|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-469 |
2.07e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLtetcDLKTKVAVLEGDLKQQQKSIQ 277
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR----ELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 278 amEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMvRHQESLQAKQRTLLQQLD 357
Cdd:COG1196 334 --ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-RAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 358 CLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELK 437
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
250 260 270
....*....|....*....|....*....|..
gi 755536300 438 ERERLLVAFPDLHQPEEAQIQSPTGGEQAAPV 469
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-440 |
9.92e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 9.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 174 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqrqteEAERtlakCEHDRHQLLT 253
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--------------EVEQ----LEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 254 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE---GERRAAAERQvqqleeqvqllagRLDGASQQIRWASTELDK 330
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqLKEELKALRE-------------ALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 331 EKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQ 410
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270
....*....|....*....|....*....|
gi 755536300 411 EKQDLEQVTTDLQLTISELRQQLEELKERE 440
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRL 931
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-459 |
2.40e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 206 EGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQ 285
Cdd:COG1196 199 ERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 286 LEEEGERRAAAERQVQQLEEQVqllAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREE 365
Cdd:COG1196 279 LELELEEAQAEEYELLAELARL---EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 366 LRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLVA 445
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250
....*....|....
gi 755536300 446 FPDLHQPEEAQIQS 459
Cdd:COG1196 436 EEEEEEEALEEAAE 449
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-493 |
7.66e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 198 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 277
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAEL-----------EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 278 AMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLD 357
Cdd:COG1196 313 ELE---ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 358 CLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELK 437
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755536300 438 ERERLLVAFPDLHQPEEAQIQSPTGGEQAAPVDADQNPRGGPAGRPQDGPAGPALV 493
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-391 |
1.15e-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: 68.16 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 254
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL-----------AEAEAEIEELEAQIEQLKEE 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 255 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLE---EEGERRA-AAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDK 330
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLErriAATERRLeDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755536300 331 EKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-459 |
9.32e-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: 65.08 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 198 LRAQLEDAE-----GQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQ 272
Cdd:TIGR02168 218 LKAELRELElallvLRLEELREELEELQEELKEAEEEL----EELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 273 QKSIQAMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTL 352
Cdd:TIGR02168 294 ANEISRLE---QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 353 LQQLDCLDQEREELRGSLDEAE-------AQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQ-----DLEQVTT 420
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLElqiaslnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELqaeleELEEELE 450
|
250 260 270
....*....|....*....|....*....|....*....
gi 755536300 421 DLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQS 459
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-443 |
6.87e-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: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 277
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAEL------EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 278 AMEAKAQQLEE----EGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLL 353
Cdd:COG1196 292 ELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 354 QQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQL 433
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250
....*....|
gi 755536300 434 EELKERERLL 443
Cdd:COG1196 452 AELEEEEEAL 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-441 |
9.70e-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: 9.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEG---DLKQQQK 274
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLE---ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERsiaEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 275 SIQAMEAKAQ---------------QLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMV 339
Cdd:TIGR02169 319 DAEERLAKLEaeidkllaeieelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 340 RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVT 419
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
250 260
....*....|....*....|..
gi 755536300 420 TDLQLTISELRQQLEELKERER 441
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQAR 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-447 |
9.96e-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: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 198 LRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ 277
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQEL----SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 278 AMEAKAQQLEEEGERRaaaERQVQQLEEQVQLLAGRLDGAS-QQIRWASTELDKEKARVDSMVRHQES------------ 344
Cdd:TIGR02169 755 NVKSELKELEARIEEL---EEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLREIEQklnrltlekeyl 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 345 ------LQAKQRTLLQQLDCLDQEREELRGS-------LDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQE 411
Cdd:TIGR02169 832 ekeiqeLQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270
....*....|....*....|....*....|....*.
gi 755536300 412 KQDLEQVTTDLQLTISELRQQLEELKERERLLVAFP 447
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
175-391 |
1.63e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTE 254
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 255 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAR 334
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755536300 335 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-439 |
2.10e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 257 DLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVD 336
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-----------------ELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 337 SMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLE 416
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180
....*....|....*....|...
gi 755536300 417 QVTTDLQLTISELRQQLEELKER 439
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQ 846
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-439 |
3.17e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 176 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEE---AERTLAKCEHDRHQLL 252
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 253 TETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEegerraaaerqvqqleeqvqllagRLDGASQQIRWASTELDKEK 332
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEA------------------------QIEQLKEELKALREALDELR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 333 ARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQ----LQAQQELLQSL 408
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESElealLNERASLEEAL 889
|
250 260 270
....*....|....*....|....*....|....
gi 755536300 409 QQEKQDLEQVTTDLQ---LTISELRQQLEELKER 439
Cdd:TIGR02168 890 ALLRSELEELSEELReleSKRSELRRELEELREK 923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
174-391 |
4.90e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 174 AAEQSKDLTR-LNKHVGALTQL---VGPLRAQLEDAEGQKDGLRKQVSKLE---QALQQEQGQRQRQTEEAERTLAKCEH 246
Cdd:TIGR02168 251 AEEELEELTAeLQELEEKLEELrleVSELEEEIEELQKELYALANEISRLEqqkQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 247 DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE-EGERRAAAERQvqqleeqvqllAGRLDGASQQIRWAS 325
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrLEELEEQLETL-----------RSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755536300 326 TELDKEKARVDSMVRHQESLQAKQRTLLQ------------QLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKkleeaelkelqaELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
200-441 |
1.12e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 200 AQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAM 279
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKEL-----------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 280 EAKAQQLEEEGERRAAAerqvqqleeqvqlLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCL 359
Cdd:COG4942 89 EKEIAELRAELEAQKEE-------------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 360 DQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 439
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
..
gi 755536300 440 ER 441
Cdd:COG4942 236 AA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
261-441 |
5.61e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 261 KVAVLEGDLKQQQKSIQAMEAKAQQLEEEgeRRAAAERQVQqleeqvqllAGRLDGAS-QQIRWAST-----ELDKEKAR 334
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAE--LDALQERREA---------LQRLAEYSwDEIDVASAereiaELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 335 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 414
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
170 180
....*....|....*....|....*..
gi 755536300 415 LEQVTTDLQLTISELRQQLEELKERER 441
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAE 786
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-391 |
1.40e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 198 LRAQLEDAegqkdglRKQVSKLEQAlqqeqGQRQRQTEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQ 277
Cdd:COG4913 240 AHEALEDA-------REQIELLEPI-----RELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 278 AMEAKAQQLEEegERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQ 346
Cdd:COG4913 306 RLEAELERLEA--RLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFA 383
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755536300 347 AKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
200-442 |
3.93e-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: 53.52 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 200 AQLEDA----EGQKDGLRKQVSKLEQALQQeqgqrqrqtEEAERtlakcEHDRHQLLTETCDLKTKVAVLEGDLKQQQKS 275
Cdd:TIGR02168 189 DRLEDIlnelERQLKSLERQAEKAERYKEL---------KAELR-----ELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 276 IQAMEAKAQQLEEEGERRAAAErqvqqleeqvqllaGRLDGASQQIRWASTELDKEKARVDSMVRHQeslQAKQRTLLQQ 355
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEV--------------SELEEEIEELQKELYALANEISRLEQQKQIL---RERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 356 LDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEE 435
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
....*...
gi 755536300 436 L-KERERL 442
Cdd:TIGR02168 398 LnNEIERL 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
269-454 |
1.62e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 269 LKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARvdsmvRHQESLQAK 348
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-----AELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 349 QRTLLQQLdcldQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQslqqekQDLEQVTTDLQLTISE 428
Cdd:COG4717 148 LEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL------EELQQRLAELEEELEE 217
|
170 180
....*....|....*....|....*.
gi 755536300 429 LRQQLEELKERERLLVAFPDLHQPEE 454
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEE 243
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
202-445 |
1.39e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.03 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 202 LEDAEGQKDGLRKQVSKLEQALQ--QEQGQRQRQTEEAERTLAKCE----HDRHQLLTETcDLKTKVAVLEGDLKQQQKS 275
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAeyTKSIDIKKATESLEEQLAAAEaeqeLEESKRETET-GIQNLTAEIEQGQESLTEN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 276 IQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllagrLDGASQQIRwaSTELDKEKARVDSMVRHQESLQAKQRTLLQQ 355
Cdd:COG5185 356 LEAIKEEIENIVGEVELSKSSEE---------------LDSFKDTIE--STKESLDEIPQNQRGYAQEILATLEDTLKAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 356 ldclDQEREELRGSLDEAEAQRSELEEQLQSLQS--DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQL 433
Cdd:COG5185 419 ----DRQIEELQRQIEQATSSNEEVSKLLNELISelNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRV 494
|
250
....*....|..
gi 755536300 434 EELKERERLLVA 445
Cdd:COG5185 495 STLKATLEKLRA 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-390 |
1.86e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 199 RAQLEDAEGQKDGLRKQVSKLEQALQQEqgqrqrqtEEAERTLAKcEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 278
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEAL--------EAELDALQE-RREALQRLAEYSWDEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 279 MEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVR-----HQESLQAKQRTLL 353
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarleLRALLEERFAAAL 759
|
170 180 190
....*....|....*....|....*....|....*..
gi 755536300 354 QQlDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 390
Cdd:COG4913 760 GD-AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
174-386 |
2.32e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 174 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAER---TLAKCEHDRHQ 250
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEareEVAELNSKLAE 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 251 lLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEE-EGERRAA-AERQVQQLEEQVQLLAGRLDGASQQIRWASTEL 328
Cdd:PRK02224 584 -LKERIESLERIRTLLAAIADAEDEIERLREKREALAElNDERRERlAEKRERKRELEAEFDEARIEEAREDKERAEEYL 662
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755536300 329 DKEKARVDSMVRHQESLQAK---QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEqLQS 386
Cdd:PRK02224 663 EQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEALEALYDEAEE-LES 722
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
175-389 |
4.19e-05 |
|
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: 46.97 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 175 AEQSKDLTRLNKHVGALTQLVGPLRAQ-------LEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTL---AKC 244
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRiaaterrLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASL 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 245 EHDRHQLLTETCDLKTKVAVLEgdlKQQQKSIQAMEAKAQQLEEEGERRAAAErqvqqleeqvqllaGRLDGASQQIR-W 323
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELE---SKRSELRRELEELREKLAQLELRLEGLE--------------VRIDNLQERLSeE 948
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755536300 324 ASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLD-------QEREELRGSLDEAEAQRSELEEQLQSLQS 389
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
257-477 |
4.43e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 257 DLKTKVAVLEGDLKQQQKSIQAMEakaQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVd 336
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLE---EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 337 smvrhqESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQ---SDREQEQCQLQAQQELLQSLQQEKQ 413
Cdd:COG4372 118 ------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQeelAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536300 414 DLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQIQSPTGGEQAAPVDADQNPRG 477
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
200-439 |
4.75e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 200 AQLEDAEGQKDGLRKQVSKLEQAlqqeqGQRQRQTEEAERTLAKCEHDRHQLLTETcdLKTKVAVLEGDLKQQQKSIQAM 279
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPI-----RELAERYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 280 EAKAQQLEEEgeRRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRH-----------QESLQAK 348
Cdd:COG4913 308 EAELERLEAR--LDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglplpasAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 349 QRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQslqsdreqeqcqlqaqqellqslqqekqDLEQVTTDLQLTISE 428
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELR----------------------------ELEAEIASLERRKSN 437
|
250
....*....|.
gi 755536300 429 LRQQLEELKER 439
Cdd:COG4913 438 IPARLLALRDA 448
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
175-382 |
5.08e-05 |
|
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: 46.60 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 175 AEQSKDLTRLNKHVGALT---QLvgPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEH----- 246
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGeeeQL--RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerei 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 247 -----DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE----GERRAAAERQVQQLEEQVQLLAGRLDGA 317
Cdd:TIGR02169 346 eeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklKREINELKRELDRLQEELQRLSEELADL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755536300 318 SQQI---RWASTELDKEKARVDSMVRHQE-----------SLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEE 382
Cdd:TIGR02169 426 NAAIagiEAKINELEEEKEDKALEIKKQEwkleqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-373 |
7.27e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 167 AATVGHWAAEQSKDLtrlnkhvgaLTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEH 246
Cdd:COG4913 278 RAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERLEARLDALREEL-----------DELEAQIRGNGG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 247 DRHQlltetcDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQleeqvqllAGRLDGASQQIRWA 324
Cdd:COG4913 338 DRLE------QLEREIERLERELEERERRRARLEALLAALGLPlpASAEEFAALRAEA--------AALLEALEEELEAL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 755536300 325 STELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEA 373
Cdd:COG4913 404 EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
199-442 |
9.77e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 199 RAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAErTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQA 278
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERL-----------ERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 279 MEAKAQQLEEEGE--RRAAAErqvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDSMVrhqESLqAKQRTLLQQL 356
Cdd:PRK02224 542 LRERAAELEAEAEekREAAAE----------------AEEEAEEAREEVAELNSKLAELKERI---ESL-ERIRTLLAAI 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 357 DCLDQEREEL---RGSLDEAEAQRSE-LEE------QLQS-LQSDREQEQCQLQAQQELLQSLQQEK-QDLEQVTTDLQL 424
Cdd:PRK02224 602 ADAEDEIERLrekREALAELNDERRErLAEkrerkrELEAeFDEARIEEAREDKERAEEYLEQVEEKlDELREERDDLQA 681
|
250
....*....|....*....
gi 755536300 425 TISELRQQLEELKE-RERL 442
Cdd:PRK02224 682 EIGAVENELEELEElRERR 700
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
272-440 |
9.90e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 272 QQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRT 351
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 352 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQ 431
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI-------AELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
....*....
gi 755536300 432 QLEELKERE 440
Cdd:COG4372 172 ELQALSEAE 180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
215-389 |
1.10e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 215 QVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGdlkQQQKSIQAMEAKAQQLEEEGERRA 294
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ---AKQDSEHKRKKLEGQLQELQARLS 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 295 AAERQVQQLEEQVQLLAGRLDGASQQIRWA---STELDKEKARVDSMVRH-QESLQAKQRTLLQ---QLDCLDQEREELR 367
Cdd:pfam01576 423 ESERQRAELAEKLSKLQSELESVSSLLNEAegkNIKLSKDVSSLESQLQDtQELLQEETRQKLNlstRLRQLEDERNSLQ 502
|
170 180
....*....|....*....|..
gi 755536300 368 GSLDEAEAQRSELEEQLQSLQS 389
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQA 524
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
175-456 |
1.12e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRqrqtEEAERTLA--KC-------E 245
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV----EEAEALLEagKCpecgqpvE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 246 HDRHQLLTETCDlkTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQiRWAS 325
Cdd:PRK02224 463 GSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEK-RERA 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 326 TELDKEKARVDSMVRHQESLQAKQRtllqqldcldQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELL 405
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAE----------EEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE 609
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755536300 406 QSLQQEKQDLEQVTtdlqltisELRQQLEELKERERLLVAFPDLHQPEEAQ 456
Cdd:PRK02224 610 RLREKREALAELND--------ERRERLAEKRERKRELEAEFDEARIEEAR 652
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
180-451 |
1.52e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 180 DLTRLNKHvgalTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQL------LT 253
Cdd:TIGR00618 171 NLFPLDQY----TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTqqshayLT 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 254 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqlEEQVQLLAGRLDGASQQIRWASTELDKEKA 333
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 334 RVDSMVRHQESLQAKQRTLLQQ---LDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDReqeqcqlqaqqellqslqQ 410
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQrrlLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH------------------T 383
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755536300 411 EKQDLEQVTTDLQLTISELRQQLEELKERERLLVAFPDLHQ 451
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQG 424
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
191-389 |
1.76e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 191 LTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqRQTE-EAERTLA-KCEHDRHQLLTETCDLKTKVAVLEGD 268
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQ----------LTTElAAERSTSqKSESARQQLERQNKELKAKLQEMEGT 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 269 LKQQQK-SIQAMEAKAQQLEE----EGERRAAAERQvqqleeqvqllagrLDGASQQIRWASTELDKEKARVDSMVRHQE 343
Cdd:pfam01576 961 VKSKFKsSIAALEAKIAQLEEqleqESRERQAANKL--------------VRRTEKKLKEVLLQVEDERRHADQYKDQAE 1026
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 755536300 344 SLQAKQRTLLQQLDCLDQE-------REELRGSLDEAEAQRSELEEQLQSLQS 389
Cdd:pfam01576 1027 KGNSRMKQLKRQLEEAEEEasranaaRRKLQRELDDATESNESMNREVSTLKS 1079
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
273-441 |
2.03e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 273 QKSIQAMEAKAQQLEEEGERRAAAERQVQQLEeqvqllagrldgASQQIRWASTELDKE-KARVDSMVRHQESLQAKQRT 351
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLE------------AKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 352 LLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSdreqeqcqlqaqqellqSLQQEKQDLEQVTtdlQLTISELRQ 431
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE-----------------LIEEQLQELERIS---GLTAEEAKE 157
|
170
....*....|.
gi 755536300 432 Q-LEELKERER 441
Cdd:PRK12704 158 IlLEKVEEEAR 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
205-557 |
2.19e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 205 AEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQ 284
Cdd:COG3883 14 ADPQIQAKQKELSELQAEL-----------EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 285 QLEEEGERRAAAERQVQQLEEQVQLLAGrldgaSQQIrwaSTELDKEKArVDSMVRHQESLQAKQRTLLQQLDcldQERE 364
Cdd:COG3883 83 ERREELGERARALYRSGGSVSYLDVLLG-----SESF---SDFLDRLSA-LSKIADADADLLEELKADKAELE---AKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 365 ELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLLV 444
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 445 AFPDLHQPEEAQIQSPTGGEQAAPVDADQNPRGGPAGRPQDGPAGPALVPSLQGHPGSNPSSPGPECILRVDRQTAVSWQ 524
Cdd:COG3883 231 AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGA 310
|
330 340 350
....*....|....*....|....*....|...
gi 755536300 525 QDKQHRQDPSWRAPYIPVSAARRLAQQVLFGGW 557
Cdd:COG3883 311 GGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGG 343
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
287-439 |
2.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 287 EEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREEL 366
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755536300 367 RGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 439
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
100-442 |
2.82e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 100 TSEKTKSVYSQTVETALVPCDACTSVQGSLWEVGKVVIslcQSQNlpSSLGQFQKLVKDSlglkplpaATVGHWAAEQSK 179
Cdd:pfam05483 167 SAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRV---QAEN--ARLEMHFKLKEDH--------EKIQHLEEEYKK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 180 DLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqrQTEEAERTLAKCEHDRHQLLTETCDLK 259
Cdd:pfam05483 234 EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE-----------KTKLQDENLKELIEKKDHLTKELEDIK 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 260 TKV-------AVLEGDLKQQQKSI-QAMEAKAQQLEEEGERRAAA-------ERQVQQLEEQVQLLAGRLDGASQQIRWA 324
Cdd:pfam05483 303 MSLqrsmstqKALEEDLQIATKTIcQLTEEKEAQMEELNKAKAAHsfvvtefEATTCSLEELLRTEQQRLEKNEDQLKII 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 325 STELDKEKARVDSMVRhqesLQAKQRTLLQQLDCLDQEREELrgsLDEAEaQRSELEEQLQSLQSDreqeqcqlqaQQEL 404
Cdd:pfam05483 383 TMELQKKSSELEEMTK----FKNNKEVELEELKKILAEDEKL---LDEKK-QFEKIAEELKGKEQE----------LIFL 444
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 755536300 405 LQSLQQEKQDLEQVTTDLQLTISELRQQLEELK---ERERL 442
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKtelEKEKL 485
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
183-439 |
3.37e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 183 RLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQA---LQQEQGQRQRQTEEAERTLAKCEHDRHQLLTETCDLK 259
Cdd:pfam01576 149 KLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 260 TKVAVLEGDLKQQQKSIQAMEAKaqqLEEEGERRAAAERQVQQLEEQVQLLAGRLDG-------ASQQIRWASTELDKEK 332
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKIRELEAQISELQEDLESeraarnkAEKQRRDLGEELEALK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 333 ARV----DSMVRHQEsLQAKQRTLLQQLD-CLDQER------------------EELRGSLDEAEAQRSELEEQLQSLQS 389
Cdd:pfam01576 306 TELedtlDTTAAQQE-LRSKREQEVTELKkALEEETrsheaqlqemrqkhtqalEELTEQLEQAKRNKANLEKAKQALES 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755536300 390 DREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKER 439
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEK 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
181-388 |
4.07e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 181 LTRLNKHVGALTQLVGPLRAQLEDAE------------GQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDR 248
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEarlshsripeiqAELSKLEEEVSRIEARL-----------REIEQKLNRLTLEK 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 249 HQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDgasQQIRWASTEL 328
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE---AQLRELERKI 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 329 DKEKARVDSMVRHQESLQAKQRTLLQQLDCLD-----------------------------------------QEREELR 367
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledvqaelqrveeeiralepvnmlaiQEYEEVL 985
|
250 260
....*....|....*....|.
gi 755536300 368 GSLDEAEAQRSELEEQLQSLQ 388
Cdd:TIGR02169 986 KRLDELKEKRAKLEEERKAIL 1006
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
153-388 |
5.03e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 153 QKLVKDSlGLKPLPAATVGHWAAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqr 232
Cdd:COG4717 56 DELFKPQ-GRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 233 qteeaertlakcehDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERqvqqleeqvqllag 312
Cdd:COG4717 126 --------------QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE-------------- 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755536300 313 RLDGASQQIRWAsteldkEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLD--EAEAQRSELEEQLQSLQ 388
Cdd:COG4717 178 ELEELLEQLSLA------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEAR 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-445 |
5.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 268 DLKQQQKSIQAMEAKAQQLEEEGERRAAAERQvqqleeqvqllagrldgasqqirwasteldKEKARVDSMVRHQESLQA 347
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERLAELEYL------------------------------RAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 348 KQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEK-QDLEQVTTDLQLTI 426
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRrARLEALLAALGLPL 375
|
170
....*....|....*....
gi 755536300 427 SELRQQLEELKERERLLVA 445
Cdd:COG4913 376 PASAEEFAALRAEAAALLE 394
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
337-443 |
1.02e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 337 SMVR-HQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQR-SELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQD 414
Cdd:COG0542 400 ARVRmEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEE 479
|
90 100
....*....|....*....|....*....
gi 755536300 415 LEQVTTDLQLTISELRQQLEELKERERLL 443
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
241-446 |
1.05e-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: 41.06 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 241 LAKCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAaerqvqqleeqvqllagRLDGASQQ 320
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-----------------RIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 321 IRWASTEldKEkarVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLqsdreqeqcqlqa 400
Cdd:COG1579 82 LGNVRNN--KE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK------------- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 755536300 401 qqellqslqqeKQDLEQVTTDLQLTISELRQQLEELKER--ERLLVAF 446
Cdd:COG1579 144 -----------KAELDEELAELEAELEELEAEREELAAKipPELLALY 180
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
174-454 |
1.10e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 174 AAEQSKDL-TRLNkhvgALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQT------EEAERTLAKCEH 246
Cdd:PRK02224 197 EEKEEKDLhERLN----GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleaeiEDLRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 247 DRHQLLTETCDLKTKVAVLEGDLKQQQKSIQ----AMEAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIR 322
Cdd:PRK02224 273 EREELAEEVRDLRERLEELEEERDDLLAEAGlddaDAEAVEARREELEDRDEELRD--------------RLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 323 WASTELDKEKARVDSMVRHQESLQAKQRTLlqqldclDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQ 402
Cdd:PRK02224 339 AHNEEAESLREDADDLEERAEELREEAAEL-------ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 755536300 403 ELLQSLQQEKQDLEQVTTDLQLTISELRQQLEelkERERLLVA--FPDLHQPEE 454
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVE---EAEALLEAgkCPECGQPVE 462
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-391 |
1.22e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 200 AQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQtEEAERTLAKCEHDRHQLltetcDLKTKVAVLEGDLKQQQKSIQAM 279
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 280 EAKAQQLEEEGERRAAAERqvqqleeqvqllagRLDGASQQIRWASTELDKEKARVDSMVRHQ-ESLQAKQRTLLQQLDC 358
Cdd:COG4717 145 PERLEELEERLEELRELEE--------------ELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAE 210
|
170 180 190
....*....|....*....|....*....|...
gi 755536300 359 LDQEREELRgslDEAEAQRSELEEQLQSLQSDR 391
Cdd:COG4717 211 LEEELEEAQ---EELEELEEELEQLENELEAAA 240
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
175-443 |
1.27e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKD----GLRKQVSKLEQaLQQEQGQRQRQTEEAERTLAkcehDRHQ 250
Cdd:pfam05483 345 AAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEE-MTKFKNNKEVELEELKKILA----EDEK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 251 LLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVqqleeqvqllagrldgaSQQIRWASTELDK 330
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY-----------------LKEVEDLKTELEK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 331 EKAR---------------------VDSMV----RHQESL---QAKQRTLLQQLDCLDQEREELRgslDEAEAQRSELEE 382
Cdd:pfam05483 483 EKLKnieltahcdklllenkeltqeASDMTlelkKHQEDIincKKQEERMLKQIENLEEKEMNLR---DELESVREEFIQ 559
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755536300 383 QLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEELKERERLL 443
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
136-390 |
1.34e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 136 VISLCQSQNLPSSLGQFQK-LVKDSLGLKPLPAAT-VGHWAAEQSKDLT--------RLNKHVGALTQLVGPLRAQLEDA 205
Cdd:TIGR00606 628 LFDVCGSQDEESDLERLKEeIEKSSKQRAMLAGATaVYSQFITQLTDENqsccpvcqRVFQTEAELQEFISDLQSKLRLA 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 206 EGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTetcdLKTKVAVLEGDLKQQQKSIQAMEAKA-- 283
Cdd:TIGR00606 708 PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK----VNRDIQRLKNDIEEQETLLGTIMPEEes 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 284 -----------QQLEEEGErraaaERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTL 352
Cdd:TIGR00606 784 akvcltdvtimERFQMELK-----DVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
250 260 270
....*....|....*....|....*....|....*...
gi 755536300 353 LQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 390
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
198-471 |
1.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 198 LRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLA--KCEHDRHQLLTETCDLKTKVAVLEGDLKQQQKS 275
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL-----------EEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 276 IQAMEAKAQQLEEEGERRAAAerqvqqleEQVQLLAGRLDGASQQIRWASTELDKEKARVDSmvRHQE--SLQAKQRTLL 353
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDA--------LPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHPDviALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 354 QQLdcldqeREELRGSLDEAEAQRSELEEQLQSLQsdreqeqcqlqaqqellqslqqekQDLEQVTTDLQlTISELRQQL 433
Cdd:COG3206 305 AQL------QQEAQRILASLEAELEALQAREASLQ------------------------AQLAQLEARLA-ELPELEAEL 353
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755536300 434 EELKER----ERLLVAFpdLHQPEEAQIQSPTGGEQAAPVDA 471
Cdd:COG3206 354 RRLEREvevaRELYESL--LQRLEEARLAEALTVGNVRVIDP 393
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
174-390 |
1.42e-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: 42.08 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 174 AAEQSKDLTRLNKHvgaltqlvgpLRAQLEDAEGQKDGLRKQVSKLEQ---ALQQEQGQRQRQTEEAERTLAKCEHDRHQ 250
Cdd:pfam01576 648 ALEAKEELERTNKQ----------LRAEMEDLVSSKDDVGKNVHELERskrALEQQVEEMKTQLEELEDELQATEDAKLR 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 251 LLTETCDLKTKvavLEGDL-----------KQQQKSIQAMEAkaqQLEEEGERRAAAerqvqqleeqvqlLAGRldgasq 319
Cdd:pfam01576 718 LEVNMQALKAQ---FERDLqardeqgeekrRQLVKQVRELEA---ELEDERKQRAQA-------------VAAK------ 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755536300 320 qiRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSD 390
Cdd:pfam01576 773 --KKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAE 841
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
316-391 |
1.78e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536300 316 GASQQIRWASTELDKEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-388 |
2.44e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 174 AAEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLT 253
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-----------AALARRIRALEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 254 ETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEG--------------------------ERRAAAE---RQVQQLE 304
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPplalllspedfldavrrlqylkylapARREQAEelrADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 305 EQVQllagRLDGASQQIRWASTELDKEKARVdsmvrhqESLQAKQRTLLQQldcLDQEREELRGSLDEAEAQRSELEEQL 384
Cdd:COG4942 164 ALRA----ELEAERAELEALLAELEEERAAL-------EALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALI 229
|
....
gi 755536300 385 QSLQ 388
Cdd:COG4942 230 ARLE 233
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
248-387 |
2.79e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.39 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 248 RHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAA--AErqvqqleeqvqllagrldgASQQIRWAS 325
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYERELVlhAE-------------------DIKALQALR 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536300 326 TELDKEKARVDSMV----RHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSL 387
Cdd:pfam07926 64 EELNELKAEIAELKaeaeSAKAELEESEESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLESL 129
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
175-443 |
3.12e-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: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALqqeqgqrqrqtEEAERTLAKCEHDRHQLLTE 254
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL-----------EEKQNEIEKLKKENQSYKQE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 255 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGErraaaerqvQQLEEQVQLLAGRLDGASQQIRWASTELDKEKAr 334
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELI- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 335 VDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQlqslqsdreqeqcqlqaqqellqslqqeKQD 414
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----------------------------KKE 507
|
250 260
....*....|....*....|....*....
gi 755536300 415 LEQvttdlqlTISELRQQLEELKERERLL 443
Cdd:TIGR04523 508 LEE-------KVKDLTKKISSLKEKIEKL 529
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-454 |
3.36e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 193 QLVGPLRAQLEDAEGQKDGLRKQVSKLEQAlqqeqGQRQRQTEEAERtLAKCEHDR---HQLLTETCDLKTKVAVLEGDL 269
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRA-----RKAAPLAAHIKA-VTQIEQQAqriHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 270 KQQQKSIQAMEAKAQQLEEEGER-RAAAERQvqqleeqvqllAGRLDGASQQIrwasteldkekarvdSMVRHQESLQAK 348
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEIHiRDAHEVA-----------TSIREISCQQH---------------TLTQHIHTLQQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 349 QRTLLQQLDCLDQEREELRgsldeaeAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLTISE 428
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQ-------REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
250 260
....*....|....*....|....*.
gi 755536300 429 LRQQLEELKERERLLVAFPDLHQPEE 454
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQET 486
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
313-448 |
3.50e-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: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 313 RLDGASQQIRWASTELD---KEKARVDSMVRHQESLQAKQRTLLQQ------LDCLDQEREELRGSLDEAEAQRSELEEQ 383
Cdd:COG1579 39 ELAALEARLEAAKTELEdleKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeYEALQKEIESLKRRISDLEDEILELMER 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755536300 384 LQSLQSDReqeqcqlqaqQELLQSLQQEKQDLEQVTTDLQLTISELRQQLEEL-KERERLLVAFPD 448
Cdd:COG1579 119 IEELEEEL----------AELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPP 174
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
311-388 |
4.10e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 4.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755536300 311 AGRLdGASQQ-IRWASTELDKEKARVDSMVrhqESLQAKQRTllqqldcLDQEREELRGSLDEAEAQRSELEEQLQSLQ 388
Cdd:PRK00409 494 AKRL-GLPENiIEEAKKLIGEDKEKLNELI---ASLEELERE-------LEQKAEEAEALLKEAEKLKEELEEKKEKLQ 561
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
319-438 |
4.31e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 319 QQIRWASTELDKEKARVDS-MVRHQESL-QAKQR-TLLQQL---------DCLDQEREELRGSLDEA-EAQR-------- 377
Cdd:COG3096 839 AALRQRRSELERELAQHRAqEQQLRQQLdQLKEQlQLLNKLlpqanlladETLADRLEELREELDAAqEAQAfiqqhgka 918
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755536300 378 -SELEEQLQSLQSDreqeqcqlqaqqelLQSLQQEKQDLEQVTTDLQltisELRQQLEELKE 438
Cdd:COG3096 919 lAQLEPLVAVLQSD--------------PEQFEQLQADYLQAKEQQR----RLKQQIFALSE 962
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
179-431 |
4.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 179 KDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEE---AERTLAKCEHDRHQLLTET 255
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEElesLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 256 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWASTELDKEKARV 335
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 336 DSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDREQEQCQLQAQQELLQSLQQEKQDL 415
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250
....*....|....*.
gi 755536300 416 EQVTTDLQLTISELRQ 431
Cdd:COG4372 285 LEALEEAALELKLLAL 300
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
179-439 |
5.02e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 179 KDLTRLNKHVGALTqlVGPLRAQLEDAEGQKDGLRKQVSKLEQ---ALQQEQGQRQRQTEEAERTLAKC--------EHD 247
Cdd:PRK03918 372 EELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITArigELKKEIKELKKAIEELKKAKGKCpvcgreltEEH 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 248 RHQLLTE-TCDLKTkvavLEGDLKQQQKSIQAMEAKAQQLEEE--GERRAAAERQVQQLEEQVQLLAGRLDGASQQIRWA 324
Cdd:PRK03918 450 RKELLEEyTAELKR----IEKELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 325 STELDKEKA--------RVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDE-AEAQRSELEEQLQSLQS---DRE 392
Cdd:PRK03918 526 EYEKLKEKLiklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElGFESVEELEERLKELEPfynEYL 605
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755536300 393 QEQCQLQAQQELLQSLQQEKQDLEQVTTDLQLT---ISELRQQLEELKER 439
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAETekrLEELRKELEELEKK 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
175-374 |
5.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 175 AEQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQalqqeqgqrqrqTEEAERTLAKCEHDRHQLLTE 254
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEFYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 255 TCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQL--LAGRLDGASQQIRWASTELDKEK 332
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeEAKAKKEELERLKKRLTGLTPEK 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755536300 333 --ARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAE 374
Cdd:PRK03918 389 leKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
312-441 |
5.21e-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: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 312 GRLDGASQQIRWASTELDKEKARVDSMVRHQESLQAkqrtllqQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:TIGR02169 653 GAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR-------ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755536300 392 EQEQCQLQAQQELLQSLQ--------------QEKQDLEQVTTDLQLTISELRQQLEELKERER 441
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEedlssleqeienvkSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-456 |
6.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 330 KEKARVDSMVRHQESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQsLQSDREQEQCQLQAQQELLQSLQ 409
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 755536300 410 QEKQDLEQVTtDLQLTISELRQQLEELKERERLLVAFPDLHQPEEAQ 456
Cdd:COG4717 150 ELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
176-289 |
6.91e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 176 EQSKDLTRLNKHVGALTQLVGPLRAQLEDAEGQKDGLRKQVSKLEQALQQEQGQRQRQTEEAERTLAKCEHDRHQLLTET 255
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
90 100 110
....*....|....*....|....*....|....
gi 755536300 256 CDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEE 289
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
418-521 |
7.22e-03 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 39.42 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 418 VTTDLQLTISELRQQLEELKERERLLVAFPdlhQPEEAQIQ------SPTGGEQAAPVDADQNPRGGPAGRPQDGPAGPA 491
Cdd:PRK13729 70 ATTEMQVTAAQMQKQYEEIRRELDVLNKQR---GDDQRRIEklgqdnAALAEQVKALGANPVTATGEPVPQMPASPPGPE 146
|
90 100 110
....*....|....*....|....*....|
gi 755536300 492 LVPSlqghPGSNPSSPGPECILRVDRQTAV 521
Cdd:PRK13729 147 GEPQ----PGNTPVSFPPQGSVAVPPPTAF 172
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
343-391 |
7.66e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 35.70 E-value: 7.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755536300 343 ESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDR 391
Cdd:pfam06005 7 EQLETKIQAAVDTIALLQMENEELKEENEELKEEANELEEENQQLKQER 55
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
343-458 |
9.04e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 37.96 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 343 ESLQAKQRTLLQQLDCLDQEREELRGSLDEAEAQRSELEEQLQSLQSDreqeqcqlqaqqellqslqqeKQDLEQVT--- 419
Cdd:pfam13851 36 AELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKD---------------------KQSLKNLKarl 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 755536300 420 TDLQLTISELRQQLEELKER-ERLLVAFPDLHQPEEAQIQ 458
Cdd:pfam13851 95 KVLEKELKDLKWEHEVLEQRfEKVERERDELYDKFEAAIQ 134
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
248-387 |
9.53e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 37.63 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 248 RHQLLTETCDLKTKVAVLEGDLKQQQKSIQAMEAKAQQLEEEGERRAAAERQVQQLEEQVQLLAGRLDGASqqirwastE 327
Cdd:PRK07352 52 REAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIEKQAIEDMARLKQTAAA--------D 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755536300 328 LDKEKARVDSMVRHQESLQAkqrtllqqldcLDQEREELRGSLDEAeAQRSELEEQLQSL 387
Cdd:PRK07352 124 LSAEQERVIAQLRREAAELA-----------IAKAESQLPGRLDED-AQQRLIDRSIANL 171
|
|
| |
