNQNSMYMRQLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 152 QLQTKVAVLEQEIKDK-----DQLVLRTKEAFDTIQEQKVVLEENGEKNQvQLGKLEATIKSLSAELLKANEIIKKL--- 223
Cdd:pfam15921 328 QLRSELREAKRMYEDKieeleKQLVLANSELTEARTERDQFSQESGNLDD-QLQKLLADLHKREKELSLEKEQNKRLwdr 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 224 -QGDLKT---LMGKLKLKNTVTIQQEKLL----AEKEEKLQKEQKELQDVGQSLrikeQEVCKLQEQLEAT-------VK 288
Cdd:pfam15921 407 dTGNSITidhLRRELDDRNMEVQRLEALLkamkSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTkemlrkvVE 482
|
250 260
....*....|....*....|....*..
gi 2462505358 289 KLEESKQLLKNNEKLITWLNKELNENQ 315
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQEKE 509
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
108-321 |
1.19e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 108 IRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVV 187
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 188 LEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQ 267
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462505358 268 SLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 321
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
181-292 |
1.33e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 181 IQEQKVVLEENGEKNQVQLGKLEAtiKSLSAE-LLKANEIIKKLQ----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEKL 255
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEA--EAIKKEaLLEAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110
....*....|....*....|....*....|....*..
gi 2462505358 256 QKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEE 292
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
93-260 |
1.52e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 93 ANKDLTERKYKGDSTIRELKAKLSGVEEE-LQRTKQEVLSLRREnstLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLV 171
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEaLLEAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 172 LRTKEAFDTiqeqkvvLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGD------LKTLMGKLKLKNTVTIQQe 245
Cdd:PRK12704 106 EKREEELEK-------KEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKE- 177
|
170
....*....|....*
gi 2462505358 246 kllAEKEEKLQKEQK 260
Cdd:PRK12704 178 ---IEEEAKEEADKK 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
120-307 |
1.52e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 120 EELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLvlrtKEAFDTIQEQKVvLEENGEKNQVQL 199
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL----LQLLPLYQELEA-LEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 200 GKLEA---TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQeklLAEKEEKLQKEQKELQdvgQSLRIKEQEV 276
Cdd:COG4717 149 EELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELE---EELEEAQEEL 222
|
170 180 190
....*....|....*....|....*....|.
gi 2462505358 277 CKLQEQLEATVKKLEESKQLLKNNEKLITWL 307
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
22-323 |
2.98e-05 |
|
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: 46.55 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 22 KQELDKLRNEWASHTAALTNKHSQ--ELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQnIHQLQNRLSEL-----EAAN 94
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ-LNQLKSEISDLnnqkeQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 95 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQ----L 170
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQeiknL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 171 VLRTKEAFDTIQEQKVV---LEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKL 247
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLnqqKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 248 LAEKEEKLQKEQKELQDVGQSLRIKEQE--------------VCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKElkklneekkeleekVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
330
....*....|
gi 2462505358 314 NQLVRKQDVL 323
Cdd:TIGR04523 550 DDFELKKENL 559
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
72-305 |
3.76e-05 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 45.98 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 72 LEILHQQNiHQLQNRLSELEAANKDLTERkykgdstIRELKAKLsgveeelqrTKQEVLslrrenstLDVechekekhVN 151
Cdd:pfam15066 320 LQKLKHTN-RKQQMQIQDLQCSNLYLEKK-------VKELQMKI---------TKQQVF--------VDI--------IN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 152 QLQTKVavlEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENgeKNQVQLGKLEATIKSLSAELLKANEIikKLQGDLKTLM 231
Cdd:pfam15066 367 KLKENV---EELIEDKYNVILEKNDINKTLQNLQEILANT--QKHLQESRKEKETLQLELKKIKVNYV--HLQERYITEM 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 232 GKLKLKNTVTIQQEKLLAEKEE---KLQKEQKELQDVGQSL--------RIKEQEVCKLQEQLEATVKK-LEESKQLLKN 299
Cdd:pfam15066 440 QQKNKSVSQCLEMDKTLSKKEEeveRLQQLKGELEKATTSAldllkrekETREQEFLSLQEEFQKHEKEnLEERQKLKSR 519
|
....*.
gi 2462505358 300 NEKLIT 305
Cdd:pfam15066 520 LEKLVA 525
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-261 |
3.89e-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: 45.91 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 16 KTLAEKKQELDKLRNEwashtAALTNKHSQELTNEKEKALqaqvqyqqqheqqkKDLEILhQQNIHQLQNRLSELEAANK 95
Cdd:COG4942 20 DAAAEAEAELEQLQQE-----IAELEKELAALKKEEKALL--------------KQLAAL-ERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 96 DLTERkykgdstIRELKAKLSGVEEELQRTKQE----VLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLV 171
Cdd:COG4942 80 ALEAE-------LAELEKEIAELRAELEAQKEElaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 172 LRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKntvtIQQEKLLAEK 251
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL----QQEAEELEAL 228
|
250
....*....|
gi 2462505358 252 EEKLQKEQKE 261
Cdd:COG4942 229 IARLEAEAAA 238
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
45-309 |
4.49e-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: 46.32 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 45 QELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIHQlQNRLSELEAANKDLTerkykgdSTIRELKAKLSGVEEELQR 124
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEE-KNALQEQLQAETELC-------AEAEEMRARLAARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 125 TKQEvlslrrenstLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA 204
Cdd:pfam01576 76 ILHE----------LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 205 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 284
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
250 260
....*....|....*....|....*.
gi 2462505358 285 ATVKKLEESK-QLLKNNEKLITWLNK 309
Cdd:pfam01576 226 ELQAQIAELRaQLAKKEEELQAALAR 251
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
71-321 |
4.54e-05 |
|
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: 46.17 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 71 DLEILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDvechEKEKHV 150
Cdd:TIGR04523 61 KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLE----KQKKEN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 151 NQLQTKVAVleqEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKAN---EIIKKLQGDL 227
Cdd:TIGR04523 137 KKNIDKFLT---EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 228 KTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 307
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
250
....*....|....
gi 2462505358 308 NKELNENQLVRKQD 321
Cdd:TIGR04523 294 KSEISDLNNQKEQD 307
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
72-318 |
4.96e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 72 LEILHQQNIHQLQNrLSELEAANKDLTERKYKGD-----STIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEK 146
Cdd:PRK05771 22 LEALHELGVVHIED-LKEELSNERLRKLRSLLTKlsealDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 147 EkhVNQLQTKVAVLEQEIKDKDQLVLRTK--EAFDTiqeqKVVLEENGEKNQVQLGKLEATIKS-LSAELLKANEIIKKl 223
Cdd:PRK05771 101 E--IKELEEEISELENEIKELEQEIERLEpwGNFDL----DLSLLLGFKYVSVFVGTVPEDKLEeLKLESDVENVEYIS- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 224 qgdlktlmgKLKLKNTVTIQQEKLLAEK-EEKLQK---EQKELQDVG---QSLRIKEQEVCKLQEQLEATVKKLEESKQl 296
Cdd:PRK05771 174 ---------TDKGYVYVVVVVLKELSDEvEEELKKlgfERLELEEEGtpsELIREIKEELEEIEKERESLLEELKELAK- 243
|
250 260
....*....|....*....|..
gi 2462505358 297 lKNNEKLITWlnKELNENQLVR 318
Cdd:PRK05771 244 -KYLEELLAL--YEYLEIELER 262
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
78-294 |
5.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 78 QNIHQLQNRLSELEAANKDLTERKYKgdstiRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEkhVNQLQTKV 157
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQ-----IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 158 AVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQ-LGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgKLKL 236
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAAL--GLPL 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 237 KNTVTI--QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK 294
Cdd:COG4913 376 PASAEEfaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
37-289 |
5.82e-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: 45.14 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 37 AALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLeilhQQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLS 116
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARR-------IRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 117 GVEEELQRTKQEVLSLRREnstLDVECHEKEKHVNQLQTkvavleQEIKDKDQLVLRTKEAFDTIQEQKvVLEENGEKNQ 196
Cdd:COG4942 80 ALEAELAELEKEIAELRAE---LEAQKEELAELLRALYR------LGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 197 VQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEV 276
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|...
gi 2462505358 277 CKLQEQLEATVKK 289
Cdd:COG4942 230 ARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-217 |
6.82e-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: 45.14 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALtnkhsqeltNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIH 81
Cdd:COG4942 62 RRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQPPLALLLSPEDFL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 82 QLQNRLSELEAANKDLTERkykgdstIRELKAKLsgveEELQRTKQEVLSLRRenstldvechEKEKHVNQLQTKVAVLE 161
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQ-------AEELRADL----AELAALRAELEAERA----------ELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505358 162 QEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKAN 217
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
19-317 |
8.71e-05 |
|
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: 45.49 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 19 AEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKAlqaqVQYQQQHEQQKKDLEILHQQNIHQ---LQNRLSELEAA-- 93
Cdd:pfam15921 252 SESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKA----SSARSQANSIQSQLEIIQEQARNQnsmYMRQLSDLESTvs 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 94 --NKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLD-------VECHEKEKHVN--QLQTK------ 156
Cdd:pfam15921 328 qlRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDdqlqkllADLHKREKELSleKEQNKrlwdrd 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 157 ------VAVLEQEIKDKDQLVLRTKEAFDTIQ-EQKVVLEENGEKNQVQLGKLEaTIKSLSAELLKANEIIKKLQGDLKT 229
Cdd:pfam15921 408 tgnsitIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 230 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ---EQLEATVKKLEESKQLLKNNEKLITW 306
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEI 566
|
330
....*....|..
gi 2462505358 307 LNKEL-NENQLV 317
Cdd:pfam15921 567 LRQQIeNMTQLV 578
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
145-320 |
8.88e-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: 44.75 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 145 EKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQ 224
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 225 GDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLI 304
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170
....*....|....*.
gi 2462505358 305 TWLNKELNENQLVRKQ 320
Cdd:COG4942 184 EEERAALEALKAERQK 199
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-350 |
9.35e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 5 DDATKQLDFTRKtlAEKKQELDKLRN-EWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEilhqQNIHQL 83
Cdd:PTZ00121 1506 AEAKKKADEAKK--AEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE----EDKNMA 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 84 QNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEElQRTKQEvlSLRREnstldvecHEKEKHVNQLQTKVavlEQE 163
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAE--ELKKA--------EEEKKKVEQLKKKE---AEE 1645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 164 IKDKDQLvlRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 243
Cdd:PTZ00121 1646 KKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 244 QEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKqllKNNEKLItwlNKELNENQLVRKQDVl 323
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR---KEKEAVI---EEELDEEDEKRRMEV- 1796
|
330 340
....*....|....*....|....*..
gi 2462505358 324 gPSTTPPAHSSSNTIRSGISPNLNVVD 350
Cdd:PTZ00121 1797 -DKKIKDIFDNFANIIEGGKEGNLVIN 1822
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
77-281 |
1.37e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 77 QQNIHQLQNRLSELEAANkDLTERKYKGDST---IRELKAKLSGVEEELQRTKQEVLSLRREnstLDVECHEKEKHVNQL 153
Cdd:pfam15905 121 SASVASLEKQLLELTRVN-ELLKAKFSEDGTqkkMSSLSMELMKLRNKLEAKMKEVMAKQEG---MEGKLQVTQKNLEHS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 154 QTKVAVLEQEIKDKDQLVLRTK----EAFDTIQEQKVVLEEnGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 229
Cdd:pfam15905 197 KGKVAQLEEKLVSTEKEKIEEKseteKLLEYITELSCVSEQ-VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSK 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462505358 230 LMGKLKLK-NTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQE 281
Cdd:pfam15905 276 QIKDLNEKcKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
76-315 |
1.41e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 76 HQQNI--HQLQNRLSELEAAN-KDLTERKYKGDSTIRELKAKLSGVEEELQR-----TKQEVLSLRRENSTLDVECHEKE 147
Cdd:pfam17380 280 HQKAVseRQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 148 KHVNQL-QTKVAVLEQEIKDKDQLVL-------RTKEAFDTIQEQKVVLEENGEKNQVQLGKLEatikSLSAELLKANEI 219
Cdd:pfam17380 360 RELERIrQEEIAMEISRMRELERLQMerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 220 -IKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQdvgqslriKEQEVCKLQEQLEATV--KKLEESKQL 296
Cdd:pfam17380 436 eVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--------KEKRDRKRAEEQRRKIleKELEERKQA 507
|
250
....*....|....*....
gi 2462505358 297 LKNNEKLITWLNKELNENQ 315
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQ 526
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
23-323 |
1.64e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 23 QELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQ---QNIHQLQNRLSELEAANKDLTE 99
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 100 RKykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTldvechEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFD 179
Cdd:COG4717 154 RL----EELRELEEELEELEAELAELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 180 TIQEQKVVLEENGEKNQV--QLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQK 257
Cdd:COG4717 224 ELEEELEQLENELEAAALeeRLKEARLLLLIAAA-LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462505358 258 EQKELQDVGQSLRIKEQEVCKL-----------QEQLEATVKKLEESKQLLKNNEKlitwLNKELNENQLVRKQDVL 323
Cdd:COG4717 303 EAEELQALPALEELEEEELEELlaalglppdlsPEELLELLDRIEELQELLREAEE----LEEELQLEELEQEIAAL 375
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
35-320 |
1.69e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 35 HTAALTNKHSQELTN-EKEKALQAQVQYQQQHEQQKKDLEILHQQNI-------HQLQNRLSELEAANKDLTERKYKGDS 106
Cdd:PRK03918 449 HRKELLEEYTAELKRiEKELKEIEEKERKLRKELRELEKVLKKESELiklkelaEQLKELEEKLKKYNLEELEKKAEEYE 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 107 TIRE----LKAKLSGVEEELQRTKQevlsLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFdtiq 182
Cdd:PRK03918 529 KLKEklikLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPF---- 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 183 EQKVVLEENGEKnqvQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKE-EKLQKEQKE 261
Cdd:PRK03918 601 YNEYLELKDAEK---ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE-------ELEKKYSEEEyEELREEYLE 670
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505358 262 LQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 320
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
71-312 |
1.75e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 71 DLEILH-QQNIHQLQNRLSELEAANKDLTERKykgdstirelKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH 149
Cdd:PHA02562 187 DMKIDHiQQQIKTYNKNIEEQRKKNGENIARK----------QNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 150 VNQLQTKVAVLEQEIK--DKDQLVLRT-------KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEII 220
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEqfQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 221 KKLQgDLKTLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDvgqSLRIKEQEVCKLQEQLEATVKKLEESKQ----- 295
Cdd:PHA02562 337 KKLL-ELKNKISTNK-------QSLITLVDKAKKVKAAIEELQA---EFVDNAEELAKLQDELDKIVKTKSELVKekyhr 405
|
250 260
....*....|....*....|....*....
gi 2462505358 296 -----LLKNN-------EKLITWLNKELN 312
Cdd:PHA02562 406 givtdLLKDSgikasiiKKYIPYFNKQIN 434
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
70-302 |
2.21e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 70 KDLEILHQQN---IHQLQNRLSELEaanKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQevlslrrENSTLDVEchEK 146
Cdd:PRK04778 129 QELLESEEKNreeVEQLKDLYRELR---KSLLANRFSFGPALDELEKQLENLEEEFSQFVE-------LTESGDYV--EA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 147 EKHVNQLQTKVAVLEQEIKDKDQLVLRT-----------KEAFDTIQEQKVVLEENGEKNQV-----QLGKLEATIKSLs 210
Cdd:PRK04778 197 REILDQLEEELAALEQIMEEIPELLKELqtelpdqlqelKAGYRELVEEGYHLDHLDIEKEIqdlkeQIDENLALLEEL- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 211 aELLKANEIIKKLQGDLKTLMGKL----KLKNTVTIQQEKL---LAEKEEKLQKEQKELQDVGQSLRIKEQEVCK---LQ 280
Cdd:PRK04778 276 -DLDEAEEKNEEIQERIDQLYDILerevKARKYVEKNSDTLpdfLEHAKEQNKELKEEIDRVKQSYTLNESELESvrqLE 354
|
250 260
....*....|....*....|..
gi 2462505358 281 EQLEATVKKLEESKQLLKNNEK 302
Cdd:PRK04778 355 KQLESLEKQYDEITERIAEQEI 376
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
77-314 |
2.59e-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: 43.47 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 77 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 156
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 157 VAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 236
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 237 KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSL---------RIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 307
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
....*..
gi 2462505358 308 NKELNEN 314
Cdd:TIGR04523 602 IKEIEEK 608
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
95-303 |
3.06e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 95 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRT 174
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 175 KEAFDTIQEQKVVLEEngeknqvqLGKLEATIKSLSaELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 254
Cdd:PRK03918 262 RELEERIEELKKEIEE--------LEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462505358 255 LQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 303
Cdd:PRK03918 333 LEEKEERLEE----LKKKLKELEKRLEELEERHELYEEAKAKKEELERL 377
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
105-303 |
3.12e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 105 DSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 184
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 185 KVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-LKNTVTIQQEKLLAEKEEKLQKEQKELQ 263
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEsLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462505358 264 DVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 303
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
86-313 |
3.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 86 RLSELEAANKDLTErkykgdsTIRELKAKLSGVEEELQRTkQEVLSLRRENSTldvECHEKEKHVNQLQTKVAVLEQEIK 165
Cdd:PRK03918 156 GLDDYENAYKNLGE-------VIKEIKRRIERLEKFIKRT-ENIEELIKEKEK---ELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 166 DKDQLVLR---TKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQgdlktlmgKLKLKNTVTI 242
Cdd:PRK03918 225 KLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------ELKEKAEEYI 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462505358 243 QQEKLLAEKEEKLQKEQKELQDVgqslrikEQEVCKLQEQLeatvKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRL-------EEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEE 356
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
194-313 |
4.64e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 194 KNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMGK---LKLKNtvtiQQEKLLAEKEEKLQKEQKELQDVGQSLR 270
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKE----ALLEAKeeiHKLRN----EFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462505358 271 IKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
9-199 |
4.81e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 9 KQLDFTRKTLAEKKQELDKLRNE----WASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDL--------EILH 76
Cdd:COG3206 182 EQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 77 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVL-SLRRENSTLDVECHEKEKHVNQLQT 155
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEA 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462505358 156 KVAVL---EQEIKDKDQLVLRTKEAFDTIQE--QKVVLEENGEKNQVQL 199
Cdd:COG3206 342 RLAELpelEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
86-330 |
5.29e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 86 RLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRR-ENSTLDVECHEKEKHVnqlQTKVAVLEQEI 164
Cdd:PRK05771 80 SVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwGNFDLDLSLLLGFKYV---SVFVGTVPEDK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 165 KDKDQLVLrtkeafdtiqEQKVVLEENGEKNQVQLgkLEATIKSLSAELlkaNEIIKKLQGDlktlmgKLKLKNTVTIQQ 244
Cdd:PRK05771 157 LEELKLES----------DVENVEYISTDKGYVYV--VVVVLKELSDEV---EEELKKLGFE------RLELEEEGTPSE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 245 ekLLAEKEEKLQKEQKELQDVGQSLR----IKEQEVCKLQEQLEATVKKLEESKQLL--------------KNNEKLITW 306
Cdd:PRK05771 216 --LIREIKEELEEIEKERESLLEELKelakKYLEELLALYEYLEIELERAEALSKFLktdktfaiegwvpeDRVKKLKEL 293
|
250 260
....*....|....*....|....
gi 2462505358 307 LNKELNENQLVRKQDVLGPSTTPP 330
Cdd:PRK05771 294 IDKATGGSAYVEFVEPDEEEEEVP 317
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
77-319 |
5.41e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 77 QQNIHQLQNRLSELEAANKDLTErkykgdstireLKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKhVNQLQTK 156
Cdd:PRK11281 62 QQDLEQTLALLDKIDRQKEETEQ-----------LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLSTLS-LRQLESR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 157 VAVLEQEIKDkdqlvlrTKEAFDTIQEQKVVLEENGEK-------NQVQLGKLEATIKSLSAELLKAN-EIIKKLQGDLK 228
Cdd:PRK11281 130 LAQTLDQLQN-------AQNDLAEYNSQLVSLQTQPERaqaalyaNSQRLQQIRNLLKGGKVGGKALRpSQRVLLQAEQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 229 TLMGKLK-----LKNTVTIQ-----QEKLLAEKEEKLQKEQKELQDVGQSLRIK--EQEVCKLQEQLEAT-------VKK 289
Cdd:PRK11281 203 LLNAQNDlqrksLEGNTQLQdllqkQRDYLTARIQRLEHQLQLLQEAINSKRLTlsEKTVQEAQSQDEAAriqanplVAQ 282
|
250 260 270
....*....|....*....|....*....|....*
gi 2462505358 290 -----LEESKQLLKNNEKLitwlnkelneNQLVRK 319
Cdd:PRK11281 283 eleinLQLSQRLLKATEKL----------NTLTQQ 307
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
5-317 |
5.54e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 5 DDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKhSQELTNEKEKAlQAQVQYQQQHEQQKKDLEILHQQNIHQLQ 84
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK-ADEAKKKAEEA-KKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 85 NRLSELEAANKDLTERKYKGDSTIREL-KAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQE 163
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 164 IKDKDQLVLRTKEAfdTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 243
Cdd:PTZ00121 1605 KKMKAEEAKKAEEA--KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462505358 244 QEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCK---LQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLV 317
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
80-298 |
6.20e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 80 IHQLQN----RLSELEAANKDLTERKYKGDSTirelkaklsGVEEELQRTKQEVLSLRRENSTLDVEchEKEKHVNQLQT 155
Cdd:PRK04778 221 LKELQTelpdQLQELKAGYRELVEEGYHLDHL---------DIEKEIQDLKEQIDENLALLEELDLD--EAEEKNEEIQE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 156 KV----AVLEQEIKDK---DQLVLRTKEAFDTIQEQKVVLEEN----GEKNQVQLGKLEaTIKSLSAELlkaNEIIKKLQ 224
Cdd:PRK04778 290 RIdqlyDILEREVKARkyvEKNSDTLPDFLEHAKEQNKELKEEidrvKQSYTLNESELE-SVRQLEKQL---ESLEKQYD 365
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462505358 225 GDLKTLMGKLKLKNTVTIQQEKLLAEKEEkLQKEQKELQDVGQSLRIKEQEVcklQEQLEATVKKLEESKQLLK 298
Cdd:PRK04778 366 EITERIAEQEIAYSELQEELEEILKQLEE-IEKEQEKLSEMLQGLRKDELEA---REKLERYRNKLHEIKRYLE 435
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
77-319 |
8.37e-04 |
|
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: 42.27 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 77 QQNIHQLQNRLSELEAANKDLTERKYKgdsTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 156
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKK---ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 157 VAVLEQEIKDKDQLVLRTKEAFDTIQE-QKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG--- 232
Cdd:pfam02463 259 EIEKEEEKLAQVLKENKEEEKEKKLQEeELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEeie 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 233 -KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 311
Cdd:pfam02463 339 eLEKELKELEIKREAEEEEEEELEKLQEKLEQL----EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
....*...
gi 2462505358 312 NENQLVRK 319
Cdd:pfam02463 415 RQLEDLLK 422
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
14-320 |
1.16e-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: 41.50 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 14 TRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIHQLQNRLSELEAA 93
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 94 NKDLTERKYKGDSTIRELKAKLSgvEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLR 173
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKS--ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 174 TKEAFDTIQEQKVVLEENGEKN-QVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtvTIQQEKLLAEKE 252
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEeQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL--ESKEEKEKEEKK 900
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505358 253 EKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 320
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLA 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
101-322 |
1.33e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 101 KYKgdSTIRELKAKLSGVEEELQRtkqevLSLRREnstldvechEKEKHVNQL--QTKVA----VLEQEIKDKDQLVLRT 174
Cdd:COG1196 169 KYK--ERKEEAERKLEATEENLER-----LEDILG---------ELERQLEPLerQAEKAeryrELKEELKELEAELLLL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 175 KeaFDTIQEQKVVLEEngeknqvQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 254
Cdd:COG1196 233 K--LRELEAELEELEA-------ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505358 255 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDV 322
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
82-303 |
1.34e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 82 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDV---ECHEKEKHVNQL----Q 154
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLewrqQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 155 TKVAVLEQEIkdkdQLVLRTKEAFDTIQEQKVVLEENGEKN---------QVQLGKLEATIKSLSAELLKANEIIKKLQG 225
Cdd:COG1340 127 TEVLSPEEEK----ELVEKIKELEKELEKAKKALEKNEKLKelraelkelRKEAEEIHKKIKELAEEAQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 226 DLKTLMGKL-KLKNTVTIQQEKL--LAEKEEKLQKEQKELQDVGQSLRIKEQEVcKLQEQLEATVKKLEESKQLLKNNEK 302
Cdd:COG1340 203 EADELRKEAdELHKEIVEAQEKAdeLHEEIIELQKELRELRKELKKLRKKQRAL-KREKEKEELEEKAEEIFEKLKKGEK 281
|
.
gi 2462505358 303 L 303
Cdd:COG1340 282 L 282
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
244-315 |
1.36e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462505358 244 QEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQ 315
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
75-299 |
1.36e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 75 LHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEeelqRTKQEVLSLRREnstLDVECHEKEKHVNQLQ 154
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE----KGRQELEKAKRK---LEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 155 TKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKL 234
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505358 235 KLKNTVTIQQEKLLAEKEEKLQKEQKELQDVG-------QSLRIKE-QEVCKLQEQLEATVK---KLEESKQLLKN 299
Cdd:pfam01576 309 EDTLDTTAAQQELRSKREQEVTELKKALEEETrsheaqlQEMRQKHtQALEELTEQLEQAKRnkaNLEKAKQALES 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-145 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEWASH-TAALtnkhsQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQ-- 78
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNgGDRL-----EQLEREIERLERELEERERRRARLEALLAALGLPlp 376
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462505358 79 -NIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHE 145
Cdd:COG4913 377 aSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
108-304 |
2.40e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 108 IRELKAKLSGVEEELQRtkqEVLSLRRENSTLDVECHEKEkhvNQLQTKVAVLEQEIKDKDQLVLRTK---EAFDTIQEQ 184
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKE---NKMKDLTFLLEESRDKANQLEEKTKlqdENLKELIEK 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 185 KVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNT----VTIQQEKLLAEKEEKLQKEQK 260
Cdd:pfam05483 291 KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEELLRTEQQ 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462505358 261 ELQDVGQSLRIKEQEVCKLQEQLEATVK-------KLEESKQLLKNNEKLI 304
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLL 421
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-313 |
2.68e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 198 QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKL-----QKE----QKELQDVGQS 268
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEyealQKEIESLKRR 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462505358 269 LRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
172-318 |
2.85e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 172 LRTKEAFDTIQEqkVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtIQQEKLLAEK 251
Cdd:PRK12705 30 RLAKEAERILQE--AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL-----------VQKEEQLDAR 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462505358 252 EEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEAtvkKLEESKQLLKN--NEKLITWLNKELNENQLVR 318
Cdd:PRK12705 97 AEKLDNLENQLEEREKALSARELELEELEKQLDN---ELYRVAGLTPEqaRKLLLKLLDAELEEEKAQR 162
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1-285 |
2.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 1 MQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAAL--TNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQ 78
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELeqLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 79 nIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKE--KHVNQLQTK 156
Cdd:COG4372 117 -LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldELLKEANRN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 157 VAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 236
Cdd:COG4372 196 AEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462505358 237 KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEA 285
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| TOP4c |
cd00187 |
DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), ... |
193-313 |
3.06e-03 |
|
DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), bacterial DNA gyrases (A subunit, GyrA),mammalian DNA toposiomerases II. DNA topoisomerases are essential enzymes that regulate the conformational changes in DNA topology by catalysing the concerted breakage and rejoining of DNA strands during normal cellular growth.
Pssm-ID: 238111 [Multi-domain] Cd Length: 445 Bit Score: 39.86 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 193 EKNQVQLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKElqdvgqslrik 272
Cdd:cd00187 341 GKAEARLHILEGLLKAILN-IDEVINLIRSSDEAKKALIEELEKLGFSEIQADAILDMRLRRLTKLERE----------- 408
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462505358 273 eqevcKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:cd00187 409 -----KLLKELKELEAEIEDLEKILASEERPKDLWKEELDE 444
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
77-313 |
3.78e-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: 40.03 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 77 QQNIHQLQNRLSELEAANKDLTERKYKGDSTiRELKAKLSGVEEELQRTKQE--------------VLSLRRENSTLDVE 142
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQramlagatavysqfITQLTDENQSCCPV 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 143 CH-------EKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLK 215
Cdd:TIGR00606 683 CQrvfqteaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 216 ANEIIKKLQGDLKTLMGKLKLKN------TVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKE--QEVCKLQEQLEATV 287
Cdd:TIGR00606 763 LKNDIEEQETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQvnQEKQEKQHELDTVV 842
|
250 260
....*....|....*....|....*.
gi 2462505358 288 KKLEESKQLLKNNEKLITWLNKELNE 313
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNE 868
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
100-313 |
3.78e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.06 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 100 RKYKGD--STIRELKAKLsgVEEELQRTKQEVLSLRRENSTLD--VECHEKEKHVNQLQTKVAVLeqeikdkdQLVLRTK 175
Cdd:COG5022 809 RKEYRSylACIIKLQKTI--KREKKLRETEEVEFSLKAEVLIQkfGRSLKAKKRFSLLKKETIYL--------QSAQRVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 176 EAFDTIQEQKvvlEENGEKNQVqlgkleatiKSLSAELLK-ANEIIKKLQGDLktlMGKLKLKNTVTIQQEKLLAEKEEK 254
Cdd:COG5022 879 LAERQLQELK---IDVKSISSL---------KLVNLELESeIIELKKSLSSDL---IENLEFKTELIARLKKLLNNIDLE 943
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462505358 255 LQKE-QKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK-QLLKNNEKLITWlNKELNE 313
Cdd:COG5022 944 EGPSiEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVrEGNKANSELKNF-KKELAE 1003
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
76-275 |
3.91e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 76 HQQNIHQLQNRLSELEAANKDLteRKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH------ 149
Cdd:COG4913 260 LAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngg 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 150 --VNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQ----LGKLEATIKSLSAELLKANEIIKKL 223
Cdd:COG4913 338 drLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505358 224 QGDLKTLMGKLKL----KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQE 275
Cdd:COG4913 418 RRELRELEAEIASlerrKSNIPARLLALRDALAEALGLDEAELPFVGELIEVRPEE 473
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-323 |
4.22e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 192 GEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLL--AEKEEKLQKEQKELQDVGQSl 269
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAS- 683
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462505358 270 rikEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELN--ENQLVRKQDVL 323
Cdd:COG4913 684 ---SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaEEELDELQDRL 736
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
80-299 |
4.29e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.45 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 80 IHQLQN----RLSELEAANKDLTERKYKGDSTirELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEchEKEKHVNQLQt 155
Cdd:pfam06160 202 YEELKTelpdQLEELKEGYREMEEEGYALEHL--NVDKEIQQLEEQLEENLALLENLELDEAEEALE--EIEERIDQLY- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 156 kvAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEK-NQVQL-----GKLEATIKSLSAELlkaNEIIKKLQGDLKT 229
Cdd:pfam06160 277 --DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEElERVQQsytlnENELERVRGLEKQL---EELEKRYDEIVER 351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 230 LMGKLKLKNTVTIQQEKLLAEKEEkLQKEQKELQDVGQSLRIKEQEVcklQEQLEATVKKLEESKQLLKN 299
Cdd:pfam06160 352 LEEKEVAYSELQEELEEILEQLEE-IEEEQEEFKESLQSLRKDELEA---REKLDEFKLELREIKRLVEK 417
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
45-302 |
4.39e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.70 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 45 QELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNihqlQNRLSELEaankdltERKYKGDSTIRELKAKLSGVEEELQR 124
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES----RDKANQLE-------EKTKLQDENLKELIEKKDHLTKELED 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 125 TKQEVLSLRRENSTLDVECHEKEKHVNQL-QTKVAVLEQEIKDKDQLVLRTKEAFDTIqeqkVVLEENGEKNQVQLGKLE 203
Cdd:pfam05483 301 IKMSLQRSMSTQKALEEDLQIATKTICQLtEEKEAQMEELNKAKAAHSFVVTEFEATT----CSLEELLRTEQQRLEKNE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 204 ATIKSLSAELLKANEIIKKlqgdlktlMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 283
Cdd:pfam05483 377 DQLKIITMELQKKSSELEE--------MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
250
....*....|....*....
gi 2462505358 284 EATVKKLEESKQLLKNNEK 302
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEE 467
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2-301 |
4.91e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 2 QSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtAALTNKHSQELTNEKE---KALQAQVQYQQQHEQQKKDLEILHQQ 78
Cdd:pfam15921 496 RTVSDLTASLQEKERAIEATNAEITKLRSR-----VDLKLQELQHLKNEGDhlrNVQTECEALKLQMAEKDKVIEILRQQ 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 79 --NIHQLQNR--------LSELEAANKDLTER----------KYKGDSTIRELKAKLSGVEeelqrtkqevlslrrenst 138
Cdd:pfam15921 571 ieNMTQLVGQhgrtagamQVEKAQLEKEINDRrlelqefkilKDKKDAKIRELEARVSDLE------------------- 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 139 ldvecHEKEKHVNQLQTKVAVLEQEIKDKDQL---VLRTKEAFDTIQEQKVVLEEN----GEKNQVQLGKLEATIKSLSA 211
Cdd:pfam15921 632 -----LEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDYEVLKRNfrnkSEEMETTTNKLKMQLKSAQS 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 212 ELLKANEIIKKLQGD----LKTLMGKLK-----------LKNTVTIQQEKLL-AEKEEKLQKEQKelQDVGQSLRIKEQE 275
Cdd:pfam15921 707 ELEQTRNTLKSMEGSdghaMKVAMGMQKqitakrgqidaLQSKIQFLEEAMTnANKEKHFLKEEK--NKLSQELSTVATE 784
|
330 340
....*....|....*....|....*.
gi 2462505358 276 VCKLQEQLEATVKKLEESKQLLKNNE 301
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANME 810
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2-222 |
6.09e-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: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 2 QSLDDATKQLDFTRKTLaekKQELDKLRNEWASHTAALTNKhsqeltnekekalqaqvqyqqqheqqkkdleilhQQNIH 81
Cdd:COG1579 13 QELDSELDRLEHRLKEL---PAELAELEDELAALEARLEAA----------------------------------KTELE 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 82 QLQNRLSELEAANKDLTERkykgdstIRELKAKLSGV--EEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAV 159
Cdd:COG1579 56 DLEKEIKRLELEIEEVEAR-------IKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAE 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462505358 160 LEQEIKDKDQLVLRTKEAFDTIQEQkvvLEENGEKNQVQLGKLEATIkslSAELLKANEIIKK 222
Cdd:COG1579 129 LEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREELAAKI---PPELLALYERIRK 185
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
77-316 |
6.86e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 77 QQNIHQLQNRLSELEAANKDLTErkykgdSTIRELKAKLSGVEE--ELQRTK-------QEVLSLRRENSTLdvecheke 147
Cdd:PRK11281 169 SQRLQQIRNLLKGGKVGGKALRP------SQRVLLQAEQALLNAqnDLQRKSlegntqlQDLLQKQRDYLTA-------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 148 kHVNQLQTKVAVLEQEIKDKdqlvlRTKEAFDTIQEQkVVLEENGEKNQVQLGKLEATI-KSLSAELLKANEiikklqgD 226
Cdd:PRK11281 235 -RIQRLEHQLQLLQEAINSK-----RLTLSEKTVQEA-QSQDEAARIQANPLVAQELEInLQLSQRLLKATE-------K 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 227 LKTLMGK-LKLKNTV--TIQQEKLLAEKEEKLQ----------KEQ------KELQDVGQS---LRIKEQEVCKLQEQL- 283
Cdd:PRK11281 301 LNTLTQQnLRVKNWLdrLTQSERNIKEQISVLKgslllsrilyQQQqalpsaDLIEGLADRiadLRLEQFEINQQRDALf 380
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2462505358 284 --EATVKKLEES-------------KQLLKNNEKLITWLNKELNeNQL 316
Cdd:PRK11281 381 qpDAYIDKLEAGhksevtdevrdalLQLLDERRELLDQLNKQLN-NQL 427
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
72-297 |
8.61e-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: 38.65 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 72 LEILHQQNIHQLQNRLSELEAANKDLterkykgdstiRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVN 151
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKEN-----------KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 152 QLqtkvavlEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQvqlgkleaTIKSLSAELLKANEIIKKLQGDLKTLM 231
Cdd:pfam10174 521 SL-------EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIND--------RIRLLEQEVARYKEESGKAQAEVERLL 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 232 GKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEV--------------------CKLQEQLEATVKKLE 291
Cdd:pfam10174 586 GILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMkkkgaqlleearrrednladNSQQLQLEELMGALE 665
|
....*.
gi 2462505358 292 ESKQLL 297
Cdd:pfam10174 666 KTRQEL 671
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
209-315 |
8.74e-03 |
|
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: 38.21 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 209 LSAELLKANEIIKKLQGDLKTLmgklklkntvtiQQEklLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVK 288
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQL------------QQE--IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ 76
|
90 100
....*....|....*....|....*..
gi 2462505358 289 KLEESKQLLKNNEKLITWLNKELNENQ 315
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQK 103
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
69-313 |
9.72e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.73 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 69 KKDLEILHQQNIHQLQNRLSELEAANKDLTERKYKgDSTIRELKAKLSGVEEELQRTKQEVLSLRREN--------STLD 140
Cdd:PRK01156 503 KKRKEYLESEEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLKLEDLDSKRTSwlnalaviSLID 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 141 VEC-----HEKEKHVNQLQTKVAVLEQEIKD----KDQLVLRTKEAFDTIQEQKVVLEENgeknQVQLGKLEATIKSLSA 211
Cdd:PRK01156 582 IETnrsrsNEIKKQLNDLESRLQEIEIGFPDdksyIDKSIREIENEANNLNNKYNEIQEN----KILIEKLRGKIDNYKK 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462505358 212 ELLKANEIIKKlqgdlktlmgklklKNTVTIQqeklLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLE 291
Cdd:PRK01156 658 QIAEIDSIIPD--------------LKEITSR----INDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIN 719
|
250 260
....*....|....*....|....
gi 2462505358 292 ESKQLLKNNEKLITWLN--KELNE 313
Cdd:PRK01156 720 DINETLESMKKIKKAIGdlKRLRE 743
|
|
| |
