|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
245-514 |
5.46e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 245 TEEEASKLTALRLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLsilkEAHQDELGRMSE 324
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL----EEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 325 DLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDcDL 404
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA-EL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 405 RASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKL 484
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270
....*....|....*....|....*....|
gi 226495417 485 QRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 514
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
231-514 |
3.23e-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: 72.78 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 231 RQERSRLpWEDTAATEEEASKLTALRLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSI 310
Cdd:TIGR02168 676 RREIEEL-EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 311 LKEAHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAewgrrerLETEKLGLERENKKLRAQVGDLEEALA 390
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-------LREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 391 RRRRQTASALDcDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQA 470
Cdd:TIGR02168 828 SLERRIAATER-RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 226495417 471 EDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 514
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
316-509 |
1.37e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 70.59 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 316 QDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQ 395
Cdd:pfam01576 888 EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 396 TASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELD 475
Cdd:pfam01576 968 SIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAS 1047
|
170 180 190
....*....|....*....|....*....|....
gi 226495417 476 EAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRL 509
Cdd:pfam01576 1048 RANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-516 |
5.07e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 276 LSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQD---ELGRMSEDLEDELGARSSMDRKMAELRGEMERLQA 352
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 353 ENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQtasaldcdLRASQAALFEKNKELADLKHVHGKLKKQF 432
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA--------LDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 433 QEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQ 512
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
....
gi 226495417 513 QQNA 516
Cdd:TIGR02168 914 RREL 917
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
247-544 |
1.80e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 247 EEASKLTALRLRLDESQKVLLKEREDKLalSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGRMSEDL 326
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 327 EDElgarssmdrkmAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDcDLRA 406
Cdd:COG1196 288 AEE-----------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE-ELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 407 SQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQR 486
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 226495417 487 SLDEQTEQSENLQVQLEHLQSRLRRQQQnaplfgKIRSARFGTEEAEDGTSDLDEDED 544
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLE------LLAELLEEAALLEAALAELLEELA 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-510 |
4.90e-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: 65.85 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 246 EEEASKLTALRLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLsilkEAHQDELGRMSED 325
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI----EELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 326 LEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDcDLR 405
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES-RLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 406 ASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQ------------HEAEVKKLRLRVEELKKELAQAEDE 473
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERlqqeieellkklEEAELKELQAELEELEEELEELQEE 455
|
250 260 270
....*....|....*....|....*....|....*..
gi 226495417 474 LDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLR 510
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
267-515 |
1.14e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 267 LKEREDKLALSRNIEKLEGELSQWKikyEELSKTKQEMLKQLSILKEAHQdELGRMSEDLEDELGARSSMDRKMAELRGE 346
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRLDELSQELSDASR-KIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 347 MERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRR----RQTASALDCDLRASQAALFEKNKELADLK 422
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 423 HVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDEL--------------DEAHNQARKLQRSL 488
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrdlesrlgdlkkerDELEAQLRELERKI 905
|
250 260
....*....|....*....|....*..
gi 226495417 489 DEQTEQSENLQVQLEHLQSRLRRQQQN 515
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-511 |
1.42e-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: 64.32 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 231 RQERSRLPWEDTAATEEEASKLTALRLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSI 310
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 311 LKEAhqdelgrmSEDLEDELGAR--SSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEA 388
Cdd:TIGR02169 777 LEEA--------LNDLEARLSHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 389 LARRRRQTASaLDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELA 468
Cdd:TIGR02169 849 IKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 226495417 469 QAEDELDEAHNQARKLQrSLDEQTEQSENLQVQLEHLQSRLRR 511
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
240-499 |
3.03e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 240 EDTAATEEEASKLTALRLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDEL 319
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 320 GRMSEDLEDElgarssmdrkmAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASA 399
Cdd:COG1196 337 EELEELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 400 LDcDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHN 479
Cdd:COG1196 406 EE-AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260
....*....|....*....|
gi 226495417 480 QARKLQRSLDEQTEQSENLQ 499
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
296-517 |
1.38e-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: 57.08 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 296 ELSKTKQEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLEREN 375
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 376 KKLRAQVGDLEEALARRRRQTASALdcdlRASQAALFEKNKELADLKHVHGKLKKQ---FQEKVAELAHANRRVEQHEAE 452
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAL----LLSPEDFLDAVRRLQYLKYLAPARREQaeeLRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226495417 453 VKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAP 517
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
247-513 |
7.19e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 247 EEASKLTALRLRLDESQKVLLKEREDKLALSRNIEKLEGEL------SQWKIKYEELSKTKQEMLKQLSILK-EAHQDEL 319
Cdd:TIGR02168 162 EEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLkslerqAEKAERYKELKAELRELELALLVLRlEELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 320 GRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQtASA 399
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ-LEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 400 LDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHN 479
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270
....*....|....*....|....*....|....
gi 226495417 480 QARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQ 513
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
261-473 |
1.01e-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: 55.06 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 261 ESQKVLLKEREDklALSRNIEKLEGELSQW---KIKYEELSKTKQEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMD 337
Cdd:TIGR02168 301 EQQKQILRERLA--NLERQLEELEAQLEELeskLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 338 RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRrrqtasaldcDLRASQAALFEKNKE 417
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA----------ELKELQAELEELEEE 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 226495417 418 LADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDE 473
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
247-487 |
1.57e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 247 EEASKLTALRLRLDE-SQKVLLKE----REDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSIL----KEAHQD 317
Cdd:TIGR02169 208 EKAERYQALLKEKREyEGYELLKEkealERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 318 ELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRR---- 393
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeele 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 394 --RQTASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELK------- 464
Cdd:TIGR02169 368 dlRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEeekedka 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 226495417 465 -----------------------------------KELAQAEDELDEAHNQARKLQRS 487
Cdd:TIGR02169 448 leikkqewkleqlaadlskyeqelydlkeeydrveKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
268-511 |
2.21e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 268 KEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMDRKMAELRGEM 347
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 348 ERLQA---ENAAEWGRRERL------ETEKLGlERENKKLRAQVGDLEEALARRRRQTASALDcDLRASQAALFEKNKEL 418
Cdd:TIGR02169 254 EKLTEeisELEKRLEEIEQLleelnkKIKDLG-EEEQLRVKEKIGELEAEIASLERSIAEKER-ELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 419 ADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENL 498
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
250
....*....|...
gi 226495417 499 QVQLEHLQSRLRR 511
Cdd:TIGR02169 412 QEELQRLSEELAD 424
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
247-506 |
1.30e-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: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 247 EEASKLTALRLRLDESQKVLLKEREDKLALSRN-----IEKLEGELSQWKIKYEELSKTKQEMLKQLSILK---EAHQDE 318
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsiNKIKQN 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 319 LGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTAs 398
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE- 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 399 aldcdlrasqaaLFEKNKELADLKHVHGKLKKQfQEKVAELahanrrVEQHEAEVKKLRLRVEELKKELAQAEDELDEAH 478
Cdd:TIGR04523 563 ------------IDEKNKEIEELKQTQKSLKKK-QEEKQEL------IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
250 260
....*....|....*....|....*...
gi 226495417 479 NQARKLQRSLDEQTEQSENLQVQLEHLQ 506
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
242-543 |
1.46e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 242 TAATEEEASKLTALRLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGR 321
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 322 MSEDLEDELGARSSM---DRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTAS 398
Cdd:COG1196 374 LAEAEEELEELAEELleaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 399 ------ALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAED 472
Cdd:COG1196 454 leeeeeALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226495417 473 ELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAPLfGKIRSARFGTEEAEDGTSDLDEDE 543
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL-DKIRARAALAAALARGAIGAAVDL 603
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
110-550 |
1.86e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 110 KVRAERNRAREEVR----QLRQRLDALTKELAGARRERQEAQGECEARGRELARLRG-----------ARGVADQTRDGP 174
Cdd:PTZ00121 1308 KKKAEEAKKADEAKkkaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEkaeaaekkkeeAKKKADAAKKKA 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 175 EPEAEREPVRDVGSERPPGSQELELVESLLKSMPEESEDCWEARSLGAGGPRGSSGRQErsrlpwEDTAATEEEASKLTA 254
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA------DEAKKKAEEAKKAEE 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 255 LRLRLDESQKVllKEREDKLALSRNIEKLEGELSQWKIKYEELSKtKQEMLKQLSILKEAHQ----DELGRMSEDLEDEL 330
Cdd:PTZ00121 1462 AKKKAEEAKKA--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKADEAKKAEEakkaDEAKKAEEAKKADE 1538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 331 GARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLR----AQVGDLEEALARRRRQTASALDCDLRA 406
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 407 SQAAlfEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQR 486
Cdd:PTZ00121 1619 KIKA--EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226495417 487 SLDEQTEQSENLQVQLEHLQSRLRRQQQNAPLFGKIRSARFGTEEAEDGTSDLDEDEDLQIQVA 550
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
279-507 |
2.24e-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: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 279 NIEKLEGELSQWKIKYEELSKTKQEMLKQLSILkeahQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEW 358
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK----EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 359 GRRERLETEKLGLE---RENKKLRAQVGDLEEAlARRRRQTASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEK 435
Cdd:TIGR04523 194 NKLLKLELLLSNLKkkiQKNKSLESQISELKKQ-NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 436 VAELAHANRRVEQHEAEVKKLRLRVEELKK------------ELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLE 503
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
....
gi 226495417 504 HLQS 507
Cdd:TIGR04523 353 NSES 356
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
110-494 |
3.10e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 110 KVRAERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLRGARGVADQTRdgpepEAEREPVRDVGSE 189
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI-----EELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 190 RPPGSQELELVESLLKSMPEEsedcwearslgaggprgssgrqersrlpwedtaateeeaskLTALRLRLDESQKVLLKE 269
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEE-----------------------------------------LKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 270 REDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAH---QDELGRMSEDLEDELGARSSMDRKMAELRGE 346
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIeelEELIEELESELEALLNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 347 MERLQAEnaaewgrRERLETEKLGLERENKKLRAQVGDLEEALAR---RRRQTASALDCDLRAS-QAALFEKNKELADLK 422
Cdd:TIGR02168 896 LEELSEE-------LRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERLSEEYSLTlEEAEALENKIEDDEE 968
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226495417 423 HVHGKLkKQFQEKVAELAHANRRVEQHEAEVKKlrlRVEELKKELaqaeDELDEAHNQARKLQRSLDEQTEQ 494
Cdd:TIGR02168 969 EARRRL-KRLENKIKELGPVNLAAIEEYEELKE---RYDFLTAQK----EDLTEAKETLEEAIEEIDREARE 1032
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-548 |
4.61e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 102 ANWREKWSKVRAERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLRGARGVADQTRDGPEPEAERE 181
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 182 pvrdvgserppgSQELELVESLLKSMPEESEDCWEARSlgaggpRGSSGRQERSRLPWEDTAATEEEASKLTALRLRLDE 261
Cdd:COG1196 343 ------------EEELEEAEEELEEAEAELAEAEEALL------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 262 SQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMDRKMA 341
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 342 ELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGD------------LEEALARRRRQTASALDCDLRASQA 409
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvligveaayeaaLEAALAAALQNIVVEDDEVAAAAIE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 410 ALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLD 489
Cdd:COG1196 565 YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG 644
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 226495417 490 EQTEQSENLQVQLEHLQSRLRRQQQNAPLFGKIRSARFGTEEAEDGTSDLDEDEDLQIQ 548
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
105-512 |
4.85e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 105 REKWSKVRAERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLRGARGVADQTRDG--PEPEAEREP 182
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 183 VRDVGSERppgSQELELVESLLKSMPE--ESEDCWEARSLGAGGPRGSSGRQERSRLPWEDTAATEEEASKLTALRLRLD 260
Cdd:COG1196 444 LEEAAEEE---AELEEEEEALLELLAEllEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 261 ESQKVLLKEREDKLALSRNIEKLEGELSQWKI--------KYEELSKTKQEMLKQLSILKEAHQDELGRMSEDLEDELGA 332
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEAALAAALQNIVveddevaaAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAA 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 333 RSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASAldcdlRASQAALF 412
Cdd:COG1196 601 VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR-----RELLAALL 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 413 EKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQT 492
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
410 420
....*....|....*....|
gi 226495417 493 EQSENLQVQLEHLQSRLRRQ 512
Cdd:COG1196 756 LPEPPDLEELERELERLERE 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
317-515 |
7.41e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 317 DELGRMSEDLEDELGARSSMD--RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAqvgDLEEALARRRR 394
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEdaREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL---ELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 395 QTASALDCDLRASQAALFEKNKELADLKHVH--------GKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRV----EE 462
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLpasaEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 226495417 463 LKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQN 515
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
267-542 |
7.65e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 267 LKEREDKLA-LSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKE------AHQDELGRMSEDLEDELGARSSMDRK 339
Cdd:PRK01156 192 LKSSNLELEnIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSalnelsSLEDMKNRYESEIKTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 340 MAELRGEMERL-QAENAAEWGRRERLeteklgleRENKKLRAQVGDLEEALARRRRQTASALDC-----DLRASQAALFE 413
Cdd:PRK01156 272 NNYYKELEERHmKIINDPVYKNRNYI--------NDYFKYKNDIENKKQILSNIDAEINKYHAIikklsVLQKDYNDYIK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 414 KNKELADLKHVHGKLKK---QFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARklqRSLDE 490
Cdd:PRK01156 344 KKSRYDDLNNQILELEGyemDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEIN---VKLQD 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 226495417 491 QTEQSENLQVQLEHLQSRLRRQQQNAP-LFGKIRSARFGTEEAEDGTSDLDED 542
Cdd:PRK01156 421 ISSKVSSLNQRIRALRENLDELSRNMEmLNGQSVCPVCGTTLGEEKSNHIINH 473
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
117-496 |
1.13e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 117 RAREEVRQLRQRL---DALTKELAGARRERQEAQGECEARGRELARLRGARGVADQTRDGPEPEAE--REPVRDVGSERP 191
Cdd:COG1196 219 KEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 192 PGSQELELVESLLKSMPEESEDC-WEARSLGAggprgssgRQErsrlpwEDTAATEEEASKLTALRLRLDESQKVLLKER 270
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELeEELAELEE--------ELE------ELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 271 EDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGRMS---EDLEDELGARSSMDRKMAELRGEM 347
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErleEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 348 ERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDCDLRA---SQAALFEKNKELADLKHV 424
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegfLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226495417 425 HGKL---KKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSE 496
Cdd:COG1196 525 AVAVligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
113-399 |
2.82e-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: 46.98 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 113 AERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLrgARGVADQTRDgpEPEAEREPVRDVGSERPP 192
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL--NKKIKDLGEE--EQLRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 193 GSQELELVESLLKSMPEESEDCWEARSLGAGGPRGSSGRQersrlpwedtaatEEEASKLTALRLRLDESQKVLLKERED 272
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI-------------EEERKRRDKLTEEYAELKEELEDLRAE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 273 KLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILkeahQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQA 352
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL----QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 226495417 353 ENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASA 399
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
110-476 |
3.07e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 110 KVRAERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLRGARGVADQTRDGPEPEAEREPVRDVGSE 189
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 190 RPPGSQELELVESLLKSMPEesedcWEARSLGAGGPRGSSGRQERSRLPWEDTAATEEEASKLTALRLRLDESQKVLLKE 269
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIG-----VEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 270 REDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMDRKMAELRGEMER 349
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 350 LQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTAsaldcdLRASQAALFEKNKELADLkhvhgklk 429
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE------ERLEEELEEEALEEQLEA-------- 732
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 226495417 430 kQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDE 476
Cdd:COG1196 733 -EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
338-514 |
3.53e-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: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 338 RKMAELRGEMERLQAENAAewgrrerleteklgLERENKKLRAQVGDLEE-ALARRRRQTASALDCDLRASQAALFEKNK 416
Cdd:COG4913 610 AKLAALEAELAELEEELAE--------------AEERLEALEAELDALQErREALQRLAEYSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 417 ELADLK---HVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRS-LDEQT 492
Cdd:COG4913 676 ELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERF 755
|
170 180 190
....*....|....*....|....*....|..
gi 226495417 493 EQ----------SENLQVQLEHLQSRLRRQQQ 514
Cdd:COG4913 756 AAalgdaverelRENLEERIDALRARLNRAEE 787
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-391 |
3.59e-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: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 105 REKWSKVRAERNRAREEVRQLRQRLDALTKELAGARRER-------QEAQGECEARGRELARLRGARGVADQTRDGPEPE 177
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeiEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 178 AER--EPVRDVGSERPPGSQELELVESLLKSMPEESEDCwearslgaggprgssgrqersrlpwedTAATEEEASKLTAL 255
Cdd:TIGR02168 318 LEEleAQLEELESKLDELAEELAELEEKLEELKEELESL---------------------------EAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 256 RLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEEL----SKTKQEMLKQLSILKEAHQDELGRMSEDLEDELg 331
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrrERLQQEIEELLKKLEEAELKELQAELEELEEEL- 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 332 arssmdrkmAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALAR 391
Cdd:TIGR02168 450 ---------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
302-520 |
4.30e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 302 QEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQ 381
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 382 VGDLEEALArRRRQTASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVE 461
Cdd:pfam07888 117 KDALLAQRA-AHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226495417 462 ELKKELAQAEDELDEAHNQARKLQRSLDE---QTEQSENLQVQLEHLQSRLRRQQQNAPLFG 520
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTLTQKLTTahrKEAENEALLEELRSLQERLNASERKVEGLG 257
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
338-503 |
5.18e-05 |
|
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: 44.92 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 338 RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDcdlrasqaalfekNKE 417
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-------------NKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 418 LADLKHvhgklkkqfqekvaELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 497
Cdd:COG1579 91 YEALQK--------------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....*.
gi 226495417 498 LQVQLE 503
Cdd:COG1579 157 ELEELE 162
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
232-514 |
6.35e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.84 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 232 QERSRLPWEDTAATEEEASKLTALRLRLdESQKVLLKEREDKL-ALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSI 310
Cdd:pfam05622 158 EERNAEYMQRTLQLEEELKKANALRGQL-ETYKRQVQELHGKLsEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 311 LKEAHqDELgRMSEDLEDELGARSSMDRKMAELRGEM--ERLQAEnaaewgRRERLETeklgLERENKKLR-AQVGDLEE 387
Cdd:pfam05622 237 LRETN-EEL-RCAQLQQAELSQADALLSPSSDPGDNLaaEIMPAE------IREKLIR----LQHENKMLRlGQEGSYRE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 388 ALArrrrqtasaldcdlrASQAALFEKNKELADLKhvhGKLKKQfQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKEL 467
Cdd:pfam05622 305 RLT---------------ELQQLLEDANRRKNELE---TQNRLA-NQRILELQQQVEELQKALQEQGSKAEDSSLLKQKL 365
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 226495417 468 AQAEDELDEAHNQARKLQRSLDE-QTEQSENLQVQLEHLQSRLRRQQQ 514
Cdd:pfam05622 366 EEHLEKLHEAQSELQKKKEQIEElEPKQDSNLAQKIDELQEALRKKDE 413
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
312-517 |
6.63e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 312 KEAHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAewgrrerLETEKLGLERENKKLRAQVGDLEEALAR 391
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-------LQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 392 RRRQ------TASALDCDLRASQAAlfeknkELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKK 465
Cdd:COG3883 91 RARAlyrsggSVSYLDVLLGSESFS------DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 226495417 466 ELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAP 517
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
105-544 |
7.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 105 REKWSKVRAERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLRGAR--GVADQTRDGPEPEAerep 182
Cdd:PRK02224 236 RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERddLLAEAGLDDADAEA---- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 183 vrdvgserppgsqeLELVESLLKSMPEESEDCWEARSLGAGgprgssgrqersrlpwedtaATEEEASKLTALRLRLDES 262
Cdd:PRK02224 312 --------------VEARREELEDRDEELRDRLEECRVAAQ--------------------AHNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 263 QKVLlkeREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLsilkEAHQDELGRMSEDLEDELGARSSMDRKMAE 342
Cdd:PRK02224 358 AEEL---REEAAELESELEEAREAVEDRREEIEELEEEIEELRERF----GDAPVDLGNAEDFLEELREERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 343 LRGEMErlQAENAAEWGRReRLETEKLGLERENKKLRAQVGDLEEAlaRRRRQTASALDCDLRASQAALFEKNKELADLK 422
Cdd:PRK02224 431 LEATLR--TARERVEEAEA-LLEAGKCPECGQPVEGSPHVETIEED--RERVEELEAELEDLEEEVEEVEERLERAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 423 hvhgKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQL 502
Cdd:PRK02224 506 ----EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 226495417 503 EHLQSRLRRQQQNAPLFGKIRSARFGTEEAEDGTSDLDEDED 544
Cdd:PRK02224 582 AELKERIESLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
260-505 |
7.84e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 260 DESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQlsILKEAhQDELgrmsEDLEDELgarSSMDRK 339
Cdd:PRK05771 39 ELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEE--LIKDV-EEEL----EKIEKEI---KELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 340 MAELRGEMERLQAEnaaewgrRERLE-----TEKLGLERENKKLRAQVGDLEEALarrrrqtasaldcDLRASQAALFEK 414
Cdd:PRK05771 109 ISELENEIKELEQE-------IERLEpwgnfDLDLSLLLGFKYVSVFVGTVPEDK-------------LEELKLESDVEN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 415 NKELADLKHVHG----KLKKQFQEKVAELA-HANRRVEQHE-----AEVKKLRLRVEELKKELAQAEDELDEAHNQARKL 484
Cdd:PRK05771 169 VEYISTDKGYVYvvvvVLKELSDEVEEELKkLGFERLELEEegtpsELIREIKEELEEIEKERESLLEELKELAKKYLEE 248
|
250 260
....*....|....*....|.
gi 226495417 485 QRSLDEQTEQSENLQVQLEHL 505
Cdd:PRK05771 249 LLALYEYLEIELERAEALSKF 269
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
239-474 |
8.59e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 239 WEDTAATEEEASKLTALRLRLDesqkvlLKEREDKLALSRN-IEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQD 317
Cdd:COG4913 261 AERYAAARERLAELEYLRAALR------LWFAQRRLELLEAeLEELRAELARLEAELERLEARLDALREELDELEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 318 ELGrmsedledelgarssmdRKMAELRGEMERLQAEnaaewgrRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTA 397
Cdd:COG4913 335 NGG-----------------DRLEQLEREIERLERE-------LEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226495417 398 SALDcdlrASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRlrvEELKKELAQAEDEL 474
Cdd:COG4913 391 ALLE----ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR---DALAEALGLDEAEL 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
370-517 |
1.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 370 GLERENKKLRAQVGDLEEALA---RRRRQTASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRV 446
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRElaeRYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226495417 447 EQHEAEVKKLRL--------RVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAP 517
Cdd:COG4913 319 DALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
246-443 |
1.24e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 246 EEEASKLTALRLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGRMSED 325
Cdd:COG4942 51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPED 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 326 LEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALArRRRQTASALDCDLR 405
Cdd:COG4942 131 FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA-ERQKLLARLEKELA 209
|
170 180 190
....*....|....*....|....*....|....*...
gi 226495417 406 ASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHAN 443
Cdd:COG4942 210 ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
106-516 |
1.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 106 EKWSKVRAERNRAREEVRQLRQRLDALTKELAGARRERQEAQgeceargRELARLRGARGVADQTRdgpEPEAEREPVRD 185
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR-------EELEKLEKLLQLLPLYQ---ELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 186 VGSERPPGSQELELVESLLKSMPEESEDCWEARslgaggprgSSGRQERSRLPWEDTAATEEEASKLTALRLRLDESQKV 265
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQ---------EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 266 LLKEREDKLALSRNIEKLEGELSQWKiKYEELSKTKQ---------EMLKQLSILKEAHQDELGRMSEDLEDELGARSSM 336
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAA-LEERLKEARLllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 337 DRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDCDLRASQAALFEKNK 416
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 417 ELADLKHV--------HGKLKKQFQEKVAELAHANRRVEQHEAEVK---------KLRLRVEELKKELAQAEDELDEAHN 479
Cdd:COG4717 374 ALLAEAGVedeeelraALEQAEEYQELKEELEELEEQLEELLGELEellealdeeELEEELEELEEELEELEEELEELRE 453
|
410 420 430
....*....|....*....|....*....|....*..
gi 226495417 480 QARKLQRSLdEQTEQSENLQVQLEHLQSRLRRQQQNA 516
Cdd:COG4717 454 ELAELEAEL-EQLEEDGELAELLQELEELKAELRELA 489
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
112-533 |
1.95e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 112 RAERNRAREEVRQLRQ-RLDALTKELAGARRERQEAQGECEARGRELARlRGARGVADQTRDGPEPEAEREPVRdvgSER 190
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEaKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR-RQAAIKAEEARKADELKKAEEKKK---ADE 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 191 PPGSQELELVESLlKSMPEESEDCWEARSLGAGGPRGSSGRQERSRLPWEDTAATEEEASKltalrlRLDESQKVLLKER 270
Cdd:PTZ00121 1295 AKKAEEKKKADEA-KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA------AADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 271 EDKLALSRNIEKLEG--ELSQWKIKYEELSKTKQEMLKQLSILKEAHQ-----DELGRMSEDLE--DELGARSSMDRKMA 341
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAakkkaDEAKKKAEEKKkaDEAKKKAEEAKKAD 1447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 342 ELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDCDLRASQAALFEKNKELADL 421
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA 1527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 422 KHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKElaqaEDELDEAHNQARKLQRSLDEQTEQSENLQVQ 501
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
410 420 430
....*....|....*....|....*....|..
gi 226495417 502 LEHLQSRLRRQQQNAplfgKIRSARFGTEEAE 533
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEA----KIKAEELKKAEEE 1631
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
241-514 |
2.07e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 241 DTAATEEEASKL----TALRLRLDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLsilkeAHQ 316
Cdd:PRK04863 273 DYMRHANERRVHleeaLELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL-----RQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 317 DELGRMSEDLEDelgarssmdrkmAELRGEMERLQAENAAEwgRRERLETEKLGLERENKKLRAQVGDLEEAL------A 390
Cdd:PRK04863 348 EKIERYQADLEE------------LEERLEEQNEVVEEADE--QQEENEARAEAAEEEVDELKSQLADYQQALdvqqtrA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 391 RRRRQTASALDCDLRASQAALFeknkELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAevkkLRLRVEELKKELAQA 470
Cdd:PRK04863 414 IQYQQAVQALERAKQLCGLPDL----TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKI 485
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 226495417 471 EDELD--EAHNQARKLQRSLDEQ---TEQSENLQVQLEHLQSRLRRQQQ 514
Cdd:PRK04863 486 AGEVSrsEAWDVARELLRRLREQrhlAEQLQQLRMRLSELEQRLRQQQR 534
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
112-546 |
2.70e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 112 RAERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLRGARGVADQTRDGPEPEAEREPVRDVGSERP 191
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 192 PGSQELELVESLLKSMP-EESEDCWEARSLGAGGPRGSSGRQERSRLPWEDTA----ATEEEASKLTALRlRLDESQKVL 266
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARmahfARRQAAIKAEEAR-KADELKKAE 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 267 LKEREDKLALSRNIEKLE--GELSQWKIKYEELSKTKQEMLKQLSILKEAHQ-----DELGRMSEDLEDELGARSSMDRK 339
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeakkaAEAAKAEAEAAADEAEAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 340 MAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEA------LARRRRQTASALDCDLRASQAALFE 413
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkkkadeAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 414 KNKELADLKHVHGKLKKQFQEK-----VAELAHANRRVEQHEAEVKKLRLRVEELKK--ELAQAEDELDEAHNQARKLQR 486
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAkkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEA 1527
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 487 SLDEQTEQSENLQVQLEHLQSRLRRQQQNAPLFGKIRSARFGTEEAEDGTSDLDEDEDLQ 546
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
271-512 |
3.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 271 EDKLA-LSRNIEKLEGELSQWKIKYEELsktkQEMLKQLSILKEAHQDeLGRMSEDLEDELGARSSMDRKMAELR----- 344
Cdd:COG4913 609 RAKLAaLEAELAELEEELAEAEERLEAL----EAELDALQERREALQR-LAEYSWDEIDVASAEREIAELEAELErldas 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 345 -GEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDcDLRASQAALFEKNKELADLKH 423
Cdd:COG4913 684 sDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED-LARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 424 VHGKLKKQFQEkvaELAHANRRVEQHEAEVKKLRLR------------------VEELKKELAQAEDelDEAHNQARKLQ 485
Cdd:COG4913 763 VERELRENLEE---RIDALRARLNRAEEELERAMRAfnrewpaetadldadlesLPEYLALLDRLEE--DGLPEYEERFK 837
|
250 260
....*....|....*....|....*..
gi 226495417 486 RSLDEQTEQSenlqvqLEHLQSRLRRQ 512
Cdd:COG4913 838 ELLNENSIEF------VADLLSKLRRA 858
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
343-502 |
3.18e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 42.77 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 343 LRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASaldcdlrasqaalfekNKELADLK 422
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSN----------------LKEISDLE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 423 HVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEElkkELAQAEDELDEAHNQA---RKLQRSLDEQTEQSENLQ 499
Cdd:pfam15294 195 EKMAALKSDLEKTLNASTALQKSLEEDLASTKHELLKVQE---QLEMAEKELEKKFQQTaayRNMKEMLTKKNEQIKELR 271
|
...
gi 226495417 500 VQL 502
Cdd:pfam15294 272 KRL 274
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
376-478 |
5.51e-04 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.36 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 376 KKLRAQVGDLEEALARRRR----QTASALDCDLRASQaalfeknKELADLKHVHGKLKKQfqekVAELAHANRRVEQHEA 451
Cdd:PRK05431 5 KLIRENPEAVKEALAKRGFpldvDELLELDEERRELQ-------TELEELQAERNALSKE----IGQAKRKGEDAEALIA 73
|
90 100
....*....|....*....|....*..
gi 226495417 452 EVKKLRLRVEELKKELAQAEDELDEAH 478
Cdd:PRK05431 74 EVKELKEEIKALEAELDELEAELEELL 100
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-439 |
6.27e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 106 EKWSKVRAERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLRGARGVADQTRDGPEPEAEREPVRD 185
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEE 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 186 VGSERppgSQELELVESLLKSMPEESEDCWEARSLGAGGPRGSSGRQERSRLPWEDTAATEEEASKLTALRLRLDESQKV 265
Cdd:PRK03918 474 KERKL---RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 266 LLKEREDKLALSRNIEKLEGELSQWKIKYEELS-KTKQEMLKQLSILKEAH----------------QDELGRMSEDLED 328
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYneylelkdaekelereEKELKKLEEELDK 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 329 ELGARSSMDRKMAELRGEMERLQAENAAEwgRRERLETEKLGLERENKKLRAQVgdleEALARRRRQTASALDcDLRASQ 408
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAEL----EELEKRREEIKKTLE-KLKEEL 703
|
330 340 350
....*....|....*....|....*....|.
gi 226495417 409 AALFEKNKELADLKHVHGKLkKQFQEKVAEL 439
Cdd:PRK03918 704 EEREKAKKELEKLEKALERV-EELREKVKKY 733
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
375-497 |
6.41e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 375 NKKLRAQVGDLEEALARRRRQtasaldcdLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAEL------------AHA 442
Cdd:PRK04863 987 NEKLRQRLEQAEQERTRAREQ--------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELqdlgvpadsgaeERA 1058
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 226495417 443 NRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 497
Cdd:PRK04863 1059 RARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
280-508 |
6.48e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 280 IEKLEGELSQWKIKYEELSKTK-QEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEW 358
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQKeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 359 GRRERLETEKLGLEREN-------KKLRAQVGDLEEALaRRRRQTASALDCDLRASQAALFEKNKELADLKHVHGKLKKQ 431
Cdd:TIGR04523 363 RELEEKQNEIEKLKKENqsykqeiKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 432 F-----QEKVAELA---------HANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 497
Cdd:TIGR04523 442 IkdltnQDSVKELIiknldntreSLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
250
....*....|.
gi 226495417 498 LQVQLEHLQSR 508
Cdd:TIGR04523 522 LKEKIEKLESE 532
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
431-515 |
7.34e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 431 QFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHlqsRLR 510
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---RAR 93
|
....*
gi 226495417 511 RQQQN 515
Cdd:COG3883 94 ALYRS 98
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-494 |
8.04e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 391 RRRRQTASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQA 470
Cdd:COG4942 2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100
....*....|....*....|....
gi 226495417 471 EDELDEAHNQARKLQRSLDEQTEQ 494
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEE 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
112-511 |
1.10e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 112 RAERNRAREEVRQLRQRLDALTKELAGARRERQEAQGECEARGRELARLRGARGVADQTRDGPEPEAErepvrDVGSERP 191
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE-----ELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 192 PGSQELELVESLLKSMPEESEdcwEARSLGAGGPRGSSGRQERSRLPWEDTAATEEEASKLTALRLRLDESQKvllkERE 271
Cdd:PRK02224 423 ELREREAELEATLRTARERVE---EAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVE----EVE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 272 DKLALSRNIEKLEGELSqwkikyeelskTKQEMLKQLSILKEAHQDELGRMSEDLEdelgarsSMDRKMAELRGEME--R 349
Cdd:PRK02224 496 ERLERAEDLVEAEDRIE-----------RLEERREDLEELIAERRETIEEKRERAE-------ELRERAAELEAEAEekR 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 350 LQAENAAEWGRRERLETEKLGLER-ENKKLRAQVGDLEEALARRRrqtasaldcDLRASQAALFEKNKELADLKHVHGKL 428
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLaELKERIESLERIRTLLAAIA---------DAEDEIERLREKREALAELNDERRER 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 429 KKQFQEKVAELAHanrrvEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQR---SLDEQTEQSENLQVQLEHL 505
Cdd:PRK02224 629 LAEKRERKRELEA-----EFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigAVENELEELEELRERREAL 703
|
....*.
gi 226495417 506 QSRLRR 511
Cdd:PRK02224 704 ENRVEA 709
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
440-514 |
1.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226495417 440 AHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 514
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
259-517 |
1.22e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 259 LDESQKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDE----LGRMS-EDLEDEL--- 330
Cdd:PRK11281 54 LEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEtretLSTLSlRQLESRLaqt 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 331 -------------------GARSSMDRKMAELRGEMERLQ-----------AENAAEWGRRERLETEKLGLERENKKLR- 379
Cdd:PRK11281 134 ldqlqnaqndlaeynsqlvSLQTQPERAQAALYANSQRLQqirnllkggkvGGKALRPSQRVLLQAEQALLNAQNDLQRk 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 380 -AQVGDLEEALARRRRqtasaldcDLRASQAALFEknKELADLKHV-HGKLKKQFQEKVAELAHANRRVE-QHEAEVKKL 456
Cdd:PRK11281 214 sLEGNTQLQDLLQKQR--------DYLTARIQRLE--HQLQLLQEAiNSKRLTLSEKTVQEAQSQDEAARiQANPLVAQE 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226495417 457 RLRVEELKKELAQAEDELDEAHNQARKLQRSLDE--QTEQseNLQVQLEHLQ-----SR-LRRQQQNAP 517
Cdd:PRK11281 284 LEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRltQSER--NIKEQISVLKgslllSRiLYQQQQALP 350
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
346-498 |
1.36e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 346 EMERLQAEnaAEW---------GRRERLETEKLGLERENKKLRAQVGDLEEALARRRrQTASALDCDLRASQAALFEKNK 416
Cdd:smart00787 124 TFARLEAK--KMWyewrmklleGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLR-DRKDALEEELRQLKQLEDELED 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 417 ----ELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQT 492
Cdd:smart00787 201 cdptELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQL 280
|
....*.
gi 226495417 493 EQSENL 498
Cdd:smart00787 281 KLLQSL 286
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
313-517 |
1.61e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 313 EAHQDELGRMSEDLEDEL-GARSSMDRKMAELRGEMER-----LQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLE 386
Cdd:COG3206 167 ELRREEARKALEFLEEQLpELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 387 EALARRRRQTASAL-DCDLRASQAALFEKNKELADLKHVHG-------KLKKQFQEKVAELAHANRRV-EQHEAEVKKLR 457
Cdd:COG3206 247 AQLGSGPDALPELLqSPVIQQLRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRIlASLEAELEALQ 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226495417 458 LRVEELKKELAQAEDELD---EAHNQARKLQRSLDEQTEQSENLQVQLEhlQSRLRRQQQNAP 517
Cdd:COG3206 327 AREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYESLLQRLE--EARLAEALTVGN 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
241-512 |
1.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 241 DTAATEEEASKLTALRLRLDESQKVLlkeredklalsrniEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELG 320
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDL--------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 321 RMsEDLEDELGARSSMDRKMAELRGEmERLQAENAAEWGRRERLEteklgLERENKKLRAQVGDLEEALARRRRQ---TA 397
Cdd:COG4913 728 EL-DELQDRLEAAEDLARLELRALLE-ERFAAALGDAVERELREN-----LEERIDALRARLNRAEEELERAMRAfnrEW 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 398 SALDCDLRASQAALFEKNKELADLKHVH-----GKLKKQFQE-KVAELAHANRRVEQHEAEVKKlrlRVEELKKELAQ-- 469
Cdd:COG4913 801 PAETADLDADLESLPEYLALLDRLEEDGlpeyeERFKELLNEnSIEFVADLLSKLRRAIREIKE---RIDPLNDSLKRip 877
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 226495417 470 ----------AEDELDEAHNQARKLQRSLDEQT-----EQSENLQVQLEHLQSRLRRQ 512
Cdd:COG4913 878 fgpgrylrleARPRPDPEVREFRQELRAVTSGAslfdeELSEARFAALKRLIERLRSE 935
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
348-515 |
1.93e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 348 ERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALDcDLRASQAALFEKNKELADLKHVHGK 427
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE-ELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 428 LKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQS 507
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
....*...
gi 226495417 508 RLRRQQQN 515
Cdd:COG4372 165 ELAALEQE 172
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
399-516 |
1.94e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 40.99 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 399 ALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAH 478
Cdd:COG5283 4 ILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLS 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 226495417 479 NQARKLQRSLdEQTEQsenlqvQLEHLQSRLRR--QQQNA 516
Cdd:COG5283 84 AAQRRLRSSL-EQTNR------QLERQQQRLARlgARQDR 116
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
375-497 |
2.27e-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: 41.09 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 375 NKKLRAQVGDLEEALARRRRQtasaldcdLRASQAALFEKNKELADLKHVHG---KLKKQFQEKVAEL---------AHA 442
Cdd:COG3096 986 NEKLRARLEQAEEARREAREQ--------LRQAQAQYSQYNQVLASLKSSRDakqQTLQELEQELEELgvqadaeaeERA 1057
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 226495417 443 NRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 497
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-350 |
2.57e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 113 AERNRAREEVRQLRQRLDALTKELAG-ARRERQEAQGECEARGRELARLRGARGVADQTRDGPEPEAEREPVRDVGSERP 191
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 192 PGSQELELVESLLKSMPEESEDCWEARSLGAGGPRGSSGRQERSRlpwedtAATEEEASKLTALRLRLDESQKVLLKERE 271
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL------AALLEAEAELEELAERLAEEELELEEALL 700
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226495417 272 DKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERL 350
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
360-501 |
2.69e-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: 40.71 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 360 RRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTA------SALDCDLRASQAALfekNKELADLKHvhgklkkqfQ 433
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEelsareSDLEQDYQAASDHL---NLVQTALRQ---------Q 346
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226495417 434 EKV----AELAHANRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQteQSENLQVQ 501
Cdd:COG3096 347 EKIeryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQ--QTRAIQYQ 416
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
110-400 |
2.91e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 110 KVRAERNRAREEVRQLRQRLDALTKEL---AGARRERQEAQGECEARGRELARLRGARGVADQTRDGPEPEAEREPVRdv 186
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAkkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK-- 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 187 gSERPPGSQELELVESLLKSMPEESEDCWEARSL----GAGGPRGSSGRQERSRLPWEDTAATEEEASKLTALRlRLDES 262
Cdd:PTZ00121 1554 -AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEEE 1631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 263 QKVLLKEREDKLALSRNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEAHQDELGRMSEDLEDELGARSSMD----- 337
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkke 1711
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226495417 338 ----RKMAELRGEME--RLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASAL 400
Cdd:PTZ00121 1712 aeekKKAEELKKAEEenKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
257-492 |
3.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 257 LRLDESQKVLLKEREDKLALSRNIEKLEGELSQwKIKYEELSKTKQEMLKQlsILKEAhqDELGRMSEDLEDELGARSSM 336
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKR-TENIEELIKEKEKELEE--VLREI--NEISSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 337 DRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQTASALdcDLRASQAALFEKNK 416
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE--EYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226495417 417 ELADLKHVHGKLKKQ---FQEKVAELAHANRRVEQHEAEVKKLRLRVEELKKElAQAEDELDEAHNQARKLQRSLDEQT 492
Cdd:PRK03918 308 ELREIEKRLSRLEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLT 385
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
371-514 |
3.92e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 38.37 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 371 LERENKKLRAQVGDLEEALARRRRQTASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHE 450
Cdd:pfam08614 19 LEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226495417 451 AEVKKLRLRVEELKKELAQAEDELDEahnqarkLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 514
Cdd:pfam08614 99 RRLAALEAERAQLEEKLKDREEELRE-------KRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
447-516 |
5.18e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 5.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 447 EQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNA 516
Cdd:PRK12704 71 NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
433-505 |
6.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 433 QEKVAELahaNRRVEQHEAEVKKLRLRVEELKKELAQAEDELDEAHNQARK-----------------LQRSLDEQTEQS 495
Cdd:COG2433 412 EEEIRRL---EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERReirkdreisrldreierLERELEEERERI 488
|
90
....*....|
gi 226495417 496 ENLQVQLEHL 505
Cdd:COG2433 489 EELKRKLERL 498
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
251-496 |
8.81e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 39.07 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 251 KLTALRLRLDE--SQKVLLKEredklALSRNIEKLEGELSQWKIK---YEELsKTKQEMLKQLSILKEAhqDELGRMSED 325
Cdd:PLN03229 487 RLENLREEFSKanSQDQLMHP-----VLMEKIEKLKDEFNKRLSRapnYLSL-KYKLDMLNEFSRAKAL--SEKKSKAEK 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 326 LEDELGARSSMDRKMAELRGEMERLQAENAAEW---------GRRERLETEKLGLERENKKLRAQVG-DLEEALARRRRQ 395
Cdd:PLN03229 559 LKAEINKKFKEVMDRPEIKEKMEALKAEVASSGassgdelddDLKEKVEKMKKEIELELAGVLKSMGlEVIGVTKKNKDT 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226495417 396 TASALDCDLRASQAALFEK-NKELADLKHVHGkLKKQFQEKVAELAHANR--------RVEQHEAEVKK----------L 456
Cdd:PLN03229 639 AEQTPPPNLQEKIESLNEEiNKKIERVIRSSD-LKSKIELLKLEVAKASKtpdvtekeKIEALEQQIKQkiaealnsseL 717
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 226495417 457 RLRVEELKKELAQAEdELDEAHNQARKLQRSLDEQTEQSE 496
Cdd:PLN03229 718 KEKFEELEAELAAAR-ETAAESNGSLKNDDDKEEDSKEDG 756
|
|
| |
