|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
315-508 |
2.38e-13 |
|
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: 73.29 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 315 QDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQ 394
Cdd:pfam01576 888 EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 395 NASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELD 474
Cdd:pfam01576 968 SIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAS 1047
|
170 180 190
....*....|....*....|....*....|....
gi 755526634 475 EAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRL 508
Cdd:pfam01576 1048 RANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-545 |
3.03e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 246 EDASKLTALRLRLDESQKVLLKEREDKLalSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDElgrmSEDL 325
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL----ELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 326 EDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcDLRA 405
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-ELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 406 SQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQR 485
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 486 SLDEQTEQSENLQVQLEHLQSRLRRQQQNAPLFGKIRSTRFGTEEAGDGASDLDEDEDLQ 545
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-513 |
3.05e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 243 STEEDASKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKET---HQDELG 319
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 320 RMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEwgrRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASAL 399
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEEL---EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 400 DCDLRASQA--ALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAH 477
Cdd:COG1196 376 EAEEELEELaeELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270
....*....|....*....|....*....|....*.
gi 755526634 478 NQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-513 |
9.88e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 241 TASTEEDASKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILK--------- 311
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkdlarleae 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 312 -ETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALAR 390
Cdd:TIGR02168 742 vEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 391 RR------RQNASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKK 464
Cdd:TIGR02168 822 LRerleslERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 755526634 465 ELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
275-515 |
2.19e-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: 70.09 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 275 LSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQD---ELGRMSEDLEDELGARSSMDRKMAELRGEMERLQA 351
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 352 ENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQnasaldcdLRASQAALFEKNKELADLKHVHGKLKKQF 431
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA--------LDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 432 QEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQ 511
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
....
gi 755526634 512 QQNA 515
Cdd:TIGR02168 914 RREL 917
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
239-498 |
1.63e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 239 EDTASTEEDASKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDEL 318
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 319 GRMSEDLEDElgarssmdrkmAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASA 398
Cdd:COG1196 337 EELEELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 399 LDcDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHN 478
Cdd:COG1196 406 EE-AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260
....*....|....*....|
gi 755526634 479 QARKLQRSLDEQTEQSENLQ 498
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
266-514 |
1.88e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 266 LKEREDKLALSKNIEKLEGELSQWKikyEELSKTKQEMlKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGE 345
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRL-DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 346 MERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRR----RQNASALDCDLRASQAALFEKNKELADLK 421
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 422 HVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDEL--------------DEAHNQARKLQRSL 487
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrdlesrlgdlkkerDELEAQLRELERKI 905
|
250 260
....*....|....*....|....*..
gi 755526634 488 DEQTEQSENLQVQLEHLQSRLRRQQQN 514
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-493 |
4.74e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 111 RAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGVHSAADKthDGPEPEREQEPVRDIGAERP 190
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK--DLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 191 PGSQELDLVESLLKSRPEEPEGCWDACsvaaggprvssgRQDRNRLpwedTASTEEDASKLTALRLRLDESQKVLLKERE 270
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEA------------EAEIEEL----EAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 271 DKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILK---ETHQDELGRMSEDLEDELGARSSMDRKMAELRGEME 347
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 348 RLQAEnaaewgrRERLETEKLGLERENKKLRAQVGDLEEALAR---RRRQNASALDCDLRAS-QAALFEKNKELADLKHV 423
Cdd:TIGR02168 898 ELSEE-------LRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERLSEEYSLTlEEAEALENKIEDDEEEA 970
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 424 HGKLkKQFQEKVAELAHANRRVEQhetEVKKLRLRVEELKKELaqaeDELDEAHNQARKLQRSLDEQTEQ 493
Cdd:TIGR02168 971 RRRL-KRLENKIKELGPVNLAAIE---EYEELKERYDFLTAQK----EDLTEAKETLEEAIEEIDREARE 1032
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
295-516 |
5.18e-09 |
|
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: 58.24 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 295 ELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLEREN 374
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 375 KKLRAQVGDLEEALARRRRQNASALdcdlRASQAALFEKNKELADLKHVHGKLKKQ---FQEKVAELAHANRRVEQHETE 451
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAL----LLSPEDFLDAVRRLQYLKYLAPARREQaeeLRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755526634 452 VKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAP 516
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
242-512 |
1.82e-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: 57.37 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 242 ASTEEDASKLTALRLRLDESQKVLLKERE---DKLALSKNIEKLEGELS--QWKIKYEELSKTKQEmLKQLSILKETHQD 316
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEkaeRYKELKAELRELELALLvlRLEELREELEELQEE-LKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 317 ELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAEnaaewgrRERLETEKlgleRENKKLRAQVGDLEEALARRRRQNA 396
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANE-------ISRLEQQK----QILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 397 SALDCDlrasQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVkklrlrvEELKKELAQAEDELDEA 476
Cdd:TIGR02168 330 SKLDEL----AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-------ETLRSKVAQLELQIASL 398
|
250 260 270
....*....|....*....|....*....|....*.
gi 755526634 477 HNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQ 512
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-486 |
3.06e-08 |
|
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: 56.61 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 246 EDASKLTALRLRLDE-SQKVLLKE----REDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSIL----KETHQD 316
Cdd:TIGR02169 208 EKAERYQALLKEKREyEGYELLKEkealERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 317 ELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRR---- 392
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeele 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 393 --RQNASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQH--------------ETEVKKLR 456
Cdd:TIGR02169 368 dlRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnaaiagieakinelEEEKEDKA 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 755526634 457 LRVEE----------------------------LKKELAQAEDELDEAHNQARKLQRS 486
Cdd:TIGR02169 448 LEIKKqewkleqlaadlskyeqelydlkeeydrVEKELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-472 |
5.36e-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: 55.83 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 260 ESQKVLLKEREDklALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSE---DLEDELGARSSMD 336
Cdd:TIGR02168 301 EQQKQILRERLA--NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaELEELESRLEELE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 337 RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRrrqnasaldcDLRASQAALFEKNKE 416
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA----------ELKELQAELEELEEE 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755526634 417 LADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDE 472
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
267-510 |
6.13e-08 |
|
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: 55.84 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 267 KEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEM 346
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 347 ERLQA---ENAAEWGRRERL------ETEKLGlERENKKLRAQVGDLEEALARRRRQNASALDcDLRASQAALFEKNKEL 417
Cdd:TIGR02169 254 EKLTEeisELEKRLEEIEQLleelnkKIKDLG-EEEQLRVKEKIGELEAEIASLERSIAEKER-ELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 418 ADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENL 497
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
250
....*....|...
gi 755526634 498 QVQLEHLQSRLRR 510
Cdd:TIGR02169 412 QEELQRLSEELAD 424
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
109-490 |
9.56e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 109 KVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGVHSAADKTHDGPEPEREQEPVRDIGAE 188
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 189 RPPGSQELDLVESLLKSRPEEPEGCWDACSVAAGGPRVSSGRQDRNRLPWEDTASTEEDASKLTALRLRLDESQKvLLKE 268
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA-ALAA 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 269 REDKLALSKNIEKLEGELSQWKIKYEELSKTkqemLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMER 348
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDT----LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 349 LQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASAldcdlrasQAALFEKNKELADLKHVHGKLK 428
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELL 738
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755526634 429 KQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQ-------AEDELDEAhnQARKlqRSLDEQ 490
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEEL--EERY--DFLSEQ 803
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
258-505 |
6.08e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 258 LDESQKVLLKEREDklaLSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILK------ETHQDELGRMSEDLEDELga 331
Cdd:TIGR04523 424 LEKEIERLKETIIK---NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkiKQNLEQKQKELKSKEKEL-- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 332 rSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALarrrrqNASALDCDLRasqaalf 411
Cdd:TIGR04523 499 -KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL------KKENLEKEID------- 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 412 EKNKELADLKHVHGKLKKQfQEKVAELahanrrVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQT 491
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKK-QEEKQEL------IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
250
....*....|....
gi 755526634 492 EQSENLQVQLEHLQ 505
Cdd:TIGR04523 638 SKKNKLKQEVKQIK 651
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-513 |
1.53e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 316 DELGRMSEDLEDELGARSSMD--RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAqvgDLEEALARRRR 393
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEdaREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL---ELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 394 QNASALDCDLRASQAALFEKNKELADLKHVH----GKLKKQFQekvAELAHANRRVEQHETEVKKLRLRVEELKKELAQA 469
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIrgngGDRLEQLE---REIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755526634 470 EDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-495 |
2.50e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 104 REKWSKVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGVHsaadkthdgpepEREQEPVR 183
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI------------ARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 184 DIGAERppgsQELDLVESLLKSRPEepegcwdacsvaaggprvssgrqdrnrlpwEDTASTEEDASKLTALRLRLDESQK 263
Cdd:COG1196 313 ELEERL----EELEEELAELEEELE------------------------------ELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 264 VLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMS---EDLEDELGARSSMDRKMA 340
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErleEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 341 ELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDCDLRA---SQAALFEKNKEL 417
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegfLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 418 ADLKHVHGKL---KKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQS 494
Cdd:COG1196 519 LRGLAGAVAVligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
.
gi 755526634 495 E 495
Cdd:COG1196 599 A 599
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
258-506 |
6.28e-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: 49.25 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 258 LDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKethqdelgrmsEDLEDELGARSSMDR 337
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE-----------KEKLNIQKNIDKIKN 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 338 KMAELRGEMERLQAENAaewgRRERLETEKLGLERENKKLRAQVGDLEEalarrrrqnasaldcDLRASQAALFEKNKEL 417
Cdd:TIGR04523 195 KLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEKKQQ---------------EINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 418 ADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKK------------ELAQAEDELDEAHNQARKLQR 485
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNK 335
|
250 260
....*....|....*....|.
gi 755526634 486 SLDEQTEQSENLQVQLEHLQS 506
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSES 356
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
266-541 |
8.98e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 266 LKEREDKLA-LSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKET------HQDELGRMSEDLEDELGARSSMDRK 338
Cdd:PRK01156 192 LKSSNLELEnIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAlnelssLEDMKNRYESEIKTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 339 MAELRGEMERL-QAENAAEWGRRERLeteklgleRENKKLRAQVGDLEEALARRRRQNASALDC-----DLRASQAALFE 412
Cdd:PRK01156 272 NNYYKELEERHmKIINDPVYKNRNYI--------NDYFKYKNDIENKKQILSNIDAEINKYHAIikklsVLQKDYNDYIK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 413 KNKELADLKHVHGKLKK---QFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARklqRSLDE 489
Cdd:PRK01156 344 KKSRYDDLNNQILELEGyemDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEIN---VKLQD 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 755526634 490 QTEQSENLQVQLEHLQSRLRRQQQNAP-LFGKIRSTRFGTEEAGDGASDLDED 541
Cdd:PRK01156 421 ISSKVSSLNQRIRALRENLDELSRNMEmLNGQSVCPVCGTTLGEEKSNHIINH 473
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
337-502 |
9.69e-06 |
|
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: 47.23 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 337 RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcdlrasqaalfekNKE 416
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-------------NKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 417 LADLKHvhgklkkqfqekvaELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 496
Cdd:COG1579 91 YEALQK--------------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....*.
gi 755526634 497 LQVQLE 502
Cdd:COG1579 157 ELEELE 162
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
359-513 |
9.72e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 359 RRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDC--------DLRASQAALFEKNKELAD----------L 420
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeiDVASAEREIAELEAELERldassddlaaL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 421 KHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQ---ARKLQRSLDEQTEQ-SEN 496
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERElREN 770
|
170
....*....|....*..
gi 755526634 497 LQVQLEHLQSRLRRQQQ 513
Cdd:COG4913 771 LEERIDALRARLNRAEE 787
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-515 |
9.84e-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: 48.51 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 358 GRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASaLDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAE 437
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 438 LAHANRRVEQHE-------TEVKKLRLRVEELKKELAQAEDELDEAHNQ---ARKLQRSLDEQTEQSENLQVQLEHLQSR 507
Cdd:TIGR02168 318 LEELEAQLEELEskldelaEELAELEEKLEELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIAS 397
|
....*...
gi 755526634 508 LRRQQQNA 515
Cdd:TIGR02168 398 LNNEIERL 405
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
225-508 |
2.34e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 225 RVSSGRQDRNRLPWEDTASTEEDASKLTALRLRLDESQKvLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEML 304
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK-LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 305 KQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAenaaewgRRERLETEKLGLERENKKLRAqvgdl 384
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN-------TRESLETQLKVLSRSINKIKQ----- 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 385 eealarrrrqnasaldcDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKK 464
Cdd:TIGR04523 483 -----------------NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 755526634 465 ELAQAEDELDEahNQARKLQRSLDEQTEQSENLQVQLEHLQSRL 508
Cdd:TIGR04523 546 ELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-449 |
3.22e-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: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 116 RAREEVRQLRQRL---DTLTKELAGARRERQEAQGECEARGRELARLRGVHSAADKTHdgpepEREQEPVRDIGAErppg 192
Cdd:COG1196 219 KEELKELEAELLLlklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL-----EELELELEEAQAE---- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 193 sqeldlvESLLKSRPEEPEgcwdacsvaaggprvssgrQDRNRLpwedtasteedASKLTALRLRLDESQKVLLKEREDK 272
Cdd:COG1196 290 -------EYELLAELARLE-------------------QDIARL-----------EERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 273 LALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARssmdRKMAELRGEMERLQAE 352
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL----RAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 353 NAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcDLRASQAALFEKNKELADLKHVHGKLKKQFQ 432
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLEEAALLEAALAELLEELA 487
|
330
....*....|....*..
gi 755526634 433 EKVAELAHANRRVEQHE 449
Cdd:COG1196 488 EAAARLLLLLEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-394 |
3.64e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 112 AERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLrgvhSAADKTHDGPEPEREQEPVRDIGAERpp 191
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL----NKKIKDLGEEEQLRVKEKIGELEAEI-- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 192 gsQELDLVESLLKSRPEEPEGcwdacsvaaggpRVSSGRQDRNRLPWEDTA---STEEDASKLTALRLRLDESQKVLLKE 268
Cdd:TIGR02169 304 --ASLERSIAEKERELEDAEE------------RLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 269 REDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILkethQDELGRMSEDLEDELGARSSMDRKMAELRGEMER 348
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL----QEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 755526634 349 LQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQ 394
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
301-519 |
3.73e-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: 46.43 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 301 QEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQ 380
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 381 VGDLEEALArRRRQNASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVE 460
Cdd:pfam07888 117 KDALLAQRA-AHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755526634 461 ELKKELAQAEDELDEAHNQARKLQRSLDE---QTEQSENLQVQLEHLQSRLRRQQQNAPLFG 519
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTLTQKLTTahrKEAENEALLEELRSLQERLNASERKVEGLG 257
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
315-516 |
4.58e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 315 QDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAewgrrerLETEKLGLERENKKLRAQVGDLEEALARRRRQ 394
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-------LQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 395 ------NASALDCDLRASQAAlfeknkELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQ 468
Cdd:COG3883 95 lyrsggSVSYLDVLLGSESFS------DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 755526634 469 AEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAP 516
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
248-442 |
8.25e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 248 ASKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLED 327
Cdd:COG4942 54 LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 328 ELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASaLDCDLRASQ 407
Cdd:COG4942 134 AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR-LEKELAELA 212
|
170 180 190
....*....|....*....|....*....|....*
gi 755526634 408 AALFEKNKELADLKHVHGKLKKQFQEKVAELAHAN 442
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
240-543 |
8.33e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 240 DTASTEEDASKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQwkikYEELSKTKQEMLKQLsilkethQDELG 319
Cdd:PRK02224 305 DDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD----LEERAEELREEAAEL-------ESELE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 320 RMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALA---------- 389
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaealleagk 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 390 --------------------RRRRQNASALDCDLRASQAALFEKNKELADLKhvhgKLKKQFQEKVAELAHANRRVEQHE 449
Cdd:PRK02224 454 cpecgqpvegsphvetieedRERVEELEAELEDLEEEVEEVEERLERAEDLV----EAEDRIERLEERREDLEELIAERR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 450 TEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAPLFGKIRSTRFGTE 529
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIE 609
|
330
....*....|....
gi 755526634 530 EAGDGASDLDEDED 543
Cdd:PRK02224 610 RLREKREALAELND 623
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
369-516 |
9.17e-05 |
|
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: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 369 GLERENKKLRAQVGDLE--EALARRRRQNASALD-CDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRV 445
Cdd:COG4913 239 RAHEALEDAREQIELLEpiRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755526634 446 EQHETEVKKLRL--------RVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAP 516
Cdd:COG4913 319 DALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
259-504 |
1.26e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.92 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 259 DESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQL-SILKETHqdelgrmsEDLEDELgarSSMDR 337
Cdd:PRK05771 39 ELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELiKDVEEEL--------EKIEKEI---KELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 338 KMAELRGEMERLQAEnaaewgrRERLE-----TEKLGLERENKKLRAQVGDLEEALarrrrqnasaldcDLRASQAALFE 412
Cdd:PRK05771 108 EISELENEIKELEQE-------IERLEpwgnfDLDLSLLLGFKYVSVFVGTVPEDK-------------LEELKLESDVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 413 KNKELADLKHVHG----KLKKQFQEKVAELA-HANRRVEQHET-----EVKKLRLRVEELKKELAQAEDELDEAHNQARK 482
Cdd:PRK05771 168 NVEYISTDKGYVYvvvvVLKELSDEVEEELKkLGFERLELEEEgtpseLIREIKEELEEIEKERESLLEELKELAKKYLE 247
|
250 260
....*....|....*....|..
gi 755526634 483 LQRSLDEQTEQSENLQVQLEHL 504
Cdd:PRK05771 248 ELLALYEYLEIELERAEALSKF 269
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-544 |
1.71e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 111 RAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGVHSAADkthdgpepEREQEPVRDIGAERp 190
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE--------AELAEAEEELEELA- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 191 pgSQELDLVESLLKSRPEEpegcwdacsvAAGGPRVSSGRQDRNRLPWE---DTASTEEDASKLTALRLRLDESQKVLLK 267
Cdd:COG1196 386 --EELLEALRAAAELAAQL----------EELEEAEEALLERLERLEEEleeLEEALAELEEEEEEEEEALEEAAEEEAE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 268 EREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARSSM-DRKMAELRG-- 344
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlAGAVAVLIGve 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 345 -EMERLQAENAAEWGRRERLETEKLGLER-----ENKKLRAQVGDLEEALARRRRQNASA----------LDCDLRASQA 408
Cdd:COG1196 534 aAYEAALEAALAAALQNIVVEDDEVAAAAieylkAAKAGRATFLPLDKIRARAALAAALArgaigaavdlVASDLREADA 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 409 ALFEKNKELADL----------KHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHN 478
Cdd:COG1196 614 RYYVLGDTLLGRtlvaarleaaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755526634 479 QARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAPLFGKIRSTRFGTEEAGDGASDLDEDEDL 544
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
276-507 |
1.83e-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: 44.24 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 276 SKNIEKLEGELSQWKIKYEELSKTKQEML------------KQLSILK----ETHQ--DELGRMSEDLEDEL----GARS 333
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNNQKEQDWnkelkselknqeKKLEEIQnqisQNNKiiSQLNEQISQLKKELtnseSENS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 334 SMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALaRRRRQNASALDCDLRASQAALFEK 413
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI-KKLQQEKELLEKEIERLKETIIKN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 414 NKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQ 493
Cdd:TIGR04523 439 NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
250
....*....|....
gi 755526634 494 SENLQVQLEHLQSR 507
Cdd:TIGR04523 519 ISSLKEKIEKLESE 532
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
109-500 |
2.03e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 109 KVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQgECEARGRELARLRGVHSAADKTHDGPEPEREQEPVRDigAE 188
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK--AE 1460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 189 RPPGSQELDLVESLLKSRPEEPEGCWDAcsvaagGPRVSSGRQDRNRLPWEDTASTEEDASKLTALRLRLDESQKVLLKE 268
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEA------KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 269 REDKLALSKNIEKLEgELSqwkiKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMER 348
Cdd:PTZ00121 1535 KADEAKKAEEKKKAD-ELK----KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 349 LQAENAAEwgrrERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDCDL--RASQAALFEKNKELADLKHVHGK 426
Cdd:PTZ00121 1610 EEAKKAEE----AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEE 1685
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755526634 427 LKKQFQEKVAELAHANRRVEQ----HETEVKKlrlrVEELKKELAQAEDELDEAHNQARKLQRSLDE-QTEQSENLQVQ 500
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEElkkkEAEEKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEaKKDEEEKKKIA 1760
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-515 |
2.06e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 104 REKWSKVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGVHSAADKTHDGPEPEREQEPVR 183
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 184 DIGAERPPGSQELDLVESLLksrpeepegcwdacsvaaggprvssgRQDRNRLPWEDTASTEEDASKLTALRLRLDESQK 263
Cdd:COG4717 160 ELEEELEELEAELAELQEEL--------------------------EELLEQLSLATEEELQDLAEELEELQQRLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 264 VLLKEREDKLALSKNIEKLEGELSQWKIkYEELSKTKQ---------EMLKQLSILKETHQDELGRMSEDLEDELGARSS 334
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAAL-EERLKEARLllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 335 MDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDCDLRASQAALFEKN 414
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 415 KELADLKHV--------HGKLKKQFQEKVAELAHANRRVEQHETEVK---------KLRLRVEELKKELAQAEDELDEAH 477
Cdd:COG4717 373 AALLAEAGVedeeelraALEQAEEYQELKEELEELEEQLEELLGELEellealdeeELEEELEELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|....*...
gi 755526634 478 NQARKLQRSLdEQTEQSENLQVQLEHLQSRLRRQQQNA 515
Cdd:COG4717 453 EELAELEAEL-EQLEEDGELAELLQELEELKAELRELA 489
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
109-549 |
2.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 109 KVRAERNRAREEvrqLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGVHSAADKTHDGPEPEREQEPVRDIGAE 188
Cdd:PTZ00121 1308 KKKAEEAKKADE---AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 189 RPpgSQELDLVESLLKSRPEEPEGCWDACSVAAGGPRVSSGRQDRNRLPWEDTASTE-EDASKLTALRLRLDESQKV--L 265
Cdd:PTZ00121 1385 KK--AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKKAeeA 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 266 LKERED---------KLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQ---DELGRMSEDLEDELGARS 333
Cdd:PTZ00121 1463 KKKAEEakkadeakkKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkkaDEAKKAEEAKKADEAKKA 1542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 334 SMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLR----AQVGDLEEALARRRRQNASALDCDLRASQAA 409
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 410 lfEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDE 489
Cdd:PTZ00121 1623 --EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 490 QTEQSENLQVQLEHLQSRLRRQQQNAPLFGKIRSTRFGTEEAGDGASDLDEDEDLQIQVA 549
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-390 |
3.29e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 104 REKWSKVRAERNRAREEVRQLRQRLDTLTKELAGARRER-------QEAQGECEARGRELARLrgvhsaadkthdgpEPE 176
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeiEELQKELYALANEISRL--------------EQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 177 REQEPVRDIGAERPPGSQELDLVEslLKSRPEEpegcwDACSVAAGGPRVSSGRQDRNRLPwedtASTEEDASKLTALRL 256
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEE--LESKLDE-----LAEELAELEEKLEELKEELESLE----AELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 257 RLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEEL----SKTKQEMLKQLSILKETHQDELGRMSEDLEDELgar 332
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrrERLQQEIEELLKKLEEAELKELQAELEELEEEL--- 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 755526634 333 ssmdrkmAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALAR 390
Cdd:TIGR02168 450 -------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
342-501 |
3.59e-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: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 342 LRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASaldcdlrasqaalfekNKELADLK 421
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSN----------------LKEISDLE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 422 HVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEElkkELAQAEDELDEAHNQA---RKLQRSLDEQTEQSENLQ 498
Cdd:pfam15294 195 EKMAALKSDLEKTLNASTALQKSLEEDLASTKHELLKVQE---QLEMAEKELEKKFQQTaayRNMKEMLTKKNEQIKELR 271
|
...
gi 755526634 499 VQL 501
Cdd:pfam15294 272 KRL 274
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
267-510 |
3.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 267 KEREDKLALSKNIEKLEGElsqwkiKYEELSKTKQEMlkqlsilkethqDELGRMSEDLEDELGARSSMDRKMAELRGEM 346
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKE------KEKELEEVLREI------------NEISSELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 347 ERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALdcDLRASQAALFEKNKELADLKHVHGK 426
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE--EYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 427 LKKQ---FQEKVAELAHANRRVEQHETEVKKLRLRVEELKK------ELAQAEDELDE-----AHNQARKLQRSLDEQTE 492
Cdd:PRK03918 319 LEEEingIEERIKELEEKEERLEELKKKLKELEKRLEELEErhelyeEAKAKKEELERlkkrlTGLTPEKLEKELEELEK 398
|
250
....*....|....*...
gi 755526634 493 QSENLQVQLEHLQSRLRR 510
Cdd:PRK03918 399 AKEEIEEEISKITARIGE 416
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
439-513 |
4.08e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755526634 439 AHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-515 |
4.18e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 111 RAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGVHSAADKthdgpEPEREQEPVRDIGAERp 190
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE-----ELEELEEELEEAEEEL- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 191 pgSQELDLVESLLKSRPEEpegcwdacsvaaggprvSSGRQDRNRLPWEDTASTEEDASKLTALRLRLDESQKVLLKERE 270
Cdd:COG1196 354 --EEAEAELAEAEEALLEA-----------------EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 271 DKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQ 350
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 351 AENAAEWGRRERLETEKLGLERENKKLRAQVGD------------LEEALARRRRQNASALDCDLRASQAALFEKNKELA 418
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvligveaayeaaLEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 419 DLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQ 498
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
410
....*....|....*..
gi 755526634 499 VQLEHLQSRLRRQQQNA 515
Cdd:COG1196 655 GGSAGGSLTGGSRRELL 671
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
374-496 |
4.70e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 374 NKKLRAQVGDLEEALARRRRQnasaldcdLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAEL------------AHA 441
Cdd:PRK04863 987 NEKLRQRLEQAEQERTRAREQ--------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELqdlgvpadsgaeERA 1058
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 755526634 442 NRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 496
Cdd:PRK04863 1059 RARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
406-511 |
5.14e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 406 SQAALFEKNKELADLKHvhgKLKKQFQEKVAELAHANRRVEQHE-------TEVKKLRLRVEELKKELAQAEDELDEAHN 478
Cdd:PRK12704 55 KKEALLEAKEEIHKLRN---EFEKELRERRNELQKLEKRLLQKEenldrklELLEKREEELEKKEKELEQKQQELEKKEE 131
|
90 100 110
....*....|....*....|....*....|....*....
gi 755526634 479 QARKLQRSLDEQTEQSENL------QVQLEHLQSRLRRQ 511
Cdd:PRK12704 132 ELEELIEEQLQELERISGLtaeeakEILLEKVEEEARHE 170
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
258-516 |
5.34e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 258 LDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDE----LGRMS-EDLEDEL--- 329
Cdd:PRK11281 54 LEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEtretLSTLSlRQLESRLaqt 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 330 -------------------GARSSMDRKMAELRGEMERLQ-----------AENAAEWGRRERLETEKLGLERENKKLR- 378
Cdd:PRK11281 134 ldqlqnaqndlaeynsqlvSLQTQPERAQAALYANSQRLQqirnllkggkvGGKALRPSQRVLLQAEQALLNAQNDLQRk 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 379 -AQVGDLEEALARRRRqnasaldcDLRASQAALFEknKELADLKHV-HGKLKKQFQEKVAELAHANRRVE-QHETEVKKL 455
Cdd:PRK11281 214 sLEGNTQLQDLLQKQR--------DYLTARIQRLE--HQLQLLQEAiNSKRLTLSEKTVQEAQSQDEAARiQANPLVAQE 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755526634 456 RLRVEELKKELAQAEDELDEAHNQARKLQRSLDE--QTEQseNLQVQLEHLQ-----SR-LRRQQQNAP 516
Cdd:PRK11281 284 LEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRltQSER--NIKEQISVLKgslllSRiLYQQQQALP 350
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
405-493 |
5.91e-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: 42.44 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 405 ASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQ 484
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
....*....
gi 755526634 485 RSLDEQTEQ 493
Cdd:COG4942 97 AELEAQKEE 105
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
430-514 |
6.10e-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: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 430 QFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHlqsRLR 509
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---RAR 93
|
....*
gi 755526634 510 RQQQN 514
Cdd:COG3883 94 ALYRS 98
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
370-514 |
6.10e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 370 LERENKKLRAQVGDLEEALARRRRQNAsaldcDLRASQAALFEKNKELADLKHVHGKL-----KKQFQEKVAELAHANRR 444
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEE-----ELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755526634 445 VEQHETEVKKLRLRVEELKKELAQAEDELDEA--------HNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQN 514
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
345-497 |
6.50e-04 |
|
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: 41.93 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 345 EMERLQAEnaAEW---------GRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNaSALDCDLRASQAALFEKNK 415
Cdd:smart00787 124 TFARLEAK--KMWyewrmklleGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRK-DALEEELRQLKQLEDELED 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 416 ----ELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQT 491
Cdd:smart00787 201 cdptELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQL 280
|
....*.
gi 755526634 492 EQSENL 497
Cdd:smart00787 281 KLLQSL 286
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-480 |
7.55e-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: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 241 TASTEEDASKLTALRLRLDESQKVL-------------LKEREDKLA-LSKNIEKLEGELSQWKIKYEELSKTKQEMLKQ 306
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELaalkkeekallkqLAALERRIAaLARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 307 LsilkethqdelgrmsEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLeteklgLERENKKLRAQVGDLEE 386
Cdd:COG4942 99 L---------------EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY------LKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 387 ALARRRRQNASAldcdlrasQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKEL 466
Cdd:COG4942 158 DLAELAALRAEL--------EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....
gi 755526634 467 AQAEDELDEAHNQA 480
Cdd:COG4942 230 ARLEAEAAAAAERT 243
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
398-515 |
7.57e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 42.53 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 398 ALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAH 477
Cdd:COG5283 4 ILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLS 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 755526634 478 NQARKLQRSLdEQTEQsenlqvQLEHLQSRLRR--QQQNA 515
Cdd:COG5283 84 AAQRRLRSSL-EQTNR------QLERQQQRLARlgARQDR 116
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
238-473 |
7.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 238 WEDTASTEEDASKLTALRLRLDesqkvlLKEREDKLALSKN-IEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQD 316
Cdd:COG4913 261 AERYAAARERLAELEYLRAALR------LWFAQRRLELLEAeLEELRAELARLEAELERLEARLDALREELDELEAQIRG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 317 ELGrmsedledelgarssmdRKMAELRGEMERLQAEnaaewgrRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNA 396
Cdd:COG4913 335 NGG-----------------DRLEQLEREIERLERE-------LEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755526634 397 SALDcDLRASQAALFEknkELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRlrvEELKKELAQAEDEL 473
Cdd:COG4913 391 ALLE-ALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALR---DALAEALGLDEAEL 460
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
243-508 |
9.94e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 243 STEEDASKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQD-----E 317
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKaeeyiK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 318 LGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKL----------RAQVGDLEEA 387
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerhelyeeaKAKKEELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 388 LARRRRQNASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEK---VAELAHANRRV--------EQHETEV-KKL 455
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELkkaIEELKKAKGKCpvcgreltEEHRKELlEEY 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 755526634 456 RLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQV--QLEHLQSRL 508
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKL 512
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
249-510 |
1.37e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 249 SKLTALRLRL------DESQKVLLKE----REDKLALSKNIEKLEGELSQwkiKYEELSKTKQEmLKQLSILKETHQDEL 318
Cdd:TIGR04523 194 NKLLKLELLLsnlkkkIQKNKSLESQiselKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQ-LNQLKDEQNKIKKQL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 319 GRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWgrrerleteklglereNKKLRAQVGDLEEALarrrrqnaSA 398
Cdd:TIGR04523 270 SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW----------------NKELKSELKNQEKKL--------EE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 399 LDCDLRASQAALFEKNKELADLKHV-------HGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAED 471
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKEltnseseNSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405
|
250 260 270
....*....|....*....|....*....|....*....
gi 755526634 472 ELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRR 510
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
280-514 |
1.52e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 280 EKLEGELSQWKIKYEELSKTKQEM--LKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEW 357
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELeeMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 358 GRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNAsaldcDLRASQAALFEKNKELA-DLKHVHGKLKKQFQEKVA 436
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNI-----ELTAHCDKLLLENKELTqEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 437 ELAHANRRVEQHETEVKK---LRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKemnLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
.
gi 755526634 514 N 514
Cdd:pfam05483 605 N 605
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
250-518 |
1.61e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 250 KLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWK--IKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLED 327
Cdd:COG5022 770 RIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKeyRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQ 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 328 ELGaRSSMDRKMAELrgemerLQAENAAEWG--RRERLETEKLGLERENKKLrAQVGDLEEALARRRRQNASALDCDLRA 405
Cdd:COG5022 850 KFG-RSLKAKKRFSL------LKKETIYLQSaqRVELAERQLQELKIDVKSI-SSLKLVNLELESEIIELKKSLSSDLIE 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 406 SqaaLFEKNKELADLKHVhgKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQR 485
Cdd:COG5022 922 N---LEFKTELIARLKKL--LNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN 996
|
250 260 270
....*....|....*....|....*....|...
gi 755526634 486 SLDEQTEQSENLQVQLEHLQSRLRRQQQNAPLF 518
Cdd:COG5022 997 FKKELAELSKQYGALQESTKQLKELPVEVAELQ 1029
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
374-496 |
1.65e-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: 41.48 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 374 NKKLRAQVGDLEEALARRRRQnasaldcdLRASQAALFEKNKELADLKHVHG---KLKKQFQEKVAEL---------AHA 441
Cdd:COG3096 986 NEKLRARLEQAEEARREAREQ--------LRQAQAQYSQYNQVLASLKSSRDakqQTLQELEQELEELgvqadaeaeERA 1057
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 755526634 442 NRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 496
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
337-500 |
1.66e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 337 RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARR----RRQNASALDCDLRASQAALFE 412
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 413 KNKELADLKHVHGKLKKQFQEKVAELAHANRRV-EQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQT 491
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
....*....
gi 755526634 492 EQSENLQVQ 500
Cdd:COG4717 234 NELEAAALE 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-515 |
1.87e-03 |
|
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: 41.20 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 370 LERENKKLRAQVgdleEALARRRRQNASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHE 449
Cdd:TIGR02168 198 LERQLKSLERQA----EKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755526634 450 TEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNA 515
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
231-513 |
2.01e-03 |
|
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: 40.83 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 231 QDRNRLPWEDTASTEEDASKLTALRLRLdESQKVLLKEREDKL-ALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSI 309
Cdd:pfam05622 158 EERNAEYMQRTLQLEEELKKANALRGQL-ETYKRQVQELHGKLsEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDT 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 310 LKETHqDELgRMSEDLEDELGARSSMDRKMAELRGEM--ERLQAEnaaewgRRERLETeklgLERENKKLR-AQVGDLEE 386
Cdd:pfam05622 237 LRETN-EEL-RCAQLQQAELSQADALLSPSSDPGDNLaaEIMPAE------IREKLIR----LQHENKMLRlGQEGSYRE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 387 ALArrrrqnasaldcdlrASQAALFEKNKELADLKhvhgklkkqfqekvAELAHANRRVeqhetevKKLRLRVEE----- 461
Cdd:pfam05622 305 RLT---------------ELQQLLEDANRRKNELE--------------TQNRLANQRI-------LELQQQVEElqkal 348
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755526634 462 ------------LKKELAQAEDELDEAHNQARKLQRSLDE-QTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:pfam05622 349 qeqgskaedsslLKQKLEEHLEKLHEAQSELQKKKEQIEElEPKQDSNLAQKIDELQEALRKKDE 413
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
375-477 |
2.04e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.82 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 375 KKLRAQVGDLEEALARRRR----QNASALDCDLRASQaalfeknKELADLKHVHGKLKKQfqekVAELAHANRRVEQHET 450
Cdd:PRK05431 5 KLIRENPEAVKEALAKRGFpldvDELLELDEERRELQ-------TELEELQAERNALSKE----IGQAKRKGEDAEALIA 73
|
90 100
....*....|....*....|....*..
gi 755526634 451 EVKKLRLRVEELKKELAQAEDELDEAH 477
Cdd:PRK05431 74 EVKELKEEIKALEAELDELEAELEELL 100
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
370-513 |
2.11e-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: 39.14 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 370 LERENKKLRAQVGDLEEALARRRRQNASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHE 449
Cdd:pfam08614 19 LEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755526634 450 TEVKKLRLRVEELKKELAQAEDELDEahnqarkLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:pfam08614 99 RRLAALEAERAQLEEKLKDREEELRE-------KRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
340-508 |
2.28e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 340 AELRGEMERLQAEnaaewgrRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASAL-DCDL-RASQAALFEKNKEL 417
Cdd:PRK02224 247 EERREELETLEAE-------IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaEAGLdDADAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 418 AD----LKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQ 493
Cdd:PRK02224 320 EDrdeeLRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
170
....*....|....*
gi 755526634 494 SENLQVQLEHLQSRL 508
Cdd:PRK02224 400 FGDAPVDLGNAEDFL 414
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
254-514 |
2.35e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 254 LRLRLDESQKVllKEREDKLALS-KNIEKLEGELSQWKIKYE-------ELSKTKQEMLKQLSILKETHQDELGRMSEDL 325
Cdd:pfam01576 7 MQAKEEELQKV--KERQQKAESElKELEKKHQQLCEEKNALQeqlqaetELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 326 EDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEA---LARRRRQNASALDcD 402
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQnskLSKERKLLEERIS-E 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 403 LRASQAALFEKNKELADLKHVHGKLKKQFQEKVA-------ELAHANRRVEQHETEVK----KLRLRVEELKKELAQAED 471
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeekgrqELEKAKRKLEGESTDLQeqiaELQAQIAELRAQLAKKEE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 755526634 472 ELDEAhnqarklQRSLDEQTEQSENLQVQLEHLQSRLRRQQQN 514
Cdd:pfam01576 244 ELQAA-------LARLEEETAQKNNALKKIRELEAQISELQED 279
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
373-500 |
2.38e-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: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 373 ENKKLRAQVGDLEEALARRRRQnasaldcdLRASQAALFEKNKELADLKHVHGKLKK----------------QFQEKV- 435
Cdd:COG3096 279 ERRELSERALELRRELFGARRQ--------LAEEQYRLVEMARELEELSARESDLEQdyqaasdhlnlvqtalRQQEKIe 350
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755526634 436 ---AELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQteQSENLQVQ 500
Cdd:COG3096 351 ryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQ--QTRAIQYQ 416
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
243-510 |
2.39e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 243 STEEDASKLTALRLRLDE--SQKVLLKEREDKL-----ALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQ 315
Cdd:COG1340 2 KTDELSSSLEELEEKIEElrEEIEELKEKRDELneelkELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 316 DELGRMSEdLEDELGARSSMDRKMAELRGEMERLQAENAAEwgrRERLETEKLGLEREnKKLRAQVGDLEEALARRRRQN 395
Cdd:COG1340 82 ELNEKLNE-LREELDELRKELAELNKAGGSIDKLRKEIERL---EWRQQTEVLSPEEE-KELVEKIKELEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 396 asaldcdlrasqaalfEKNKELADLKhvhgklkKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDE 475
Cdd:COG1340 157 ----------------EKNEKLKELR-------AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE 213
|
250 260 270
....*....|....*....|....*....|....*
gi 755526634 476 AHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRR 510
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRELRKELKK 248
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
108-508 |
2.55e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 108 SKVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELA----RLRGVHSAADKTHDGPEPEREQEPV- 182
Cdd:pfam15921 324 STVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGnlddQLQKLLADLHKREKELSLEKEQNKRl 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 183 --RDIG---------AERPPGSQELDLVESLLKSRPEEPEGCWDACSVAAGGPRVSSGRQDRNRLPWEDTAST-EEDASK 250
Cdd:pfam15921 404 wdRDTGnsitidhlrRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMlRKVVEE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 251 LTALRLRLDESQKVL------LKEREDKL-ALSKNIEKLEgelSQWKIKYEELS--KTKQEMLKQLSILKET---HQDEL 318
Cdd:pfam15921 484 LTAKKMTLESSERTVsdltasLQEKERAIeATNAEITKLR---SRVDLKLQELQhlKNEGDHLRNVQTECEAlklQMAEK 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 319 GRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRReRLETEKLGLERENK-----KLRAQVGDLEeaLARRRR 393
Cdd:pfam15921 561 DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDR-RLELQEFKILKDKKdakirELEARVSDLE--LEKVKL 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 394 QNASALdcDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDEL 473
Cdd:pfam15921 638 VNAGSE--RLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 755526634 474 D-------EAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRL 508
Cdd:pfam15921 716 KsmegsdgHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
275-504 |
2.67e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 275 LSKNIEKLEGELSQWKIKYEE-LSKTKQEMLKQLSILKE--THQDELGRMSEDLEDELGAR-SSMDRKMAELRGEMErlq 350
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEarTERDQFSQESGNLDDQLQKLlADLHKREKELSLEKE--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 351 aENAAEWGR-----------RERLETEKLGLERENKKLRAQ----VGDLEEALARRRRQN-----ASALDCDLRASQAAL 410
Cdd:pfam15921 399 -QNKRLWDRdtgnsitidhlRRELDDRNMEVQRLEALLKAMksecQGQMERQMAAIQGKNeslekVSSLTAQLESTKEML 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 411 FEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQ---AEDELDEAHNQARKLQRSL 487
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknEGDHLRNVQTECEALKLQM 557
|
250
....*....|....*..
gi 755526634 488 DEQTEQSENLQVQLEHL 504
Cdd:pfam15921 558 AEKDKVIEILRQQIENM 574
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
347-514 |
3.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 347 ERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcDLRASQAALFEKNKELADLKHVHGK 426
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE-ELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 427 LKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQS 506
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
....*...
gi 755526634 507 RLRRQQQN 514
Cdd:COG4372 165 ELAALEQE 172
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
239-508 |
4.81e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 239 EDTASTEEDASKLT----ALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMlkqlsilkETH 314
Cdd:pfam01576 138 EDILLLEDQNSKLSkerkLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQEL--------EKA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 315 QDELGRMSEDLEDELgarSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRR-- 392
Cdd:pfam01576 210 KRKLEGESTDLQEQI---AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERaa 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 393 RQNASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHA-NRRVEQHETEVKKLRLR----VEELKKELA 467
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKAlEEETRSHEAQLQEMRQKhtqaLEELTEQLE 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 755526634 468 QA--------------EDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRL 508
Cdd:pfam01576 367 QAkrnkanlekakqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARL 421
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
240-511 |
4.91e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 240 DTASTEEDASKLTALRLRLDESQKVLlkeredklalskniEKLEGELSQWKIKYEELSKTKQEMLKQLSILkETHQDELG 319
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDL--------------AALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 320 RMSEDLEDELGARSSMDRKMAELRGEmERLQAENAAEWGRRERLEteklgLERENKKLRAQVGDLEEALARRRRQNAS-- 397
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLE-ERFAAALGDAVERELREN-----LEERIDALRARLNRAEEELERAMRAFNRew 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 398 -ALDCDLRASQAALFEKNKELADLKHVH-----GKLKKQFQE-KVAELAHANRRVEQHETEVKKlrlRVEELKKELAQ-- 468
Cdd:COG4913 801 pAETADLDADLESLPEYLALLDRLEEDGlpeyeERFKELLNEnSIEFVADLLSKLRRAIREIKE---RIDPLNDSLKRip 877
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 755526634 469 ----------AEDELDEAHNQARKLQRSLDEQT-----EQSENLQVQLEHLQSRLRRQ 511
Cdd:COG4913 878 fgpgrylrleARPRPDPEVREFRQELRAVTSGAslfdeELSEARFAALKRLIERLRSE 935
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
446-515 |
5.25e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 5.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 446 EQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNA 515
Cdd:PRK12704 71 NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-498 |
5.50e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 111 RAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGVHSAADKTHDGPEPeREQEPVRDIGAERP 190
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEEL-RKAEDARKAEAARK 1207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 191 pgSQELDLVESLLKS----RPEEPEGCWDACSVAAGGPRVSSGRQDRNRLPWEDtASTEEDASKLTALRL----RLDESQ 262
Cdd:PTZ00121 1208 --AEEERKAEEARKAedakKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE-ARMAHFARRQAAIKAeearKADELK 1284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 263 KVLLKEREDKLALSKNIEKLE--GELSQWKIKYEELSKTKQEMLKQLSILKETHQ-----DELGRMSEDLEDELGARSSM 335
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeakkaAEAAKAEAEAAADEAEAAEE 1364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 336 DRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEA------LARRRRQNASALDCDLRASQAA 409
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkkkadeAKKKAEEKKKADEAKKKAEEAK 1444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 410 LFEKNKELADLKHVHGKLKKQFQEK-----VAELAHANRRVEQHETEVKKLRLRVEELKK--ELAQAEDELDEAHNQARK 482
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAkkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKA 1524
|
410
....*....|....*.
gi 755526634 483 LQRSLDEQTEQSENLQ 498
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAK 1540
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
116-513 |
6.42e-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: 39.55 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 116 RAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGVHSAADKTHDGPEP--EREQEPVRdigAERPPGS 193
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlNLVQTALR---QQEKIER 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 194 QELDLVEslLKSRPEEPEGcwdacsVAAGGPRVSSGRQDRNRLPWEDTastEEDASKLTALRLRLDESQKVLLKEREDKL 273
Cdd:COG3096 352 YQEDLEE--LTERLEEQEE------VVEEAAEQLAEAEARLEAAEEEV---DSLKSQLADYQQALDVQQTRAIQYQQAVQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 274 ALSK----------NIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEthqdelgrmsedledelgARSSMDRKMAELR 343
Cdd:COG3096 421 ALEKaralcglpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA------------------ARRQFEKAYELVC 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 344 ---GEMERLQAENAAewgrRERLET---EKLGLERENKkLRAQVGDLEEALarRRRQNASALDCDLRASQAALFEKNKEL 417
Cdd:COG3096 483 kiaGEVERSQAWQTA----RELLRRyrsQQALAQRLQQ-LRAQLAELEQRL--RQQQNAERLLEEFCQRIGQQLDAAEEL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 418 ADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRlrveelkKELAQAEDELDEAHNQARKLQRSLDEQTEQSENL 497
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI-------KELAARAPAWLAAQDALERLREQSGEALADSQEV 628
|
410
....*....|....*.
gi 755526634 498 QVQLEHLQSRLRRQQQ 513
Cdd:COG3096 629 TAAMQQLLEREREATV 644
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
255-502 |
7.78e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 38.95 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 255 RLRLDESQKVLLKEREDKLALS----KNIEKLEGELSQwkikYEELSKTKQEMLKQLSILKETHQDELGRMSEDLE---- 326
Cdd:pfam17380 352 RIRQEERKRELERIRQEEIAMEisrmRELERLQMERQQ----KNERVRQELEAARKVKILEEERQRKIQQQKVEMEqira 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 327 DELGARSSMDRKMAELRG-EMERLQAENAAEWGRRERLETEklglERENKKLRAQVGDLEEALARRRRQNASALDCDLRA 405
Cdd:pfam17380 428 EQEEARQREVRRLEEERArEMERVRLEEQERQQQVERLRQQ----EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 406 S-QAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEdeldeahnqARKLQ 484
Cdd:pfam17380 504 RkQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE---------AMERE 574
|
250
....*....|....*...
gi 755526634 485 RSLDEQTEQSENLQVQLE 502
Cdd:pfam17380 575 REMMRQIVESEKARAEYE 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
266-511 |
8.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 266 LKEREDKLA-LSKNIEKLEGELSqwkiKYEELSKTKqEMLKQLSILKEthqdELGRMS-EDLEDELGARSSMDRKMAELR 343
Cdd:PRK03918 468 LKEIEEKERkLRKELRELEKVLK----KESELIKLK-ELAEQLKELEE----KLKKYNlEELEKKAEEYEKLKEKLIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 344 GEMERLqaenAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcdlrasqaalfEKNKELadlkhv 423
Cdd:PRK03918 539 GEIKSL----KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-----------ERLKEL------ 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 424 hgklkKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQT-EQSENLQVQLE 502
Cdd:PRK03918 598 -----EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELS 672
|
....*....
gi 755526634 503 HLQSRLRRQ 511
Cdd:PRK03918 673 RELAGLRAE 681
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
396-490 |
9.24e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 396 ASALDCDLRASQAALFEKNKELADLKHVHGKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDE 475
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90
....*....|....*
gi 755526634 476 AHNQARKLQRSLDEQ 490
Cdd:COG4942 95 LRAELEAQKEELAEL 109
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
432-504 |
9.74e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 38.69 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755526634 432 QEKVAELahaNRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARK-----------------LQRSLDEQTEQS 494
Cdd:COG2433 412 EEEIRRL---EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERReirkdreisrldreierLERELEEERERI 488
|
90
....*....|
gi 755526634 495 ENLQVQLEHL 504
Cdd:COG2433 489 EELKRKLERL 498
|
|
| |
