|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-581 |
1.72e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.77 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 225 DLSQKLEELQRHYSTLEeqRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLE 304
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 305 KRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQI 384
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 385 QELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFE 464
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 465 LKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQ 544
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350
....*....|....*....|....*....|....*..
gi 2217376813 545 LQAELEALRTLKAEEAAVVAEQEDLLRLRGPLQAEAL 581
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
178-658 |
5.35e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 178 QQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESK 257
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 258 ITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQ 337
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 338 LLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEA 417
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 418 QIVALERTRAADQTTAEQGMRQLEQENAALKECRneyERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQ 497
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVK---AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 498 QQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELE---ALRTLKAEEAAVVAEQEDLLRLRG 574
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDlreADARYYVLGDTLLGRTLVAARLEA 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 575 PLQAEALSVNESHVTSRAMQDPVFQLPTAGRTPNGEVGAMDLTQLQKEKQDLEQQLLEKNKTIKQMQQRMLELRKTLQKE 654
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
....
gi 2217376813 655 LKIR 658
Cdd:COG1196 715 ERLE 718
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
62-573 |
5.88e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 62 RRNEQIRKLEA------RLSD-YAEQVRNLQKIKEKLEIAlekhqdssmRKFQEQNETFQANRAKMAeGLALALARKDQE 134
Cdd:COG1196 173 RKEEAERKLEAteenleRLEDiLGELERQLEPLERQAEKA---------ERYRELKEELKELEAELL-LLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 135 W-SEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQ 213
Cdd:COG1196 243 ElEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 214 EELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVI 293
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 294 THLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQS 373
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 374 KGIV--AAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAA----- 446
Cdd:COG1196 483 LEELaeAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEvaaaa 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 447 ---LKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANL------TAIIDEKEQNLREK 517
Cdd:COG1196 563 ieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgrtlvAARLEAALRRAVTL 642
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376813 518 TEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRTLKAEEAAVVAEQEDLLRLR 573
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-447 |
1.37e-14 |
|
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: 78.17 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 121 AEGLALALARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQ 200
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 201 ELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQ 280
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 281 KVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELE 360
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 361 QTLQASEEQLQQSKGIVAAQETQIQELaaanqesshvQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQL 440
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGL----------EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
....*..
gi 2217376813 441 EQENAAL 447
Cdd:TIGR02168 978 ENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
115-423 |
2.27e-13 |
|
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: 73.95 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 115 ANRAKMAEGLALALARKDQEWSEKMDQLEKEKNILTAQLQEMKNQsmnLFQRRDEMDELEGfQQQELSKIKHMLLKKEEs 194
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR---LDELSQELSDASR-KIGEIEKEIEQLEQEEE- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 195 lgKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQ--------RDHVIASKTGAESKITA----LE 262
Cdd:TIGR02169 734 --KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlSHSRIPEIQAELSKLEEevsrIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 263 QKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAAR 342
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 343 SSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERtQALEAQIVAL 422
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL-QRVEEEIRAL 970
|
.
gi 2217376813 423 E 423
Cdd:TIGR02169 971 E 971
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
225-573 |
1.69e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 225 DLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDV---ITHLQEKVA 301
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELaeeVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 302 SLEKRLEQNLSG-----------EEHLQELLKEKTLAEQNLEDTRQQLLAARS---SQAKAINTLETR-------VRELE 360
Cdd:PRK02224 290 ELEEERDDLLAEaglddadaeavEARREELEDRDEELRDRLEECRVAAQAHNEeaeSLREDADDLEERaeelreeAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 361 QTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQL 440
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 441 EQ----------ENAALKECRNEYERSLQNHQFELKKLKEEWSQREiVSVAMAQALEEVRKQREEFQQQAANLTAIIDEK 510
Cdd:PRK02224 450 EAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLEELIAER 528
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376813 511 EQNLREKTEVLLQKEQEILQLE----RGHNSALLQIHQLQAELEALRTLKAEEAAVVAEQEDLLRLR 573
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEaeaeEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR 595
|
|
| Grip |
smart00755 |
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245; |
692-737 |
4.99e-12 |
|
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
Pssm-ID: 197860 Cd Length: 46 Bit Score: 61.08 E-value: 4.99e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2217376813 692 EINFEYLKHVVLKFMSCRESEAFHLIKAVSVLLNFSQEEENMLKET 737
Cdd:smart00755 1 EANFEYLKNVLLQFLTLRESERETLLPVISTVLQLSPEEMQKLLEV 46
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-519 |
7.13e-11 |
|
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: 64.79 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 297 QEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGI 376
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 377 VAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYER 456
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376813 457 SLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTE 519
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-649 |
8.01e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 59 QLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALE--KHQDSSM-RKFQEQNETFQANRAKMAEglalaLARKDQEW 135
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEelRLEVSELeEEIEELQKELYALANEISR-----LEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 136 SEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDElegfQQQELSKIKHMLLKKEESLGKMEQELEARTRELsrtQEE 215
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEE----KLEELKEELESLEAELEELEAELEELESRLEEL---EEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 216 LmnsNQMSSDLSQKLEELQRHYSTLEEqrdhviasktgAESKITALEQKEQELQALIQQLSIDLQKvtaetQEKEDVITH 295
Cdd:TIGR02168 381 L---ETLRSKVAQLELQIASLNNEIER-----------LEARLERLEDRRERLQQEIEELLKKLEE-----AELKELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 296 LQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQlLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKG 375
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE-LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 376 IV--------------AAQETQIQE---------LAAANQESSHvQQQALALEQQFLERTQALEAQIVALERTRAADQTT 432
Cdd:TIGR02168 521 ILgvlselisvdegyeAAIEAALGGrlqavvvenLNAAKKAIAF-LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 433 AEQGMRQLEQENAALK--------------------ECRNEYER---------------------------SLQNHQFEL 465
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRkalsyllggvlvvddldnalELAKKLRPgyrivtldgdlvrpggvitggsaktnsSILERRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 466 KKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQL 545
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 546 QAELEALRTLKAEEAAVVAEQEDllrLRGPLQAEALSVNESHVTSRAMQDpvfQLPTAGRTPNGEVG--AMDLTQLQKEK 623
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEA---EIEELEAQIEQLKEELKALREALD---ELRAELTLLNEEAAnlRERLESLERRI 833
|
650 660
....*....|....*....|....*.
gi 2217376813 624 QDLEQQLLEKNKTIKQMQQRMLELRK 649
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAA 859
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-653 |
2.03e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 54 EDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQdssmRKFQEQNETFQANRAKMAEgLALALARKDQ 133
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE----SKLDELAEELAELEEKLEE-LKEELESLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 134 EWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGfQQQELSKIKHMLlkkEESLGKMEQELEARTRELSRTQ 213
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-EIERLEARLERL---EDRRERLQQEIEELLKKLEEAE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 214 EELMNSNqmSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALI----------QQLSIDLQKVT 283
Cdd:TIGR02168 435 LKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslerlqenlEGFSEGVKALL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 284 AETQEKEDVITHLQEKVaSLEKRLEQNLS--GEEHLQ--------------ELLKEK-----------TLAEQNLEDTRQ 336
Cdd:TIGR02168 513 KNQSGLSGILGVLSELI-SVDEGYEAAIEaaLGGRLQavvvenlnaakkaiAFLKQNelgrvtflpldSIKGTEIQGNDR 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 337 QLLAARSSQAKAINTLETRVRELEQTLQAseeqLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALE 416
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSY----LLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAK 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 417 AQIVALERTRAADQttAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEF 496
Cdd:TIGR02168 668 TNSSILERRREIEE--LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 497 QQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRT-LKAEEAAVVAEQEDLLRLRgp 575
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaLDELRAELTLLNEEAANLR-- 823
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217376813 576 lQAEALSVNESHVTSRAMQDPVFQLptAGRTPNGEVGAMDLTQLQKEKQDLEQQLLEKNKTIKQMQQRMLELRKTLQK 653
Cdd:TIGR02168 824 -ERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-509 |
2.76e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 190 KKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQ 269
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 270 ALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAI 349
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 350 NTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESShvqqqalALEQQFLERTQALEAQIVALE---RTR 426
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-------SELEALLNERASLEEALALLRselEEL 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 427 AADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVR-KQREEFQQQAANLTA 505
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIeDDEEEARRRLKRLEN 979
|
....
gi 2217376813 506 IIDE 509
Cdd:TIGR02168 980 KIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-594 |
2.46e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 53 REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALALARKD 132
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 133 QEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQ---------QQELSKIKHMLLKKEESLGKMEQELE 203
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvkallknQSGLSGILGVLSELISVDEGYEAAIE 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 204 ARTRElsRTQEELMNSNQMSSD----LSQK-------LEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALI 272
Cdd:TIGR02168 541 AALGG--RLQAVVVENLNAAKKaiafLKQNelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 273 QQLS------------IDLQK---------------------VTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQE 319
Cdd:TIGR02168 619 SYLLggvlvvddldnaLELAKklrpgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEK 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 320 LLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESShvqq 399
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE---- 774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 400 qalaleqqflERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEY---ERSLQNHQF-------ELKKLK 469
Cdd:TIGR02168 775 ----------EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERriaaterRLEDLE 844
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 470 EEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAEL 549
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2217376813 550 EALRTLKAEEAAVVAEQEDLLRLRGPLQAEALSVNESHVTSRAMQ 594
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
53-509 |
2.93e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 53 REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALALARKD 132
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 133 QEwSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSRT 212
Cdd:COG1196 391 AL-RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 213 QEELMNSNQMSSDLSQKLEELQRHYSTLEEQRD-----------HVIASKTGAESKITALEQKEQELQALIQQLSIDL-- 279
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADyegflegvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAlq 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 280 QKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQ--NLEDTRQQLLAARSSQAKAINTLETRVR 357
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAavDLVASDLREADARYYVLGDTLLGRTLVA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 358 ELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEqqfLERTQALEAQIVALERTRAADQTTAEQGM 437
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA---EAELEELAERLAEEELELEEALLAEEEEE 706
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217376813 438 RQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDE 509
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-527 |
6.20e-09 |
|
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: 59.65 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 55 DLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSsmRKFQEQNETFQANRAKMAEGLALALARKDQE 134
Cdd:TIGR04523 86 DLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQ--KKENKKNIDKFLTEIKKKEKELEKLNNKYND 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 135 WSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRR----------DEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEA 204
Cdd:TIGR04523 164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLlklelllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 205 RTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALE-QKEQELQALI--QQLSIDLQK 281
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnQKEQDWNKELksELKNQEKKL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 282 VTAETQ--EKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLaarssqaKAINTLETRVREL 359
Cdd:TIGR04523 324 EEIQNQisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK-------QEIKNLESQINDL 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 360 EQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQ 439
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 440 LEQENAALKECRNEYERSLQnhqfELKKLKEEWSQREivsvamaQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTE 519
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEK----ELKKLNEEKKELE-------EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
....*...
gi 2217376813 520 VLLQKEQE 527
Cdd:TIGR04523 546 ELNKDDFE 553
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
54-547 |
1.08e-08 |
|
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: 58.98 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 54 EDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKhQDSSMRKFQEQNETFQANraKMAEGLALALARKDq 133
Cdd:pfam15921 345 EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK-REKELSLEKEQNKRLWDR--DTGNSITIDHLRRE- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 134 ewsekMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSrtq 213
Cdd:pfam15921 421 -----LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE--- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 214 eelmNSNQMSSDLSQKLEELQRhysTLEEQRDHVIASKTGAESKITALEQKEQELQALiQQLSIDLQKVTAETQEKEDVI 293
Cdd:pfam15921 493 ----SSERTVSDLTASLQEKER---AIEATNAEITKLRSRVDLKLQELQHLKNEGDHL-RNVQTECEALKLQMAEKDKVI 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 294 THLQEKVASLEKRLEQN--LSGEEHLQELLKEKTLAEQNLEdtRQQLLAARSSQAKAINTLETRVRELE----QTLQASE 367
Cdd:pfam15921 565 EILRQQIENMTQLVGQHgrTAGAMQVEKAQLEKEINDRRLE--LQEFKILKDKKDAKIRELEARVSDLElekvKLVNAGS 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 368 EQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENA-- 445
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGsd 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 446 ----------------------ALKECRNEYERSLQNHQFELKKLKEEWSQ--REIVSVA-----MAQALEEVRKQREEF 496
Cdd:pfam15921 723 ghamkvamgmqkqitakrgqidALQSKIQFLEEAMTNANKEKHFLKEEKNKlsQELSTVAteknkMAGELEVLRSQERRL 802
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2217376813 497 QQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNsalLQIHQLQA 547
Cdd:pfam15921 803 KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHT---LDVKELQG 850
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-552 |
2.01e-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: 58.16 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 160 SMNLFQRRDEMDELEGfqqqelskikhmllkkeesLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYST 239
Cdd:TIGR02169 149 SMSPVERRKIIDEIAG-------------------VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 240 LEEQRDhVIASKTGAESKITALEQKEQELQaliqqlsidLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQE 319
Cdd:TIGR02169 210 AERYQA-LLKEKREYEGYELLKEKEALERQ---------KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 320 LLKEKTLAEQNLEDTRqqllaarssqakaINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQ 399
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEK-------------IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 400 QALALEQQFLERTQALEAQIVALERTRAADQTTAeqgmRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVS 479
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEELEDLRAELEEVDKEF----AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376813 480 VAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEAL 552
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
190-393 |
3.44e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 190 KKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQ 269
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 270 ALIQQLSIDLQKvtAETQEKEDVITHlQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAI 349
Cdd:COG4942 104 EELAELLRALYR--LGRQPPLALLLS-PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217376813 350 NTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQE 393
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
192-582 |
5.41e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 192 EESLGKMEQELEARtRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQ----RDHViasktgaESKITALEQKEQe 267
Cdd:PRK04863 279 NERRVHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDyqaaSDHL-------NLVQTALRQQEK- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 268 lqalIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQN-------------------------------LSGEEH 316
Cdd:PRK04863 350 ----IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAeeevdelksqladyqqaldvqqtraiqyqqaVQALER 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 317 LQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVA------AQETQIQELAAA 390
Cdd:PRK04863 426 AKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGevsrseAWDVARELLRRL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 391 NQESSHVqqqalaleqqflERTQALEAQIVALERtRAADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKE 470
Cdd:PRK04863 506 REQRHLA------------EQLQQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 471 EWSQREIVSVAMAQALEEVRKQREEFQQQA-ANLTAiiDEKEQNLREKTEVLLQKEQEILQLerghnsallqihqLQAEL 549
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQRLAARApAWLAA--QDALARLREQSGEEFEDSQDVTEY-------------MQQLL 637
|
410 420 430
....*....|....*....|....*....|...
gi 2217376813 550 EALRTLKAEEAAVVAEQEDLLRlrgplQAEALS 582
Cdd:PRK04863 638 ERERELTVERDELAARKQALDE-----EIERLS 665
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
58-555 |
5.46e-08 |
|
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: 56.57 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 58 SQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEialekhqdssmRKFQEQNETFQANRAKMAEGLALALARKDQeWSE 137
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ-----------QEINEKTTEISNTQTQLNQLKDEQNKIKKQ-LSE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 138 KMDQLEKEKNI---LTAQLQEMKNQSMNLFQRRDEmdELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQE 214
Cdd:TIGR04523 272 KQKELEQNNKKikeLEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 215 ELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVIT 294
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 295 HLQEKVASLEKRLEQnlsgeehLQELLKEKTLAEQNLEDTRQQllaarssQAKAINTLETRVRELEQTLQASEEQLQQsk 374
Cdd:TIGR04523 430 RLKETIIKNNSEIKD-------LTNQDSVKELIIKNLDNTRES-------LETQLKVLSRSINKIKQNLEQKQKELKS-- 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 375 givaaQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIvalertraadqTTAEQGMRQLEQENAALKE--CRN 452
Cdd:TIGR04523 494 -----KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK-----------KEKESKISDLEDELNKDDFelKKE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 453 EYERSLQNHQFELKKLKEEWsqreivsvamaqalEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLE 532
Cdd:TIGR04523 558 NLEKEIDEKNKEIEELKQTQ--------------KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
490 500
....*....|....*....|...
gi 2217376813 533 RGHNSALLQIHQLQAELEALRTL 555
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQE 646
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
329-565 |
7.38e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 329 QNLEDTRQQLLAARssqaKAINTLEtRVRELEQTLQASEEQLQQSKGIVAA-----QETQIQELAAANQESSHVQQQALA 403
Cdd:COG4913 235 DDLERAHEALEDAR----EQIELLE-PIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 404 LEQQFLERTQALEAQIVALERTRAADQTTAEQgmrQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIvsvAMA 483
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRGNGGDRLE---QLEREIERLERELEERERRRARLEALLAALGLPLPASAE---EFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 484 QALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRTLKAEEAAVV 563
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFV 463
|
..
gi 2217376813 564 AE 565
Cdd:COG4913 464 GE 465
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
68-389 |
7.80e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 68 RKLEARLSDYAEQVRNLQKIKEKLEIALEKHQ--DSSMRKFQEQNETFQANRAKMAEGLALALARKDQEWSEKMdqleKE 145
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIErlDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELL----KE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 146 KNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKM-EQELEARTRELSRTQEELMNSNQMSS 224
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 225 DLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLE 304
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 305 KRLEQNLSGEEHLQ----ELLKEKTLAEQNLEDTRQQLLAARSsqakAINTLETRVRELEQTLQASEEQLQQSKGIVAAQ 380
Cdd:TIGR02169 392 EKLEKLKREINELKreldRLQEELQRLSEELADLNAAIAGIEA----KINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
|
....*....
gi 2217376813 381 ETQIQELAA 389
Cdd:TIGR02169 468 EQELYDLKE 476
|
|
| GRIP |
pfam01465 |
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ... |
692-734 |
1.06e-07 |
|
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.
Pssm-ID: 460221 [Multi-domain] Cd Length: 44 Bit Score: 48.50 E-value: 1.06e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217376813 692 EINFEYLKHVVLKFMSCRE-SEAFHLIKAVSVLLNFSQEEENML 734
Cdd:pfam01465 1 GANLEYLKNVLLQFLESKEsSERKQLLPVIATLLKFSPEEEQKI 44
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
114-323 |
1.21e-07 |
|
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: 54.77 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 114 QANRAKMAEGLALALARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEE 193
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 194 SLGKMEQELEARTRELSRTQE----ELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQ 269
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217376813 270 ALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKE 323
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-459 |
1.24e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 225 DLSQKLEELQRHYSTLEEQRDHVIAsktgAESKITALEQkeqelqalIQQLSIDLQKVTAETQEKEDVITHL-----QEK 299
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALED----AREQIELLEP--------IRELAERYAAARERLAELEYLRAALrlwfaQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 300 VASLEKRLEQNlsgEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTletRVRELEQTLQASEEQLQQSKGIVAA 379
Cdd:COG4913 290 LELLEAELEEL---RAELARLEAELERLEARLDALREELDELEAQIRGNGGD---RLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 380 QETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYERSLQ 459
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
46-737 |
2.02e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 46 ASDGSSSREDLSSQLLRRNEQIRKLE-ARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANR--AKMAE 122
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEdAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRqaAIKAE 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 123 GLALALARKDQEWSEKMDQLEKEKNILTAQlqEMKNQSmnlfQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKME--- 199
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKAD--EAKKKA----EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaak 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 200 QELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRhysTLEEQRDHVIASKTGAESKITALEQKEQELQaliQQLSIDL 279
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK---KAEEKKKADEAKKKAEEDKKKADELKKAAAA---KKKADEA 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 280 QKVTAETQEKEDVITHLQE--KVASLEKRLEQNLSGEEhlqelLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVR 357
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKAEE-----AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 358 ELEqtLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGM 437
Cdd:PTZ00121 1499 ADE--AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 438 RQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREK 517
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 518 TEVLLQKEQEILQLERGHNSAllqiHQLQAELEALRtlKAEEaAVVAEQEDLLRLRGPLQAEALSVNESHVTSRAMQDPV 597
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKA----EEAKKAEEDEK--KAAE-ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 598 FQLPTAGRTPNGEVGAMDLTQLQKEKQDLEQQLleKNKTIKQMQQRMLELRKTLQKELKIRPDNELFEVREKPGPEMANM 677
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL--KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376813 678 APSV----TNNTDLTDAREINFEYLKHVVL-KFMSCRESEAF--HLIKAVSVLLNFSQEEENMLKET 737
Cdd:PTZ00121 1808 ANIIeggkEGNLVINDSKEMEDSAIKEVADsKNMQLEEADAFekHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-345 |
2.13e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 52 SREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKmaeglalaLARK 131
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS--------LERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 132 DQEWSEKMDQLEKEKNILTAQLQEMKnqsmnlfQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSR 211
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLL-------AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 212 TQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQAliqqlsiDLQKVTAETQEKED 291
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE-------EKEDKALEIKKQEW 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2217376813 292 VITHLQEKVASLEKRLEQNlsgEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQ 345
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDL---KEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
338-605 |
2.14e-07 |
|
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: 54.00 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 338 LLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKgivAAQETQIQELAAANQESSHVQqqalaleqqflERTQALEA 417
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALK---KEEKALLKQLAALERRIAALA-----------RRIRALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 418 QIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQ 497
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 498 QQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRtlkAEEAAVVAEQEDLLRLRGPLQ 577
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|....*....
gi 2217376813 578 AE-ALSVNESHVTSRAMQDPVFQLPTAGR 605
Cdd:COG4942 234 AEaAAAAERTPAAGFAALKGKLPWPVSGR 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
124-395 |
2.91e-07 |
|
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: 53.23 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 124 LALALARKDQEWSEKMDQLEKEKNILTAQLQEMKnqsmnlfQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELE 203
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELE-------KELAALKKEEKALLKQLAALERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 204 ARTRELSRTQEELmnsnqmsSDLSQKLEELQRHYSTLEeqrdhVIASKTGAESKITALEQKEQELQALiqQLSIDLQKVT 283
Cdd:COG4942 80 ALEAELAELEKEI-------AELRAELEAQKEELAELL-----RALYRLGRQPPLALLLSPEDFLDAV--RRLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 284 AETQEKEDVITHLQEKVASLEKRLEQNlsgeehlqelLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTL 363
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAE----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250 260 270
....*....|....*....|....*....|..
gi 2217376813 364 QASEEQLQQSKGIVAAQETQIQELAAANQESS 395
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-372 |
4.63e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 53 REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSsmrkFQEQNETFQANRAKMAEglalaLARKD 132
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE----LKALREALDELRAELTL-----LNEEA 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 133 QEWSEKMDQLEKEKNILTAQLQEMKNQSMNLfqrrdemdelegfqQQELSKIKHMLLKKEESLGKMEQELEARTRELSRT 212
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEEL--------------SEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 213 QEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQ-ALIQQLSIDLQKVTAETQEKED 291
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQeRLSEEYSLTLEEAEALENKIED 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 292 VITHLQEKVASLEKRLEQ----NLSGEEHLQELLKEKTLAEQNLEDtrqqLLAARSSQAKAINTLETRVRE-LEQTLQAS 366
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYDFLTAQKED----LTEAKETLEEAIEEIDREARErFKDTFDQV 1041
|
....*.
gi 2217376813 367 EEQLQQ 372
Cdd:TIGR02168 1042 NENFQR 1047
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
192-573 |
9.02e-07 |
|
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: 52.65 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 192 EESLGKMEQELEARtRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEeqrdhviasktgaeskitaleqkeQELQAL 271
Cdd:COG3096 278 NERRELSERALELR-RELFGARRQLAEEQYRLVEMARELEELSARESDLE------------------------QDYQAA 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 272 IQQLSIDLQKVTAetQEKedvITHLQEKVASLEKRLEQNlsgEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQA---KA 348
Cdd:COG3096 333 SDHLNLVQTALRQ--QEK---IERYQEDLEELTERLEEQ---EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqQA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 349 INTLETRVRELEQTLQASEEqlqqskgivAAQETQIQELAAANQESSHvqqqalaleQQFLERTQALEAQIVALErTRAA 428
Cdd:COG3096 405 LDVQQTRAIQYQQAVQALEK---------ARALCGLPDLTPENAEDYL---------AAFRAKEQQATEEVLELE-QKLS 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 429 DqttAEQGMRQLEQENAALKECRNEYERSlQNHQfELKKLKEEWSQREIVS---VAMAQALEEVRK---QREEFQQQAAN 502
Cdd:COG3096 466 V---ADAARRQFEKAYELVCKIAGEVERS-QAWQ-TARELLRRYRSQQALAqrlQQLRAQLAELEQrlrQQQNAERLLEE 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376813 503 LTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRT----LKAEEAAVVAEQEDLLRLR 573
Cdd:COG3096 541 FCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRArikeLAARAPAWLAAQDALERLR 615
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-363 |
9.66e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 9.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 192 EESLGKMEQELEARTRELSRTQEELMNSNQMS--SDLSQKLEELQRHYSTLEEQRDHVIASKtgaeSKITALEQKEQELQ 269
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERLDASS----DDLAALEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 270 ALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQakaI 349
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER---I 775
|
170
....*....|....
gi 2217376813 350 NTLETRVRELEQTL 363
Cdd:COG4913 776 DALRARLNRAEEEL 789
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
137-658 |
1.08e-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: 52.33 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 137 EKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEEL 216
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 217 MNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIqqlsIDLQKVTAETQEKEDVITHL 296
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL----SNLKKKIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 297 QEKVASLEKRLEQnlsgeehLQELLKEKTLAeqnLEDTRQQLLAARSSQAKAINTLETRVRELEQT---LQASEEQLQQS 373
Cdd:TIGR04523 224 KKQNNQLKDNIEK-------KQQEINEKTTE---ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkIKELEKQLNQL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 374 KgivaaqeTQIQELaaANQESSHVQQQALALEQQFLERTQALEAQIvalertraadqttaeqgmRQLEQENAALKECRNE 453
Cdd:TIGR04523 294 K-------SEISDL--NNQKEQDWNKELKSELKNQEKKLEEIQNQI------------------SQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 454 YERSLQNHQFELKKLKEEWSQREivsvamaQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLER 533
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQ-------NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 534 GHNSALLQIHQLQAEL----EALRTLKAEEAAVVAEQEDLLRLRGPLQAEALSVNESHVTSRAMQDPVFQlptagrtpNG 609
Cdd:TIGR04523 420 EKELLEKEIERLKETIiknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK--------EL 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2217376813 610 EVGAMDLTQLQKEKQDLEQQLLEKNKTIKQMQQRMLELRKT-LQKELKIR 658
Cdd:TIGR04523 492 KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEkKEKESKIS 541
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
50-630 |
1.56e-06 |
|
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: 51.99 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 50 SSSREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQ---DSSMRKFQEQNETFQANRAKMAEglal 126
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrrDKLTEEYAELKEELEDLRAELEE---- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 127 aLARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEART 206
Cdd:TIGR02169 376 -VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 207 RELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQ------------- 273
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvg 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 274 ---QLSID------LQKVTAETQE-KEDVITHLQEKVASLEKRLEQN-LSGEEHLQELLKEK------------------ 324
Cdd:TIGR02169 535 eryATAIEvaagnrLNNVVVEDDAvAKEAIELLKRRKAGRATFLPLNkMRDERRDLSILSEDgvigfavdlvefdpkyep 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 325 --------TLAEQNLEDTRQQLLAAR------------------SSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVA 378
Cdd:TIGR02169 615 afkyvfgdTLVVEDIEAARRLMGKYRmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQ 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 379 AQETQI--------QELAAANQESSHVQQQALA---LEQQFLERTQALEAQIVALERTRAAD---QTTAEQGMRQLEQEN 444
Cdd:TIGR02169 695 SELRRIenrldelsQELSDASRKIGEIEKEIEQleqEEEKLKERLEELEEDLSSLEQEIENVkseLKELEARIEELEEDL 774
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 445 AALKECRNEYERSLQNHQF-----ELKKLKEEWSQREIVSVAMAQALEEV-------RKQREEFQQQAANLTAIIDEKEQ 512
Cdd:TIGR02169 775 HKLEEALNDLEARLSHSRIpeiqaELSKLEEEVSRIEARLREIEQKLNRLtlekeylEKEIQELQEQRIDLKEQIKSIEK 854
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 513 -------NLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRTlKAEEAAVVAEQEDLLRLRGPLQAEALSVNE 585
Cdd:TIGR02169 855 eienlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER-KIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 2217376813 586 SHVTsramqdpvfQLPTAGRTPNGEVgaMDLTQLQKEKQDLEQQL 630
Cdd:TIGR02169 934 SEIE---------DPKGEDEEIPEEE--LSLEDVQAELQRVEEEI 967
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
149-361 |
1.70e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 51.23 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 149 LTAQLQEMKNQSMnlfQRRDEMDELEgFQQQELSKIKhmlLKKEEslgkmEQELEARTRELSRTQE---------ELMNS 219
Cdd:COG0497 170 LKKELEELRADEA---ERARELDLLR-FQLEELEAAA---LQPGE-----EEELEEERRRLSNAEKlrealqealEALSG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 220 NQMS-----SDLSQKLEELQRHYSTLEEQRDHViasktgaESKITALEQKEQELQALIQQLSIDLQKVtAETQEKEDVIT 294
Cdd:COG0497 238 GEGGaldllGQALRALERLAEYDPSLAELAERL-------ESALIELEEAASELRRYLDSLEFDPERL-EEVEERLALLR 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376813 295 HLQEK-----------VASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARssqAKAINTLETRV-RELEQ 361
Cdd:COG0497 310 RLARKygvtveellayAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAAR---KKAAKKLEKAVtAELAD 385
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
130-427 |
1.84e-06 |
|
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: 51.66 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 130 RKDQEWSEKMDQlekekniltAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKI-------KHMLLKKEESLGKMEQEL 202
Cdd:pfam17380 287 RQQQEKFEKMEQ---------ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQaaiyaeqERMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 203 EARTRELSRTQEELMNSNQMSSDLSQKLE------------ELQRHYSTLEEQRDHVIASKTGAESKITAL--EQKEQEL 268
Cdd:pfam17380 358 RKRELERIRQEEIAMEISRMRELERLQMErqqknervrqelEAARKVKILEEERQRKIQQQKVEMEQIRAEqeEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 269 QALIQQLSIDLQKVTAETQEKEDVITHLQEKVASlEKRLEQNLSGEEHLQELLKE--KTLAEQNLEDTRQQLLAARSSQA 346
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEE-RKRKKLELEKEKRDRKRAEEqrRKILEKELEERKQAMIEEERKRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 347 KAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQE-LAAANQESSHVQQqalaleqqfLERTQALEAQIVALERT 425
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEqMRKATEERSRLEA---------MEREREMMRQIVESEKA 587
|
..
gi 2217376813 426 RA 427
Cdd:pfam17380 588 RA 589
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
70-563 |
1.92e-06 |
|
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: 51.66 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 70 LEARLSDYAEQVRNLQKIKEKLEIALEKHQ---DSSMRKFQEQNETFQANRAKMAEglalALARKDQEWSEKMDQLEKEK 146
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfylRQSVIDLQTKLQEMQMERDAMAD----IRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 147 NILTAQ--LQE--MKNQSMNLFQRRDEMDELEGFqqqeLSKIKHMLLKKEESLGKMEQELEARTRelsrtqeelMNSNQM 222
Cdd:pfam15921 152 HELEAAkcLKEdmLEDSNTQIEQLRKMMLSHEGV----LQEIRSILVDFEEASGKKIYEHDSMST---------MHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 223 SSDLSQKLEELQRHYSTLEEQ----RDHVIASKTGAESKITALEQKEQElqaLIQQLsidlqkvtaeTQEKEDVITHLQE 298
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRifpvEDQLEALKSESQNKIELLLQQHQD---RIEQL----------ISEHEVEITGLTE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 299 KVASLEKRLEQNLSGEEHLQELLK-EKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIV 377
Cdd:pfam15921 286 KASSARSQANSIQSQLEIIQEQARnQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 378 A--AQET-----QIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALErtRAADQTTAEqgMRQLEQENAALK-E 449
Cdd:pfam15921 366 DqfSQESgnlddQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR--RELDDRNME--VQRLEALLKAMKsE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 450 CRNEYER---SLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQR---EEFQQQAANLTAIIDEKEQ----------N 513
Cdd:pfam15921 442 CQGQMERqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKmtlESSERTVSDLTASLQEKERaieatnaeitK 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2217376813 514 LREKTEVLLQKEQEiLQLERGHnsallqIHQLQAELEALRTLKAEEAAVV 563
Cdd:pfam15921 522 LRSRVDLKLQELQH-LKNEGDH------LRNVQTECEALKLQMAEKDKVI 564
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
409-669 |
2.92e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 409 LERTQALEAQIVALERTRAADQTTAEQgMRQLEQenaalkecrneyersLQNHQFELKKLKEEwsQREIVSVAMAQALEE 488
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQ-IELLEP---------------IRELAERYAAARER--LAELEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 489 VRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSA-LLQIHQLQAELEALRTLKAEEAAVVAEQE 567
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 568 DLLR-LRGPLQAEALSVNESHVTSRAMQDPVFQLPTAGRTPNGEVGAmDLTQLQKEKQDLEQQL--LEKNKtiKQMQQRM 644
Cdd:COG4913 366 ALLAaLGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA-ALRDLRRELRELEAEIasLERRK--SNIPARL 442
|
250 260 270
....*....|....*....|....*....|
gi 2217376813 645 LELRKTLQKELKIRPDN-----ELFEVREK 669
Cdd:COG4913 443 LALRDALAEALGLDEAElpfvgELIEVRPE 472
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-462 |
3.97e-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: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 254 AESKITALEQKEQELQALIQQLSIDLQKvtaetqekedvithLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQnLED 333
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEA--------------LEAELDALQERREALQRLAEYSWDEIDVASAERE-IAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 334 TRQQLLAARSSQAKaINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQqfLERTQ 413
Cdd:COG4913 673 LEAELERLDASSDD-LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRA 749
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217376813 414 ALEAQIVALERTRAADQTTAEQGmRQLEQENAALKECRNEYERSLQNHQ 462
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLE-ERIDALRARLNRAEEELERAMRAFN 797
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
350-567 |
3.99e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 350 NTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESShvqqqALALEQQFLERTQALEAQIVALERTRAAD 429
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 430 QTTAEQGMRQLEQENAALKECRN-----EYERSLQNHQFELKKLKEEWSQReivSVAMAQALEEVRKQREEFQQQAANLT 504
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQspviqQLRAQLAELEAELAELSARYTPN---HPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376813 505 AIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRTL------KAEEAAVVAEQE 567
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELyesllqRLEEARLAEALT 384
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
129-573 |
4.31e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 129 ARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDE-LEGFQQ--QELSKIKHMLLKKEESLGKMEQELEA- 204
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvLEEHEErrEELETLEAEIEDLRETIAETEREREEl 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 205 --RTRELSRTQEELMNSN------------------QMSSDLSQKLEELQRhysTLEEQRDHVIASKTGAES---KITAL 261
Cdd:PRK02224 278 aeEVRDLRERLEELEEERddllaeaglddadaeaveARREELEDRDEELRD---RLEECRVAAQAHNEEAESlreDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 262 EQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLE----QNLSGEEHLQELLKEKTLAEQNLEDTRQQ 337
Cdd:PRK02224 355 EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 338 LLAARSSQAKA-------------------------------INTLETRVRELEQTLQASEEQLQQSKGIVAAqETQIQE 386
Cdd:PRK02224 435 LRTARERVEEAealleagkcpecgqpvegsphvetieedrerVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 387 LAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEyerslqnhqfeLK 466
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK-----------LA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 467 KLKEEWSQREIVSVAMAqALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQE-----ILQLERGHNSALLQ 541
Cdd:PRK02224 583 ELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdearIEEAREDKERAEEY 661
|
490 500 510
....*....|....*....|....*....|....*.
gi 2217376813 542 IHQLQAELEALR----TLKAEEAAVVAEQEDLLRLR 573
Cdd:PRK02224 662 LEQVEEKLDELReerdDLQAEIGAVENELEELEELR 697
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
188-554 |
4.48e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 188 LLKKEESLGKMEQELEARTRELSRTQEELMNS---------------NQMSSDLSQKLEELQRHYSTLEEQRDHVIASKT 252
Cdd:PRK04863 221 LLPENSGVRKAFQDMEAALRENRMTLEAIRVTqsdrdlfkhlitestNYVAADYMRHANERRVHLEEALELRRELYTSRR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 253 GAES----------KITALEQKEQELQALIQQLSIDLQKV-TAETQEKEdvITHLQEKVASLEKRLEQNLSGEEHLQELL 321
Cdd:PRK04863 301 QLAAeqyrlvemarELAELNEAESDLEQDYQAASDHLNLVqTALRQQEK--IERYQADLEELEERLEEQNEVVEEADEQQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 322 KE----KTLAEQNLEDTRQQLlaarSSQAKAINTLETRVRELEQTLQASEE----------QLQQSKGIVAAQETQIQEL 387
Cdd:PRK04863 379 EEnearAEAAEEEVDELKSQL----ADYQQALDVQQTRAIQYQQAVQALERakqlcglpdlTADNAEDWLEEFQAKEQEA 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 388 AAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQttAEQGMRQLEQENA------ALKECRNEYERSLQNH 461
Cdd:PRK04863 455 TEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDV--ARELLRRLREQRHlaeqlqQLRMRLSELEQRLRQQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 462 QfELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAanltaiiDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQ 541
Cdd:PRK04863 533 Q-RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESL-------SESVSEARERRMALRQQLEQLQARIQRLAARAPA 604
|
410
....*....|...
gi 2217376813 542 IHQLQAELEALRT 554
Cdd:PRK04863 605 WLAAQDALARLRE 617
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
112-346 |
4.73e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 112 TFQANRAKMAEGLALALARKDQEWS--EKMDQLEKEKNILTAQLQEMKNQ------SMNLFQRRDEMDELEGFQQQELSK 183
Cdd:COG3206 141 SYTSPDPELAAAVANALAEAYLEQNleLRREEARKALEFLEEQLPELRKEleeaeaALEEFRQKNGLVDLSEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 184 IKHMllkkEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQK--LEELQRHYSTLEEQRDHVIASKTGAESKITAL 261
Cdd:COG3206 221 LSEL----ESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 262 EQKEQELQALIQQ-LSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLA 340
Cdd:COG3206 297 RAQIAALRAQLQQeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
....*.
gi 2217376813 341 ARSSQA 346
Cdd:COG3206 377 ARLAEA 382
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
130-564 |
5.96e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 130 RKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEgfQQQELSKIKHMLLKKEESLGKMEQELEARTREL 209
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELE--AELEELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 210 SRTQEELmnsnqmssdlsQKLEELQRHYSTLEEQRDHVIASKTGAESKI-TALEQKEQELQALIQQLSIDLQKVTAETQE 288
Cdd:COG4717 142 AELPERL-----------EELEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 289 KEDVITHLQEKVASLEKRLEQ---NLSGEEHLQELLKEKTLA------------EQNLEDTRQQLLAARSSQAKAINTLE 353
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQlenELEAAALEERLKEARLLLliaaallallglGGSLLSLILTIAGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 354 TRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQttA 433
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE--L 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 434 EQGMRQLEQENAAlkECRNEYERSLQNHQfELKKLKEEWS--QREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKE 511
Cdd:COG4717 369 EQEIAALLAEAGV--EDEEELRAALEQAE-EYQELKEELEelEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2217376813 512 QNLREKTEVLLQKEQEILQLERGHnsALLQIHQLQAELEALRTLKAEEAAVVA 564
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDG--ELAELLQELEELKAELRELAEEWAALK 496
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
133-555 |
6.54e-06 |
|
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: 49.79 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 133 QEWSEKMDQLEKEKNILTAQLQemknQSMNLFQRRDEMDELEGFQQQELSKIKHmllkkeeslgkmeqELEARTRELSRT 212
Cdd:pfam01576 29 KELEKKHQQLCEEKNALQEQLQ----AETELCAEAEEMRARLAARKQELEEILH--------------ELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 213 QEELMNSNQmssDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDV 292
Cdd:pfam01576 91 SQQLQNEKK---KMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 293 ITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQ 372
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 373 SKGIVAAQETQIQELAAANQE-SSHVQQQALALEQQFLERTQA----------LEAQIVALERTraADQTTAEQGMR-QL 440
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRElEAQISELQEDLESERAARNKAekqrrdlgeeLEALKTELEDT--LDTTAAQQELRsKR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 441 EQENAALKECRNEYERS--------LQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQ 512
Cdd:pfam01576 326 EQEVTELKKALEEETRSheaqlqemRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEH 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2217376813 513 NlREKTEVLLQKEQEIL-QLERGHNSALLQIHQLQAELEALRTL 555
Cdd:pfam01576 406 K-RKKLEGQLQELQARLsESERQRAELAEKLSKLQSELESVSSL 448
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
129-337 |
6.62e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 129 ARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKikhmllkkeeslgkmeQELEARTRE 208
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV----------------ASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 209 LSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKItalEQKEQELQALIQQLSidlqkvTAETQE 288
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLE------AAEDLA 743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217376813 289 KEDVITHLQEKVASL-----EKRLEQNLsgEEHLQELLKEKTLAEQNLEDTRQQ 337
Cdd:COG4913 744 RLELRALLEERFAAAlgdavERELRENL--EERIDALRARLNRAEEELERAMRA 795
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
178-502 |
1.39e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 178 QQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESK 257
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 258 ITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLeQNLSGEEHLQELLKEKTLAEQNLEDTRQQ 337
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL-QALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 338 LLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEA 417
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 418 QIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQ 497
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362
|
....*
gi 2217376813 498 QQAAN 502
Cdd:COG4372 363 AEAGV 367
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
148-571 |
1.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 148 ILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLS 227
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 228 QKLE--ELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAE----TQEKEDVITHLQEKVA 301
Cdd:COG4717 123 KLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELleqlSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 302 SLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQL-LAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQ 380
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 381 ETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEY-----E 455
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAeeleeE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 456 RSLQNHQFELKKLKEEWSQREIVS-VAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKE-----QEIL 529
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEleeleEELE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2217376813 530 QLERGHNSALLQIHQLQAELEALRT------LKAEEAAVVAEQEDLLR 571
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEdgelaeLLQELEELKAELRELAE 490
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
58-655 |
1.49e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 58 SQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQAnrakmaEGLALALARKDQEWSE 137
Cdd:TIGR00618 146 VVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS------QLLTLCTPCMPDTYHE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 138 KMDQLEKEKNILTAQLQEMKnQSMNLFQRRDEMDELEGFQQQELSKIKhmllkkeeslgKMEQELEARTRELSRTQEELM 217
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLKKQQLLKQLR-----------ARIEELRAQEAVLEETQERIN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 218 NSNQMSsdlsqKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQAliQQLSIDLQKVTAET-QEKEDVITHL 296
Cdd:TIGR00618 288 RARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTlHSQEIHIRDA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 297 QEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKaINTLETRVRELEQTLQASEEQLQQSKGI 376
Cdd:TIGR00618 361 HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT-IDTRTSAFRDLQGQLAHAKKQQELQQRY 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 377 VAAQETQIQELAaanQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYE- 455
Cdd:TIGR00618 440 AELCAAAITCTA---QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPa 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 456 -----------RSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDE--KEQNLREKTEVLL 522
Cdd:TIGR00618 517 rqdidnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRskEDIPNLQNITVRL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 523 QKEQEILQLERGHNSALLQIHQLQAELEALRTLKAEEAAVVAEQEDLLRLRgpLQAEALSVNESHVTSRAMQDPVFQLPT 602
Cdd:TIGR00618 597 QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA--LHALQLTLTQERVREHALSIRVLPKEL 674
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376813 603 AGRTPNGEVGAMD-----------LTQLQKEKQDLEQQLLEKNKTIKQMQQRMLELRKTLQKEL 655
Cdd:TIGR00618 675 LASRQLALQKMQSekeqltywkemLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-309 |
1.50e-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: 47.84 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 50 SSSREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEkhqdssmrkfqeqnetfqanrakmaeglalALA 129
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------------------------------ALA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 130 RKDQEWSEKMDQLEKEKNILTAQLQEMKNQsmnLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEArTREL 209
Cdd:COG4942 69 RRIRALEQELAALEAELAELEKEIAELRAE---LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 210 SRTQEELMNsnqmssDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEK 289
Cdd:COG4942 145 APARREQAE------ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|
gi 2217376813 290 EDVITHLQEKVASLEKRLEQ 309
Cdd:COG4942 219 QQEAEELEALIARLEAEAAA 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
188-582 |
1.54e-05 |
|
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: 48.80 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 188 LLKKEESLGKMEQELEARTRELSRTQEELMNS---------------NQMSSDLSQKLEELQRHY-STLEEQRDHVIASK 251
Cdd:COG3096 220 LLPENSGVRKAFQDMEAALRENRMTLEAIRVTqsdrdlfkhliteatNYVAADYMRHANERRELSeRALELRRELFGARR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 252 TGAESK---------ITALEQKEQELQALIQQLSIDLQKVTAETQEKEDvITHLQEKVASLEKRLEQNlsgEEHLQELLK 322
Cdd:COG3096 300 QLAEEQyrlvemareLEELSARESDLEQDYQAASDHLNLVQTALRQQEK-IERYQEDLEELTERLEEQ---EEVVEEAAE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 323 EKTLAEQNLEDTRQQLLAARSSQA---KAINTLETRVRELEQTLQASEE----------QLQQSKGIVAAQETQIQELAA 389
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLAdyqQALDVQQTRAIQYQQAVQALEKaralcglpdlTPENAEDYLAAFRAKEQQATE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 390 ANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADqtTAEQGMRQ------LEQENAALKECRNEYERSLQNHQf 463
Cdd:COG3096 456 EVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQ--TARELLRRyrsqqaLAQRLQQLRAQLAELEQRLRQQQ- 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 464 ELKKLKEEWSQREIVSVAMAQALEEVRK----QREEFQQQAANLTA---IIDEKEQNLREKTEVLLQKE------QEILQ 530
Cdd:COG3096 533 NAERLLEEFCQRIGQQLDAAEELEELLAeleaQLEELEEQAAEAVEqrsELRQQLEQLRARIKELAARApawlaaQDALE 612
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217376813 531 LERGHNSALLQ-----IHQLQAELEALRTLKAEEAAVVAEQEDLLRlrgplQAEALS 582
Cdd:COG3096 613 RLREQSGEALAdsqevTAAMQQLLEREREATVERDELAARKQALES-----QIERLS 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
37-556 |
1.54e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 37 MGADSGDDFASDGSSSREDLSSQL---LRRNEQIRKL-EARLSDYAEQVRNLQKIKEKLEIALEK-------HQDSSMRK 105
Cdd:pfam15921 124 MERDAMADIRRRESQSQEDLRNQLqntVHELEAAKCLkEDMLEDSNTQIEQLRKMMLSHEGVLQEirsilvdFEEASGKK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 106 FQEQNETFQANRAKMAEGLALALARKDQEWSekmdQLEKEKNILTAQLQEMKNQSMNlfqrrdemdELEGFQQQELSKIK 185
Cdd:pfam15921 204 IYEHDSMSTMHFRSLGSAISKILRELDTEIS----YLKGRIFPVEDQLEALKSESQN---------KIELLLQQHQDRIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 186 HMLLKKE-ESLGKMEQELEARTR------ELSRTQEELMNSNQM--------SSDLSQKLEELQRHYSTLEEQRDHVIAS 250
Cdd:pfam15921 271 QLISEHEvEITGLTEKASSARSQansiqsQLEIIQEQARNQNSMymrqlsdlESTVSQLRSELREAKRMYEDKIEELEKQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 251 KTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQN 330
Cdd:pfam15921 351 LVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQR 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 331 LEdtrqQLLAARSSQAKAintletRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLE 410
Cdd:pfam15921 431 LE----ALLKAMKSECQG------QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 411 RTQALEAQIVALERTRAADQTTAEQGMRQLEQenaaLKECRNEyERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVR 490
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLRSRVDLKLQE----LQHLKNE-GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMT 575
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376813 491 -------KQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLE-RGHNSALLQIHQLQAELEALRTLK 556
Cdd:pfam15921 576 qlvgqhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEaRVSDLELEKVKLVNAGSERLRAVK 649
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-516 |
2.74e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 54 EDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEialekHQDSSMRKFQEQNETFqanrakmaeglaLALARKDQ 133
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-----EKVKELKELKEKAEEY------------IKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 134 EWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQ---QQELSKIKHMLLKKEESLGKMEQELEARTRELS 210
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 211 RTQEELMNsnqmssdlsqKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQA-------------------L 271
Cdd:PRK03918 384 LTPEKLEK----------ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkeL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 272 IQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRL--EQNLSGEEHLQELLK--EKTLAEQNLEDTRQ---------QL 338
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLkkESELIKLKELAEQLKelEEKLKKYNLEELEKkaeeyeklkEK 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 339 LAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQ 418
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 419 IVALERTRAADQTTAEQGMRQLEQENAALKECRNEYERSLQNH-QFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQ 497
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
490
....*....|....*....
gi 2217376813 498 QQAANLTAIIDEKEQNLRE 516
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKE 712
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
100-652 |
3.75e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 100 DSSMRKFQEQNETFQANRAKMAEGLALALARKDQEWSEKMDQLEKEKNILTAQLQemkNQSMNLFQRRDEMDELEgFQQQ 179
Cdd:TIGR00606 389 ERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIE---LKKEILEKKQEELKFVI-KELQ 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 180 ELSKIKHMLLKKEESLGKMEQEL---------EARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEeQRDHVIAS 250
Cdd:TIGR00606 465 QLEGSSDRILELDQELRKAERELskaeknsltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT-QMEMLTKD 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 251 KTGAESKITALE-QKEQELQALI------QQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRleqnlsgEEHLQELLKE 323
Cdd:TIGR00606 544 KMDKDEQIRKIKsRHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQN-------KNHINNELES 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 324 KTLAEQNLEDtrqQLLAARSSQAkaintLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQ----------- 392
Cdd:TIGR00606 617 KEEQLSSYED---KLFDVCGSQD-----EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrvfq 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 393 ---ESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLK 469
Cdd:TIGR00606 689 teaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 470 EEWSQREIVS-------------VAMAQALEEVRKQREEFQQQAANLTAI-----IDEKEQNLREKTEVLLQKEQEILQL 531
Cdd:TIGR00606 769 EQETLLGTIMpeeesakvcltdvTIMERFQMELKDVERKIAQQAAKLQGSdldrtVQQVNQEKQEKQHELDTVVSKIELN 848
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 532 ERGHNSALLQIHQLQAELEALRTLKAEEAAVVAEQEDLLRLRGPLQAEALSVNESHVTSRAMQDPVFQLPTAGRTPNGEV 611
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2217376813 612 gamdLTQLQKEKQDLEQQLLEKNKTIKQMQQRMLELRKTLQ 652
Cdd:TIGR00606 929 ----ISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-546 |
4.22e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 229 KLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASlEKRLE 308
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES-AKVCL 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 309 QNLSGEEHLQELLK--EKTLAEQ-------NLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGI--- 376
Cdd:TIGR00606 789 TDVTIMERFQMELKdvERKIAQQaaklqgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKtne 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 377 VAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYER 456
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 457 SLQNHQFELKKL--------KEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLR--EKTEVLLQKEQ 526
Cdd:TIGR00606 949 KVKNIHGYMKDIenkiqdgkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlQDNLTLRKREN 1028
|
330 340
....*....|....*....|
gi 2217376813 527 EILQLERGHNSALLQIHQLQ 546
Cdd:TIGR00606 1029 ELKEVEEELKQHLKEMGQMQ 1048
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
177-436 |
4.46e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 177 QQQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIAS--KTGA 254
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 255 ESKITALEQKEQELQALIQQLSIdLQKVTAETQEKEDVITHLQEKVASLEKRLEQNlsgeehlqelLKEKTLAEQNLEDT 334
Cdd:COG3883 101 SVSYLDVLLGSESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAKKAELEAK----------LAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 335 RQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQA 414
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
250 260
....*....|....*....|..
gi 2217376813 415 LEAQIVALERTRAADQTTAEQG 436
Cdd:COG3883 250 GAAGAAGAAAGSAGAAGAAAGA 271
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-579 |
4.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 198 MEQELEARTRELSRTQEELMNSNQMSSD-LSQKLEELQRHYSTLEEQRDhviaSKTGAESKITALEQKEQELQALIQQLS 276
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKeLEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 277 --IDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQ----AKAIN 350
Cdd:COG4717 123 klLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 351 TLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQES---------------SHVQQQALALEQQFLERTQAL 415
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallalLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 416 EAQIVALERTRAADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREE 495
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 496 FQQQAAN-----------------LTAIIDEKEQNLREKTEVLLQKEQeiLQLERGHNSALLQIHQLQAELEALRTLKAE 558
Cdd:COG4717 363 LQLEELEqeiaallaeagvedeeeLRAALEQAEEYQELKEELEELEEQ--LEELLGELEELLEALDEEELEEELEELEEE 440
|
410 420
....*....|....*....|.
gi 2217376813 559 EAAVVAEQEDLLRLRGPLQAE 579
Cdd:COG4717 441 LEELEEELEELREELAELEAE 461
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
327-557 |
5.56e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 327 AEQNLEDTRQQLLAAR---SSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELaaaNQESSHVQQQALA 403
Cdd:COG4942 18 QADAAAEAEAELEQLQqeiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 404 LEQQFLERTQALEAQIVALERTRAADQTtaeqgMRQLEQENAALKECRNEYERSLQNHQFE-LKKLKEEWSQREIVSVAM 482
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPL-----ALLLSPEDFLDAVRRLQYLKYLAPARREqAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376813 483 AQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRTLKA 557
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
65-574 |
5.62e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 65 EQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKhqdssmrkFQEQNETFQANRAKMAEglalaLARKDQEWSEKMDQLEK 144
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEK--------LEKEVKELEELKEEIEE-----LEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 145 EKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQ--ELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSNQM 222
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 223 SSDLSQKLEELQRHYSTLEEQR---DHVIASKTGAESKITALEQKE-QELQALIQQLSIDLQKVTAETQEKEDVITHLQE 298
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 299 KVASLEKRLEQNLSG------------EEHLQELLKEKTLAEQNLEDTRQQL------LAARSSQAKAINTLETRVRELE 360
Cdd:PRK03918 420 EIKELKKAIEELKKAkgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIeekerkLRKELRELEKVLKKESELIKLK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 361 QTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERT-RAADQTTAE----- 434
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKlDELEEELAEllkel 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 435 -----QGMRQLEQENAALKECRNEY------ERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANL 503
Cdd:PRK03918 580 eelgfESVEELEERLKELEPFYNEYlelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376813 504 TaiIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRTLKAEEAAVVAEQEDLLRLRG 574
Cdd:PRK03918 660 E--YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE 728
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
51-653 |
6.49e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 51 SSREDLSSQLLRRNEQIRKLEARLSDYAEQvRNLQKIKEKLeIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALALAR 130
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAVLEETQER-INRARKAAPL-AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 131 KDQEWSekMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDelegfQQQELSKIKHMLLKKEESLGKMEQELEARTRELS 210
Cdd:TIGR00618 334 VKQQSS--IEEQRRLLQTLHSQEIHIRDAHEVATSIREISC-----QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 211 RTQEELMNSNQMSSDLSQKL----EELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSiDLQKVTAET 286
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLahakKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ-TKEQIHLQE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 287 QEKEDVITHLQEKVASLEKRLEQNLSGEE--------------HLQELLKEKTLAEQNLEDTRQQLLAARssqaKAINTL 352
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIHPNparqdidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSER----KQRASL 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 353 ETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQ--------ALEAQIVALER 424
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQpeqdlqdvRLHLQQCSQEL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 425 TRAADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQ-------REEFQ 497
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELethieeyDREFN 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 498 QQAANLTAIIDEKEQNLREKTEVLlqKEQEILQLERGHNSALLQIHQLQAELEALRTLkAEEAAVVAEQEDLLRLRGPLQ 577
Cdd:TIGR00618 722 EIENASSSLGSDLAAREDALNQSL--KELMHQARTVLKARTEAHFNNNEEVTAALQTG-AELSHLAAEIQFFNRLREEDT 798
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217376813 578 AEALSVNESHVTSRamqdpvfqlptagrTPNGEVGAMDLTQLQKEKQDLEQQLLEKNKTIKQMQQRMLELRKTLQK 653
Cdd:TIGR00618 799 HLLKTLEAEIGQEI--------------PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
254-449 |
7.14e-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: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 254 AESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQ---N 330
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrsgG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 331 LEDTRQQLLAARS-----SQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALE 405
Cdd:COG3883 101 SVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217376813 406 QQFLERTQALEAQIVALERTRAADQTTAEQGMRQLEQENAALKE 449
Cdd:COG3883 181 EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
125-372 |
8.70e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 125 ALALARKDQEWSEKMDQLEKEKNILTAQLQEMKnqsmnlfqrrdemDELEGFQQQELSKIKHMLLKkeESLGKMEQELEA 204
Cdd:PRK11281 68 TLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQ-------------AELEALKDDNDEETRETLST--LSLRQLESRLAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 205 RTRELSRTQEELMNSNQMSSDLSQKLEELQRHYST----LEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQ 280
Cdd:PRK11281 133 TLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 281 KVTAETQEKEDVITHLQEKVASLEKRLEQNLsgeEHLQELLKEKTLAEQnlEDTRQQLLAARSSQAKAINTLetRVRELE 360
Cdd:PRK11281 213 KSLEGNTQLQDLLQKQRDYLTARIQRLEHQL---QLLQEAINSKRLTLS--EKTVQEAQSQDEAARIQANPL--VAQELE 285
|
250
....*....|..
gi 2217376813 361 QTLQASEEQLQQ 372
Cdd:PRK11281 286 INLQLSQRLLKA 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
240-435 |
8.83e-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: 45.53 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 240 LEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQE 319
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 320 LLKE--KTLAEQNLEDTRQQLLAARSS----------------QAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQE 381
Cdd:COG4942 105 ELAEllRALYRLGRQPPLALLLSPEDFldavrrlqylkylapaRREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217376813 382 TQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQ 435
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
445-560 |
1.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 445 AALKECRNEYERSLQNHQFELKKLKEEwsqreivsvAMAQALEEVRKQREEFQQQA-------ANLTAIIDEKEQNLREK 517
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKE---------ALLEAKEEIHKLRNEFEKELrerrnelQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2217376813 518 TEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRT-----------LKAEEA 560
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEeqlqelerisgLTAEEA 155
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
65-517 |
1.77e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 65 EQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALALARKDQEWSEKMDQLEK 144
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 145 ekniLTAQLQEMKNQSMNLFQRRDEMDELegfQQQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSNQMSS 224
Cdd:COG4717 151 ----LEERLEELRELEEELEELEAELAEL---QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 225 DLSQKLEELQ-RHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLsIDLQKVTAETQEKEDVITHLQEKVASL 303
Cdd:COG4717 224 ELEEELEQLEnELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI-AGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 304 EKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQ-QLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQET 382
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSpEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 383 QIQELAAAnqesshvqQQALALEQQFLERTQALEAQIVAL--ERTRAADQTTAEQGMRQLEQENAALKECRNEYERsLQN 460
Cdd:COG4717 383 DEEELRAA--------LEQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELEE-LRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376813 461 HQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAAN--LTAIIDEKEQNLREK 517
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALklALELLEEAREEYREE 512
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
65-656 |
2.61e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 65 EQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALALARKDQEWSEKMDQLEK 144
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 145 EKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHM----------LLKKEESLGKMEQEL----EARTRELS 210
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEArkaedakkaeAVKKAEEAKKDAEEAkkaeEERNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 211 RTQEELMNSNQMSSDLSQKLEELQR--HYSTLEEQRDHVIASKTGAESKITALEQKEQEL--------QALIQQLSIDLQ 280
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKadELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAkkadeakkKAEEAKKKADAA 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 281 KVTAETQEKEDVITHLQEKVAS--LEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRE 358
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAAdeAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 359 LEQtlQASEEQLQQSKGIVAAQEtqIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQGMR 438
Cdd:PTZ00121 1415 AAK--KKADEAKKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 439 QLEQENAALKECRNEYERSLQNHQF----ELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNL 514
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAkkaeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 515 R--EKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRTLKAEEAAVVAEQ-----EDLLRLRGPLQAEALSVNESH 587
Cdd:PTZ00121 1571 KaeEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkaeEEKKKVEQLKKKEAEEKKKAE 1650
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 588 VTSRAMQDPVFQLPTAGRTPNGEV-GAMDLTQLQKEKQDLEQQLLEKNKTIKQMQQrmleLRKTLQKELK 656
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE----LKKKEAEEKK 1716
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
478-658 |
3.99e-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: 43.60 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 478 VSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEALRTLKA 557
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 558 EEAAVVAEQEDLLRLRgpLQAEALSVNESHVTSRAMQDPVFQLPTAGR-----TPNGEVGAMDLTQLQKEKQDLEQQLLE 632
Cdd:COG4942 94 ELRAELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEA 171
|
170 180
....*....|....*....|....*.
gi 2217376813 633 KNKTIKQMQQRMLELRKTLQKELKIR 658
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAER 197
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1-347 |
4.31e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 1 MFAKLKKKIAEETAVAQRPGGATRIPRSVSKEsVASMGADSGDDFASDGSS-SREDLSSQLLRRNEQIRKLEARLSDYAE 79
Cdd:PRK11281 71 LLDKIDRQKEETEQLKQQLAQAPAKLRQAQAE-LEALKDDNDEETRETLSTlSLRQLESRLAQTLDQLQNAQNDLAEYNS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 80 QVRNLQKIKEK--------------LEIALEKHQDSSMRKFQEQNETFQANRA----------KMAEG----LALALARK 131
Cdd:PRK11281 150 QLVSLQTQPERaqaalyansqrlqqIRNLLKGGKVGGKALRPSQRVLLQAEQAllnaqndlqrKSLEGntqlQDLLQKQR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 132 DqEWSEKMDQLEKEknilTAQLQEMKNQSmNLFQRRDEMDELEgfQQQELSKIKH-MLLKKEESLG-KMEQELEARTREL 209
Cdd:PRK11281 230 D-YLTARIQRLEHQ----LQLLQEAINSK-RLTLSEKTVQEAQ--SQDEAARIQAnPLVAQELEINlQLSQRLLKATEKL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 210 -SRTQEELMNSNQmssdlsqkLEELQRHYSTLEEQrdhvIASKTGAE--SKItaLEQKEQELQA--LIQQLSI---DLQK 281
Cdd:PRK11281 302 nTLTQQNLRVKNW--------LDRLTQSERNIKEQ----ISVLKGSLllSRI--LYQQQQALPSadLIEGLADriaDLRL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 282 VTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEH--LQELLKE---------KTLAEQ-----NLEDTRQQLLA-ARSS 344
Cdd:PRK11281 368 EQFEINQQRDALFQPDAYIDKLEAGHKSEVTDEVRdaLLQLLDErrelldqlnKQLNNQlnlaiNLQLNQQQLLSvSDSL 447
|
...
gi 2217376813 345 QAK 347
Cdd:PRK11281 448 QST 450
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
410-581 |
4.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 410 ERTQALEAQIVALERTRAAdqttAEQGMRQLEQENAALKECRNEYERsLQNHQFELKKLKEewSQREIvsvamaQALEEV 489
Cdd:COG4913 610 AKLAALEAELAELEEELAE----AEERLEALEAELDALQERREALQR-LAEYSWDEIDVAS--AEREI------AELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 490 RKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAELEAlrtlkAEEAAVVAEQEDL 569
Cdd:COG4913 677 LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA-----AEDLARLELRALL 751
|
170
....*....|..
gi 2217376813 570 LRLRGPLQAEAL 581
Cdd:COG4913 752 EERFAAALGDAV 763
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-282 |
4.47e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 53 REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALALARKD 132
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 133 QEwsEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDE--MDELEgfqqqelskikhMLLKKEESLGKMEQELEARTRELS 210
Cdd:TIGR02168 913 LR--RELEELREKLAQLELRLEGLEVRIDNLQERLSEeySLTLE------------EAEALENKIEDDEEEARRRLKRLE 978
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217376813 211 RTQEELMNSNQMSSDlsqKLEELQRHYSTLEEQRDHVIASKTGAESKITAL-EQKEQELQALIQQLSIDLQKV 282
Cdd:TIGR02168 979 NKIKELGPVNLAAIE---EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIdREARERFKDTFDQVNENFQRV 1048
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
208-433 |
5.38e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 208 ELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVTAETQ 287
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 288 EKEDVITHLQ-----EKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQT 362
Cdd:COG3883 97 RSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217376813 363 LQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTA 433
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
346-517 |
7.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 346 AKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALeqqflERTQALEAQIVALERT 425
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 426 ----RAADQT--TAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQRE-IVSVAMAQALEEVRKQ------ 492
Cdd:COG4913 684 sddlAALEEQleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAalgdav 763
|
170 180
....*....|....*....|....*....
gi 2217376813 493 ----REEFQQQAANLTAIIDEKEQNLREK 517
Cdd:COG4913 764 erelRENLEERIDALRARLNRAEEELERA 792
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
30-553 |
7.41e-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: 43.29 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 30 SKESVASMGADSGDDFASDGSSSREDLSSQLLRRNEQIRKLEARLSDyaEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQ 109
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGE--LKLRLNQATATPELLLQLENFDERIERAREE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 110 NETFQANRAKMAEGLALALARKDQewsekmdqlekekniltaQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLL 189
Cdd:pfam12128 480 QEAANAEVERLQSELRQARKRRDQ------------------ASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLR 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 190 KK----EESLGKMeqeleARTRELSRTQEElmnsnqMSSDLSQKLEELQRHYSTLEEQRDHVIASktgaeskitalEQKE 265
Cdd:pfam12128 542 KEapdwEQSIGKV-----ISPELLHRTDLD------PEVWDGSVGGELNLYGVKLDLKRIDVPEW-----------AASE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 266 QELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQ 345
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 346 AkaintlETRVRELEQTLQASEEQLQQSKgivAAQETQIQELAAANQEsshvqqqalaleqQFLERTQALEAQIVALERT 425
Cdd:pfam12128 680 A------NERLNSLEAQLKQLDKKHQAWL---EEQKEQKREARTEKQA-------------YWQVVEGALDAQLALLKAA 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 426 RAADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQreiVSVAMAQALEEVRKQREEFQQQAANLTA 505
Cdd:pfam12128 738 IAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIER---IAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2217376813 506 IIDEKEQNLREKTEVLLQKEQE----ILQLERGHNSALLQIHQLQAELEALR 553
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADtklrRAKLEMERKASEKQQVRLSENLRGLR 866
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
124-369 |
8.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 124 LALALARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLfqrrdemdelegfqQQELSKIKHMLLKKEESLGKMEQELE 203
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQL--------------EEELEQARSELEQLEEELEELNEQLQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 204 ARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQLSIDLQKVT 283
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 284 AETQEKEDviTHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTL 363
Cdd:COG4372 171 QELQALSE--AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
....*.
gi 2217376813 364 QASEEQ 369
Cdd:COG4372 249 EELLEE 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-275 |
9.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 72 ARLSDYAEQVRNLQKIKEKLEIALEKHQdssmrKFQEQNETFQANRAKMAEGLALALARKDQEWSEKMDQLEKEKNILTA 151
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAE-----RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 152 QLQEMKNQSMNLFQRRDEM-DELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSnqmSSDLSQKL 230
Cdd:COG4913 310 ELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALR 386
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217376813 231 EELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQL 275
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
146-323 |
1.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 146 KNILTAQLQEMKNQSMNLFQrrDEMDELEGFQQQELSKIKHMLLKKEEslgKMEQELEARTRELSRTQEELMnsnQMSSD 225
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRN---EFEKELRERRNELQKLEKRLL---QKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 226 LSQKLEELQRHYSTLEEQRDhviasktgaeskitALEQKEQELQALIQQlsidlqkvtaetqekedvithLQEKVASLEK 305
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEK--------------ELEQKQQELEKKEEE---------------------LEELIEEQLQ 142
|
170 180
....*....|....*....|
gi 2217376813 306 RLEQ--NLSGEEHLQELLKE 323
Cdd:PRK12704 143 ELERisGLTAEEAKEILLEK 162
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
187-341 |
1.25e-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: 42.63 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 187 MLLKKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQ 266
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217376813 267 ELQALIQQLSidlqKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAA 341
Cdd:COG3096 589 QLRARIKELA----ARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
487-656 |
1.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 487 EEVRKQREEFQQQAANLTAIIDEKEQNLREktevlLQKEQEILQLERGHNSALLQIHQLQAELEALRTLKAEEAAVVAEQ 566
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 567 EDLLRLRGPLQAEALsvneshvtsramQDPVFQLPTAgrtpngevgamDLTQLQKEKQDLEQQLLEKNKTIKQMQQRMLE 646
Cdd:COG3206 246 RAQLGSGPDALPELL------------QSPVIQQLRA-----------QLAELEAELAELSARYTPNHPDVIALRAQIAA 302
|
170
....*....|
gi 2217376813 647 LRKTLQKELK 656
Cdd:COG3206 303 LRAQLQQEAQ 312
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
230-521 |
1.52e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 230 LEELQRHYSTLEEQRDHVIASKTGAESKItaleQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQ 309
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFI----KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 310 NLSGEEHLQELLKEKTLAEQNLEDTRQQllaarssqakaINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIqELAA 389
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEK-----------IRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-KLSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 390 ANQESSHVQQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQgMRQLEQENAALKECRNEYERSLQNhQFELKKLK 469
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK-LKELEKRLEELEERHELYEEAKAK-KEELERLK 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2217376813 470 EEWSQREIVSVamAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVL 521
Cdd:PRK03918 379 KRLTGLTPEKL--EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
121-397 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 121 AEGLALALARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLfqrRDEMDELegfqQQELSKIKHMLLKKEESLGKMEQ 200
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL---QAELEAL----QAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 201 ELEARTRELSRTQ------EELMNSNQMSsDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALIQQ 274
Cdd:COG3883 87 ELGERARALYRSGgsvsylDVLLGSESFS-DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 275 LSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLET 354
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2217376813 355 RVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHV 397
Cdd:COG3883 246 AAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGG 288
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
163-669 |
1.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 163 LFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEA---RTRELSRTQEELMNSNQMSSDLSQKLEELQRHYST 239
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKlekEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 240 LEEQRDHViasktgaESKITALEQKEQELQAL------IQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSG 313
Cdd:PRK03918 264 LEERIEEL-------KKEIEELEEKVKELKELkekaeeYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 314 EEHLQELLKEKTLAEQNLEDtrqqllaarssqakaintLETRVRELEqTLQASEEQLQQSKGIVAAQEtqIQELAAANQE 393
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEE------------------LEERHELYE-EAKAKKEELERLKKRLTGLT--PEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 394 SSHVQQQALALEQQFLERTQALEAQI----VALERTRAADQTTAEQGmRQLEQENAalKECRNEYERSLQNHQFELKKLK 469
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIkelkKAIEELKKAKGKCPVCG-RELTEEHR--KELLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 470 EEWSQREivsvAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNSALLQIHQLQAEL 549
Cdd:PRK03918 473 EKERKLR----KELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 550 EALRTLKAEEAAVVAEQEDLLRLRGPLQAEALSVNESHVtsRAMQDPVFQLPTAGRTPNGEVGA-MDLTQLQKEKQDLEQ 628
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV--EELEERLKELEPFYNEYLELKDAeKELEREEKELKKLEE 626
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2217376813 629 QLLEKNKTIKQMQQRMLELRKTLQKELKIRPDNELFEVREK 669
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE 667
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
148-563 |
1.77e-03 |
|
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: 41.42 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 148 ILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKhmllkkeESLGKMEQELEARTRELsrtQEELMNSNQMSSDLS 227
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDR-------EQWERQRRELESRVAEL---KEELRQSREKHEELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 228 QKLEELQRHYSTLEEQRDhviasktgaeskitALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRL 307
Cdd:pfam07888 101 EKYKELSASSEELSEEKD--------------ALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 308 EQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVaAQETQIQEL 387
Cdd:pfam07888 167 KEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALL-EELRSLQER 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 388 AAANQESSHVQQQALALEQQFLERTQALEAQIvaleRTRAADQTTaeqgmrQLEQENAALKECRNEYERSLQNHQFELKK 467
Cdd:pfam07888 246 LNASERKVEGLGEELSSMAAQRDRTQAELHQA----RLQAAQLTL------QLADASLALREGRARWAQERETLQQSAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 468 LKEEWSQREIVSVAMAQALEEVRKQREEF-----QQQAANLTAIIDEKEQNLREKTEV-LLQKEQEILQLERghNSALLQ 541
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEREKLevelgREKDCNRVQLSESRRELQELKASLrVAQKEKEQLQAEK--QELLEY 393
|
410 420
....*....|....*....|..
gi 2217376813 542 IHQLQAELEALRTLKAEEAAVV 563
Cdd:pfam07888 394 IRQLEQRLETVADAKWSEAALT 415
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
46-495 |
1.91e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 46 ASDGSSSREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLqkikeKLEIALEKHQdssmrkFQEQNETFQANRAKMAEGLA 125
Cdd:COG4913 333 RGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL-----GLPLPASAEE------FAALRAEAAALLEALEEELE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 126 LALARKDQEWSEKmDQLEKEKNILTAQLQEMKNQSMN----LFQRRDEMDELEGFQQQELSKI-KHMLLKKEES------ 194
Cdd:COG4913 402 ALEEALAEAEAAL-RDLRRELRELEAEIASLERRKSNiparLLALRDALAEALGLDEAELPFVgELIEVRPEEErwrgai 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 195 ---LG-----------------------KMEQELeaRTRELSRTQEELMNSNQMSSDLSQKL------------------ 230
Cdd:COG4913 481 ervLGgfaltllvppehyaaalrwvnrlHLRGRL--VYERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawleaelgrr 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 231 ---------EELQRH-------------YSTLEEQRDHVIASK----TGAESKITALEQKEQELQALIQQLSIDLQKVTA 284
Cdd:COG4913 559 fdyvcvdspEELRRHpraitragqvkgnGTRHEKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEA 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 285 ETQEKEDVITHL----------------QEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARssqaKA 348
Cdd:COG4913 639 ELDALQERREALqrlaeyswdeidvasaEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELK----GE 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 349 INTLETRVRELEQTLQASEEQLQQ-SKGIVAAQETQIQELAAANQESSHVQQQAlaleqqflertQALEAQIVALERTRA 427
Cdd:COG4913 715 IGRLEKELEQAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDAVERELR-----------ENLEERIDALRARLN 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 428 ADQTTAEQGMRQ---------------LEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIV--SVAMAQALEEVR 490
Cdd:COG4913 784 RAEEELERAMRAfnrewpaetadldadLESLPEYLALLDRLEEDGLPEYEERFKELLNENSIEFVAdlLSKLRRAIREIK 863
|
....*
gi 2217376813 491 KQREE 495
Cdd:COG4913 864 ERIDP 868
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
133-297 |
2.26e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 133 QEWSEKMDQLEKEKNiltaqlqemknqsmnlfQRRDEMDELEGFQQQElskiKHMLLKKEESLGKMEQELEARTRELSRT 212
Cdd:PRK12704 64 EEIHKLRNEFEKELR-----------------ERRNELQKLEKRLLQK----EENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 213 QEELmnsNQMSSDLSQKLEELQRHystLEEqrdhvIASKTGAESKITALEQKEQELQALIQQL---SIDLQKVTAETQEK 289
Cdd:PRK12704 123 QQEL---EKKEEELEELIEEQLQE---LER-----ISGLTAEEAKEILLEKVEEEARHEAAVLikeIEEEAKEEADKKAK 191
|
....*...
gi 2217376813 290 EDVITHLQ 297
Cdd:PRK12704 192 EILAQAIQ 199
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
260-387 |
2.58e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 260 ALEQKEQELQALIQQLSIDLQKVTAETQEKEDvithLQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLL 339
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLLSLERQGNQD----LQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2217376813 340 AARSSQ-------AKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQEL 387
Cdd:PRK09039 123 QELDSEkqvsaraLAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
162-537 |
2.88e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 162 NLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLE 241
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 242 EQRDHVIASKTGAESKITALEQKEQELQ--------ALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQNLSG 313
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQeeelkllaKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 314 EEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAaanqe 393
Cdd:pfam02463 337 IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL----- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 394 sshvqQQALALEQQFLERTQALEAQIVALERTRAADQTTAEQgmRQLEQENAALKECRNEYERSLQNHQFELKKLKEEws 473
Cdd:pfam02463 412 -----ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE--EKEELEKQELKLLKDELELKKSEDLLKETQLVKL-- 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376813 474 QREIVSVAMAQALEEVRKQREEFQQQAANLTAIIDEKEQNLREKTEVLLQKEQEILQLERGHNS 537
Cdd:pfam02463 483 QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
54-509 |
2.94e-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: 41.31 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 54 EDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALAL----- 128
Cdd:pfam01576 232 AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTeledt 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 129 -----------ARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSmnlFQRRDEMDElegfQQQELSKIKHMLLKKEESLGK 197
Cdd:pfam01576 312 ldttaaqqelrSKREQEVTELKKALEEETRSHEAQLQEMRQKH---TQALEELTE----QLEQAKRNKANLEKAKQALES 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 198 MEQELEARTRELSRTQEElmnSNQMSSDLSQKLEELQRHYSTLEEQRdhviasktgaeskitaleqkeQELQALIQQLSI 277
Cdd:pfam01576 385 ENAELQAELRTLQQAKQD---SEHKRKKLEGQLQELQARLSESERQR---------------------AELAEKLSKLQS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 278 DLQKVTAETQEKEDVITHLQEKVASLEKRLEQNlsgeehlQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVR 357
Cdd:pfam01576 441 ELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-------QELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKR 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 358 ELEQTLQASEEQLQQSKgivaaqeTQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALERTR----------A 427
Cdd:pfam01576 514 NVERQLSTLQAQLSDMK-------KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKnrlqqelddlL 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 428 ADQTTAEQGMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQREEFQQQAANLTAII 507
Cdd:pfam01576 587 VDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEM 666
|
..
gi 2217376813 508 DE 509
Cdd:pfam01576 667 ED 668
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-428 |
3.05e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 51 SSREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALALAR 130
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 131 KDQEwsEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESL----------GKMEQ 200
Cdd:COG1196 459 EALL--ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligVEAAY 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 201 ELEARTRELSRTQEELMNSnqmSSDLSQKLEELQRH---------YSTLEEQRDHVIASKTGAESKITALEQKEQELQAL 271
Cdd:COG1196 537 EAALEAALAAALQNIVVED---DEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 272 IQQLSIDLQKVTAETQEKEDVITH--------LQEKVASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARS 343
Cdd:COG1196 614 RYYVLGDTLLGRTLVAARLEAALRravtlagrLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 344 SQAKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQESSHVQQQALALEQQFLERTQALEAQIVALE 423
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
....*
gi 2217376813 424 RTRAA 428
Cdd:COG1196 774 REIEA 778
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
179-349 |
3.89e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 179 QELSKIKHMLLKKEESLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKtgaesKI 258
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 259 TALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEqnlsgeehlqELLKEKTLAEQNLEDTRQQL 338
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE----------EKKAELDEELAELEAELEEL 161
|
170
....*....|.
gi 2217376813 339 LAARSSQAKAI 349
Cdd:COG1579 162 EAEREELAAKI 172
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
63-309 |
3.98e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 63 RNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEkhQDSSMRKFQEQNETFQANRAKMAEGLAlalarkdqEWSEKMDQL 142
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVE--AEDRIERLEERREDLEELIAERRETIE--------EKRERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 143 EKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLlkkeESLGKMEQELEART---RELSRTQEELMNS 219
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI----ESLERIRTLLAAIAdaeDEIERLREKREAL 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 220 NQMSSDLSQKLEELQRHYSTLEEQRDhviasktgaESKITALEQKEQELQALIQQlsidlqkVTAETQEKEDVITHLQEK 299
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEFD---------EARIEEAREDKERAEEYLEQ-------VEEKLDELREERDDLQAE 682
|
250
....*....|
gi 2217376813 300 VASLEKRLEQ 309
Cdd:PRK02224 683 IGAVENELEE 692
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
301-580 |
3.99e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 301 ASLEKRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQL---------LAARSSQAKAINTLETRVRELEQTLQASEEQLQ 371
Cdd:PRK04863 782 AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFsrfigshlaVAFEADPEAELRQLNRRRVELERALADHESQEQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 372 QSKGIVAAQETQIQELAAANQESShvqqqaLALEQQFLERTQALEAQIVALERtraADQTTAEQGMR--QLEQENAALKE 449
Cdd:PRK04863 862 QQRSQLEQAKEGLSALNRLLPRLN------LLADETLADRVEEIREQLDEAEE---AKRFVQQHGNAlaQLEPIVSVLQS 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 450 CRNEYERSLQNHQfELKKLKEEWSQReivsvamAQALEEVRKQREEFQ-QQAANLTAIIDEKEQNLREKTEVLLQKEQEI 528
Cdd:PRK04863 933 DPEQFEQLKQDYQ-QAQQTQRDAKQQ-------AFALTEVVQRRAHFSyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRA 1004
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2217376813 529 LQLERGHNSALLQIHQLQAELEALRTLKAEEAAVVAEQEDLLRLRGPLQAEA 580
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEE 1056
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
265-531 |
4.27e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 265 EQELQAliqQLSIdLQKVTAETQEKEDVITHLQEKVASLEKRLEQNlsgeehlqellKEKTLAEQNLEDTRQQLLAAR-- 342
Cdd:PRK11281 38 EADVQA---QLDA-LNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK-----------EETEQLKQQLAQAPAKLRQAQae 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 343 ------SSQAKAINTLETR-VRELEQTLQASEEQLQQskgivaAQEtqiqELAAANQESSHVQQQALALEQQF---LERT 412
Cdd:PRK11281 103 lealkdDNDEETRETLSTLsLRQLESRLAQTLDQLQN------AQN----DLAEYNSQLVSLQTQPERAQAALyanSQRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 413 QALEAQIVALeRTRAADQTTAEQGMRQLEQenaALKECRNEYER----------SLQNHQFELKKLKEEWSQREIvsvam 482
Cdd:PRK11281 173 QQIRNLLKGG-KVGGKALRPSQRVLLQAEQ---ALLNAQNDLQRkslegntqlqDLLQKQRDYLTARIQRLEHQL----- 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2217376813 483 aQALEEV--RKQREEFQQQAANLtaiiDEKEQNLREKTEVLLQKEQEI-LQL 531
Cdd:PRK11281 244 -QLLQEAinSKRLTLSEKTVQEA----QSQDEAARIQANPLVAQELEInLQL 290
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
434-498 |
4.30e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.62 E-value: 4.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217376813 434 EQGMRQLEQENAALKECRNEYERsLQNHQFELKKLKEEWSQREIVSVAM----AQALEEVRKQREEFQQ 498
Cdd:PLN02316 238 EGGMDEHSFEDFLLEEKRRELEK-LAKEEAERERQAEEQRRREEEKAAMeadrAQAKAEVEKRREKLQN 305
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
72-369 |
4.87e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.58 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 72 ARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQAnrakmaEGLALALARKDQewseKMDQLEKEKNILTA 151
Cdd:pfam10174 185 RRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKT------KALQTVIEMKDT----KISSLERNIRDLED 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 152 QLQEMK-NQSMNLFQRRDEMDELEGFQqqelSKIKHMLLKkeesLGKMEQELEARTRELSRTQEELMNSNQMSSDLSQKL 230
Cdd:pfam10174 255 EVQMLKtNGLLHTEDREEEIKQMEVYK----SHSKFMKNK----IDQLKQELSKKESELLALQTKLETLTNQNSDCKQHI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 231 EELQRHYsTLEEQRDHVIASKTGA-----ESKITALEQKEQELQALIQQLSIDlqkvTAETQEKEDVITHLQEKVASLEK 305
Cdd:pfam10174 327 EVLKESL-TAKEQRAAILQTEVDAlrlrlEEKESFLNKKTKQLQDLTEEKSTL----AGEIRDLKDMLDVKERKINVLQK 401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217376813 306 RLEqnlsgeeHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQ 369
Cdd:pfam10174 402 KIE-------NLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQ 458
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
65-376 |
4.93e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 65 EQIRKLEARLSDYAEQvrnlqKIKEKLEIALEKHQDSSMRKFQEQNETFQANRAKMAEGLALALARKDQEWSEKMDQLEK 144
Cdd:TIGR00618 587 PNLQNITVRLQDLTEK-----LSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVR 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 145 EKNILTAQLQEMKNQsmnlfQRRDEMDELEGFQQQeLSKIKHMLLKKEESLGKMEQELEARTRELsrtQEELMNSNQMSS 224
Cdd:TIGR00618 662 EHALSIRVLPKELLA-----SRQLALQKMQSEKEQ-LTYWKEMLAQCQTLLRELETHIEEYDREF---NEIENASSSLGS 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 225 DLSQKLEELQRHYSTLEEQRDhviasktgaeskiTALEQKEQELQALIQQLSIDLQKVTAETQEKEDVITHLQEKVASLE 304
Cdd:TIGR00618 733 DLAAREDALNQSLKELMHQAR-------------TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217376813 305 KRLEQNLSGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQAKAINTLETRVRELEQTLQASEEQLQQSKGI 376
Cdd:TIGR00618 800 LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKI 871
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
65-540 |
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: 40.54 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 65 EQIRKLEARLSDYAEQVRNLQKIKEKL--------------EIALEKHQ------DSSMRKFQE-------QNETFQANR 117
Cdd:pfam01576 75 EILHELESRLEEEEERSQQLQNEKKKMqqhiqdleeqldeeEAARQKLQlekvttEAKIKKLEEdillledQNSKLSKER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 118 AKMAEGLAlALARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKIKHMLLKKEESLGK 197
Cdd:pfam01576 155 KLLEERIS-EFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 198 MEQELEARTRELSRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALeqkEQELQALIQQLSi 277
Cdd:pfam01576 234 LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL---GEELEALKTELE- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 278 DLQKVTAETQE----KEDVITHLQEKVASLEKRLEQNL--------SGEEHLQELLKEKTLAEQNLEDTRQQLLAARSSQ 345
Cdd:pfam01576 310 DTLDTTAAQQElrskREQEVTELKKALEEETRSHEAQLqemrqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAEL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 346 AKAINTLETRVRELEQTLQASEEQLQQSKGIVAAQETQIQELAAANQES-------SHVQQQALALEQQFLERTQALEAQ 418
Cdd:pfam01576 390 QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLqselesvSSLLNEAEGKNIKLSKDVSSLESQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 419 I-----VALERTRAADQTTAEqgMRQLEQENAALKECRNEYERSLQNHQFELKKLKEEWSQREIVSVAMAQALEEVRKQR 493
Cdd:pfam01576 470 LqdtqeLLQEETRQKLNLSTR--LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGK 547
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2217376813 494 EEFQQQAANLTAIIDEKEQNLR--EKTEVLLQKEQEILQLERGHNSALL 540
Cdd:pfam01576 548 KRLQRELEALTQQLEEKAAAYDklEKTKNRLQQELDDLLVDLDHQRQLV 596
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
42-309 |
5.38e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 42 GDDFASDGSSS-REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKL---EIALEKHQDSSMRKFQEQNETFQANR 117
Cdd:PRK01156 459 GTTLGEEKSNHiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeseEINKSINEYNKIESARADLEDIKIKI 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 118 AKMAEGLALALARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDE-----MDELEGFQQQELSKIKHMLLKKE 192
Cdd:PRK01156 539 NELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNeikkqLNDLESRLQEIEIGFPDDKSYID 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 193 ESLGKMEQELeartrelsRTQEELMNSNQMSSDLSQKLEELQRHYSTLEEQRDHVIASKTGAESKITALEQKEQELQALI 272
Cdd:PRK01156 619 KSIREIENEA--------NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKAL 690
|
250 260 270
....*....|....*....|....*....|....*..
gi 2217376813 273 QQLSIDLQKVTAETQEKEDVITHLQEKVASLEKRLEQ 309
Cdd:PRK01156 691 DDAKANRARLESTIEILRTRINELSDRINDINETLES 727
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
128-215 |
7.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217376813 128 LARKDQEWSEKMDQLEKEKNILTAQLQEMKNQSMNLFQRRDEMDELEGFQQQELSKI--------KHMLLKkeeslgKME 199
Cdd:PRK12704 91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltaeeaKEILLE------KVE 164
|
90
....*....|....*.
gi 2217376813 200 QELEARTRELSRTQEE 215
Cdd:PRK12704 165 EEARHEAAVLIKEIEE 180
|
|
| |
