|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-522 |
2.04e-11 |
|
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: 67.39 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 186 EFYEAKLQEKTGLLEEA------QEDVRQQLREFEETKKQIEEDED-----------REIQDIKTKYERKLRDEKESNlr 248
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAagiskyKERRKETERKLERTRENLDRLEDilnelerqlksLERQAEKAERYKELKAELREL-- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 249 lkgETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEK 328
Cdd:TIGR02168 226 ---ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 329 FKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVR 408
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 409 RFKTDLHncvayiqepgLLKEKIRGLfekyvqradMVEIAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYV 488
Cdd:TIGR02168 383 TLRSKVA----------QLELQIASL---------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443
|
330 340 350
....*....|....*....|....*....|....
gi 1907157138 489 RIMQENVSLIKEINELRRELKLTRSQIYDLESAL 522
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
145-409 |
6.21e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 145 LLLEYEKYQElQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDE 224
Cdd:COG1196 230 LLLKLRELEA-ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 225 DReiqdiktkyerkLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQE 304
Cdd:COG1196 309 ER------------RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 305 RDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQ 384
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260
....*....|....*....|....*
gi 1907157138 385 KLRATDQEMRKEQQKERDLEALVRR 409
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
164-523 |
1.54e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 164 EEYEKQLRDNDETKSQALEELTEfYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQdiktkYERKLRDEK 243
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-----LEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 244 ESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKN 323
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 324 QELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDL 403
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 404 EALVRRFKTDLHNCVAYIQE-PGLLKEKIRGLFEKYVQRADMVEIAGLNSDLQQEYARQRehlernLATLKKKVIKEGEL 482
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR------LKRLENKIKELGPV 987
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907157138 483 hrtdyvrimqeNVSLIKEINELRRELKLTRSQIYDLESALK 523
Cdd:TIGR02168 988 -----------NLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
121-404 |
2.04e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 121 ERLEELVDKQTRELQDLECCNNQKllleyEKYQELQLKSQ-RMQEEYEKQLRDNDETKSQALEELTEFyEAKLQEKTGLL 199
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKA-----ERYQALLKEKReYEGYELLKEKEALERQKEAIERQLASL-EEELEKLTEEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 200 EEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKY----------ERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEE 269
Cdd:TIGR02169 261 SELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIgeleaeiaslERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 270 RTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQ-------DKEKRIYDLKKKNQELEKFKFVLDYKIKELKK 342
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelkDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157138 343 QIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLE 404
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-395 |
4.42e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 117 ISHRERLEELVDKQTRELQDLEccnnqKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEEltefYEAKLQEKT 196
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDAS-----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN----VKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 197 GLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIEL 276
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 277 LKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKE 356
Cdd:TIGR02169 845 LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907157138 357 QIQEMEAELERFHKQNTQL------ELNITELLQKLRATDQEMRK 395
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEEIRA 969
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
53-425 |
4.94e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 53 EKAQIMLELKTRVEELKMENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELVD-KQT 131
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaEEA 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 132 RELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLR 211
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 212 EFEETKKQIE-----EDEDREIQDIKTKYERKLRDEKESNlrlKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKlqg 286
Cdd:PTZ00121 1614 KAEEAKIKAEelkkaEEEKKKVEQLKKKEAEEKKKAEELK---KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--- 1687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 287 iirslEKDIQGLKREIQERDETIQDKeKRIYDLKKKNQELEKFKFVLDYKIKELKKQieprENEIKVMKEQIQEMEAELE 366
Cdd:PTZ00121 1688 -----KKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKK 1757
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907157138 367 RFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEalVRRFKTDLHNCVAYIQEPG 425
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIEGG 1814
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-394 |
7.08e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 53 EKAQIMLELKTRVEELkmenEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELvDKQTR 132
Cdd:TIGR02169 208 EKAERYQALLKEKREY----EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL-NKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 133 ELQDLECCNNQKLLLEYEKYQElqlKSQRMQEEYEKQLRDNDETKSQALEELTefyeaKLQEKTGLLEEAQEDVRQQLRE 212
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEAEIA---SLERSIAEKERELEDAEERLAKLEAEID-----KLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 213 FEEtkkqieededrEIQDIKTKYERKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQgiirsle 292
Cdd:TIGR02169 355 LTE-----------EYAELKEELEDLRAELEE----VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ------- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 293 kdiqglkREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQN 372
Cdd:TIGR02169 413 -------EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340
....*....|....*....|..
gi 1907157138 373 TQLELNITELLQKLRATDQEMR 394
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVR 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-475 |
7.50e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 198 LLEEAQE-DVRQQLREFEETKKQIEEDEdREIQDIKTKYERKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIEL 276
Cdd:COG1196 218 LKEELKElEAELLLLKLRELEAELEELE-AELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 277 LKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKE 356
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 357 QIQEMEAELERFHKQNTQLELNITELLQKLRATDQEM-RKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLF 435
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEeALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907157138 436 EKYVQRADMVEIAGLNSDLQQEYARQREHLERNLATLKKK 475
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-472 |
8.55e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 221 EEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKR 300
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 301 EIQERDETIQDKEKRIYDLKKKNQELEK-----FKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQL 375
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 376 ELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYvqRADMVEIAGLNSDLQ 455
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL--EAQLRELERKIEELE 909
|
250
....*....|....*..
gi 1907157138 456 QEYARQREHLERNLATL 472
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKL 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
53-366 |
5.89e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 53 EKAQIMLELKTRVEELkmenEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTR 132
Cdd:COG1196 210 EKAERYRELKEELKEL----EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 133 ELQDLECCNNQKLLLEyekyQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEfyEAKLQEKTGLLEEAQEDVRQQLRE 212
Cdd:COG1196 286 AQAEEYELLAELARLE----QDIARLEERRRELEERLEELEEELAELEEELEEL--EEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 213 FEETKKQIEEDEDREIQDiktkyERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLE 292
Cdd:COG1196 360 LAEAEEALLEAEAELAEA-----EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157138 293 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELE 366
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-580 |
8.36e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 150 EKYQELQLKSQRMQEEYEKqLRDNDETKSQALEELtEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQ 229
Cdd:TIGR02168 239 EELEELQEELKEAEEELEE-LTAELQELEEKLEEL-RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 230 DIKtKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETI 309
Cdd:TIGR02168 317 QLE-ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 310 QDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRE-----NEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQ 384
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 385 KLRATDQEMRKEQQKERDLEALVRRFKtDLHNCVAYIQEPGLLKEKIRGLF-------EKYVQ--------RADMVEIAG 449
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLE-GFSEGVKALLKNQSGLSGILGVLselisvdEGYEAaieaalggRLQAVVVEN 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 450 LNSDLQqEYARQREHLERNLATLKKKVIKEGELHRTDYVRIMQEN------VSLIKEINELRRELKLTRSQIY---DLES 520
Cdd:TIGR02168 555 LNAAKK-AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvaKDLVKFDPKLRKALSYLLGGVLvvdDLDN 633
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 521 ALKVSKKTRSQEVpeSVISKDVVGSTSTMRLNEQEETGRIIEMQRLEIRRLRDQIQEQEQ 580
Cdd:TIGR02168 634 ALELAKKLRPGYR--IVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEE 691
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
83-385 |
1.51e-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: 51.17 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 83 YTEKIKELTDkfiqEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTRELQDLECCNNQKLLLEyEKYQELQlKSQRM 162
Cdd:TIGR04523 209 KIQKNKSLES----QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS-EKQKELE-QNNKK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 163 QEEYEKQLR----DNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIE---------EDEDREIQ 229
Cdd:TIGR04523 283 IKELEKQLNqlksEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkeltnsESENSEKQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 230 DIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETI 309
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157138 310 QDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQK 385
Cdd:TIGR04523 443 KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
257-414 |
2.25e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 257 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKfkfVLDYK 336
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 337 IKELKKQI-----EPRENEIKV-----------------------MKEQIQEMEAELERFHKQNTQLELNITELLQKLRA 388
Cdd:COG4942 103 KEELAELLralyrLGRQPPLALllspedfldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180
....*....|....*....|....*.
gi 1907157138 389 TDQEMRKEQQKERDLEALVRRFKTDL 414
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKEL 208
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
49-362 |
2.51e-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: 50.40 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 49 TDMEEKAQIMLELKTRVEELKMENEyQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKT-EKEKQDISHR-ERLEEL 126
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQ-SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKlQQEKELLEKEiERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 127 VDKQTRELQDLECCNNQKLLlEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYE--AKLQEKTGLLEEAQE 204
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKEL-IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKelKKLNEEKKELEEKVK 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 205 DVRQQLREFEETKKQIEededREIQDIKTKYERKLRDEKESNLRLKGETgiMRKKFSSLQKEIEERTNDIELLKSEQMKL 284
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLE----SEKKEKESKISDLEDELNKDDFELKKEN--LEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907157138 285 QGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEME 362
Cdd:TIGR04523 588 QELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEII 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-468 |
4.49e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 257 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKR--EIQERDETIQDKEKRIYDLKKKNQELEKFkfvlD 334
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAS----S 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 335 YKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQ-------KERDLEALV 407
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRalleerfAAALGDAVE 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157138 408 RRFKTDLHNCV-AYIQEPGLLKEKIRGLFEKYVQRADMvEIAGLNSDLQ--QEYARQREHLERN 468
Cdd:COG4913 765 RELRENLEERIdALRARLNRAEEELERAMRAFNREWPA-ETADLDADLEslPEYLALLDRLEED 827
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
293-527 |
4.69e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 293 KDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKfkfvldyKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQN 372
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK-------QLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 373 TQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEpglLKEKIRGLFEKYvqRADMVEIAGLNS 452
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY---LAPARREQAEEL--RADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907157138 453 DLQQEYARQREhLERNLATLKKKVIKEGELHRTDYVRIMQENVSLIKEINELRRELKLTRSQIYDLESALKVSKK 527
Cdd:COG4942 168 ELEAERAELEA-LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
153-393 |
6.11e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 153 QELQLKSQRMQEEyEKQLRDNDETKSQALEELTEFyEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIK 232
Cdd:COG4942 27 AELEQLQQEIAEL-EKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELAELEKEIAELR-AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 233 TKYERKLRdekesNLRLKGETGIMRKKFSSlqkeieertNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDK 312
Cdd:COG4942 104 EELAELLR-----ALYRLGRQPPLALLLSP---------EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 313 EKRIYDLKKKNQELEKfkfvldyKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQE 392
Cdd:COG4942 170 EAERAELEALLAELEE-------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
.
gi 1907157138 393 M 393
Cdd:COG4942 243 T 243
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
199-342 |
8.00e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.70 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 199 LEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKEsnlRLKGETGIMRKKFSSLQKEIEERTNDIELLK 278
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---RLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157138 279 SEQmklqgiIRSLEKDiqglkREIQERDETIQDKEKRIYDLKKKNQELEKfkfvldyKIKELKK 342
Cdd:COG2433 455 SEE------RREIRKD-----REISRLDREIERLERELEEERERIEELKR-------KLERLKE 500
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
170-412 |
1.73e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 170 LRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQedvrQQLREFEETKKQIEededreiqdiktkyerklrdekesnlrL 249
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQKNGLVD---------------------------L 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 250 KGETGIMRKKFSSLQKEIEErtndielLKSEQMKLQGIIRSLEKDIQGLKREIQE--RDETIQDKEKRIYDLKKKNQELE 327
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAE-------ARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 328 KfKFVLDY-KIKELKKQIEPRENEIKVMKEQI-QEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEA 405
Cdd:COG3206 284 A-RYTPNHpDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
....*..
gi 1907157138 406 LVRRFKT 412
Cdd:COG3206 363 ARELYES 369
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
32-304 |
1.76e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 32 IKREREVGFAEEVLVTKTDMEEKAQIMLELKtRVEELKMENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTE 111
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 112 KEKQDISHRERLEELVDKQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQAleeltefYEAK 191
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA-------EEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 192 LQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNlRLKGETGIMRKKFSSLQKEIEERT 271
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKEEEKKAEEIRKEKEAVI 1781
|
250 260 270
....*....|....*....|....*....|...
gi 1907157138 272 NdiELLKSEQMKLQGIIRSLEKDIQGLKREIQE 304
Cdd:PTZ00121 1782 E--EELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
264-367 |
2.01e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 264 QKEIEERTNDIEL-LKSEQMKLQgiiRSLEKDIQGLKREIQERDETIQDKEKRiydLKKKNQELEKFKFVLDYKIKELKK 342
Cdd:PRK12704 48 KKEAEAIKKEALLeAKEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEEN---LDRKLELLEKREEELEKKEKELEQ 121
|
90 100
....*....|....*....|....*
gi 1907157138 343 QIEPRENEIKVMKEQIQEMEAELER 367
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQLQELER 146
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
178-409 |
2.69e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 178 SQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQdiktkYERKLRDekesnlrLKGETGIMR 257
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-----LARRIRA-------LEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 258 KKFSSLQKEIEERTNDIELLKSEqmkLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKI 337
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157138 338 KELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRR 409
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-408 |
3.08e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 156 QLKSQrMQEEYEKQLRDNDETKSQALEELTEFYEaKLQEKTGLLEEAQEDVRQQLREFEETKKQIE--EDEDREIQDIKT 233
Cdd:PRK02224 191 QLKAQ-IEEKEEKDLHERLNGLESELAELDEEIE-RYEEQREQARETRDEADEVLEEHEERREELEtlEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 234 KYERKlRDEkesnlrLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKE 313
Cdd:PRK02224 269 ETERE-REE------LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 314 K-------RIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEaelERFHKQNTQLElNITELLQKL 386
Cdd:PRK02224 342 EeaeslreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR---ERFGDAPVDLG-NAEDFLEEL 417
|
250 260
....*....|....*....|..
gi 1907157138 387 RATDQEMRkeqQKERDLEALVR 408
Cdd:PRK02224 418 REERDELR---EREAELEATLR 436
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
96-408 |
3.17e-05 |
|
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: 47.04 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 96 QEMESLKTKNQVLKTEKEKQDISHRERLEELVDKQTRELQDleccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDE 175
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQ----EKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 176 TKSQALEELTEFYEAKLQEKTGLLEEA-QEDVR---QQLREFEETKKQIEEDEDREIQDIKTKYERKLRdEKESNLRLKG 251
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRELERIrQEEIAmeiSRMRELERLQMERQQKNERVRQELEAARKVKIL-EEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 252 ETGIMRK--------KFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETiQDKEKRIYDLKKK- 322
Cdd:pfam17380 418 QKVEMEQiraeqeeaRQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-KRDRKRAEEQRRKi 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 323 -NQELEKFKFVL---DYKIKELKKQIEPRENEIKvmkEQIQEMEAELERFHKQNtqlelnitelLQKLRATDQEMRKEQQ 398
Cdd:pfam17380 497 lEKELEERKQAMieeERKRKLLEKEMEERQKAIY---EEERRREAEEERRKQQE----------MEERRRIQEQMRKATE 563
|
330
....*....|
gi 1907157138 399 KERDLEALVR 408
Cdd:pfam17380 564 ERSRLEAMER 573
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
257-409 |
4.07e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 257 RKKFSSLQKEIEERTnDIELLKSEQMK---LQGIIRSLEKDIQGLK-----REIQERDETIQDKEKRIYDLKKKNQELEK 328
Cdd:COG2433 349 KNKFERVEKKVPPDV-DRDEVKARVIRglsIEEALEELIEKELPEEepeaeREKEHEERELTEEEEEIRRLEEQVERLEA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 329 FKFVLDYKIKELKKQIEPRENEIKVMKEQIQE---MEAELERFHKQNTQLElnitELLQKLRATDQEMRKEQQKERDLEA 405
Cdd:COG2433 428 EVEELEAELEEKDERIERLERELSEARSEERReirKDREISRLDREIERLE----RELEEERERIEELKRKLERLKELWK 503
|
....
gi 1907157138 406 LVRR 409
Cdd:COG2433 504 LEHS 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
333-532 |
5.78e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 333 LDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQN--TQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRF 410
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 411 KTDL---HNCVAYIQEPGLLKEKIRGLFEKYVQRADMV---------------EIAGLNSDLQQEYARQREHLERNLATL 472
Cdd:COG3206 246 RAQLgsgPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvialraQIAALRAQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157138 473 KKkviKEGELHRT--DYVRIMQENVSLIKEINELRRELKLTRSQiydLESALKVSKKTRSQE 532
Cdd:COG3206 326 QA---REASLQAQlaQLEARLAELPELEAELRRLEREVEVAREL---YESLLQRLEEARLAE 381
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
42-367 |
5.91e-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: 46.26 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 42 EEVLVTKTDMEEKAQIMLELKTRVEElkmeNEYQLRLKDMNYTeKIKELTDKFIQEMESLKTKNQVLKT-----EKEKQD 116
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQE----KERAIEATNAEIT-KLRSRVDLKLQELQHLKNEGDHLRNvqtecEALKLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 117 ISHRERLEELVDKQTRELQDLECCNNQKL-LLEYEKYQ-ELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAklqE 194
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQLVGQHGRTAgAMQVEKAQlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL---E 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 195 KTGLLEEAQEDVRQqLREFEETKKQIEED---EDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERT 271
Cdd:pfam15921 634 KVKLVNAGSERLRA-VKDIKQERDQLLNEvktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 272 NDIELLKSEQ-------MKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQI 344
Cdd:pfam15921 713 NTLKSMEGSDghamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL 792
|
330 340
....*....|....*....|...
gi 1907157138 345 EPRENEIKVMKEQIQEMEAELER 367
Cdd:pfam15921 793 EVLRSQERRLKEKVANMEVALDK 815
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
148-486 |
8.29e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 148 EYEKYQELQLKSQRMQEEYEK-QLRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEE--DE 224
Cdd:COG5022 811 EYRSYLACIIKLQKTIKREKKlRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQElkID 890
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 225 DREIQDIKTKYER------KLRDEKESNLRLKGEtgIMRKKFSSLQKEIEERtnDIELLKSEQMKLQGIIRSLEKDIQGL 298
Cdd:COG5022 891 VKSISSLKLVNLEleseiiELKKSLSSDLIENLE--FKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLHEVESKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 299 KREIQERDETIQDKEKRIYDLKKKNQELEKFKfvldykiKELkkqiepreNEIKVMKEQIQEMEAELERFHKQNTQLElN 378
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFK-------KEL--------AELSKQYGALQESTKQLKELPVEVAELQ-S 1030
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 379 ITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNcVAYIQEPGLLKEKirglfEKYVQRADMVEIAGLNSDLQQEY 458
Cdd:COG5022 1031 ASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKA-LKLRRENSLLDDK-----QLYQLESTENLLKTINVKDLEVT 1104
|
330 340
....*....|....*....|....*...
gi 1907157138 459 ARQREHLERNLATLKKKVIKEGELHRTD 486
Cdd:COG5022 1105 NRNLVKPANVLQFIVAQMIKLNLLQEIS 1132
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-300 |
9.23e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 34 REREVGFAEEVLVTKTDMEEKAQIMLELKTRVEELKmeNEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKE 113
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQ--AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 114 KQDISHRERLEELVDKQTRELQDLECCNNQKLLLEyEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQ 193
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 194 EKTglLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKEsNLRLKGETGIMRKKFSSLQKEIEERTND 273
Cdd:COG1196 409 EEA--LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE-EEALLELLAELLEEAALLEAALAELLEE 485
|
250 260
....*....|....*....|....*..
gi 1907157138 274 IELLKSEQMKLQGIIRSLEKDIQGLKR 300
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-378 |
1.21e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 53 EKAQIMLELKTRVEELkmeneyQLRLKDMNYTEKIKEL------TDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEEL 126
Cdd:TIGR02168 210 EKAERYKELKAELREL------ELALLVLRLEELREELeelqeeLKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 127 VDKQTR------ELQDLEccNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTGLLE 200
Cdd:TIGR02168 284 EELQKElyalanEISRLE--QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 201 EAQEDVRQQLREFEETKKQIEEdedreiqdiktkYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSE 280
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLET------------LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 281 QMKLQgiirsLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEkfkfvldyKIKELKKQIEPRENEIKVMKEQIQE 360
Cdd:TIGR02168 430 LEEAE-----LKELQAELEELEEELEELQEELERLEEALEELREELE--------EAEQALDAAERELAQLQARLDSLER 496
|
330
....*....|....*...
gi 1907157138 361 MEAELERFHKQNTQLELN 378
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKN 514
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
163-367 |
1.32e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 163 QEEYEKQLRDNDETKSQALEELTEfYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEdREIQDIKTKYERKLRDE 242
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDA-LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE-AEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 243 KESNlrlkGETGIMRKKFSSlqKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKK 322
Cdd:COG3883 96 YRSG----GSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907157138 323 NQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELER 367
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
199-404 |
3.30e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 199 LEEAQEDVRQQLREFEETKKQIEEDEDREiQDIKTKYERKlRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLK 278
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRT-ENIEELIKEK-EKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 279 SEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLD--YKIKELKKQIEPRENEIKVMKE 356
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907157138 357 QIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLE 404
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE 365
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
199-383 |
4.35e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 199 LEEAQEDVRQQLRE-----FEETKKQIEEDEDREIQDIKTKYER---KLRDEKESNLRLKGETGIMRKK----------- 259
Cdd:PRK05771 14 LKSYKDEVLEALHElgvvhIEDLKEELSNERLRKLRSLLTKLSEaldKLRSYLPKLNPLREEKKKVSVKsleelikdvee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 260 -FSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEK------DIQ-------------GLKREIQERDETI---------- 309
Cdd:PRK05771 94 eLEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfdlDLSlllgfkyvsvfvgTVPEDKLEELKLEsdvenveyis 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 310 QDKEKRIY-------DLKKKNQELEKF---KFVLDYK--IKELKKQIEPRENEIkvmKEQIQEMEAELERFHKQNTQLEL 377
Cdd:PRK05771 174 TDKGYVYVvvvvlkeLSDEVEEELKKLgfeRLELEEEgtPSELIREIKEELEEI---EKERESLLEELKELAKKYLEELL 250
|
....*.
gi 1907157138 378 NITELL 383
Cdd:PRK05771 251 ALYEYL 256
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
43-306 |
6.58e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 43 EVLVTKTDMEEKAQIMLELKTRVEELKMENEYQLRLKDMNYtEKIKELTDkFIQEMESLKTKNQVLKTEkekqdisHRER 122
Cdd:COG5022 862 SLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNL-ELESEIIE-LKKSLSSDLIENLEFKTE-------LIAR 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 123 LEELVDKQTRELQdleccnnqkLLLEYEKYQELqlksQRMQEEyEKQLRDNDETKSQALEELTEFYEAKLQEKTGLLEEA 202
Cdd:COG5022 933 LKKLLNNIDLEEG---------PSIEYVKLPEL----NKLHEV-ESKLKETSEEYEDLLKKSTILVREGNKANSELKNFK 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 203 QE--DVRQQLREFEETKKQIEEdEDREIQDIKTKYeRKLRDEKESNLRLKGETGIMR---KKFSSLQKEIEERTNDIE-- 275
Cdd:COG5022 999 KElaELSKQYGALQESTKQLKE-LPVEVAELQSAS-KIISSESTELSILKPLQKLKGlllLENNQLQARYKALKLRREns 1076
|
250 260 270
....*....|....*....|....*....|.
gi 1907157138 276 LLKSEQMKLQGIIRSLEKDIQGLKREIQERD 306
Cdd:COG5022 1077 LLDDKQLYQLESTENLLKTINVKDLEVTNRN 1107
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
204-405 |
9.28e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 204 EDVRQQLRE-FEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQ---KEIEERTNDIELLKS 279
Cdd:PRK02224 179 ERVLSDQRGsLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 280 EQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQ 359
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907157138 360 EMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEA 405
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
334-548 |
1.10e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 334 DYKIKELKKQIEPRENEIKVMKEQIQEMEAELErfhkqntQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTD 413
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 414 LHNCVAYIQEPGLLKEKIRGL-----FEKYVQRADMVE-IAGLNSDLQQEYARQREHLERNLATLKKKvIKEGELHRTDY 487
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLlgsesFSDFLDRLSALSkIADADADLLEELKADKAELEAKKAELEAK-LAELEALKAEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907157138 488 VRIMQENVSLIKEINELRRELKLTRSQIYDLESALKVSKKTRSQEVPESVISKDVVGSTST 548
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
173-370 |
1.38e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 173 NDETKSQALEELTEFYEAKLQEKTGLLEEAQEdVRQQLREFEetkKQIEEDEDrEIQDIKTKYERKLRDEKESnlrlkge 252
Cdd:cd22656 108 DDEELEEAKKTIKALLDDLLKEAKKYQDKAAK-VVDKLTDFE---NQTEKDQT-ALETLEKALKDLLTDEGGA------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 253 tgIMRKKFSSLQKEIEErtndiellkseqmKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKknqelekfkfv 332
Cdd:cd22656 176 --IARKEIKDLQKELEK-------------LNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTA----------- 229
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907157138 333 LDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHK 370
Cdd:cd22656 230 ADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDSLKD 267
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
258-579 |
1.78e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 258 KKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKfvldYKI 337
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 338 KELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITEL------LQKLRATDQEMRKEQQKERDLEALVRRFK 411
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 412 TDLHNCVAYIQEPGLLKEKIRGLFEKYVQRADMVEI----AGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDY 487
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 488 VRIMQENVSLIKEINELRRELKLTRSQIYDLESALKVSKKTRsqevpesviskdvvgststmRLNEQEETGRIIEMQRLE 567
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG--------------------RELTEEHRKELLEEYTAE 460
|
330
....*....|..
gi 1907157138 568 IRRLRDQIQEQE 579
Cdd:PRK03918 461 LKRIEKELKEIE 472
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
33-515 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 33 KREREVGFAEEVLVTKTDMEEKAQIMLELKTRVEELKMENEyQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEK 112
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 113 EKQDISHRERLEELVDKQTRELQDLECCNNQKLLLEYEKYQELQLKS----QRMQEEYEKQLRDNDETKSQALEELTEFY 188
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAllerLERLEEELEELEEALAELEEEEEEEEEAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 189 EAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQK--- 265
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlag 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 266 ---------EIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYK 336
Cdd:COG1196 525 avavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 337 IKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRfktdlhn 416
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA------- 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 417 cvayIQEPGLLKEKIRGLFEKYVQRADMVEIAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYVRIMQENVS 496
Cdd:COG1196 678 ----EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
490 500
....*....|....*....|...
gi 1907157138 497 LIKE----INELRRELKLTRSQI 515
Cdd:COG1196 754 EELPeppdLEELERELERLEREI 776
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
257-405 |
2.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 257 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIqdkEKRIYDLKKKNQELEKFKFVLDYK 336
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GERARALYRSGGSVSYLDVLLGSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 337 -------------------------IKELKKQIEPRENEIKVMKEQIQEMEAELERFHKqntQLELNITELLQKLRATDQ 391
Cdd:COG3883 113 sfsdfldrlsalskiadadadlleeLKADKAELEAKKAELEAKLAELEALKAELEAAKA---ELEAQQAEQEALLAQLSA 189
|
170
....*....|....
gi 1907157138 392 EMRKEQQKERDLEA 405
Cdd:COG3883 190 EEAAAEAQLAELEA 203
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
66-302 |
2.63e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 66 EELKMENEYQLRLKDMN--YTEKIKELTDKFIQEMESLKT-----KNQVLKTEKEKQDIShrERLEELVDKQTRELQDLE 138
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNgeNIARKQNKYDELVEEAKTIKAeieelTDELLNLVMDIEDPS--AALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 139 CCnnQKLLLEYEKYQELQLKSQRMQEEYEKqLRDNDETKSQALEELTefyeaKLQEKTGLLEEAQEDVRQQLREFEETKK 218
Cdd:PHA02562 273 QF--QKVIKMYEKGGVCPTCTQQISEGPDR-ITKIKDKLKELQHSLE-----KLDTAIDELEEIMDEFNEQSKKLLELKN 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 219 QIEEdEDREIQdiktKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLqGIIRSLEKDiQGL 298
Cdd:PHA02562 345 KIST-NKQSLI----TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR-GIVTDLLKD-SGI 417
|
....
gi 1907157138 299 KREI 302
Cdd:PHA02562 418 KASI 421
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
53-528 |
2.64e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 53 EKAQIMLELKTRVEELKmENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKN-QVLKTEKE----KQDISHRERLEELV 127
Cdd:TIGR04523 65 KDEEKINNSNNKIKILE-QQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKeQKNKLEVElnklEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 128 DKQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALE-ELTEFYEAKLQEKTGLLEEAQEDV 206
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlELLLSNLKKKIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 207 RQQLREFEETKKQiEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSE-----Q 281
Cdd:TIGR04523 224 KKQNNQLKDNIEK-KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 282 MKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEM 361
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 362 EAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKtdlhncvayiQEPGLLKEKIRGLFEKYVQR 441
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK----------ETIIKNNSEIKDLTNQDSVK 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 442 ADMVEiaglnsdlqqEYARQREHLERNLATLKKKVIKEgelhRTDYVRIMQENVSLIKEINELRRELKLTRSQIYDLESA 521
Cdd:TIGR04523 453 ELIIK----------NLDNTRESLETQLKVLSRSINKI----KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
....*..
gi 1907157138 522 LKVSKKT 528
Cdd:TIGR04523 519 ISSLKEK 525
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
42-414 |
2.71e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 42 EEVLVTKTDMEEKAQIMLELKTRVEELKmENEYQLRLKDMNYTEKIKELTDKfIQEMESLKTKNQVLKTEKE--KQDISH 119
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEEEINGIEER-IKELEEKEERLEELKKKLKelEKRLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 120 RERLEELVDKQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEA--KLQEKTG 197
Cdd:PRK03918 357 LEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAieELKKAKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 198 --------LLEEAQEDV----RQQLREFEETKKQIEEDEdREIQDIKTKYERKLRDEKE--SNLRLKGETGIMRKKFSSL 263
Cdd:PRK03918 437 kcpvcgreLTEEHRKELleeyTAELKRIEKELKEIEEKE-RKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 264 QKE-IEERTNDIELLKSEQMKLQGIIRSLEKDI---QGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKF-VLDYKIK 338
Cdd:PRK03918 516 NLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELeklEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLK 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 339 EL-------------KKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLraTDQEMRKEQQKERDLEA 405
Cdd:PRK03918 596 ELepfyneylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSR 673
|
....*....
gi 1907157138 406 LVRRFKTDL 414
Cdd:PRK03918 674 ELAGLRAEL 682
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
148-414 |
3.01e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 148 EYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEEL---TEFY------EAKLQEKTGLLEEAQEDVRQQLREFEETKK 218
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaeTELCaeaeemRARLAARKQELEEILHELESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 219 QIEEDEDREIQDIKtKYERKLRDEKESNLRLKGETgimrkkfSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGL 298
Cdd:pfam01576 93 QLQNEKKKMQQHIQ-DLEEQLDEEEAARQKLQLEK-------VTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 299 KREIQERDE--------------TIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAE 364
Cdd:pfam01576 165 TSNLAEEEEkakslsklknkheaMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157138 365 LE--------------RFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDL 414
Cdd:pfam01576 245 LQaalarleeetaqknNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL 308
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
161-415 |
3.12e-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: 40.73 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 161 RMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTGLLEE--AQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERK 238
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAkkALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 239 LRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIyd 318
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEK-- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 319 lKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEMRKEQQ 398
Cdd:pfam02463 324 -KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250
....*....|....*..
gi 1907157138 399 KERDLEALVRRFKTDLH 415
Cdd:pfam02463 403 EEKEAQLLLELARQLED 419
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-347 |
3.48e-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: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 173 NDETKSQALEELTEfYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDrEIQDIKTKYERKLRDEKESNLRLKGE 252
Cdd:COG1579 1 AMPEDLRALLDLQE-LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKT-ELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 253 TGIMR-----KKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRiydLKKKNQELE 327
Cdd:COG1579 79 EEQLGnvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELE 155
|
170 180
....*....|....*....|
gi 1907157138 328 KFKFVLDYKIKELKKQIEPR 347
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
50-343 |
3.72e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 50 DMEEKAQIMLELKTRVEELKMENEYQLRLKDmNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDISHRERLEELVDK 129
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELK-ELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 130 QTRELQDLEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDETKSQ--ALEELTEFYEAKLQEKTGLLEEAQEDVR 207
Cdd:TIGR02169 810 IEARLREIE-----------QKLNRLTLEKEYLEKEIQELQEQRIDLKEQikSIEKEIENLNGKKEELEEELEELEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 208 QQLREFEETKKQIEEDED--REIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQmKLQ 285
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAqlRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-DVQ 957
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157138 286 GIIRSLEKDIQGLK----REIQERDETiqdkEKRIYDLKKKNQELEKFKFVLDYKIKELKKQ 343
Cdd:TIGR02169 958 AELQRVEEEIRALEpvnmLAIQEYEEV----LKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
64-523 |
3.97e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 64 RVEELKMENEYQLRLKDMNYTEKIKELTDKfiqEMESLKTKNQVLKTEKEKQDIShrERLEELVDKQT---RELQDlecc 140
Cdd:COG5022 919 LIENLEFKTELIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKETS--EEYEDLLKKSTilvREGNK---- 989
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 141 NNQKLLLEYEKYQELQLKSQRMQEEyEKQLRDNDeTKSQALEELTEFY---------EAKLQEKTGLLEEAQEDVRQQLR 211
Cdd:COG5022 990 ANSELKNFKKELAELSKQYGALQES-TKQLKELP-VEVAELQSASKIIssestelsiLKPLQKLKGLLLLENNQLQARYK 1067
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 212 EFEETKKQIEEDEDREIQDIKTKYERK---LRDEKESNLRLKGETGIMR------KKFSSLQKEIEERTNDIELLKSEQM 282
Cdd:COG5022 1068 ALKLRRENSLLDDKQLYQLESTENLLKtinVKDLEVTNRNLVKPANVLQfivaqmIKLNLLQEISKFLSQLVNTLEPVFQ 1147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 283 KLQGiirsLEKDIQGLKREIQERDETIQDKEKRIYdlkkknQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEmE 362
Cdd:COG5022 1148 KLSV----LQLELDGLFWEANLEALPSPPPFAALS------EKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFS-G 1216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 363 AELERFHKQNTQLELNITELLQKLRAT-DQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQR 441
Cdd:COG5022 1217 WPRGDKLKKLISEGWVPTEYSTSLKGFnNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVG 1296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 442 ADMVEIAGLNSdLQQEYARQrehLERNlATLKKKVIKEGELHRTDYVRIMQENVSLIKE-----INELRRELKLTRSQIY 516
Cdd:COG5022 1297 LFNALRTKASS-LRWKSATE---VNYN-SEELDDWCREFEISDVDEELEELIQAVKVLQllkddLNKLDELLDACYSLNP 1371
|
....*..
gi 1907157138 517 DLESALK 523
Cdd:COG5022 1372 AEIQNLK 1378
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-530 |
4.61e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 262 SLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLkkkNQELEKFKfvldYKIKELK 341
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL---EQEEEKLK----ERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 342 KQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRatDQEMRKEQQKERDLEALVRRFKTDLHNCVAYI 421
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 422 QEPGLLKEkirglfekyvqradmveiagLNSDLQQEYARQREHLERNLATLKKKVikegelhrtdyvrimqenVSLIKEI 501
Cdd:TIGR02169 822 NRLTLEKE--------------------YLEKEIQELQEQRIDLKEQIKSIEKEI------------------ENLNGKK 863
|
250 260
....*....|....*....|....*....
gi 1907157138 502 NELRRELKLTRSQIYDLESALKVSKKTRS 530
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERD 892
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
97-527 |
4.64e-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: 40.10 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 97 EMESLKTKNQvlkTEKEKQDISHRERLEELVDKQTRELQDLEccnnqkllleyEKYQELQLKSQRMQEEYEKQLRDNDET 176
Cdd:pfam15921 246 QLEALKSESQ---NKIELLLQQHQDRIEQLISEHEVEITGLT-----------EKASSARSQANSIQSQLEIIQEQARNQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 177 KSQALEELTEfyeaklqektglLEEAQEDVRQQLREfeetKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIM 256
Cdd:pfam15921 312 NSMYMRQLSD------------LESTVSQLRSELRE----AKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 257 RKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQ---------------DKEKRIYDLKK 321
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQrleallkamksecqgQMERQMAAIQG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 322 KNQELEKF----------KFVLDYKIKEL---KKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLra 388
Cdd:pfam15921 456 KNESLEKVssltaqlestKEMLRKVVEELtakKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL-- 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 389 tdQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQepgLLKEKIRGLFEKYVQR-----ADMVEIAGLNSDLQ------QE 457
Cdd:pfam15921 534 --QHLKNEGDHLRNVQTECEALKLQMAEKDKVIE---ILRQQIENMTQLVGQHgrtagAMQVEKAQLEKEINdrrlelQE 608
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907157138 458 YARQREHLERNLATLKKKViKEGELHRTDYVRIMQENVSLIKEI----NELRRELKLTRSQIYDLESALKVSKK 527
Cdd:pfam15921 609 FKILKDKKDAKIRELEARV-SDLELEKVKLVNAGSERLRAVKDIkqerDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
86-407 |
4.96e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 86 KIKELTDKfIQEMESLKTKNQVLKTEKEKQDISHRERLEELvdkqtrelqdleccnnQKLLLEYEKYQELQLKSQRMQEE 165
Cdd:PRK02224 214 ELAELDEE-IERYEEQREQARETRDEADEVLEEHEERREEL----------------ETLEAEIEDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 166 YEKQLRDNDETKSQALEELTEfyeakLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRdEKES 245
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDD-----LLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES-LRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 246 NLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEK----------DIQGLKREIQE-RDETIQDKEK 314
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgNAEDFLEELREeRDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 315 RIYDLKKKNQELEKFKFVLDY-KIKELKKQIE--PRENEIKVMKEQIQEMEAELERFHKQNTQLELNItELLQKLRATDQ 391
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAgKCPECGQPVEgsPHVETIEEDRERVEELEAELEDLEEEVEEVEERL-ERAEDLVEAED 509
|
330
....*....|....*.
gi 1907157138 392 EMRKEQQKERDLEALV 407
Cdd:PRK02224 510 RIERLEERREDLEELI 525
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
72-416 |
5.52e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 72 NEYQLRLKDMNyTEKIKELTDKFIQEMESLKTKNQVLKTE--KEKQDIShreRLEELVDKQTRELQDLECCNNQKLLLEY 149
Cdd:TIGR04523 291 NQLKSEISDLN-NQKEQDWNKELKSELKNQEKKLEEIQNQisQNNKIIS---QLNEQISQLKKELTNSESENSEKQRELE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 150 EKYQELQlKSQRMQEEYEKQLRdNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDED---- 225
Cdd:TIGR04523 367 EKQNEIE-KLKKENQSYKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikd 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 226 --REIQDIKTKYER--KLRDEKESNLR-LKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKR 300
Cdd:TIGR04523 445 ltNQDSVKELIIKNldNTRESLETQLKvLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 301 EIQERDETIQDKEKRIYDLKK---------KNQELEKFKFVLDYKIKELKKQI-------EPRENEIKVMKEQIQEMEAE 364
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQkslkkkqEEKQELIDQKEKEKKDLIKE 604
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907157138 365 LERFHKQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHN 416
Cdd:TIGR04523 605 IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
248-527 |
5.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 248 RLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELE 327
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 328 KFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFhkQNTQLELNITELLQKLRATDQEMRKEQQKERDLEALV 407
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL--EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 408 RRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQRADMVEIAGLNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDY 487
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907157138 488 VRIMQENVSLIKEINELRRELKLTRSQIYDLESALKVSKK 527
Cdd:COG4372 287 ALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
57-580 |
6.79e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 57 IMLELKTRVEELKMENEYQLRLKDMNYTEKIKELTDKFIQEMESLKTKNQVLKTEKEKQDI------SHRERLEELVDKQ 130
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLlyldylKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 131 TRELQDLECCNNQKLLLEYEKYQELQLKSQRMQEEYEKQLRDNDETKSQALEELTEFYEAKLQEKTGLLEEAQEDVRQQL 210
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 211 REFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLqgiiRS 290
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL----KS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 291 LEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHK 370
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 371 QNTQLELNITELLQklratDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKYVQRADMVEIAGL 450
Cdd:pfam02463 482 LQEQLELLLSRQKL-----EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 451 NSDLQQEYARQREHLERNLATLKKKVIKEGELHRTDYVRImQENVSLIKEINELRRELKLTRSQIYDLESALKVSKKTRS 530
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV-LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907157138 531 QEVPESVISKDVVGSTSTMRLNEQEETGRIIEMQRLEIRRLRDQIQEQEQ 580
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
87-416 |
6.87e-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: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 87 IKELTDKFIQEMESLKTKNQVLKT--EKEKQDISHRERLEELVDKQTRELQDLECCNNQKLLLEYEKYQELQLKSQRMQE 164
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASlqEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEK 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 165 EYEKQ-LRDNDETKSQALEELTEFYEAKLQEKTGLlEEAQEDVRQQLREFeetkKQIEEDEDREIQDIktkyERKLRDEK 243
Cdd:pfam15921 561 DKVIEiLRQQIENMTQLVGQHGRTAGAMQVEKAQL-EKEINDRRLELQEF----KILKDKKDAKIREL----EARVSDLE 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 244 ESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEqmklqgiIRSLEKDIQGLKREIQERDETIQDKEKRI-YDLKKK 322
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE-------LNSLSEDYEVLKRNFRNKSEEMETTTNKLkMQLKSA 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 323 NQELEKFKFVLD-------YKIK---ELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQE 392
Cdd:pfam15921 705 QSELEQTRNTLKsmegsdgHAMKvamGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
330 340
....*....|....*....|....
gi 1907157138 393 MRKEQQKERDLEALVRRFKTDLHN 416
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVAN 808
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
26-330 |
7.42e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.34 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 26 DKDGRGIKREREVGFAEEVLVTKTDMEEKAQIMLELktrvEELKMENEYQLrlkdmnytEKIKELTDKfiQEMESLKTKN 105
Cdd:pfam17380 304 EKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQ----ERMAMEREREL--------ERIRQEERK--RELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 106 QVLKTEKekqdISHRERLE-ELVDKQTRELQDLECCNNQKLLLEyekyqELQLKSQRMQEEYEKQLRDNDETKSQALEEL 184
Cdd:pfam17380 370 IAMEISR----MRELERLQmERQQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 185 TEFYEAKLQEKTGLLEEAQEDVRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGIMRKKfSSLQ 264
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKR-KLLE 519
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907157138 265 KEIEERTNDIelLKSEQMKLQGIIRSLEKDIQGlKREIQERDETIQDKEKRIYDLKKKNQELEKFK 330
Cdd:pfam17380 520 KEMEERQKAI--YEEERRREAEEERRKQQEMEE-RRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
146-399 |
7.43e-03 |
|
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: 39.02 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 146 LLEYEKYQELQLKSQRMQEEYEKQLRD------NDETKSQALEELTEFYEAKLQ----EKTGLLEEAQEDVRQQL---RE 212
Cdd:pfam15905 58 SLELKKKSQKNLKESKDQKELEKEIRAlvqergEQDKRLQALEEELEKVEAKLNaavrEKTSLSASVASLEKQLLeltRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 213 FEETKKQIEEDEDREIQDIKTKYERKLRDEKESNLRLKGETGI-MRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSL 291
Cdd:pfam15905 138 NELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEgMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 292 EKDIQGLKREIQERDETIQDKEKRIYD-------LKKKNQELEKFKFVLDYKIKELKKQIEPRENEIKVMKEQIQEMEAE 364
Cdd:pfam15905 218 KSETEKLLEYITELSCVSEQVEKYKLDiaqleelLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE 297
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907157138 365 L-ERFHKQNTQLElnitELLQKLRATDQEMRKEQQK 399
Cdd:pfam15905 298 YeEKEQTLNAELE----ELKEKLTLEEQEHQKLQQK 329
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
206-402 |
7.92e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 206 VRQQLREFEETKKQIEEDEDREIQDIKTKYERKLRDEKEsnlrLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQ 285
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKT----IKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 286 GIIRSLEKDI-------------QGLKREiQERDETIQDK----EKRIYDLKKKNQELEKFKFVLD---YKIKELKKQIE 345
Cdd:PHA02562 269 SKIEQFQKVIkmyekggvcptctQQISEG-PDRITKIKDKlkelQHSLEKLDTAIDELEEIMDEFNeqsKKLLELKNKIS 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907157138 346 PRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELLQKLRATDQEmRKEQQKERD 402
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT-KSELVKEKY 403
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
288-383 |
8.67e-03 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 38.80 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 288 IRSLEKDIQGLKREIQERDETIQDKEKRIYDLKKKNQEL-EKFKFVL------------------------DYKIKELKK 342
Cdd:pfam17060 149 YKSLELRVESMKDELEFKDETIMEKDRELTELTSTISKLkDKYDFLSrefefykqhhehggnnsiktatkhEFIISELKR 228
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907157138 343 QIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELL 383
Cdd:pfam17060 229 KLQEQNRLIRILQEQIQFDPGALHDNGPKNLVLNGAIAAVL 269
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
38-246 |
9.00e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 38 VGFAEEVLVTKTDMEEKAQIMLEL-KTRVEELKMENEYQLRLKDMNYTEKIKELTDKFIQEmesLKTKNQVLKtEKEKQD 116
Cdd:PRK12704 16 VGAVIGYFVRKKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKE---LRERRNELQ-KLEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 117 ISHrerlEELVDKQTRELQDLEccnnqkllleyekyQELQLKsqrmQEEYEKQLRDNDETKSQaLEELTEFYEAKLQEKT 196
Cdd:PRK12704 92 LQK----EENLDRKLELLEKRE--------------EELEKK----EKELEQKQQELEKKEEE-LEELIEEQLQELERIS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907157138 197 GLleeAQEDVRQQLreFEETKKQIEEDEDREIQDIKTKYerKLRDEKESN 246
Cdd:PRK12704 149 GL---TAEEAKEIL--LEKVEEEARHEAAVLIKEIEEEA--KEEADKKAK 191
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-523 |
9.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 168 KQLRDNDETKSQALEELTEFYEA--KLQEKTGLLEEAQEDVRQQLREFEETKKQIE---EDEDREIQDIKTKYER--KLR 240
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKEleELKEEIEELEKELESLEGSKRKLEEKIRELEeriEELKKEIEELEEKVKElkELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 241 DEKESNLRLKGETGIMRKKFSSLQKEIEERTNDIELLKSEQMKLQGIIRSLEKdIQGLKREIQERDETIQDKEKRIYDLK 320
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELEERHELYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 321 KKNQELEKFKFVL-DYKIKELKKQIEPRENEIKVMKEQIQEMEAELERFHKQNTQLELNITELlQKLRATDQEMRKEQQK 399
Cdd:PRK03918 369 AKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-KKAKGKCPVCGRELTE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 400 ERDLEaLVRRFKTDLHNCVAYIQEPGLLKEKIRGLFEKY-VQRADMVEIAGLNSDLQQEYARQREHLERNLATLKKKViK 478
Cdd:PRK03918 448 EHRKE-LLEEYTAELKRIEKELKEIEEKERKLRKELRELeKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKA-E 525
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907157138 479 EGELHRTDYVRIMQENVSL---IKEINELRRELKLTRSQIYDLESALK 523
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLkkeLEKLEELKKKLAELEKKLDELEEELA 573
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
151-590 |
9.87e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 38.95 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 151 KYQELQLKSQRMQEEYE-KQLRDNDETKSQALEELTEFYEAKLQEKTGlleeaqedvRQQLREFEETKKQIEEDEDREIQ 229
Cdd:pfam05557 8 KARLSQLQNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQK---------RIRLLEKREAEAEEALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 230 DIKTKYER---KLRDEKESNLRLKGETgimrkkFSSLQKEIEErtndielLKSEQMKLQGIIRSLEKDIQGLKREIQERD 306
Cdd:pfam05557 79 RLKKKYLEalnKKLNEKESQLADAREV------ISCLKNELSE-------LRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 307 ETIQDKEKRIYDLKKKNQELEkfkfVLDYKIKELKKQIEPRENEIKVMK------EQIQEMEAELERFHKQNTQLELNI- 379
Cdd:pfam05557 146 AKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLREHNKHLNENIe 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 380 -----TELLQKLRATDQEMRKEQQKERDLEALVRRFKTDLHNCVAYIQEPGL---LKEKIRGLFEKYVQR--ADMVEIAG 449
Cdd:pfam05557 222 nklllKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLnlrSPEDLSRRIEQLQQReiVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 450 LNSDLQQEYARQREHLERNLATLKKKVIKEGELHRTD-YVRIMQENVSLI-KEINELRRELKLTRSQIYDLESALKVSKK 527
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKaLVRRLQRRVLLLtKERDGYRAILESYDKELTMSNYSPQLLER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157138 528 TRSQE---------VPESVISKDVVGSTST---------------MRLNEQ-----------EETGRIIEMQRLEIRRLR 572
Cdd:pfam05557 382 IEEAEdmtqkmqahNEEMEAQLSVAEEELGgykqqaqtlerelqaLRQQESladpsyskeevDSLRRKLETLELERQRLR 461
|
490
....*....|....*...
gi 1907157138 573 DQIQEQEQVPGFHTIAGV 590
Cdd:pfam05557 462 EQKNELEMELERRCLQGD 479
|
|
| |
