|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
244-513 |
3.98e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.36 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 244 TEEDTSKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLsilkETHQDELGRMSE 323
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL----EEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 324 DLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQnasaldcdL 403
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA--------L 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 404 RASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKL 483
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270
....*....|....*....|....*....|
gi 564394541 484 QRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
315-508 |
4.96e-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: 72.13 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 315 QDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQ 394
Cdd:pfam01576 888 EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKS 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 395 NASALDCDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELD 474
Cdd:pfam01576 968 SIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAS 1047
|
170 180 190
....*....|....*....|....*....|....
gi 564394541 475 EAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRL 508
Cdd:pfam01576 1048 RANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-513 |
5.45e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 241 TAGTEEDTSKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILK--------- 311
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkdlarleae 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 312 -ETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALAR 390
Cdd:TIGR02168 742 vEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 391 RR------RQNASALDCDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKK 464
Cdd:TIGR02168 822 LRerleslERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564394541 465 ELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
266-545 |
6.77e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 266 LKEREDKLALSKnIEKLEGELSQWKIKYEELSKTKQEMLKQLSILK---ETHQDELGRMSEDLEDELGARSSMDRKMAEL 342
Cdd:COG1196 222 LKELEAELLLLK-LRELEAELEELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 343 RGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcDLRASQAALFEKNKELADLKH 422
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-ELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 423 VHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLE 502
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564394541 503 HLQSRLRRQQQNAPLFGKIRSTRFGTEEAGDGASDLDEDEDLQ 545
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
275-515 |
5.61e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 275 LSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQD---ELGRMSEDLEDELGARSSMDRKMAELRGEMERLQA 351
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 352 ENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQnasaldcdLRASQAALFEKNKELADLKHVHSKLKKQF 431
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA--------LDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 432 QEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQ 511
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
....
gi 564394541 512 QQNA 515
Cdd:TIGR02168 914 RREL 917
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
245-498 |
3.71e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 245 EEDTSKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSED 324
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 325 LEDElgarssmdrkmAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcDLR 404
Cdd:COG1196 343 EEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE-AEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 405 ASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQ 484
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
250
....*....|....
gi 564394541 485 RSLDEQTEQSENLQ 498
Cdd:COG1196 491 ARLLLLLEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
266-514 |
4.34e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 266 LKEREDKLALSKNIEKLEGELSQWKikyEELSKTKQEMlKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGE 345
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQ---SELRRIENRL-DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 346 MERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRR----RQNASALDCDLRASQAALFEKNKELADLK 421
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 422 HVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDEL--------------DEAHNQARKLQRSL 487
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrdlesrlgdlkkerDELEAQLRELERKI 905
|
250 260
....*....|....*....|....*..
gi 564394541 488 DEQTEQSENLQVQLEHLQSRLRRQQQN 514
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
245-510 |
3.08e-09 |
|
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: 60.08 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 245 EEDTSKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEThqdelgrmSED 324
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA--------LND 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 325 LEDELGAR--SSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASaLDCD 402
Cdd:TIGR02169 784 LEARLSHSriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGK 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 403 LRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARK 482
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
250 260
....*....|....*....|....*...
gi 564394541 483 LQrSLDEQTEQSENLQVQLEHLQSRLRR 510
Cdd:TIGR02169 943 DE-EIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
295-516 |
7.46e-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: 57.85 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 295 ELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLEREN 374
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 375 KKLRAQVGDLEEALARRRRQNASALdcdlRASQAALFEKNKELADLKHVHSKLKKQ---FQEKVAELAHANRRVEQHETE 451
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAL----LLSPEDFLDAVRRLQYLKYLAPARREQaeeLRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564394541 452 VKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAP 516
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-512 |
5.17e-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: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 195 ELDLVESLLKSRPEELEGCWDAcsvAAGGSRVSSGRQD-RNRLpwedtAGTEEDTSKLTALRLRLDESQKVLLKERE--- 270
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEE---AAGISKYKERRKEtERKL-----ERTRENLDRLEDILNELERQLKSLERQAEkae 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 271 DKLALSKNIEKLEGELS--QWKIKYEELSKTKQEmLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMER 348
Cdd:TIGR02168 214 RYKELKAELRELELALLvlRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 349 LQAEnaaewgrRERLETEKlgleRENKKLRAQVGDLEEALARRRRQNASALDCDlrasQAALFEKNKELADLKHVHSKLK 428
Cdd:TIGR02168 293 LANE-------ISRLEQQK----QILRERLANLERQLEELEAQLEELESKLDEL----AEELAELEEKLEELKEELESLE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 429 KQFQEKVAELAHANRRVEQHETEVkklrlrvEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRL 508
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQL-------ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
....
gi 564394541 509 RRQQ 512
Cdd:TIGR02168 431 EEAE 434
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-472 |
7.11e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 260 ESQKVLLKEREDklALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSE---DLEDELGARSSMD 336
Cdd:TIGR02168 301 EQQKQILRERLA--NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEleaELEELESRLEELE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 337 RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRrrqnasaldcDLRASQAALFEKNKE 416
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA----------ELKELQAELEELEEE 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564394541 417 LADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDE 472
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
267-510 |
9.58e-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: 55.07 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 267 KEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEM 346
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 347 ERLQA---ENAAEWGRRERL------ETEKLGlERENKKLRAQVGDLEEALARRRRQNASALDcDLRASQAALFEKNKEL 417
Cdd:TIGR02169 254 EKLTEeisELEKRLEEIEQLleelnkKIKDLG-EEEQLRVKEKIGELEAEIASLERSIAEKER-ELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 418 ADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENL 497
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
250
....*....|...
gi 564394541 498 QVQLEHLQSRLRR 510
Cdd:TIGR02169 412 QEELQRLSEELAD 424
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
109-465 |
1.25e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 109 KVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGARGAADKTQEGPEAEREhepvrDIGAE 188
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-----EAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 189 RSPGSQELDLVESLLKSRPEELEgcwdacsvaAGGSRVSSGRQDRNRLpwEDTAGTEedTSKLTALRLRLDESQKVLLKE 268
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELK---------ALREALDELRAELTLL--NEEAANL--RERLESLERRIAATERRLEDL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 269 REDKLALSKNIEKLEGELSQWKIKYEELSKTkqemLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMER 348
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESE----LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 349 LQAENAAEwgrRERLETEKLGLERENKKLRAQVGDLEEALArrrrQNASALDCDLRASQAALFEKNKELADLKHVHSKLK 428
Cdd:TIGR02168 920 LREKLAQL---ELRLEGLEVRIDNLQERLSEEYSLTLEEAE----ALENKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992
|
330 340 350
....*....|....*....|....*....|....*..
gi 564394541 429 KQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKE 465
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
246-486 |
6.72e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 246 EDTSKLTALRLRLDE-SQKVLLKE----REDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSIL----KETHQD 316
Cdd:TIGR02169 208 EKAERYQALLKEKREyEGYELLKEkealERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkiKDLGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 317 ELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRR---- 392
Cdd:TIGR02169 288 EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeele 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 393 --RQNASALDCDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQH--------------ETEVKKLR 456
Cdd:TIGR02169 368 dlRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnaaiagieakinelEEEKEDKA 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 564394541 457 LRVEE----------------------------LKKELAQAEDELDEAHNQARKLQRS 486
Cdd:TIGR02169 448 LEIKKqewkleqlaadlskyeqelydlkeeydrVEKELSKLQRELAEAEAQARASEER 505
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
258-505 |
1.09e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 258 LDESQKVLLKEREDklaLSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILK---ETHQDELGRMSEDLEDELGARSS 334
Cdd:TIGR04523 424 LEKEIERLKETIIK---NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsiNKIKQNLEQKQKELKSKEKELKK 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 335 MDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALarrrrqNASALDCDLRasqaalfEKN 414
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL------KKENLEKEID-------EKN 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 415 KELADLKHVHSKLKKQfQEKVAELahanrrVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQS 494
Cdd:TIGR04523 568 KEIEELKQTQKSLKKK-QEEKQEL------IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
250
....*....|.
gi 564394541 495 ENLQVQLEHLQ 505
Cdd:TIGR04523 641 NKLKQEVKQIK 651
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-514 |
2.23e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 316 DELGRMSEDLEDELGARSSMD--RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAqvgDLEEALARRRR 393
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEdaREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL---ELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 394 QNASALDCDLRASQAALFEKNKELADLKHVHSK--------LKKQFQEKVAELAHANRRVEQHETEVKKLRLRV----EE 461
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLpasaEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564394541 462 LKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQN 514
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-449 |
4.37e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 111 RAERNRArEEVRQLRQRLDTLTKELAGARRERQEAQgeCEARGRELARLRGARGAADKTQEgpEAEREHEPVRDIGAERS 190
Cdd:COG1196 206 ERQAEKA-ERYRELKEELKELEAELLLLKLRELEAE--LEELEAELEELEAELEELEAELA--ELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 191 PGSQELDLVESLLKSRPEELEgcwdacsvaaggsrvssgrQDRNRLpwedtagteedTSKLTALRLRLDESQKVLLKERE 270
Cdd:COG1196 281 LELEEAQAEEYELLAELARLE-------------------QDIARL-----------EERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 271 DKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARssmdRKMAELRGEMERLQ 350
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL----RAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 351 AENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcDLRASQAALFEKNKELADLKHVHSKLKKQ 430
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLEEAALLEAALAELLEE 485
|
330
....*....|....*....
gi 564394541 431 FQEKVAELAHANRRVEQHE 449
Cdd:COG1196 486 LAEAAARLLLLLEAEADYE 504
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
266-541 |
7.76e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 266 LKEREDKLA-LSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKET------HQDELGRMSEDLEDELGARSSMDRK 338
Cdd:PRK01156 192 LKSSNLELEnIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAlnelssLEDMKNRYESEIKTAESDLSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 339 MAELRGEMERL-QAENAAEWGRRERLeteklgleRENKKLRAQVGDLEEALARRRRQNASALDC-----DLRASQAALFE 412
Cdd:PRK01156 272 NNYYKELEERHmKIINDPVYKNRNYI--------NDYFKYKNDIENKKQILSNIDAEINKYHAIikklsVLQKDYNDYIK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 413 KNKELADLKHVHSKLKK---QFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARklqRSLDE 489
Cdd:PRK01156 344 KKSRYDDLNNQILELEGyemDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEIN---VKLQD 420
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 564394541 490 QTEQSENLQVQLEHLQSRLRRQQQNAP-LFGKIRSTRFGTEEAGDGASDLDED 541
Cdd:PRK01156 421 ISSKVSSLNQRIRALRENLDELSRNMEmLNGQSVCPVCGTTLGEEKSNHIINH 473
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
359-513 |
1.01e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 359 RRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDC--------DLRASQAALFEKNKELAD----------L 420
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswdeiDVASAEREIAELEAELERldassddlaaL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 421 KHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQ---ARKLQRSLDEQTEQ-SEN 496
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERElREN 770
|
170
....*....|....*..
gi 564394541 497 LQVQLEHLQSRLRRQQQ 513
Cdd:COG4913 771 LEERIDALRARLNRAEE 787
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
109-475 |
1.05e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 109 KVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGARGAADKTQEGPEAEREHEPVRDIGAE 188
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 189 RSPGSQELDLVESLLKSRPEELEGCWDACSVAAGGSRVSSGRQDRNRLPWEDTAGTEEDTSKLTALRLRLDESQKvLLKE 268
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA-ALAA 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 269 REDKLALSKNIEKLEGELSQWKIKYEELSKTkqemLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMER 348
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDT----LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 349 LQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNAsaldcdLRASQAALFEKNKELADLkhvhsklk 428
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE------ERLEEELEEEALEEQLEA-------- 732
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 564394541 429 kQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDE 475
Cdd:COG1196 733 -EREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-511 |
1.22e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 104 REKWSKVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGARGAADKTQEGPEAER--EHEP 181
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeEEEA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 182 VRDIGAERSPGSQELDLVESLLKSRPEELEGcWDACSVAAGGSRVSSGRQDRNRLPWEDTAGTEEDTSKLTALRLRLDES 261
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAAL-LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 262 QKVLLKEREDKLALSKNIEKLEGELSQWKI--------KYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARS 333
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVveddevaaAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 334 SMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASAldcdlRASQAALFEK 413
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR-----RELLAALLEA 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 414 NKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQ 493
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
410
....*....|....*...
gi 564394541 494 SENLQVQLEHLQSRLRRQ 511
Cdd:COG1196 758 EPPDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-515 |
1.58e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 358 GRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASaLDCDLRASQAALFEKNKELADLKH---VHSK----LKKQ 430
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-LEEEIEELQKELYALANEISRLEQqkqILRErlanLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 431 FQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQ---ARKLQRSLDEQTEQSENLQVQLEHLQSR 507
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIAS 397
|
....*...
gi 564394541 508 LRRQQQNA 515
Cdd:TIGR02168 398 LNNEIERL 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
105-515 |
2.14e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 105 EKWSKVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGARGAADKTQEGPEAEREHEPVRD 184
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 185 IGAERSPGSQELDLVESLLKSRPEELEgcwdacsvaaggsrvssgrQDRNRLPWEDTAGTEEDTSKLTALRLRLDESQKV 264
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELE-------------------ELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 265 LLKEREDKLALSKNIEKLEGELSQWKIkYEELSKTKQ---------EMLKQLSILKETHQDELGRMSEDLEDELGARSSM 335
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAAL-EERLKEARLllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 336 DRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDCDLRASQAALFEKNK 415
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 416 ELADLKHVHS--------KLKKQFQEKVAELAHANRRVEQHETEVK---------KLRLRVEELKKELAQAEDELDEAHN 478
Cdd:COG4717 374 ALLAEAGVEDeeelraalEQAEEYQELKEELEELEEQLEELLGELEellealdeeELEEELEELEEELEELEEELEELRE 453
|
410 420 430
....*....|....*....|....*....|....*..
gi 564394541 479 QARKLQRSLdEQTEQSENLQVQLEHLQSRLRRQQQNA 515
Cdd:COG4717 454 ELAELEAEL-EQLEEDGELAELLQELEELKAELRELA 489
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
109-500 |
2.37e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 109 KVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQgECEARGRELARLRGARGAADKTQEGPEAEREHEPVRDigAE 188
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK--AE 1460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 189 RSPGSQELDLVESLLKSRPEELEGCWDAcsvaagGSRVSSGRQDRNRLPWEDTAGTEEDTSKLTALRLRLDESQKVLLKE 268
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEA------KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 269 REDKLALSKNIEKLEgELSqwkiKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMER 348
Cdd:PTZ00121 1535 KADEAKKAEEKKKAD-ELK----KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 349 LQAENAAEwgrrERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDCDL--RASQAALFEKNKELADLKHVHSK 426
Cdd:PTZ00121 1610 EEAKKAEE----AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEE 1685
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564394541 427 LKKQFQEKVAELAHANRRVEQ----HETEVKKlrlrVEELKKELAQAEDELDEAHNQARKLQRSLDE-QTEQSENLQVQ 500
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEElkkkEAEEKKK----AEELKKAEEENKIKAEEAKKEAEEDKKKAEEaKKDEEEKKKIA 1760
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
337-502 |
2.53e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 337 RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcdlrasqaalfekNKE 416
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-------------NKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 417 LADLKHvhsklkkqfqekvaELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 496
Cdd:COG1579 91 YEALQK--------------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
....*.
gi 564394541 497 LQVQLE 502
Cdd:COG1579 157 ELEELE 162
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
315-516 |
4.01e-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: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 315 QDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAewgrrerLETEKLGLERENKKLRAQVGDLEEALARRRRQ 394
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-------LQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 395 ------NASALDCDLRASQAAlfeknkELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQ 468
Cdd:COG3883 95 lyrsggSVSYLDVLLGSESFS------DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564394541 469 AEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAP 516
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
109-549 |
4.16e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 109 KVRAERNRAREEVR----QLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGARGAADKTQEgpEAEREHEPVRD 184
Cdd:PTZ00121 1308 KKKAEEAKKADEAKkkaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE--EAKKKADAAKK 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 185 iGAERSPGSQELDLVESLLKSRPEELEGCWDACSVAAGGSRVSSGRQDRNRLP--------WEDTAGTEEDTSKLTALRL 256
Cdd:PTZ00121 1386 -KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKkkaeeakkADEAKKKAEEAKKAEEAKK 1464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 257 RLDESQKVllKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQ---DELGRMSEDLEDELGARS 333
Cdd:PTZ00121 1465 KAEEAKKA--DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkkaDEAKKAEEAKKADEAKKA 1542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 334 SMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLR----AQVGDLEEALARRRRQNASALDCDLRASQAA 409
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 410 lfEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDE 489
Cdd:PTZ00121 1623 --EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 490 QTEQSENLQVQLEHLQSRLRRQQQNAPLFGKIRSTRFGTEEAGDGASDLDEDEDLQIQVA 549
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
293-507 |
4.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 293 YEELSKTKQEMLK---QLSILK--ETHQDELGRMSEDLE--DELGARSSMD---RKMAELRGEMERLQAEnaaewgrRER 362
Cdd:COG4913 234 FDDLERAHEALEDareQIELLEpiRELAERYAAARERLAelEYLRAALRLWfaqRRLELLEAELEELRAE-------LAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 363 LETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDCDLRASQAALFEKNKELAdlkhvhsklkkQFQEKVAELAHAn 442
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRA-----------RLEALLAALGLP- 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564394541 443 rrVEQHETEVKKLRLRVEELkkeLAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSR 507
Cdd:COG4913 375 --LPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
301-519 |
4.71e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 301 QEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQ 380
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 381 VGDLEEALArRRRQNASALDCDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVE 460
Cdd:pfam07888 117 KDALLAQRA-AHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQ 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564394541 461 ELKKELAQAEDELDEAHNQARKLQRSLDE---QTEQSENLQVQLEHLQSRLRRQQQNAPLFG 519
Cdd:pfam07888 196 ELRNSLAQRDTQVLQLQDTITTLTQKLTTahrKEAENEALLEELRSLQERLNASERKVEGLG 257
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
263-508 |
5.08e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 263 KVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAEL 342
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 343 RGEMERLQAenaaewgRRERLETEKLGLERENKKLRAqvgdleealarrrrqnasaldcDLRASQAALFEKNKELADLKH 422
Cdd:TIGR04523 453 ELIIKNLDN-------TRESLETQLKVLSRSINKIKQ----------------------NLEQKQKELKSKEKELKKLNE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 423 VHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEahNQARKLQRSLDEQTEQSENLQVQLE 502
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLK 581
|
....*.
gi 564394541 503 HLQSRL 508
Cdd:TIGR04523 582 KKQEEK 587
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-394 |
5.59e-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: 46.21 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 112 AERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLrgARGAADKTQEgpEAEREHEPVRDIGAERSp 191
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL--NKKIKDLGEE--EQLRVKEKIGELEAEIA- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 192 gsqELDLVESLLKSRPEELEGcwdacsvaaggsRVSSGRQDRNRLPWEDTAGTEEDTS---KLTALRLRLDESQKVLLKE 268
Cdd:TIGR02169 305 ---SLERSIAEKERELEDAEE------------RLAKLEAEIDKLLAEIEELEREIEEerkRRDKLTEEYAELKEELEDL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 269 REDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILkethQDELGRMSEDLEDELGARSSMDRKMAELRGEMER 348
Cdd:TIGR02169 370 RAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL----QEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 564394541 349 LQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQ 394
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-390 |
7.36e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 104 REKWSKVRAERNRAREEVRQLRQRLDTLTKELAGARRER-------QEAQGECEARGRELARLRGARGAADKTQEGPEAE 176
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVseleeeiEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 177 REHEPVRDIGAERSPGSQELDLVEslLKSRPEELEGCWDACSVAAggsrvssgrqdrnrlpwedtagtEEDTSKLTALRL 256
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAE--LEEKLEELKEELESLEAEL-----------------------EELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 257 RLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEEL----SKTKQEMLKQLSILKETHQDELGRMSEDLEDELgar 332
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrrERLQQEIEELLKKLEEAELKELQAELEELEEEL--- 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 564394541 333 ssmdrkmAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALAR 390
Cdd:TIGR02168 450 -------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
249-442 |
8.03e-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: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 249 SKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDE 328
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 329 LGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASaLDCDLRASQA 408
Cdd:COG4942 135 VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR-LEKELAELAA 213
|
170 180 190
....*....|....*....|....*....|....
gi 564394541 409 ALFEKNKELADLKHVHSKLKKQFQEKVAELAHAN 442
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
369-516 |
9.02e-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: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 369 GLERENKKLRAQVGDLE--EALARRRRQNASALD-CDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRV 445
Cdd:COG4913 239 RAHEALEDAREQIELLEpiRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564394541 446 EQHETEVKKLRL--------RVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNAP 516
Cdd:COG4913 319 DALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
259-504 |
9.69e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 259 DESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQL-SILKETHqdelgrmsEDLEDELgarSSMDR 337
Cdd:PRK05771 39 ELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELiKDVEEEL--------EKIEKEI---KELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 338 KMAELRGEMERLQAEnaaewgrRERLE-----TEKLGLERENKKLRAQVGDLEEALarrrrqnasaldcDLRASQAALFE 412
Cdd:PRK05771 108 EISELENEIKELEQE-------IERLEpwgnfDLDLSLLLGFKYVSVFVGTVPEDK-------------LEELKLESDVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 413 KNKELADLKH-------VHSKLKKQFQEKVAELAHANRRVEQHET---EVKKLRLRVEELKKELAQAEDELDEAHNQARK 482
Cdd:PRK05771 168 NVEYISTDKGyvyvvvvVLKELSDEVEEELKKLGFERLELEEEGTpseLIREIKEELEEIEKERESLLEELKELAKKYLE 247
|
250 260
....*....|....*....|..
gi 564394541 483 LQRSLDEQTEQSENLQVQLEHL 504
Cdd:PRK05771 248 ELLALYEYLEIELERAEALSKF 269
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
115-543 |
1.37e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 115 NRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGARGAADKTQEG-PEAEREHEPVRDIGAERSPGS 193
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETiAETEREREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 194 QELDlvesllksrpEELEGCWDACSVAAGGSRVSSGRQdrnrlpwedtagtEEDTSKLTALRLRLDESQKVLLKEREDKL 273
Cdd:PRK02224 289 EELE----------EERDDLLAEAGLDDADAEAVEARR-------------EELEDRDEELRDRLEECRVAAQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 274 ALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLsilkETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAEN 353
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAV----EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 354 AAEWGRRERLETEKLGLE---RENKKLRAQ---------------VGDLEEAlaRRRRQNASALDCDLRASQAALFEKNK 415
Cdd:PRK02224 422 DELREREAELEATLRTARervEEAEALLEAgkcpecgqpvegsphVETIEED--RERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 416 ELADLKhvhsKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSE 495
Cdd:PRK02224 500 RAEDLV----EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 564394541 496 NLQVQLEHLQSRLRRQQQNAPLFGKIRSTRFGTEEAGDGASDLDEDED 543
Cdd:PRK02224 576 ELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
374-496 |
2.02e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 374 NKKLRAQVGDLEEALARRRRQnasaldcdLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAEL------------AHA 441
Cdd:PRK04863 987 NEKLRQRLEQAEQERTRAREQ--------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELqdlgvpadsgaeERA 1058
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564394541 442 NRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 496
Cdd:PRK04863 1059 RARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
345-497 |
3.20e-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: 43.08 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 345 EMERLQAEnaAEW---------GRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNaSALDCDLRASQAALFEKNK 415
Cdd:smart00787 124 TFARLEAK--KMWyewrmklleGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRK-DALEEELRQLKQLEDELED 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 416 ----ELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQT 491
Cdd:smart00787 201 cdptELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQL 280
|
....*.
gi 564394541 492 EQSENL 497
Cdd:smart00787 281 KLLQSL 286
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
406-511 |
3.70e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 406 SQAALFEKNKELADLKhvhSKLKKQFQEKVAELAHANRRVEQHE-------TEVKKLRLRVEELKKELAQAEDELDEAHN 478
Cdd:PRK12704 55 KKEALLEAKEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEenldrklELLEKREEELEKKEKELEQKQQELEKKEE 131
|
90 100 110
....*....|....*....|....*....|....*....
gi 564394541 479 QARKLQRSLDEQTEQSENL------QVQLEHLQSRLRRQ 511
Cdd:PRK12704 132 ELEELIEEQLQELERISGLtaeeakEILLEKVEEEARHE 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
405-493 |
4.09e-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: 42.83 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 405 ASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQ 484
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
....*....
gi 564394541 485 RSLDEQTEQ 493
Cdd:COG4942 97 AELEAQKEE 105
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
342-501 |
4.82e-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: 42.38 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 342 LRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASaldcdlrasqaalfekNKELADLK 421
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSN----------------LKEISDLE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 422 HVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEElkkELAQAEDELDEAHNQA---RKLQRSLDEQTEQSENLQ 498
Cdd:pfam15294 195 EKMAALKSDLEKTLNASTALQKSLEEDLASTKHELLKVQE---QLEMAEKELEKKFQQTaayRNMKEMLTKKNEQIKELR 271
|
...
gi 564394541 499 VQL 501
Cdd:pfam15294 272 KRL 274
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
104-510 |
5.00e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 104 REKWSKVRAERNRAREEVRQLRQRLDTLTKELAGARRER----------QEAQGECEARGRELA-RLRGARGAADKTQEg 172
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaeavEARREELEDRDEELRdRLEECRVAAQAHNE- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 173 pEAEREHEPVRDIGAERSPGSQELDLVESLL----------KSRPEELEGCWDACSVAAGGSRVSSGR-QDRNRLPWEDT 241
Cdd:PRK02224 343 -EAESLREDADDLEERAEELREEAAELESELeeareavedrREEIEELEEEIEELRERFGDAPVDLGNaEDFLEELREER 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 242 AGTEEDTSKLTA----LRLRLDESQKVL-----------LKEREDKLALSKN---IEKLEGELSQWKIKYEELS------ 297
Cdd:PRK02224 422 DELREREAELEAtlrtARERVEEAEALLeagkcpecgqpVEGSPHVETIEEDrerVEELEAELEDLEEEVEEVEerlera 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 298 KTKQEMLKQLSILKETHQDELGRMSE---DLEDELGARSSMDRKMAELRGEME--RLQAENAAEWGRRERLETEKLGLER 372
Cdd:PRK02224 502 EDLVEAEDRIERLEERREDLEELIAErreTIEEKRERAEELRERAAELEAEAEekREAAAEAEEEAEEAREEVAELNSKL 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 373 -ENKKLRAQVGDLEEALARRRrqnasaldcDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHanrrvEQHETE 451
Cdd:PRK02224 582 aELKERIESLERIRTLLAAIA---------DAEDEIERLREKREALAELNDERRERLAEKRERKRELEA-----EFDEAR 647
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564394541 452 VKKLRLRVEELKKELAQAEDELDEAHNQARKLQR---SLDEQTEQSENLQVQLEHLQSRLRR 510
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigAVENELEELEELRERREALENRVEA 709
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
258-516 |
5.25e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 258 LDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDE----LGRMS-EDLEDEL--- 329
Cdd:PRK11281 54 LEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEEtretLSTLSlRQLESRLaqt 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 330 -------------------GARSSMDRKMAELRGEMERLQ-----------AENAAEWGRRERLETEKLGLERENKKLR- 378
Cdd:PRK11281 134 ldqlqnaqndlaeynsqlvSLQTQPERAQAALYANSQRLQqirnllkggkvGGKALRPSQRVLLQAEQALLNAQNDLQRk 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 379 -AQVGDLEEALARRRRqnasaldcDLRASQAALFEknKELADLKHV-HSKLKKQFQEKVAELAHANRRVE-QHETEVKKL 455
Cdd:PRK11281 214 sLEGNTQLQDLLQKQR--------DYLTARIQRLE--HQLQLLQEAiNSKRLTLSEKTVQEAQSQDEAARiQANPLVAQE 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564394541 456 RLRVEELKKELAQAEDELDEAHNQARKLQRSLDE--QTEQseNLQVQLEHLQ-----SR-LRRQQQNAP 516
Cdd:PRK11281 284 LEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRltQSER--NIKEQISVLKgslllSRiLYQQQQALP 350
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
439-513 |
6.65e-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: 6.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564394541 439 AHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-515 |
6.71e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 111 RAERNRAREEVRqlrqRLDTLTKELAGARRERQEAQGEcEARGRELARLR--GARGAADKTQEGPEAEREHEPVRDIGAE 188
Cdd:PTZ00121 1219 KAEDAKKAEAVK----KAEEAKKDAEEAKKAEEERNNE-EIRKFEEARMAhfARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 189 RSPGSQELDLVESLlKSRPEELEGCWDAcsvaagGSRVSSGRQDRNRLPWEDTAGTEEDTSKLTALRLRLDESQKVLLKE 268
Cdd:PTZ00121 1294 EAKKAEEKKKADEA-KKKAEEAKKADEA------KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 269 REDKLALSKNIEKLEG--ELSQWKIKYEELSKTKQEMLKQLSILKETHQ-----DELGRMSEDLE--DELGARSSMDRKM 339
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAakkkaDEAKKKAEEKKkaDEAKKKAEEAKKA 1446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 340 AELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDCDLRASQAALFEKNKELAD 419
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 420 LKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKElaqaEDELDEAHNQARKLQRSLDEQTEQSENLQV 499
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA----EEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
410
....*....|....*.
gi 564394541 500 QLEHLQSRLRRQQQNA 515
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEA 1618
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
220-515 |
7.87e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 220 AAGGSRVSSGRQDRNRLPWEDTAGTEEDTSKLTALR---LRLDESQKVLLK---EREDKLALSKNIEKL---------EG 284
Cdd:NF012221 1416 TYGVEASHSASVYGLRAEGHGARVSELDTYTNTSLYqdlSNLTAGEVIALSfdfARRAGLSTNNGIEVLwngevvfasSG 1495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 285 ELSQWKIKyeELSKTKQEMLKQLSILKETHQDELGRmsedLEDELGARSSMDRKMAELRGEMERLQAENAAeWGRRERLE 364
Cdd:NF012221 1496 DASAWQQK--TLKLTAKAGSNRLEFKGTGHNDGLGY----ILDNVVATSESSQQADAVSKHAKQDDAAQNA-LADKERAE 1568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 365 TEKLGLERENKKLRAQVG----DLE----EALARRRRQNASALDCDLRASQAALFEKNKEL------------------- 417
Cdd:NF012221 1569 ADRQRLEQEKQQQLAAISgsqsQLEstdqNALETNGQAQRDAILEESRAVTKELTTLAQGLdaldsqatyagesgdqwrn 1648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 418 --AD--LKHVHSKL---KKQFQEKVAELAHANR-RVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARK------L 483
Cdd:NF012221 1649 pfAGglLDRVQEQLddaKKISGKQLADAKQRHVdNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKrkddalA 1728
|
330 340 350
....*....|....*....|....*....|..
gi 564394541 484 QRSLDEQTEQSENLQVqlEHLQSRLRRQQQNA 515
Cdd:NF012221 1729 KQNEAQQAESDANAAA--NDAQSRGEQDASAA 1758
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
112-515 |
8.92e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 112 AERNRAREEVR-QLRQRLDTLTKELAgarrerqeaqgecEARGRELARLRGARGAADKTQEGPEA-EREHEPVRDIGAER 189
Cdd:pfam12128 275 ASRQEERQETSaELNQLLRTLDDQWK-------------EKRDELNGELSAADAAVAKDRSELEAlEDQHGAFLDADIET 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 190 SPGSQE-LDLVESLLKSRPEELEGCWDAC-SVAAGGSRVSSGRQDRNRlpwEDTAGTEEDTSKLTALRLRLD-------E 260
Cdd:pfam12128 342 AAADQEqLPSWQSELENLEERLKALTGKHqDVTAKYNRRRSKIKEQNN---RDIAGIKDKLAKIREARDRQLavaeddlQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 261 SQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKqlsILKETHQDELGRMSEDLEDELGARSSMDRKMA 340
Cdd:pfam12128 419 ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELL---LQLENFDERIERAREEQEAANAEVERLQSELR 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 341 ELRG----EMERLQAENAAEWGRRERLETEKLGLERENKKL----RAQVGDLEEALAR---------------------R 391
Cdd:pfam12128 496 QARKrrdqASEALRQASRRLEERQSALDELELQLFPQAGTLlhflRKEAPDWEQSIGKvispellhrtdldpevwdgsvG 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 392 RRQNASALDCDLRASQAALFEKNKElaDLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAED 471
Cdd:pfam12128 576 GELNLYGVKLDLKRIDVPEWAASEE--ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL 653
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 564394541 472 EL----DEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNA 515
Cdd:pfam12128 654 DLrrlfDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAW 701
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-498 |
9.59e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 111 RAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGARGAADKTQEGPEAeREHEPVRDIGAERS 190
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEEL-RKAEDARKAEAARK 1207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 191 pgSQELDLVESLLKS----RPEELEGCWDACSVAAGGSRVSSGRQDRNRLPWEDT--AGTEEDTSKLTALRLR-LDESQK 263
Cdd:PTZ00121 1208 --AEEERKAEEARKAedakKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEArmAHFARRQAAIKAEEARkADELKK 1285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 264 VLLKEREDKLALSKNIEKLE--GELSQWKIKYEELSKTKQEMLKQLSILKETHQ-----DELGRMSEDLEDELGARSSMD 336
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeakkaAEAAKAEAEAAADEAEAAEEK 1365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 337 RKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEA------LARRRRQNASALDCDLRASQAAL 410
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkkkadeAKKKAEEKKKADEAKKKAEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 411 FEKNKELADLKHVHSKLKKQFQEK-----VAELAHANRRVEQHETEVKKLRLRVEELKK--ELAQAEDELDEAHNQARKL 483
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAkkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKAD 1525
|
410
....*....|....*
gi 564394541 484 QRSLDEQTEQSENLQ 498
Cdd:PTZ00121 1526 EAKKAEEAKKADEAK 1540
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
267-491 |
9.77e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 267 KEREDKLALSKNIEKLEGElsqwkiKYEELSKTKQEMlkqlsilkethqDELGRMSEDLEDELGARSSMDRKMAELRGEM 346
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKE------KEKELEEVLREI------------NEISSELPELREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 347 ERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALD-CDLRASQAALFEKNKELADLKHVHS 425
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564394541 426 KLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKElAQAEDELDEAHNQARKLQRSLDEQT 491
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLT 385
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
275-510 |
1.00e-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: 41.93 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 275 LSKNIEKLEGELSQwkiKYEELSKTKQEmLKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENA 354
Cdd:TIGR04523 230 LKDNIEKKQQEINE---KTTEISNTQTQ-LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 355 AEWgrrerleteklglereNKKLRAQVGDLEEALarrrrqnaSALDCDLRASQAALFEKNKELADLKHV-------HSKL 427
Cdd:TIGR04523 306 QDW----------------NKELKSELKNQEKKL--------EEIQNQISQNNKIISQLNEQISQLKKEltnseseNSEK 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 428 KKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSR 507
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
...
gi 564394541 508 LRR 510
Cdd:TIGR04523 442 IKD 444
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
430-514 |
1.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 430 QFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHlqsRLR 509
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---RAR 93
|
....*
gi 564394541 510 RQQQN 514
Cdd:COG3883 94 ALYRS 98
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
398-515 |
1.05e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 41.76 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 398 ALDCDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAH 477
Cdd:COG5283 4 ILGAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLS 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 564394541 478 NQARKLQRSLdEQTEQsenlqvQLEHLQSRLRR--QQQNA 515
Cdd:COG5283 84 AAQRRLRSSL-EQTNR------QLERQQQRLARlgARQDR 116
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
375-477 |
1.53e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.21 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 375 KKLRAQVGDLEEALARRRR----QNASALDCDLRASQaalfeknKELADLKHVHSKLKKQfqekVAELAHANRRVEQHET 450
Cdd:PRK05431 5 KLIRENPEAVKEALAKRGFpldvDELLELDEERRELQ-------TELEELQAERNALSKE----IGQAKRKGEDAEALIA 73
|
90 100
....*....|....*....|....*..
gi 564394541 451 EVKKLRLRVEELKKELAQAEDELDEAH 477
Cdd:PRK05431 74 EVKELKEEIKALEAELDELEAELEELL 100
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
347-514 |
1.69e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 347 ERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDcDLRASQAALFEKNKELADLKHVHSK 426
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQARE-ELEQLEEELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 427 LKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQS 506
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
....*...
gi 564394541 507 RLRRQQQN 514
Cdd:COG4372 165 ELAALEQE 172
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
374-496 |
1.77e-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: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 374 NKKLRAQVGDLEEALARRRRQnasaldcdLRASQAALFEKNKELADLK---HVHSKLKKQFQEKVAEL---------AHA 441
Cdd:COG3096 986 NEKLRARLEQAEEARREAREQ--------LRQAQAQYSQYNQVLASLKssrDAKQQTLQELEQELEELgvqadaeaeERA 1057
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564394541 442 NRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSEN 496
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
105-492 |
1.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 105 EKWSKVRAERNRAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELarlrgargaaDKTQEGPEAEREHEPVRD 184
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL----------TEEHRKELLEEYTAELKR 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 185 IGAERspgsQELDLVESLLKSRPEELEgcwdacSVAAGGSRVSsgrqdRNRLPWEDTAGTEEDTSKLTALRLRLDESQKV 264
Cdd:PRK03918 464 IEKEL----KEIEEKERKLRKELRELE------KVLKKESELI-----KLKELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 265 LLKEREDKLalSKNIEKLEGELSqwkiKYEELSKTKQEMLKQLSILKETHQDELGRMS-------EDLEDELGARSSMDR 337
Cdd:PRK03918 529 KLKEKLIKL--KGEIKSLKKELE----KLEELKKKLAELEKKLDELEEELAELLKELEelgfesvEELEERLKELEPFYN 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 338 KMAELRGEMERLQAEnaaewgrRERLETEKLGLERENKKLRAQVGDLEEALARrrrqnasaldcdlrasqaaLFEKNKEL 417
Cdd:PRK03918 603 EYLELKDAEKELERE-------EKELKKLEEELDKAFEELAETEKRLEELRKE-------------------LEELEKKY 656
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564394541 418 ADLKHvhSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELaqaeDELDEAHNQARKLQRSLDEQTE 492
Cdd:PRK03918 657 SEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL----EEREKAKKELEKLEKALERVEE 725
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
116-513 |
2.12e-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: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 116 RAREEVRQLRQRLDTLTKELAGARRERQEAQGECEARGRELARLRGARG--------AADKTQEGPEAEREHEPVrdiga 187
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESdleqdyqaASDHLNLVQTALRQQEKI----- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 188 erspGSQELDLVEslLKSRPEELEGcwdacsVAAGGSRVSSGRQDRNRLPWEDTagtEEDTSKLTALRLRLDESQKVLLK 267
Cdd:COG3096 350 ----ERYQEDLEE--LTERLEEQEE------VVEEAAEQLAEAEARLEAAEEEV---DSLKSQLADYQQALDVQQTRAIQ 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 268 EREDKLALSK----------NIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKEthqdelgrmsedledelgARSSMDR 337
Cdd:COG3096 415 YQQAVQALEKaralcglpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA------------------ARRQFEK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 338 KMAELR---GEMERLQAENAAewgrRERLET---EKLGLERENKkLRAQVGDLEEALarRRRQNASALDCDLRASQAALF 411
Cdd:COG3096 477 AYELVCkiaGEVERSQAWQTA----RELLRRyrsQQALAQRLQQ-LRAQLAELEQRL--RQQQNAERLLEEFCQRIGQQL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 412 EKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRlrveelkKELAQAEDELDEAHNQARKLQRSLDEQT 491
Cdd:COG3096 550 DAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI-------KELAARAPAWLAAQDALERLREQSGEAL 622
|
410 420
....*....|....*....|..
gi 564394541 492 EQSENLQVQLEHLQSRLRRQQQ 513
Cdd:COG3096 623 ADSQEVTAAMQQLLEREREATV 644
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
266-518 |
2.48e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 266 LKEREDKLALSKNIEKLEGELSQWK--IKYEELSKTKQEMLKQLSILKETHQDELGRMSEDLEDELGaRSSMDRKMAELr 343
Cdd:COG5022 786 LVDYELKWRLFIKLQPLLSLLGSRKeyRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFG-RSLKAKKRFSL- 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 344 gemerLQAENAAEWG--RRERLETEKLGLERENKKLrAQVGDLEEALARRRRQNASALDCDLRASqaaLFEKNKELADLK 421
Cdd:COG5022 864 -----LKKETIYLQSaqRVELAERQLQELKIDVKSI-SSLKLVNLELESEIIELKKSLSSDLIEN---LEFKTELIARLK 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 422 HVhsKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQL 501
Cdd:COG5022 935 KL--LNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQ 1012
|
250
....*....|....*..
gi 564394541 502 EHLQSRLRRQQQNAPLF 518
Cdd:COG5022 1013 ESTKQLKELPVEVAELQ 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-515 |
2.52e-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: 40.81 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 370 LERENKKLRAQVgdleEALARRRRQNASALDCDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHE 449
Cdd:TIGR02168 198 LERQLKSLERQA----EKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564394541 450 TEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNA 515
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
280-514 |
2.70e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 280 EKLEGELSQWKIKYEELSKTKQEM--LKQLSILKETHQDELGRMSEDLEDELGARSSMDRKMAELRGEMERLQAENAAEW 357
Cdd:pfam05483 370 QRLEKNEDQLKIITMELQKKSSELeeMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 358 GRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNAsaldcDLRASQAALFEKNKELA-DLKHVHSKLKKQFQEKVA 436
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNI-----ELTAHCDKLLLENKELTqEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 437 ELAHANRRVEQHETEVKK---LRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKemnLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIE 604
|
.
gi 564394541 514 N 514
Cdd:pfam05483 605 N 605
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
275-504 |
3.63e-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: 40.49 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 275 LSKNIEKLEGELSQWKIKYEE-LSKTKQEMLKQLSILKE--THQDELGRMSEDLEDELGAR-SSMDRKMAELRGEMErlq 350
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEarTERDQFSQESGNLDDQLQKLlADLHKREKELSLEKE--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 351 aENAAEWGR-----------RERLETEKLGLERENKKLRAQ----VGDLEEALARRRRQN-----ASALDCDLRASQAAL 410
Cdd:pfam15921 399 -QNKRLWDRdtgnsitidhlRRELDDRNMEVQRLEALLKAMksecQGQMERQMAAIQGKNeslekVSSLTAQLESTKEML 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 411 FEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQ---AEDELDEAHNQARKLQRSL 487
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknEGDHLRNVQTECEALKLQM 557
|
250
....*....|....*..
gi 564394541 488 DEQTEQSENLQVQLEHL 504
Cdd:pfam15921 558 AEKDKVIEILRQQIENM 574
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
243-510 |
4.13e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 243 GTEEDTSKLTALRLRLDE--SQKVLLKEREDKL-----ALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQ 315
Cdd:COG1340 2 KTDELSSSLEELEEKIEElrEEIEELKEKRDELneelkELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 316 DELGRMSEdLEDELGARSSMDRKMAELRGEMERLQAENAAEwgrRERLETEKLGLEREnKKLRAQVGDLEEALARRRRQN 395
Cdd:COG1340 82 ELNEKLNE-LREELDELRKELAELNKAGGSIDKLRKEIERL---EWRQQTEVLSPEEE-KELVEKIKELEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 396 asaldcdlrasqaalfEKNKELADLKhvhsklkKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDE 475
Cdd:COG1340 157 ----------------EKNEKLKELR-------AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE 213
|
250 260 270
....*....|....*....|....*....|....*
gi 564394541 476 AHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRR 510
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRELRKELKK 248
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
254-514 |
4.94e-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: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 254 LRLRLDESQKVllKEREDKLALS-KNIEKLEGELSQWKIKYE-------ELSKTKQEMLKQLSILKETHQDELGRMSEDL 325
Cdd:pfam01576 7 MQAKEEELQKV--KERQQKAESElKELEKKHQQLCEEKNALQeqlqaetELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 326 EDELGARSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEA---LARRRRQNASALDcD 402
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQnskLSKERKLLEERIS-E 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 403 LRASQAALFEKNKELADLKHVHSKLKKQFQEKVA-------ELAHANRRVEQHETEVK----KLRLRVEELKKELAQAED 471
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKkeekgrqELEKAKRKLEGESTDLQeqiaELQAQIAELRAQLAKKEE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564394541 472 ELDEAhnqarklQRSLDEQTEQSENLQVQLEHLQSRLRRQQQN 514
Cdd:pfam01576 244 ELQAA-------LARLEEETAQKNNALKKIRELEAQISELQED 279
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
446-515 |
6.19e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 6.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 446 EQHETEVKKLRLRVEELKKELAQAEDELDEAHNQARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQNA 515
Cdd:PRK12704 71 NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
245-514 |
6.46e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 245 EEDTSKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHQDELgrmSED 324
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW---NKE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 325 LEDELgarSSMDRKMAELRGEMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASaldcdlr 404
Cdd:TIGR04523 312 LKSEL---KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS------- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 405 asqaalfeKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDEAHNQ----- 479
Cdd:TIGR04523 382 --------YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvke 453
|
250 260 270
....*....|....*....|....*....|....*..
gi 564394541 480 --ARKLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQN 514
Cdd:TIGR04523 454 liIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
396-490 |
6.81e-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: 38.98 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 396 ASALDCDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEDELDE 475
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90
....*....|....*
gi 564394541 476 AHNQARKLQRSLDEQ 490
Cdd:COG4942 95 LRAELEAQKEELAEL 109
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
370-513 |
7.44e-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: 37.60 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 370 LERENKKLRAQVGDLEEALARRRRQNASALDCDLRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHE 449
Cdd:pfam08614 19 LEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564394541 450 TEVKKLRLRVEELKKELAQAEDELDEahnqarkLQRSLDEQTEQSENLQVQLEHLQSRLRRQQQ 513
Cdd:pfam08614 99 RRLAALEAERAQLEEKLKDREEELRE-------KRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
243-530 |
7.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 243 GTEEDTSKLTALRLRLDESQKVLLKEREDKLALSKNIEKLEGELSQWKIKYEELSKTKQEMLKQLSILKETHqdelgrms 322
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH-------- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 323 EDLEDELGARSSMDRKMAELRG-EMERLQAENAAEWGRRERLETEKLGLERENKKLRAQVGDLEEALARRRRQNASALDC 401
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVC 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 402 D-----------LRASQAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHET--EVKKLRLRVEEL-KKELA 467
Cdd:PRK03918 442 GrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKYnLEELE 521
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564394541 468 QAEDELDEAHNQARKL---QRSLDEQTEQSENLQVQLEHLQSRLRR-QQQNAPLFGKIRSTRFGTEE 530
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLkgeIKSLKKELEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVE 588
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
255-502 |
9.89e-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: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 255 RLRLDESQKVLLKEREDKLALS----KNIEKLEGELSQwkikYEELSKTKQEMLKQLSILKETHQDELGRMSEDLE---- 326
Cdd:pfam17380 352 RIRQEERKRELERIRQEEIAMEisrmRELERLQMERQQ----KNERVRQELEAARKVKILEEERQRKIQQQKVEMEqira 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 327 DELGARSSMDRKMAELRG-EMERLQAENAAEWGRRERLETEklglERENKKLRAQVGDLEEALARRRRQNASALDCDLRA 405
Cdd:pfam17380 428 EQEEARQREVRRLEEERArEMERVRLEEQERQQQVERLRQQ----EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564394541 406 S-QAALFEKNKELADLKHVHSKLKKQFQEKVAELAHANRRVEQHETEVKKLRLRVEELKKELAQAEdeldeahnqARKLQ 484
Cdd:pfam17380 504 RkQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE---------AMERE 574
|
250
....*....|....*...
gi 564394541 485 RSLDEQTEQSENLQVQLE 502
Cdd:pfam17380 575 REMMRQIVESEKARAEYE 592
|
|
| |
