|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-416 |
1.04e-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: 65.08 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 101 LRSKISELTTEVNKLQKGIEMYNQENSVYLS-YEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQ 179
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 180 NDRETqsldviFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMsfENQVKYLEmkTTNEKLLQELDTLQQQLDSQNMKKE 259
Cdd:TIGR02168 278 ELEEE------IEELQKELYALANEISRLEQQKQILRERLANL--ERQLEELE--AQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 260 SLEAEIAHSQVKQEAvlLHEKLYELESHRDqmiAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEE 339
Cdd:TIGR02168 348 ELKEELESLEAELEE--LEAELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 340 IRQLDM-----DLEEHQGEMNQKYKELKKREEHMDTFIETFEETKnqelKRKAQIEANIVALLEHCSRNINRIEQISSIT 414
Cdd:TIGR02168 423 IEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
..
gi 151105223 415 NQ 416
Cdd:TIGR02168 499 EN 500
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-521 |
2.19e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 104 KISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVmndyNMLKAQNDRE 183
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL----EAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 184 TQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEA 263
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 264 EIAHSQVKQEAVLLHEKLYELESHR-----------------------------------DQMIAEDKSIGSPMEEREKL 308
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 309 LKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQgemnQKYKELKKREEHMDtfIETFEETKNQELKR-KA 387
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ----ELLREAEELEEELQ--LEELEQEIAALLAEaGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 388 QIEANIVALLEHCSRNINRIEQISSITNQElkmmqdDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQ 467
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQL------EELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 151105223 468 HSLKSKIKQMTTDLEiYNDLPALKSSGEEKIKKLHQERMILSTHRNAFKKIMEK 521
Cdd:COG4717 456 AELEAELEQLEEDGE-LAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-590 |
3.61e-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: 60.07 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 194 RQAKEKQIRSVEEEIEQEKQATDDIIKNMSfENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAhsQVKQE 273
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE--QLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 274 AVLLHEKLYELEshrdqmiaedksigspmEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEhqge 353
Cdd:TIGR02168 749 IAQLSKELTELE-----------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE---- 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 354 mnqkykelkKREEHMDTfietfeetkNQELKRKAQIEANIVALLEHCSRNINRIEQISSITNQELKMMQDDLNFKSTEVQ 433
Cdd:TIGR02168 808 ---------LRAELTLL---------NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 434 KSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLEiynDLPALKSSGEEKIKKLHQERMilsthrN 513
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE---ELREKLAQLELRLEGLEVRID------N 940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 514 AFKKIMEKQNIEYEALKTQ-----LQENETHSQLTNLERKWQHLEQNNF-AMKEFIATK-------SQESDYQPIKKNVT 580
Cdd:TIGR02168 941 LQERLSEEYSLTLEEAEALenkieDDEEEARRRLKRLENKIKELGPVNLaAIEEYEELKerydfltAQKEDLTEAKETLE 1020
|
410
....*....|
gi 151105223 581 KQIAEYNKTI 590
Cdd:TIGR02168 1021 EAIEEIDREA 1030
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
134-457 |
4.28e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 134 KRAETLAVEIKELQGQLAdynmlvdklntntemeevMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQ 213
Cdd:COG1196 213 ERYRELKEELKELEAELL------------------LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 214 ATDDIiknmsfenQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAhsQVKQEAVLLHEKLYELESHRDQMIA 293
Cdd:COG1196 275 ELEEL--------ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE--ELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 294 EDKSIgspMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQgemnQKYKELKKREEHMDTFIE 373
Cdd:COG1196 345 ELEEA---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA----AQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 374 TFEETKNQELKRKAQIEANIVALLEHCSRNINRIEQISSiTNQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDL 453
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
....
gi 151105223 454 QKME 457
Cdd:COG1196 497 LEAE 500
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
101-555 |
1.53e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 101 LRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTN----TEMEEVMNDYNML 176
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelKELKEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 177 KAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQ--EKQATDDIIKNMSFENQVKYLEMKtTNEKLLQELDTLQQQLDSQ 254
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 255 NMKKESLEAEiahsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTdtkekin 334
Cdd:PRK03918 378 KKRLTGLTPE----KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT------- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 335 qfieeirqldmdlEEHQGEMNQKY-KELKKREEHMDTFIETFEETKnqelKRKAQIEaNIVALLEHCSRNINRIEQISSI 413
Cdd:PRK03918 447 -------------EEHRKELLEEYtAELKRIEKELKEIEEKERKLR----KELRELE-KVLKKESELIKLKELAEQLKEL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 414 TNQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTE---EQHSLKSKIKQMTTDLEI--YNDLP 488
Cdd:PRK03918 509 EEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekKLDELEEELAELLKELEElgFESVE 588
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151105223 489 ALKSSGEEkIKKLHQERMILSTHRNAFKKIMEKQNIEYEALKTQLQE-NETHSQLTNLERKWQHLEQN 555
Cdd:PRK03918 589 ELEERLKE-LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEElAETEKRLEELRKELEELEKK 655
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
238-476 |
2.16e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 238 EKLLQELDTLQQQLDSQNMKKESLEAEIAH---------SQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKL 308
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAEleaeleelrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 309 LKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQ 388
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 389 iEANIVALLEHCSRNINRIEQISSITNQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQH 468
Cdd:COG1196 395 -AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
....*...
gi 151105223 469 SLKSKIKQ 476
Cdd:COG1196 474 LLEAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-564 |
3.18e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 225 ENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAV--LLHEKLYELESHRDQMIAEDKSIGSPM 302
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALanEISRLEQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 303 EEREKLLKQIKDDNQEIASMERQLTDTKEKINqfieeirqldmDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQE 382
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELE-----------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 383 LKRKAQIEANIVALLEHCSRNINRIEQISSITNQELKMMQD-DLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLES 461
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 462 KMTEEQHSLKSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQERMILSTHRNAFKKIMEKQNiEYE-ALKTQLQENETHS 540
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDE-GYEaAIEAALGGRLQAV 550
|
330 340
....*....|....*....|....*..
gi 151105223 541 QLTNLE---RKWQHLEQNNFAMKEFIA 564
Cdd:TIGR02168 551 VVENLNaakKAIAFLKQNELGRVTFLP 577
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
303-594 |
4.88e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 303 EEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQE 382
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 383 LKRKAQIEANiVALLEHCSRNINRIEQISSITNQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESK 462
Cdd:TIGR02168 319 EELEAQLEEL-ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 463 MTEEQHSLKSKIKQMTTDLEIY-------------NDLPALKSSGEEKIKKLHQERMILSTHRNAFKKIM-EKQNIEYEA 528
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLqqeieellkkleeAELKELQAELEELEEELEELQEELERLEEALEELReELEEAEQAL 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151105223 529 LKTQLQENETHSQLTNLERKWQHLEQNNFAMKEFIATKSQESDYQPIKKNVTKQIAEYNKTIVDAL 594
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAL 543
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
127-391 |
7.22e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 127 SVYLSYEKRAETLAVEIKELQGQLADynmLVDKLNtntemeEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEE 206
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSS---LQSELR------RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 207 EIEQEKQATDDIiknmsfenQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQ-------------- 272
Cdd:TIGR02169 738 RLEELEEDLSSL--------EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelskleeevsr 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 273 -EAVLLHEKLYELESHRDQMIAEDKsIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQ 351
Cdd:TIGR02169 810 iEARLREIEQKLNRLTLEKEYLEKE-IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 151105223 352 GEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQIEA 391
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
100-556 |
1.51e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 100 LLRSKISELTTEVNKLQKGIEMYNQE----NSVYLSYEKRAETLAVEIKELQGQLADYNMLVDklNTNTEMEEVMNDYNM 175
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEinekTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE--QNNKKIKELEKQLNQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 176 LKAQ-----NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDdiiknmSFENQVKYLEMKTTNekLLQELDTLQQQ 250
Cdd:TIGR04523 293 LKSEisdlnNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIIS------QLNEQISQLKKELTN--SESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 251 LDSQNMKKESLEAEIAhsqvkqeavllhEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTK 330
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQ------------SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 331 EKINQFIEEIRqldmDLEEHQGEMNQKYKELKKREEHMDTFIETFEetknqelkrkaqieanivallehcsRNINRIEQI 410
Cdd:TIGR04523 433 ETIIKNNSEIK----DLTNQDSVKELIIKNLDNTRESLETQLKVLS-------------------------RSINKIKQN 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 411 SSITNQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLEiYNDLPAL 490
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK-KENLEKE 562
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151105223 491 KSSGEEKIKKLHQERMILSTHRNAFKKIMEKQNIEYEALKTQLQENEThsQLTNLERKWQHLEQNN 556
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK--KISSLEKELEKAKKEN 626
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
271-561 |
2.21e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 271 KQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEErekLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEH 350
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDE---LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 351 QGEMNQKYKELKKREEHmdtfIETFEETKNQELKRKAQIEA--------NIVALLEHCSRNINRIEQISSITNQELKMMQ 422
Cdd:TIGR02169 750 EQEIENVKSELKELEAR----IEELEEDLHKLEEALNDLEArlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 423 DDLNFKSTEVQKSQStaqnltsdiQRLQLDLQKMELleskmTEEQHSLKSKIKQMTTDLEIY----NDLpalkssgEEKI 498
Cdd:TIGR02169 826 LEKEYLEKEIQELQE---------QRIDLKEQIKSI-----EKEIENLNGKKEELEEELEELeaalRDL-------ESRL 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151105223 499 KKLHQERMILSTHRNAFKKIMEKQNIEYEALKTQLqeNETHSQLTNLERKWQHLEQNNFAMKE 561
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRL--SELKAKLEALEEELSEIEDPKGEDEE 945
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
192-457 |
2.99e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 192 TERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVK 271
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 272 QEAvlLHEKLYELESHRDQMIAE----DKSIGSPMEEREKLLKQIKDDNQEIASMERQLTD-------TKEKINQFIEEI 340
Cdd:TIGR02169 317 LED--AEERLAKLEAEIDKLLAEieelEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaeTRDELKDYREKL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 341 RQLDMDLEEHQGEMNQKYKELKKREEHMdtfietfeETKNQELKRkaqIEANIVALLEHCSRNINRIEQISsitnQELKM 420
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEEL--------ADLNAAIAG---IEAKINELEEEKEDKALEIKKQE----WKLEQ 459
|
250 260 270
....*....|....*....|....*....|....*..
gi 151105223 421 MQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKME 457
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
102-590 |
3.06e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 102 RSKISELTTEVNKLQKGIEmynqensvylSYEKRAETLAVEIKELQGQLADYNmlVDKLNTNTEMEEVMNDYNMLKAQND 181
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKK----------ENKKNIDKFLTEIKKKEKELEKLN--NKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 182 RETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIiknmsfenqvkyLEMKTTNEKLLQELDTLQQQLDSQNMKKESL 261
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI------------SELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 262 EAEIAHSQVKQEAVL--LHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQ-----IKDDNQEIASMERQLTDTK---- 330
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQnqis 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 331 ---EKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHmdtfIETFEETKNQELKRKAQIEANIVALlehcSRNINRI 407
Cdd:TIGR04523 332 qnnKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE----IEKLKKENQSYKQEIKNLESQINDL----ESKIQNQ 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 408 EQISSITNQELKMMQDDLNFKSTEVQ-------KSQSTAQNLTSDIQRLQLDL-----------QKMELLESKMTEEQHS 469
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIErlketiiKNNSEIKDLTNQDSVKELIIknldntresleTQLKVLSRSINKIKQN 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 470 LKSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQERMILSTHRNAFKKIMEKQNIEYEALKTQLQENETHSQLTNLERKW 549
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI 563
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 151105223 550 QHLEQNNFAMKEFIA--TKSQE------SDYQPIKKNVTKQIAEYNKTI 590
Cdd:TIGR04523 564 DEKNKEIEELKQTQKslKKKQEekqeliDQKEKEKKDLIKEIEEKEKKI 612
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
72-597 |
4.45e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 72 VTQQGLTGMKTGTKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLA 151
Cdd:PRK01156 135 VGQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 152 DynMLVDKLNTNTEMEEVMNDYNMLKAQNDRETQSLDVI------FTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFE 225
Cdd:PRK01156 215 I--TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKnryeseIKTAESDLSMELEKNNYYKELEERHMKIINDPVYK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 226 NQ---VKYLEMKTTNEKLLQELDTLQQQLDS--QNMKK-ESLEAEIAHSQVKQ-EAVLLHEKLYELESHRDQMIAEDKSI 298
Cdd:PRK01156 293 NRnyiNDYFKYKNDIENKKQILSNIDAEINKyhAIIKKlSVLQKDYNDYIKKKsRYDDLNNQILELEGYEMDYNSYLKSI 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 299 GSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEET 378
Cdd:PRK01156 373 ESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQ 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 379 KNQELKRKAQIEANIVALLEHCSRNINRIEQISSITNQELKmmqdDLNFKSTEVQKSQSTAQNltSDIQRLQLDLQKMEL 458
Cdd:PRK01156 453 SVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK----DIDEKIVDLKKRKEYLES--EEINKSINEYNKIES 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 459 LESKMTEEQHSLkSKIKQMTTDLEiyndlpalksSGEEKIKKLHQErmILSTHRNAFKKIM-EKQNIEYEALKTqlQENE 537
Cdd:PRK01156 527 ARADLEDIKIKI-NELKDKHDKYE----------EIKNRYKSLKLE--DLDSKRTSWLNALaVISLIDIETNRS--RSNE 591
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 538 THSQLTNLERKWQHLEQNNFAMKEFIATKSQESDYQPIKKNVTKQIAEYNKTIVDALHST 597
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGK 651
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
239-393 |
3.46e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 239 KLLQELDTLQQQLDSQNMKKESLEAEIAhsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDD--- 315
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELA--ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 316 ---NQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQIEAN 392
Cdd:COG1579 92 ealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
.
gi 151105223 393 I 393
Cdd:COG1579 172 I 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
238-505 |
4.00e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 238 EKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEavllheklyELEshrdqmiaedksigspmEEREKLLKQIKDDNQ 317
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELA---------ELE-----------------AELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 318 EIASM-------ERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQIE 390
Cdd:COG1196 282 ELEEAqaeeyelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 391 ANIVALLEHCSRNINRIEQISSITNQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQHSL 470
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270
....*....|....*....|....*....|....*
gi 151105223 471 KSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQER 505
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
257-409 |
7.51e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 257 KKESLEAEIAHSQVKQEAvllhEKlyELESHRDQMIAEDKsigspmEE----REKLLKQIKDDNQEIASMERQLTDTKEK 332
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEA----KK--EAEAIKKEALLEAK------EEihklRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 333 INQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIE------------TFEETKNQ---ELKRKAQIEAnivall 397
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEeqlqelerisglTAEEAKEIlleKVEEEARHEA------ 171
|
170
....*....|..
gi 151105223 398 ehcSRNINRIEQ 409
Cdd:PRK12704 172 ---AVLIKEIEE 180
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
289-500 |
1.49e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 289 DQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKReehm 368
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 369 dtfietfeetkNQELKRKAQIEANIVALLEhcSRN----INRIEQISSITNQELKMMqDDLNFKSTEVQKSQSTAQNLTS 444
Cdd:COG3883 92 -----------ARALYRSGGSVSYLDVLLG--SESfsdfLDRLSALSKIADADADLL-EELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 151105223 445 DIQRLQLDLQKM-ELLESKMTEEQHSLKSKIKQMTTDLEIYNDLPALKSSGEEKIKK 500
Cdd:COG3883 158 ELEALKAELEAAkAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
238-591 |
1.99e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 238 EKLLQELDTLQQQLDsqnmkkeslEAEIAHSQVKQEAVLLHEKLYELESHRD-QMIAEDKSIGSPMEEREKLLKQIKDDN 316
Cdd:TIGR02169 173 EKALEELEEVEENIE---------RLDLIIDEKRQQLERLRREREKAERYQAlLKEKREYEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 317 QEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQK----YKELKKREEHMDTFIETFE---ETKNQELKRKAQI 389
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASLErsiAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 390 EANIVALLEHCSRNINRIE--------QISSITN--QELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQR----LQLDLQK 455
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEreieeerkRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREklekLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 456 MELLESKMTEEQHSLKSKIKQMTTDLE-IYNDLPALKSSGEEKIKKLHQERMILSThrnaFKKIMEKQNIEYEALKTQLQ 534
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAgIEAKINELEEEKEDKALEIKKQEWKLEQ----LAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 151105223 535 ENEthSQLTNLERKWQHLEqnnfamkefiATKSQESDYQPIKKNVTKQIAEYNKTIV 591
Cdd:TIGR02169 480 RVE--KELSKLQRELAEAE----------AQARASEERVRGGRAVEEVLKASIQGVH 524
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-550 |
2.37e-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: 47.42 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 105 ISELTTEVNKL-QKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTntEMEEVMNDYnmlkaqnDRE 183
Cdd:pfam15921 273 ISEHEVEITGLtEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRS--ELREAKRMY-------EDK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 184 TQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNM--SFENQVKYLEMKTTNEKLLQELDT--------LQQQLDS 253
Cdd:pfam15921 344 IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLlaDLHKREKELSLEKEQNKRLWDRDTgnsitidhLRRELDD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 254 QNMKKESLEAeiahsqvkqeavLLHEKLYELESHRDQMIAedkSIGSPMEEREKllkqikddnqeIASMERQLTDTKEKI 333
Cdd:pfam15921 424 RNMEVQRLEA------------LLKAMKSECQGQMERQMA---AIQGKNESLEK-----------VSSLTAQLESTKEML 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 334 NQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMD------TFIETFEETKNQE---LKRKAQIEANIVALLEHCSRNI 404
Cdd:pfam15921 478 RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaeiTKLRSRVDLKLQElqhLKNEGDHLRNVQTECEALKLQM 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 405 NRIEQISSITNQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQHSLKSKIkqmtTDLEIy 484
Cdd:pfam15921 558 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV----SDLEL- 632
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151105223 485 nDLPALKSSGEEK---IKKLHQERMIL----STHRNAFKKIMEkqniEYEALKTQLQENETHSQLTNLERKWQ 550
Cdd:pfam15921 633 -EKVKLVNAGSERlraVKDIKQERDQLlnevKTSRNELNSLSE----DYEVLKRNFRNKSEEMETTTNKLKMQ 700
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
182-517 |
2.86e-05 |
|
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: 47.27 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 182 RETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESL 261
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 262 EAEIAHSQVKQEAVLlheklyELESHRDQMIAEDKSIGSPMEEREKLL-KQIKDDNQEIASMERQLTDTKEKINQFIEEI 340
Cdd:pfam02463 250 QEEIESSKQEIEKEE------EKLAQVLKENKEEEKEKKLQEEELKLLaKEEEELKSELLKLERRKVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 341 RQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQIEANIVALLEHCSRNINRIEQissitnQELKM 420
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL------KEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 421 MQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMT-EEQHSLKSKIKQMTTDLEIYNDLPALKSSGEEKIK 499
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELkQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330
....*....|....*...
gi 151105223 500 KLHQERMILSTHRNAFKK 517
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKL 495
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
142-335 |
2.91e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 142 EIKELQGQLADYNMLVDKLNTntEMEEVMNDYNMLKAQNDRETQSLDvifterqAKEKQIRSVEEEIEQEKQATDDIIKN 221
Cdd:COG3883 24 ELSELQAELEAAQAELDALQA--ELEELNEEYNELQAELEALQAEID-------KLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 222 MSFE-NQVKYLEMKTTNE---KLLQELDTLQQQLDSQNMKKESLEAEIAhsQVKQEAVLLHEKLYELESHRDQMIAEDKS 297
Cdd:COG3883 95 LYRSgGSVSYLDVLLGSEsfsDFLDRLSALSKIADADADLLEELKADKA--ELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 151105223 298 IGSPMEEREKLLKQIKDD----NQEIASMERQLTDTKEKINQ 335
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEeaaaEAQLAELEAELAAAEAAAAA 214
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
104-517 |
3.07e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 104 KISELTTEVNKLQKGIEMYNQENSV-YLSYEKRAETLAVEIKELQGQLADYNMLVDKLNT-----------NTEMEEVMN 171
Cdd:PRK01156 274 YYKELEERHMKIINDPVYKNRNYINdYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVlqkdyndyikkKSRYDDLNN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 172 DYNMLKAQND------RETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELD 245
Cdd:PRK01156 354 QILELEGYEMdynsylKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 246 TLQQQLD--SQNM------------------------------KKESLEAEIAHsqVKQEAVLLHEKLYELESHRDQMIA 293
Cdd:PRK01156 434 ALRENLDelSRNMemlngqsvcpvcgttlgeeksnhiinhyneKKSRLEEKIRE--IEIEVKDIDEKIVDLKKRKEYLES 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 294 ED--KSIGS--PMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQF-IEEIRQL------------DMDLEEHQGEMNQ 356
Cdd:PRK01156 512 EEinKSINEynKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKrtswlnalavisLIDIETNRSRSNE 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 357 KYKELKKREEHMDTFIETFEETKNQELKRKAQIEANIVALlehcsRNINRIEQISSITNQELKMMQDDLNFKSTEVQKSQ 436
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNL-----NNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSII 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 437 STAQNLTSDIQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQERMILSTHRNAFK 516
Cdd:PRK01156 667 PDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFD 746
|
.
gi 151105223 517 K 517
Cdd:PRK01156 747 K 747
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
283-505 |
3.35e-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: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 283 ELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELK 362
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 363 KReehmdtfietfeetkNQELKRKAQIEANIVALLEHCSRNINRIEQISSITNQELKMMQDDLNFKSTEVQKSQSTAQNL 442
Cdd:COG4942 108 EL---------------LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 151105223 443 TSDIQRLQLDLQ-KMELLESKMTEEQHSLKSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQER 505
Cdd:COG4942 173 RAELEALLAELEeERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
143-345 |
3.80e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 143 IKELQGQLADYNMLVDKLNTNTEMEEvmNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQE--------KQA 214
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQIKTYN--KNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEllnlvmdiEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 215 TDDIIK--------NMSFENQVKYLEMKTTN-----------------EKLLQELDTLQQQLDSQNMKKESLEaEIAHsQ 269
Cdd:PHA02562 254 SAALNKlntaaakiKSKIEQFQKVIKMYEKGgvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELE-EIMD-E 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151105223 270 VKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDM 345
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
171-500 |
3.84e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 171 NDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVE-EEIEQEKQATDdiiKNMSFENQVKYLEMKTTnEKLLQELDTLQQ 249
Cdd:PLN02939 95 DDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQlEDLVGMIQNAE---KNILLLNQARLQALEDL-EKILTEKEALQG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 250 QLDSQNMKKESLEAEIA-HSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQ----IKDDNQEIASMER 324
Cdd:PLN02939 171 KINILEMRLSETDARIKlAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEenmlLKDDIQFLKAELI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 325 QLTDTKEKInqfieeirqldMDLEEHQGEMNQKYKELKKReehmdtFIETFEE-TKNQELKRKAQIEA--NIVALLEhcs 401
Cdd:PLN02939 251 EVAETEERV-----------FKLEKERSLLDASLRELESK------FIVAQEDvSKLSPLQYDCWWEKveNLQDLLD--- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 402 RNINRIEQISSITNQelkmmQDDLNFKSTEVQKSQSTAqNLTsdiqrlQLDLQKMELLESKMTEEQHSLKSKIKQMTTDL 481
Cdd:PLN02939 311 RATNQVEKAALVLDQ-----NQDLRDKVDKLEASLKEA-NVS------KFSSYKVELLQQKLKLLEERLQASDHEIHSYI 378
|
330 340
....*....|....*....|....
gi 151105223 482 EIYNDLPA-----LKSSGEEKIKK 500
Cdd:PLN02939 379 QLYQESIKefqdtLSKLKEESKKR 402
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
101-566 |
4.85e-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: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 101 LRSKISELTTEVNKLQKGIEMYNQENSVY---LSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEMEEVMndynmlk 177
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQeeqLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 178 aqndRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEmkttnEKLLQELDTLQQQLDSQNMK 257
Cdd:TIGR00618 297 ----AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL-----QTLHSQEIHIRDAHEVATSI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 258 KESLEAEIAHSQ----VKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLtdtkEKI 333
Cdd:TIGR00618 368 REISCQQHTLTQhihtLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA----ELC 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 334 NQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQIEANIVALLEHCS------------ 401
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnparqdidnp 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 402 --------RNINRIE-----------QISSITNQ------ELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKM 456
Cdd:TIGR00618 524 gpltrrmqRGEQTYAqletseedvyhQLTSERKQraslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 457 ELLESKMTEEQHSLKSKIKQMTTDLEIYNDLpalkssgeekiKKLHQERMILSTHRNAFKKIMEKQNIEYEALKTQLQEN 536
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKLQPEQDLQDVRLHL-----------QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK 672
|
490 500 510
....*....|....*....|....*....|
gi 151105223 537 ETHSQLTNLERKWQHLEQNNFAMKEFIATK 566
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKEQLTYWKEMLAQC 702
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
89-592 |
5.04e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 89 RQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTEM-- 166
Cdd:PRK01156 204 KQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERhm 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 167 ----------EEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEE------EIEQEKQATDDIIKNMSfenQVKY 230
Cdd:PRK01156 284 kiindpvyknRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVlqkdynDYIKKKSRYDDLNNQIL---ELEG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 231 LEMKTTNekLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSigSPMEEREKLLK 310
Cdd:PRK01156 361 YEMDYNS--YLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKV--SSLNQRIRALR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 311 QIKDDNQEIASM-------------------ERQLTDTKEKINQFIEEIRQLDMDLEehqgEMNQKYKELKKREEHMDTF 371
Cdd:PRK01156 437 ENLDELSRNMEMlngqsvcpvcgttlgeeksNHIINHYNEKKSRLEEKIREIEIEVK----DIDEKIVDLKKRKEYLESE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 372 -IETFEETKNQELKRKAQIEANIVALlehcSRNINRIEQISSITNQELKMMQDDLNFKSTEVQKSQStaqnltsdiqrlQ 450
Cdd:PRK01156 513 eINKSINEYNKIESARADLEDIKIKI----NELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALA------------V 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 451 LDLQKMELLESKMTEEQHSLKSKIKQMTtdlEIYNDLPALKSSGEEKIKKLHQERMILSTHRN---AFKKIMEKQNIEYE 527
Cdd:PRK01156 577 ISLIDIETNRSRSNEIKKQLNDLESRLQ---EIEIGFPDDKSYIDKSIREIENEANNLNNKYNeiqENKILIEKLRGKID 653
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151105223 528 ALKTQLQE--------NETHSQLTNLERKWQHLEqnnfamKEFIATKSQESDYQPIKKNVTKQIAEYNKTIVD 592
Cdd:PRK01156 654 NYKKQIAEidsiipdlKEITSRINDIEDNLKKSR------KALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
192-592 |
7.21e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 192 TERQAKEKQIRSVEEEIEQEKQATDDIIKNM-SFENQVKYLemKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQV 270
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLnKDEEKINNS--NNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 271 kqeavllheklyELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEH 350
Cdd:TIGR04523 111 ------------EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 351 QGEMNQKYKELKK------REEHMDTFIETFEETKNQ------ELKRKAQIEANIVAL----LEHCSRNINRIEQISSIT 414
Cdd:TIGR04523 179 EKEKLNIQKNIDKiknkllKLELLLSNLKKKIQKNKSlesqisELKKQNNQLKDNIEKkqqeINEKTTEISNTQTQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 415 NQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDL-----QKMELLESKMTEEQHSLKSKIKQMTTDLEIYNDlpa 489
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIsdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK--- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 490 LKSSGEEKIKKLHQERMILSTHRNAFKKIMEKQNIEYEALKTQLQENETH-----SQLTNLERKWQHLEQNNFAMKEFIa 564
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknleSQINDLESKIQNQEKLNQQKDEQI- 414
|
410 420 430
....*....|....*....|....*....|.
gi 151105223 565 tKSQESDYQPIKKNVTK---QIAEYNKTIVD 592
Cdd:TIGR04523 415 -KKLQQEKELLEKEIERlkeTIIKNNSEIKD 444
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
104-393 |
1.08e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 104 KISELTTEVNKLQKGIEMYNQE--NSVYLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTNTE---------------- 165
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgrel 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 166 ----MEEVMNDYNmlkaqndRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTTN---- 237
Cdd:PRK03918 446 teehRKELLEEYT-------AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynle 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 238 --EKLLQELDTLQQQLDSQNMKKESLEAEIAHSQ-VKQEAVLLHEKLYELESHRDQMIAEDKSIG-SPMEEREKLLKQI- 312
Cdd:PRK03918 519 elEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEeLKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELe 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 313 ---------KDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQ--------KYKELKKREEHMDTFIETF 375
Cdd:PRK03918 599 pfyneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkyseeEYEELREEYLELSRELAGL 678
|
330
....*....|....*...
gi 151105223 376 EETKNQELKRKAQIEANI 393
Cdd:PRK03918 679 RAELEELEKRREEIKKTL 696
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
197-486 |
1.08e-04 |
|
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: 45.42 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 197 KEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLEMKTtnEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVL 276
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI--AQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 277 L-------HEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKIN---QFIEEIRQLDMD 346
Cdd:TIGR00606 848 NrkliqdqQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpleTFLEKDQQEKEE 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 347 L--------EEHQGEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQIEANIVALLEHCSRNINRIEQISSITNQEL 418
Cdd:TIGR00606 928 LissketsnKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDI 1007
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151105223 419 -------KMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLEIYND 486
Cdd:TIGR00606 1008 dtqkiqeRWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK 1082
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
77-411 |
1.37e-04 |
|
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: 45.11 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 77 LTGMKTGTKGPQRQILDKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSVYLSYEKRAETLAVEIKELQGQLADYNML 156
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 157 VDKLNTNTE-MEEVMNDYN-------MLKAQ-----NDR--ETQSLDVIFTERQAKEKQIRSVEEEIEQEKQAtddiIKN 221
Cdd:pfam15921 564 IEILRQQIEnMTQLVGQHGrtagamqVEKAQlekeiNDRrlELQEFKILKDKKDAKIRELEARVSDLELEKVK----LVN 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 222 MSFENQVKYLEMKTTNEKLLQELDTLQQQLDS---------QNMKKESLEAEIAHSQVKQEavlLHEKLYELESHRDQMI 292
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNKSEEMETTTNKLKMQ---LKSAQSELEQTRNTLK 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 293 AEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLtdtkekinQFIEEIrQLDMDLEEH--QGEMNQKYKELKKREEHMDT 370
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKI--------QFLEEA-MTNANKEKHflKEEKNKLSQELSTVATEKNK 787
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 151105223 371 FIETFEETKNQELKRKAQIEANIVAL------LEHCSRNINRIEQIS 411
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALdkaslqFAECQDIIQRQEQES 834
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
134-342 |
1.46e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 134 KRAETLAVEIKELQGQLADYNMLVDKlnTNTEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEI----- 208
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaelra 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 209 --EQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQ---ELDTLQQQLDSQNMKKESLEAEIAhsQVKQEAVLLHEKLYE 283
Cdd:COG4942 98 elEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavrRLQYLKYLAPARREQAEELRADLA--ELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 151105223 284 LESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQ 342
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
238-409 |
1.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 238 EKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAvllHEKLYELESHRDQMIAEDKSIgspmEEREKLLKQIKDDNQ 317
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA---LQRLAEYSWDEIDVASAEREI----AELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 318 EIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQEL----------KRKA 387
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerfaaalgdAVER 765
|
170 180
....*....|....*....|..
gi 151105223 388 QIEANIVALLEHCSRNINRIEQ 409
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEE 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-390 |
2.21e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 156 LVDKLNT-NTEMEEVMNDYNMLKAQNDRETQSLD---VIFTERQAKEKQIRSVEEEIEqekqatddiiknmsfENQVKYL 231
Cdd:PRK02224 204 LHERLNGlESELAELDEEIERYEEQREQARETRDeadEVLEEHEERREELETLEAEIE---------------DLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 232 EMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLLH---------EKLYELESHRDQMIAEDKSIGSPM 302
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARreeledrdeELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 303 EEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQE 382
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
....*...
gi 151105223 383 LKRKAQIE 390
Cdd:PRK02224 429 AELEATLR 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
260-499 |
2.27e-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: 43.98 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 260 SLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEE 339
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 340 IRQLDMDLEEHQGEM-----------NQKYKELKKREEHMDTFIETFEETKNQELKRKAQIEAnIVALLEHCSRNINRIE 408
Cdd:COG4942 92 IAELRAELEAQKEELaellralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE-LRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 409 QISSITNQELKMMQDDLNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMElleskmtEEQHSLKSKIKQMTTDLEIYNDLP 488
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ-------QEAEELEALIARLEAEAAAAAERT 243
|
250
....*....|.
gi 151105223 489 ALKSSGEEKIK 499
Cdd:COG4942 244 PAAGFAALKGK 254
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
192-574 |
3.22e-04 |
|
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: 43.57 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 192 TERQAKEKQIRSVEEEIEQEKQAtddiiKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESleaeiahsqvK 271
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEE-----KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERER----------E 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 272 QEAVLLHEKLYELESHRDQMIAEDKsigSPMEEREKLlkqikddnqeiaSMERQltDTKEKINQFIEEIRQLDMDLEEHQ 351
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEI---SRMRELERL------------QMERQ--QKNERVRQELEAARKVKILEEERQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 352 GEMNQKYKELKK-REEHmdtfietfEETKNQELKRkaqieanivaLLEHCSRNINRIEQISSITNQELKMM-QDDLNFKS 429
Cdd:pfam17380 413 RKIQQQKVEMEQiRAEQ--------EEARQREVRR----------LEEERAREMERVRLEEQERQQQVERLrQQEEERKR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 430 TEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQErmils 509
Cdd:pfam17380 475 KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME----- 549
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151105223 510 tHRNAFKKIMEKQNIEYEALKTQLQENETHSQLTNLERKWQHLEQNNFAMKEFIATKSQESDYQP 574
Cdd:pfam17380 550 -ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIKPIYRPRISEYQP 613
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-393 |
3.74e-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: 43.21 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 193 ERQAKEKQIRSVEEEIEQEKQATDdiiknmsfenqvkylEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAH----- 267
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELA---------------ALKKEEKALLKQLAALERRIAALARRIRALEQELAAleael 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 268 SQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSP-------------------------MEEREKLLKQIKDDNQEIASM 322
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151105223 323 ERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQIEANI 393
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
187-521 |
4.69e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 187 LDVIFTERQAKEKQIRSVE--EEIEQEKQATDDIIKNmsFENQVKYLEmkttnekllqelDTLQQQLDSQNMKKEsLEAE 264
Cdd:PRK03918 137 IDAILESDESREKVVRQILglDDYENAYKNLGEVIKE--IKRRIERLE------------KFIKRTENIEELIKE-KEKE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 265 IAhsQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLD 344
Cdd:PRK03918 202 LE--EVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 345 mdleehqgemnQKYKELKKREEHMDTFIEtFEETKNQELKRKAQIEanivALLEHCSRNINRIEQISSitnqelkmmqdD 424
Cdd:PRK03918 280 -----------EKVKELKELKEKAEEYIK-LSEFYEEYLDELREIE----KRLSRLEEEINGIEERIK-----------E 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 425 LNFKSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQhSLKSKIKQMTTDlEIYNDLPAL---KSSGEEKIKKL 501
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE-RLKKRLTGLTPE-KLEKELEELekaKEEIEEEISKI 410
|
330 340
....*....|....*....|
gi 151105223 502 HQERMILSTHRNAFKKIMEK 521
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEE 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-427 |
6.27e-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: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 198 EKQIRSVEEEIE---QEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAhsQVKQEA 274
Cdd:COG4913 241 HEALEDAREQIEllePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE--RLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 275 VLLHEKLYELESHRDQmiaedksIGSpmeEREKLLKQikddnqEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQgem 354
Cdd:COG4913 319 DALREELDELEAQIRG-------NGG---DRLEQLER------EIERLERELEERERRRARLEALLAALGLPLPASA--- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 355 nqkyKELKKREEHMDTFIETFEETKNQELKRKAQIEANIVAL---LEHCSRNINRIEQ-ISSIT----------NQELKM 420
Cdd:COG4913 380 ----EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrreLRELEAEIASLERrKSNIParllalrdalAEALGL 455
|
....*..
gi 151105223 421 MQDDLNF 427
Cdd:COG4913 456 DEAELPF 462
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
100-428 |
7.19e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 100 LLRSKISELTTEVNKLQKGIEMYNQENSVylsyekraetLAVEIKELQGQLADYNMLVDKLNTNTEMEEvmNDYNMLKAQ 179
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIK----------NNSEIKDLTNQDSVKELIIKNLDNTRESLE--TQLKVLSRS 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 180 NDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMS-FENQVKYLEMKTTN-----EKLLQELDTLQQQLDS 253
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISsLKEKIEKLESEKKEkeskiSDLEDELNKDDFELKK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 254 QNMKKESLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKL-------LKQIKDDNQEIASMERQL 326
Cdd:TIGR04523 557 ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKisslekeLEKAKKENEKLSSIIKNI 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 327 TDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKReehMDTFIETFEETKNQELKR-----KAQIEANIVALLEHCS 401
Cdd:TIGR04523 637 KSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTK---IDDIIELMKDWLKELSLHykkyiTRMIRIKDLPKLEEKY 713
|
330 340
....*....|....*....|....*..
gi 151105223 402 RNINRIEQISSITNQELKMMQDDLNFK 428
Cdd:TIGR04523 714 KEIEKELKKLDEFSKELENIIKNFNKK 740
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
133-534 |
8.28e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 133 EKRAETLAVEIKELQGQLADYNMLV----DKLNTNTEMEEVMND-YNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEE 207
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLeesrDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEED 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 208 IE----------QEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQ--NMKKESLEAEIAHSQVKQEAV 275
Cdd:pfam05483 319 LQiatkticqltEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNedQLKIITMELQKKSSELEEMTK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 276 LLHEKLYELESHRdQMIAEDKSIGSPMEEREKLLKQIKDDNQEIASmerqLTDTKEKINQFIEEIRQLDMDLEEHQGEMN 355
Cdd:pfam05483 399 FKNNKEVELEELK-KILAEDEKLLDEKKQFEKIAEELKGKEQELIF----LLQAREKEIHDLEIQLTAIKTSEEHYLKEV 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 356 QKYKELKKREEHMDTFIETFEETKNQELKRKAQIEANIVALLEhcsrniNRIEQISSITNQELKMMQDDLNFKSTEVQKS 435
Cdd:pfam05483 474 EDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELK------KHQEDIINCKKQEERMLKQIENLEEKEMNLR 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 436 QSTAQNLTSDIQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQERMILSTHRNAF 515
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
410
....*....|....*....
gi 151105223 516 KKIMEKQNIEYEALKTQLQ 534
Cdd:pfam05483 628 NKQLNAYEIKVNKLELELA 646
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
290-470 |
8.78e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 290 QMIAE-DKSIGSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKReehM 368
Cdd:PRK11637 54 QDIAAkEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQ---L 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 369 DTFIETFEET------KNQELKRKAQIEANIVALlehcsrNINRIEQISsitnqELKMMQDDLNFKSTEVQKSQSTAQNL 442
Cdd:PRK11637 131 DAAFRQGEHTglqlilSGEESQRGERILAYFGYL------NQARQETIA-----ELKQTREELAAQKAELEEKQSQQKTL 199
|
170 180 190
....*....|....*....|....*....|....*....
gi 151105223 443 TSDIQRLQldlQKMEL-----------LESKMTEEQHSL 470
Cdd:PRK11637 200 LYEQQAQQ---QKLEQarnerkktltgLESSLQKDQQQL 235
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
133-548 |
1.11e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 133 EKRAETLAVEIKELQGQLADynmLVDKLnTNTEMEEVMNDYNM--LKAQNDRETQSLDVIFTE-RQAKEKQIRSVEEEIE 209
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEE---LEDEL-QATEDAKLRLEVNMqaLKAQFERDLQARDEQGEEkRRQLVKQVRELEAELE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 210 QEKQATDDIIknmsfenqvkylemkTTNEKLLQELDTLQQQLDSQNMKKESleaeiAHSQVKQEAVLLHEKLYELESHRd 289
Cdd:pfam01576 760 DERKQRAQAV---------------AAKKKLELDLKELEAQIDAANKGREE-----AVKQLKKLQAQMKDLQRELEEAR- 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 290 qmiaedksigspmEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEM---NQKYKELKKREE 366
Cdd:pfam01576 819 -------------ASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIasgASGKSALQDEKR 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 367 HMDTFIETFEETKNQElkrkaqiEANIVALLEHCSRNINRIEQissitnqelkmMQDDLNFKSTEVQKSQSTAQNLTSDI 446
Cdd:pfam01576 886 RLEARIAQLEEELEEE-------QSNTELLNDRLRKSTLQVEQ-----------LTTELAAERSTSQKSESARQQLERQN 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 447 QRLQLDLQKME-LLESKMTEEQHSLKSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQERMIL----STHRNAFKKIMEK 521
Cdd:pfam01576 948 KELKAKLQEMEgTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQvedeRRHADQYKDQAEK 1027
|
410 420
....*....|....*....|....*..
gi 151105223 522 QNIEYEALKTQLQENETHSQLTNLERK 548
Cdd:pfam01576 1028 GNSRMKQLKRQLEEAEEEASRANAARR 1054
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
69-419 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 69 HRPVTQQGLTGMK--TGTKGPQRQIlDKSYYLG--------LLRSKISELTTEVNKLQKGIEMYNQEnsvYLSYEKRAET 138
Cdd:COG4913 574 PRAITRAGQVKGNgtRHEKDDRRRI-RSRYVLGfdnraklaALEAELAELEEELAEAEERLEALEAE---LDALQERREA 649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 139 LA---------VEIKELQGQLADYNMLVDKL-NTNTEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEI 208
Cdd:COG4913 650 LQrlaeyswdeIDVASAEREIAELEAELERLdASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 209 EQEKQATDDIIKNMSFEnqvkylemkttnekLLQELDTLQQQLDSQNmkkesLEAEIAHSqvkqeavlLHEKLYELESHR 288
Cdd:COG4913 730 DELQDRLEAAEDLARLE--------------LRALLEERFAAALGDA-----VERELREN--------LEERIDALRARL 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 289 DQmiaedksigspmeEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQL-DMDLEEHQgemnQKYKELKKreEH 367
Cdd:COG4913 783 NR-------------AEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLeEDGLPEYE----ERFKELLN--EN 843
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 151105223 368 MDTFIETFeetknqelkrKAQIEANIvallehcsRNI-NRIEQIssitNQELK 419
Cdd:COG4913 844 SIEFVADL----------LSKLRRAI--------REIkERIDPL----NDSLK 874
|
|
| TTC8_N |
cd21341 |
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 ... |
7-50 |
1.50e-03 |
|
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 (TTC80), also known a BBS8, has been directly linked to Bardet-Biedl syndrome, an autosomal recessive ciliopathy characterized by retinal degeneration, renal failure, obesity, diabetes, male infertility, polydactyly and cognitive impairment. Mutations in BBS8 cause early vision loss. In addition to C-terminal tetratricopeptide repeats, TTC8 also contains an N-terminal domain of unknown function.
Pssm-ID: 411061 [Multi-domain] Cd Length: 139 Bit Score: 39.21 E-value: 1.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 151105223 7 SSAARPVSRggvglTGRPPSGI--------RPLSGNIRVATAMPPGTARPGS 50
Cdd:cd21341 66 SQAMRPTTS-----SGRPITGFvrpgtqsgRPGTSRQALRTPRRAGTARPVT 112
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
253-398 |
1.59e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.39 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 253 SQNMKKESLEAEIAHSQVKQEAV------------LLHEKLYELESHRDQMIAEDKSigSPMEEREKLLKQIKDDNQEIA 320
Cdd:PRK00106 23 SIKMKSAKEAAELTLLNAEQEAVnlrgkaerdaehIKKTAKRESKALKKELLLEAKE--EARKYREEIEQEFKSERQELK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 321 SMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHmdtfIETFEETKNQELKRKA---QIEANIVALL 397
Cdd:PRK00106 101 QIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQ----VEKLEEQKKAELERVAalsQAEAREIILA 176
|
.
gi 151105223 398 E 398
Cdd:PRK00106 177 E 177
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
114-594 |
1.64e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 114 KLQKGIEMYNQENSVYLSYEKRAE-TLAVEIKELQGQLADYNMLVDKLNTNtemeEVMNDYNMLKAqnDRETQSLDVIFT 192
Cdd:TIGR01612 946 ILNKNIDTIKESNLIEKSYKDKFDnTLIDKINELDKAFKDASLNDYEAKNN----ELIKYFNDLKA--NLGKNKENMLYH 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 193 ERQAKEKQIRSVEEEIEqekqatdDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKesLEAEIAHSQVKQ 272
Cdd:TIGR01612 1020 QFDEKEKATNDIEQKIE-------DANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEE--AEINITNFNEIK 1090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 273 EAVllheKLYELEShrdqmIAEDKSIgSPMEEREKLLKQIKDDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEE--H 350
Cdd:TIGR01612 1091 EKL----KHYNFDD-----FGKEENI-KYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDvaD 1160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 351 QGEMNQKYKELKKREEHMDTFIET---FEETKNQELKRKAQIEANIVALLEHCSRNINRIEQISSITNQELkmmqddlnf 427
Cdd:TIGR01612 1161 KAISNDDPEEIEKKIENIVTKIDKkknIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKI--------- 1231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 428 kSTEVQKSQSTAQNLTSDIQRLQLDLQKMELLESKMTEEQhSLKSKIKQMTTDLEIYNDLPALKSSGEEKIKKLHQERMI 507
Cdd:TIGR01612 1232 -DEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM-DIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLK 1309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 508 LSTHRNAFKKIME-KQNIEYEALKTQLQENETHSQLTNLERKWQHLEQNNfaMKEFIATksqesdyqpiKKNVTKQIAEY 586
Cdd:TIGR01612 1310 IIEDFSEESDINDiKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNK--IKKIIDE----------VKEYTKEIEEN 1377
|
....*...
gi 151105223 587 NKTIVDAL 594
Cdd:TIGR01612 1378 NKNIKDEL 1385
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
132-477 |
1.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 132 YEKRAETLAVEIKELQGQLADYNmlvdklntntemeevmndynmlkaqndretQSLDVIFTeRQAKEKQIRSVEEEIEQE 211
Cdd:PRK04863 381 NEARAEAAEEEVDELKSQLADYQ------------------------------QALDVQQT-RAIQYQQAVQALERAKQL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 212 KQATDdiiknMSFENQVKYLEMKTTNEKLL-QELDTLQQQLDSQNMKKE----------SLEAEIAHSQVKQEAVllhEK 280
Cdd:PRK04863 430 CGLPD-----LTADNAEDWLEEFQAKEQEAtEELLSLEQKLSVAQAAHSqfeqayqlvrKIAGEVSRSEAWDVAR---EL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 281 LYELESHRdqMIAEDksiGSPMEEREKLLKQikdDNQEIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEmnqkyke 360
Cdd:PRK04863 502 LRRLREQR--HLAEQ---LQQLRMRLSELEQ---RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR------- 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 361 lkkreehmdtfIETFEETKNQELKRKAQIEANIVALlehcSRNINRIEQISsitnQELKMMQDDLNFKSTEVQKSQSTAQ 440
Cdd:PRK04863 567 -----------LESLSESVSEARERRMALRQQLEQL----QARIQRLAARA----PAWLAAQDALARLREQSGEEFEDSQ 627
|
330 340 350
....*....|....*....|....*....|....*..
gi 151105223 441 NLTSDIQRLQLDLQKMELLESKMTEEQHSLKSKIKQM 477
Cdd:PRK04863 628 DVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
128-387 |
1.80e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 128 VYLSYEKRAETLAVEIKELQGQLADYNMLvdklnTNTEMEEVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEE 207
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEEL-----EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 208 I-----EQEKQATDDIIKNMSFENQVKYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAHSQVKQEAVLLHEKLY 282
Cdd:COG4717 363 LqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 283 ELEshrdqmiaedksigspmEEREKLLKQIKDDNQEIASMERQ--LTDTKEKINQFIEEIRQLDmdleehqgemnQKYKE 360
Cdd:COG4717 443 ELE-----------------EELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELA-----------EEWAA 494
|
250 260
....*....|....*....|....*..
gi 151105223 361 LKKREEHMDTFIETFEETKNQELKRKA 387
Cdd:COG4717 495 LKLALELLEEAREEYREERLPPVLERA 521
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
195-356 |
1.85e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 40.29 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 195 QAKEKQIRSVEEEIEQEKQATDDIIKNMSFEnqvkYLEMKTTNEKLLQELDTLQQQLDSQNMKKESLEAEIAH-SQVKQE 273
Cdd:pfam11932 19 LDLAEKAVAAAAQSQKKIDKWDDEKQELLAE----YRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEiERTERE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 274 AVLLhekLYELESHRDQMIAEDKsigsP--MEEREKLLKQIKDdnqeiaSMERQLTDTKEKINQfIEEIRQLDMD----L 347
Cdd:pfam11932 95 LVPL---MLKMLDRLEQFVALDL----PflLEERQARLARLRE------LMDDADVSLAEKYRR-ILEAYQVEAEygrtI 160
|
....*....
gi 151105223 348 EEHQGEMNQ 356
Cdd:pfam11932 161 EVYQGELEL 169
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
318-599 |
2.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 318 EIASMERQLTDTKEKINQFIEEIRQLDMDLEEHQGEMNQKYKELKKREEHMDTFIETFEETKNQELKRKAQIEANIVALl 397
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 398 ehcsrninrieQISSITNQELKMMQDdlnfkstevqksqstAQNLTSDIQRLQLdLQKMELLESKMTEEQHSLKSKIKQM 477
Cdd:COG3883 96 -----------YRSGGSVSYLDVLLG---------------SESFSDFLDRLSA-LSKIADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 478 TTDLEiyndlpALKSSGEEKIKKLHQErmilsthrnafKKIMEKQNIEYEALKTQL--QENETHSQLTNLERKWQHLEQN 555
Cdd:COG3883 149 KAELE------AKLAELEALKAELEAA-----------KAELEAQQAEQEALLAQLsaEEAAAEAQLAELEAELAAAEAA 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 151105223 556 NFAMKEFIATKSQESDYQPIKKNVTKQIAEYNKTIVDALHSTSG 599
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
236-417 |
4.19e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 236 TNEKLLQELDTLQQQLDSQNMKKESLEAEI-AHSQVKQEAVLLHEKLYELESHRDQMiAEDKSIGSPMEEREKLLKQIKD 314
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQeELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 315 DNQEIASMERQLtdtkEKINQFIEEIRQLDMDLEEHQGEMNQKYKELK-KREEHMDTFIETFEETKNQELKRKAQIEAnI 393
Cdd:COG4717 144 LPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEE-A 218
|
170 180
....*....|....*....|....
gi 151105223 394 VALLEHCSRNINRIEQISSITNQE 417
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALE 242
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
88-381 |
6.12e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.43 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 88 QRQILDKSYYLGllrSKISELTTEVNKLQKGIEMYNQENSV--YLSYEKRAETLAVEIKELQGQLADYNMLVDKLNTN-- 163
Cdd:PRK04778 153 RKSLLANRFSFG---PALDELEKQLENLEEEFSQFVELTESgdYVEAREILDQLEEELAALEQIMEEIPELLKELQTElp 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 164 TEMEEVMNDYNMLKAQN-DRETQSLDViftERQAKEKQIRSVEEEI--------EQEKQATDDIIKNM--SFENQVK--- 229
Cdd:PRK04778 230 DQLQELKAGYRELVEEGyHLDHLDIEK---EIQDLKEQIDENLALLeeldldeaEEKNEEIQERIDQLydILEREVKark 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 230 ------------YLEMKTTNEKLLQELDTLQQ-------QLDSQNMKKESLEAEIAHSQVKQEAVLLHEKLY-ELESHRD 289
Cdd:PRK04778 307 yveknsdtlpdfLEHAKEQNKELKEEIDRVKQsytlnesELESVRQLEKQLESLEKQYDEITERIAEQEIAYsELQEELE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 290 QMIAEDKSIGSPMEEREKLLKQIKDD----NQEIASMERQLTDTK---EKIN------QFIE-------EIRQLDMDLEE 349
Cdd:PRK04778 387 EILKQLEEIEKEQEKLSEMLQGLRKDeleaREKLERYRNKLHEIKrylEKSNlpglpeDYLEmffevsdEIEALAEELEE 466
|
330 340 350
....*....|....*....|....*....|..
gi 151105223 350 HQGEMNQKYKELKKREEHMDTFIETFEETKNQ 381
Cdd:PRK04778 467 KPINMEAVNRLLEEATEDVETLEEETEELVEN 498
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
257-566 |
9.12e-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: 39.18 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 257 KKESLEAEIAHSQVKQEAVLLHEKLYELESHRDQMIAEDKSIGSPMEEREKLLKQIKddnQEIASMERQLTDTKEKINQF 336
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERK---QVLEKELKHLREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 337 IEEIRQLDMDLEEHQgEMNQKYKELKKREEHMDTFIETFEET-KNQELKRKAQIEANIVALLEHCSRNINRIEQissiTN 415
Cdd:TIGR00618 242 HAYLTQKREAQEEQL-KKQQLLKQLRARIEELRAQEAVLEETqERINRARKAAPLAAHIKAVTQIEQQAQRIHT----EL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 416 QELKMMQDDLNFKSTEVQKSQSTAQnltsDIQRLQLDLQKMELLESKMTEEQHSLKSKIKQMTTDleiyndlpalkssgE 495
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIE----EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL--------------T 378
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151105223 496 EKIKKLHQERMILSTHRNAFKKIMEKQNIEYEALKTQLQENETHSQLTNLERKWQHLEQNNFAMKEFIATK 566
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITC 449
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
93-264 |
9.36e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 93 DKSYYLGLLRSKISELTTEVNKLQKGIEMYNQENSvylSYEKRAETLAVEIKELQGQLADY-----NMLVDKLNTNTEME 167
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEAALRDLesrlgDLKKERDELEAQLR 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151105223 168 EVMNDYNMLKAQNDRETQSLDVIFTERQAKEKQIRSVEEEIEQEKQATDDIIKNMSFENQVKYLE-----MKTTNEKLLQ 242
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEeeiraLEPVNMLAIQ 979
|
170 180
....*....|....*....|..
gi 151105223 243 ELDTLQQQLDSQNMKKESLEAE 264
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEE 1001
|
|
| |
