|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
273-617 |
2.40e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 273 AELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQH 352
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 353 RQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAmETLQEKSQHKEELG 432
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 433 AVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEA 512
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 513 EESLQQQQQEQEETLKLcrEEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQevkdtVDGQRILEKKGSAVLK 592
Cdd:COG1196 459 EALLELLAELLEEAALL--EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL-----LAGLRGLAGAVAVLIG 531
|
330 340
....*....|....*....|....*
gi 1907204915 593 DLKRqlhLERKRADKLQERLQEILT 617
Cdd:COG1196 532 VEAA---YEAALEAALAAALQNIVV 553
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
196-504 |
2.64e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 196 REEKKLLWEQLQGLELSEKLKKKQEsfcrlQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAEL 275
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEE-----LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 276 RDQRqgERLEHA-AALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQ 354
Cdd:COG1196 294 LAEL--ARLEQDiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 355 AEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAv 434
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE- 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 435 RLRHEKELLGVRARyERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGW 504
Cdd:COG1196 451 EAELEEEEEALLEL-LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-617 |
9.73e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 9.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 216 KKKQESFCRLQTEKETL--FNDSRNKIEElqQRKEADLKAQLA-RTQKLQQELEAANQSLAELRDQRQGERLEhaaALRA 292
Cdd:TIGR02168 172 ERRKETERKLERTRENLdrLEDILNELER--QLKSLERQAEKAeRYKELKAELRELELALLVLRLEELREELE---ELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 293 LQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQ 372
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 373 ESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmldelamETLQEKSQHKEELgavrlrhEKELLGVRARYere 452
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------AELEELESRLEEL-------EEQLETLRSKV--- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 453 lrelhEDKKRQEEELRGQIREEKARtreLENLQHTVEELQAQVhsmdgakgwfERRLKEAEESLQQQQQEQEETLKLCRE 532
Cdd:TIGR02168 389 -----AQLELQIASLNNEIERLEAR---LERLEDRRERLQQEI----------EELLKKLEEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 533 EHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVlkdlkRQLHLERKRADKLQERL 612
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV-----KALLKNQSGLSGILGVL 525
|
....*
gi 1907204915 613 QEILT 617
Cdd:TIGR02168 526 SELIS 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-632 |
1.03e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 193 EMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQ------QRKEADLKAQLARTQKLQQEL- 265
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerlEELEEELAELEEELEELEEELe 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 266 EAANQS------LAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgLLAENSALRTSLAALEQIQTAKTQELNML 339
Cdd:COG1196 341 ELEEELeeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 340 REQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLD-ELAM 418
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLlLLEA 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 419 ETLQE------KSQHKEELGAVRLRHEKELLGVRARYEREL------------RELHEDKKRQEEELRGQ-------IRE 473
Cdd:COG1196 500 EADYEgflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaalqnivVEDDEVAAAAIEYLKAAkagratfLPL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 474 EKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEtlKLCREEHAAELKGKDEELQNVREQLQ 553
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR--LEAALRRAVTLAGRLREVTLEGEGGS 657
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907204915 554 QAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVLSE 632
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
188-495 |
2.24e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 188 VELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEaDLKAQLARTQKLQQELEA 267
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK-DLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 268 ANQSLAELRDQRQGERLEHAAALRALQdQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTA-------KTQELNMLR 340
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 341 EQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDEL---A 417
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELeskR 910
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907204915 418 METLQEKSQHKEELGAVRLRHEKeLLGVRARYERELRELHEDkkrqeeELRGQIREEKARTRELENLQHTVEELQAQV 495
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-560 |
4.52e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 7 EEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKAL---------------SKSKKAQEVEVL 71
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellaelarleqdiaRLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 72 LSENEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEGVPGAAGAHVDGELLRLQAENTALQKNMAALQ 151
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 152 ERYGKEAVRpsavgegqgdppgdvlptplapmpLAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKET 231
Cdd:COG1196 398 LAAQLEELE------------------------EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 232 LFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGL 311
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 312 LAENSALRTSLAALEQIQTAKTQELnmLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRAN--SRLLEQLQEIG 389
Cdd:COG1196 534 AAYEAALEAALAAALQNIVVEDDEV--AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGaaVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 390 QEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRG 469
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 470 QIREEKARTRELENLQHTVEELQAQVHSMDgakgwFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEELQNVR 549
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEEL-----EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
570
....*....|.
gi 1907204915 550 EQLQQAQEERD 560
Cdd:COG1196 767 RELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-621 |
2.35e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 38 LSSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSENEMLQAK-----LHSQEEDFRLQNSTLMAEFSKLCSQLEQLEL 112
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELReeleeLQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 113 ENRQLKEGVpgaagAHVDGELLRLQAENTALQKNMAALQERYgKEAVRPSAVGEGQgdppgdvlptplapmpLAEVELKW 192
Cdd:TIGR02168 275 EVSELEEEI-----EELQKELYALANEISRLEQQKQILRERL-ANLERQLEELEAQ----------------LEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 193 EMEREEKKLLWEQLQGL-ELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQqRKEADLKAQLARTQKLQQELEAANQS 271
Cdd:TIGR02168 333 DELAEELAELEEKLEELkEELESLEAELEELEAELEELESRLEELEEQLETLR-SKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 272 LAELRDQRQGERLEHAAALRALQ-DQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASEL 350
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 351 QHRQAEYEELMGQKDDLNSQLQESLRAN---SRLLEQ------------------LQEIGQEKEQLTQDLQEARKSAEKR 409
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLSgilGVLSELisvdegyeaaieaalggrLQAVVVENLNAAKKAIAFLKQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 410 KVML--------DELAMETLQEKSQHKEELG-------------------------------AVRLRHEKELLG------ 444
Cdd:TIGR02168 572 RVTFlpldsikgTEIQGNDREILKNIEGFLGvakdlvkfdpklrkalsyllggvlvvddldnALELAKKLRPGYrivtld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 445 ---VRARY----------------ERELRELHEDKKRQEEELRgqireekARTRELENLQHTVEELQAQVHSMDGAKGWF 505
Cdd:TIGR02168 652 gdlVRPGGvitggsaktnssilerRREIEELEEKIEELEEKIA-------ELEKALAELRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 506 ERRLKEAEESLQQQQQEQEEtlklcREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEK 585
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQ-----LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
650 660 670
....*....|....*....|....*....|....*.
gi 1907204915 586 KGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKS 621
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
253-502 |
5.68e-10 |
|
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: 62.09 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 253 AQLARTQKLQQELEAANQSLAELRDQRQgerlehaaalralqdQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAK 332
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA---------------ALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 333 TQELNMLREQTSELASELQHRQAEYEEL------MGQKDDLNSQL-QESLRANSRLLEQLQEIGQEKEQLTQDLQEARKS 405
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELlralyrLGRQPPLALLLsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 406 AEKRKvmldelamETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQ 485
Cdd:COG4942 162 LAALR--------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|....*..
gi 1907204915 486 HTVEELQAQVHSMDGAK 502
Cdd:COG4942 234 AEAAAAAERTPAAGFAA 250
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
28-595 |
6.79e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 28 SDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSENEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQL 107
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 108 EQLELENRQLKEGVPGAAGAHVDGELLRLQAEntalQKNMAALQERYGKEAVRpsavgegqgdppgdvlptplapmplAE 187
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKK-------------------------AD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 188 VELKWEMEREEKKLLWEQLQGLELSEKLKKKQESfCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEA 267
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 268 ANQS--------LAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQvegllAENSALRTSlAALEQIQTAKTQELNML 339
Cdd:PTZ00121 1527 AKKAeeakkadeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE-----DKNMALRKA-EEAKKAEEARIEEVMKL 1600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 340 REQTSELASElQHRQAEYEELMGqkddlnsqlqESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAME 419
Cdd:PTZ00121 1601 YEEEKKMKAE-EAKKAEEAKIKA----------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK 1669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 420 TLQEKSQHKEelgavrLRHEKEllgvRARYERELRELHEDKKRQEEELRGQIREEKARTRELENlqhtvEELQAQVHSMD 499
Cdd:PTZ00121 1670 AEEDKKKAEE------AKKAEE----DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK-----AEEENKIKAEE 1734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 500 GAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEELqnVREQLQQAQEERDGHV-KTISNLKQEVKDTVD 578
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVdKKIKDIFDNFANIIE 1812
|
570
....*....|....*..
gi 1907204915 579 GQrileKKGSAVLKDLK 595
Cdd:PTZ00121 1813 GG----KEGNLVINDSK 1825
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
191-480 |
3.08e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 191 KWEMEREEK---KLLWEQLQGLELSEKLKKKQEsfcrLQTEKETLFNDSRNKIEELQQRKEadlkaqlaRTQKLQQELEA 267
Cdd:TIGR02169 202 RLRREREKAeryQALLKEKREYEGYELLKEKEA----LERQKEAIERQLASLEEELEKLTE--------EISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 268 ANQSLAEL----RDQRQGERLEHAAALRALQDQVSS-----------------QSADAQEQVEGLLAENSALRTSL---- 322
Cdd:TIGR02169 270 IEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASlersiaekereledaeeRLAKLEAEIDKLLAEIEELEREIeeer 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 323 ---AALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDL 399
Cdd:TIGR02169 350 krrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 400 QEARKSAEKRKVMLDELAMEtLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEdKKRQEEELRGQIREEKARTR 479
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-LQRELAEAEAQARASEERVR 507
|
.
gi 1907204915 480 E 480
Cdd:TIGR02169 508 G 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-732 |
5.99e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 197 EEKKLLWEQLQGLELSEKLKKKQEsfcrLQTEKETLFNDSRNKIEELQQRKEADLKAQLAR-TQKLQQELEAANQSLAEL 275
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADE----LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkADEAKKKAEEAKKKADAA 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 276 RDQRQgERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQI--QTAKTQELNMLREQTSELASELQHR 353
Cdd:PTZ00121 1335 KKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKaeEKKKADEAKKKAEEDKKKADELKKA 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 354 QAEYE---------ELMGQKDDLNSQLQESLRANSrlLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEK 424
Cdd:PTZ00121 1414 AAAKKkadeakkkaEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 425 SQH-KEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIR--EEKARTRELENlqhtVEELQA--QVHSMD 499
Cdd:PTZ00121 1492 AEEaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKK----AEELKKaeEKKKAE 1567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 500 GAKGWFERR---LKEAEESLQQQQQEQEETLKLCREEHA--AELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVK 574
Cdd:PTZ00121 1568 EAKKAEEDKnmaLRKAEEAKKAEEARIEEVMKLYEEEKKmkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 575 DTvDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEiltnskSRTGLEELVLSEMNSPSRTQTGDSSSVSSFSYRE 654
Cdd:PTZ00121 1648 KA-EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907204915 655 ILKEKESSAIPARSLSSSPQAQPPRPAELS-DEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIET 732
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-615 |
8.27e-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: 59.69 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 7 EEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQK---ALSK--SKKAQEVEVLLSENEMLQAK 81
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEeleSLEAelEELEAELEELESRLEELEEQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 82 LHSQEEDF---RLQNSTLMAEFSKLCSQLEQLELENRQLKEGVPGAAGAHVDGELLRLQAENTALQKNMAALQERygkea 158
Cdd:TIGR02168 381 LETLRSKVaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE----- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 159 vrpsavgegqgdppgdvlptplapmpLAEVELKWEMEREEKKLLWEQLQGLELSEK-LKKKQESFCRLQTEKETLFNDSR 237
Cdd:TIGR02168 456 --------------------------LERLEEALEELREELEEAEQALDAAERELAqLQARLDSLERLQENLEGFSEGVK 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 238 NKIEELQQRKEAD--LKAQLARTQKLQQELEA----------------ANQSLAELRDQRQG------------------ 281
Cdd:TIGR02168 510 ALLKNQSGLSGILgvLSELISVDEGYEAAIEAalggrlqavvvenlnaAKKAIAFLKQNELGrvtflpldsikgteiqgn 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 282 --ERLEHAAALRALQDQVSSQSADAQEQVEGLL---------AENSALRTSLAALEQIQTAKTQELN---MLREQTSELA 347
Cdd:TIGR02168 590 drEILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRpggVITGGSAKTN 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 348 SELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARksaekRKVMLDELAMETLQEKSQH 427
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS-----RQISALRKDLARLEAEVEQ 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 428 KEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFER 507
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 508 RLKEAEESLQQQQQEQEET------LKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQR 581
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
650 660 670
....*....|....*....|....*....|....
gi 1907204915 582 ILEKKgsavLKDLKRQLHLERKRADKLQERLQEI 615
Cdd:TIGR02168 905 ELESK----RSELRRELEELREKLAQLELRLEGL 934
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
210-409 |
1.93e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 210 ELSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAA 289
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKAL-LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 290 LRALQDQ---------VSSQSA-DAQEQVEGLLAENSALRTSLAALEQIQT---AKTQELNMLREQTSELASELQHRQAE 356
Cdd:COG4942 110 LRALYRLgrqpplallLSPEDFlDAVRRLQYLKYLAPARREQAEELRADLAelaALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907204915 357 YEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKR 409
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-499 |
3.60e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 248 EADLKAQLARTQKLQQELEAANQSLAELRDQRqgERLEHAAALralqdqvssqsADAQEQVEGLLAENSALRTSLAALEQ 327
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQI--ELLEPIREL-----------AERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 328 iqtakTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEslransrLLEQLQEI-GQEKEQLTQDLQEARKSA 406
Cdd:COG4913 287 -----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDE-------LEAQIRGNgGDRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 407 EKRKVMLDELAmetlqeksQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQH 486
Cdd:COG4913 355 EERERRRARLE--------ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
250
....*....|...
gi 1907204915 487 TVEELQAQVHSMD 499
Cdd:COG4913 427 EIASLERRKSNIP 439
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
210-617 |
9.78e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 210 ELSEKLKKKQESFCRLQTEKETL---FNDSRNKIEELQQRKE----------ADLKAQLARTQKLQQELEAANQSLAELR 276
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELaeeVRDLRERLEELEEERDdllaeaglddADAEAVEARREELEDRDEELRDRLEECR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 277 dQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAE 356
Cdd:PRK02224 335 -VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 357 YEELMGQKDDLNSQLQEsLRANSRLLEQLQEIGQEkeqltqdLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRL 436
Cdd:PRK02224 414 LEELREERDELREREAE-LEATLRTARERVEEAEA-------LLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 437 RHEKELLGVRARYER--ELRELH------EDKKRQEEELRGQIREEKARTRE-LENLQHTVEELQAQvhsmdgAKGWFER 507
Cdd:PRK02224 486 DLEEEVEEVEERLERaeDLVEAEdrierlEERREDLEELIAERRETIEEKRErAEELRERAAELEAE------AEEKREA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 508 RLKEAEESLQQQQQ-----EQEETLKLCRE---------EHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEV 573
Cdd:PRK02224 560 AAEAEEEAEEAREEvaelnSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAELNDERRERLAEKRERKREL 639
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907204915 574 KDTVDGQRILEKKGsavlkdlkrqlhlERKRADKLQERLQEILT 617
Cdd:PRK02224 640 EAEFDEARIEEARE-------------DKERAEEYLEQVEEKLD 670
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
245-490 |
1.23e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 245 QRKEADLKAQLARtqkLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSSQ--SADAQEQVEGLLAENSALRTSL 322
Cdd:COG4913 609 RAKLAALEAELAE---LEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEidVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 323 AALEQiqtaktqelnmLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEA 402
Cdd:COG4913 685 DDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 403 RKSAEKRKVMLDELAMETLQEKSQHKEELGavrlRHEKELLGVRAR---------------------YERELRELHEDK- 460
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRARLN----RAEEELERAMRAfnrewpaetadldadleslpeYLALLDRLEEDGl 829
|
250 260 270
....*....|....*....|....*....|
gi 1907204915 461 KRQEEELRGQIREEKarTRELENLQHTVEE 490
Cdd:COG4913 830 PEYEERFKELLNENS--IEFVADLLSKLRR 857
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
189-488 |
2.71e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 189 ELKWEMEREEKKLLWEQLQGLELSEKLKKKQEsfcrlqteketLFNDSRNKIEELQQRKEAD---LKAQLARTQKLQQEL 265
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-----------RLEELEEDLSSLEQEIENVkseLKELEARIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 266 EAANQSLAELRDQRQGERLEH-AAALRALQDQVSSQSADAQE---QVEGLLAENSALRTSLAALEQIQTAKTQELNMLRE 341
Cdd:TIGR02169 775 HKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 342 QTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVM-------LD 414
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKlealeeeLS 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 415 ELAMETLQEKSQHKEELGAVRLRHEKELLGVRAR------------YERELRELHEDKKRQE--EELRGQIREekaRTRE 480
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalepvnmlaiqeYEEVLKRLDELKEKRAklEEERKAILE---RIEE 1011
|
....*...
gi 1907204915 481 LENLQHTV 488
Cdd:TIGR02169 1012 YEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-408 |
3.22e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 37 ELSSLRQKVAYLdkefskAQKALSKSKKAQEVEVLLSENEMLQAKLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQ 116
Cdd:TIGR02168 678 EIEELEEKIEEL------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 117 lkegvpgaagahvdgellrLQAENTALQKNMAALQERYGKEAVRPSAVGEGqgdppgdvlptplapmpLAEVELKWEMER 196
Cdd:TIGR02168 752 -------------------LSKELTELEAEIEELEERLEEAEEELAEAEAE-----------------IEELEAQIEQLK 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 197 EEKKLLWEQLQglELSEKLKKKQESFCRLQTEKETLFNDSRNK---IEELQQRKE------ADLKAQLARTQKLQQELEA 267
Cdd:TIGR02168 796 EELKALREALD--ELRAELTLLNEEAANLRERLESLERRIAATerrLEDLEEQIEelsediESLAAEIEELEELIEELES 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 268 ANQSLAELRDQRQgerlEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELA 347
Cdd:TIGR02168 874 ELEALLNERASLE----EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY 949
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907204915 348 S-ELQHRQAEY-------EELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQ---DLQEARKSAEK 408
Cdd:TIGR02168 950 SlTLEEAEALEnkieddeEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAqkeDLTEAKETLEE 1021
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
193-497 |
4.77e-07 |
|
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: 53.82 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 193 EMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSL 272
Cdd:pfam02463 194 ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 273 AELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQH 352
Cdd:pfam02463 274 NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 353 RQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELG 432
Cdd:pfam02463 354 EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907204915 433 AVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHS 497
Cdd:pfam02463 434 EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-620 |
6.20e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 244 QQRKEADLK-----AQLARTQKLQQELEAANQSLaelrdQRQGER----LEHAAALRALQDQVSSQSAD-AQEQVEGLLA 313
Cdd:TIGR02168 172 ERRKETERKlertrENLDRLEDILNELERQLKSL-----ERQAEKaeryKELKAELRELELALLVLRLEeLREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 314 ENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKE 393
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 394 QLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEelgavrlrhekellgvraryereLRELHEDKKRQEEELRGQIRE 473
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEE-----------------------LEAELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 474 EKARTRELENlqhTVEELQAQVHSMDgakgwferrlkeaeES----LQQQQQEQEETLKLCREEHAAELKGKDEELQNVR 549
Cdd:TIGR02168 384 LRSKVAQLEL---QIASLNNEIERLE--------------ARlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907204915 550 EQLQQAQEERDGHVKTISNLKQEVkdtvdgqrileKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSK 620
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREEL-----------EEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-398 |
9.81e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 4 ALSEEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSK-SKKAQEVEVLLSENEMLQAKL 82
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQlEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 83 HSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEgvpgaagahvdgELLRLQAENTALQKNMAALQERYGKEAVRPS 162
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE------------ALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 163 AVGEGQGDppgdvlptplapmpLAE--VELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEketlfndsRNKI 240
Cdd:TIGR02168 835 ATERRLED--------------LEEqiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA--------LALL 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 241 EELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRT 320
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907204915 321 SLAALEQiQTAKTQELNMLREQtselaselqhrqaEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQD 398
Cdd:TIGR02168 973 RLKRLEN-KIKELGPVNLAAIE-------------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
281-621 |
1.08e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 281 GERLEHAAALRALQDQVSSQSAdaQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEEL 360
Cdd:TIGR02169 658 GSRAPRGGILFSRSEPAELQRL--RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 361 MGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmlDELAMETLQEKsqhkeelgavrlrhek 440
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEI---------------- 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 441 ellgvraryERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEaeeslqqqq 520
Cdd:TIGR02169 797 ---------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN--------- 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 521 qeqeetLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTvdgqrilekkgSAVLKDLKRQLHL 600
Cdd:TIGR02169 859 ------LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL-----------EAQIEKKRKRLSE 921
|
330 340
....*....|....*....|.
gi 1907204915 601 ERKRADKLQERLQEILTNSKS 621
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGE 942
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
224-485 |
1.42e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 224 RLQTEKETLFNDSRNKIEElqqRKEADLKAQLARtqkLQQELEAANQSLAELRDQRqgerlEHAAALRALQDQVSSQSAD 303
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEE---KEEKDLHERLNG---LESELAELDEEIERYEEQR-----EQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 304 AQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAE--------------YEELMGQKDDLNS 369
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeavearREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 370 QLQ-------------ESLRANSRLLE-QLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELametlqeksqhKEELGAVR 435
Cdd:PRK02224 329 RLEecrvaaqahneeaESLREDADDLEeRAEELREEAAELESELEEAREAVEDRREEIEEL-----------EEEIEELR 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907204915 436 LRHE--KELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQ 485
Cdd:PRK02224 398 ERFGdaPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
193-378 |
1.52e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 193 EMEREEKKLlwEQLQGL-ELSEKLKKKQESFCRLQTEKETL--FNDSR--NKIEELQQRKEADLKAQLARTQKLQQELEA 267
Cdd:COG4913 243 ALEDAREQI--ELLEPIrELAERYAAARERLAELEYLRAALrlWFAQRrlELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 268 ANQSLAELRDQRQ---GERLEHAAA-LRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQT 343
Cdd:COG4913 321 LREELDELEAQIRgngGDRLEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|....*
gi 1907204915 344 SELASELQHRQAEYEELMGQKDDLNSQLqESLRAN 378
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEI-ASLERR 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
225-575 |
2.05e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.66 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 225 LQTEKETLFNDSRNKIEELQQRKEAdlkaqlaRTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADA 304
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQD-------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 305 QEQVEGLLAENSALRTSLAALEQIQTAKTQElnmLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLranSRLLEQ 384
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL---ADLHKR 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 385 LQEIGQEKEQ----LTQDLQEARKSAEKRKvMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYE--RELRELHE 458
Cdd:pfam15921 390 EKELSLEKEQnkrlWDRDTGNSITIDHLRR-ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNEslEKVSSLTA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 459 DKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHsmdgakgwfERRLKEAEESLQQQQQEQEETLKLCREEHaaeL 538
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ---------EKERAIEATNAEITKLRSRVDLKLQELQH---L 536
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907204915 539 KGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKD 575
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEN 573
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
7-622 |
2.36e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.38 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 7 EEEFQRMQTQLLEL-------RTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKAQEVEVLLSENEM-L 78
Cdd:pfam12128 247 QQEFNTLESAELRLshlhfgyKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELeA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 79 QAKLHSQEEDFRLQnsTLMAEFSKLCSQLEQLELENRQLKegvpGAAGAHVDGE----------LLRLQAENTALQKNMA 148
Cdd:pfam12128 327 LEDQHGAFLDADIE--TAAADQEQLPSWQSELENLEERLK----ALTGKHQDVTakynrrrskiKEQNNRDIAGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 149 ALQERYGKEAVRPSAVGEGQGDPPGDVLPTPLAPMPLAEVELKWEMErEEKKLLWEQLQGLELSEKLKKKQESFCRLQTE 228
Cdd:pfam12128 401 KIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG-ELKLRLNQATATPELLLQLENFDERIERAREE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 229 KEtlfndSRNKIEELQQRKEADLKAqlaRTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQV 308
Cdd:pfam12128 480 QE-----AANAEVERLQSELRQARK---RRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 309 EGLLAENSALRTSLAAlEQIQTAKTQELNM----LREQTSELASELQHRQAEYEELmgqkDDLNSQLQESLRANSRLLEQ 384
Cdd:pfam12128 552 GKVISPELLHRTDLDP-EVWDGSVGGELNLygvkLDLKRIDVPEWAASEEELRERL----DKAEEALQSAREKQAAAEEQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 385 LQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVraryERELRELHEDKKRQE 464
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL----EAQLKQLDKKHQAWL 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 465 EELRGQIREekARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAeeslqqqqqeqeetLKLCREEHAAELKGKDEE 544
Cdd:pfam12128 703 EEQKEQKRE--ARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAE--------------LKALETWYKRDLASLGVD 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 545 LQNV------REQLQQ--AQEERDGHVKTI-------------SNLKQEVKDTVDGQRILEKKGSAVLKDLKR---QLHL 600
Cdd:pfam12128 767 PDVIaklkreIRTLERkiERIAVRRQEVLRyfdwyqetwlqrrPRLATQLSNIERAISELQQQLARLIADTKLrraKLEM 846
|
650 660
....*....|....*....|..
gi 1907204915 601 ERKRADKLQERLQEILTNSKSR 622
Cdd:pfam12128 847 ERKASEKQQVRLSENLRGLRCE 868
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
303-483 |
6.83e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 303 DAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEY--EELMGQKDDLNSQLQEsLRANSR 380
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELER-LDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 381 LLEQLQeigqekEQLtQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHE----KELLGVRARYERELREL 456
Cdd:COG4913 686 DLAALE------EQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaaedLARLELRALLEERFAAA 758
|
170 180
....*....|....*....|....*....
gi 1907204915 457 HEDKKRQE--EELRGQIREEKARTRELEN 483
Cdd:COG4913 759 LGDAVERElrENLEERIDALRARLNRAEE 787
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
234-402 |
6.94e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 234 NDSRNKIEELQQRKE-------------------ADLKAQLARTQKLQQELEAANQSLAElrDQRQGERLEHAAA----- 289
Cdd:PRK11281 39 ADVQAQLDALNKQKLleaedklvqqdleqtlallDKIDRQKEETEQLKQQLAQAPAKLRQ--AQAELEALKDDNDeetre 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 290 ------LRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTA------KTQELNML-----REQTSELASELQH 352
Cdd:PRK11281 117 tlstlsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAAlyansqRLQQIRNLlkggkVGGKALRPSQRVL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907204915 353 RQAEYEELMGQkddlNSQLQESLRANSrlleQLQEIGQEK-----------EQLTQDLQEA 402
Cdd:PRK11281 197 LQAEQALLNAQ----NDLQRKSLEGNT----QLQDLLQKQrdyltariqrlEHQLQLLQEA 249
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
387-640 |
7.51e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 387 EIGQEKEQLTQDLQEARKSAEKRKVMLDELA--METLQEKSQHKEELGAVRLRHEkellgvraryERELRELHEDKKRQE 464
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqLERLRREREKAERYQALLKEKR----------EYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 465 EELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEE 544
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 545 LQNVREQLQQAQEERDGHVKTISNLKQEVKDtvdgQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTG 624
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEE----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250
....*....|....*.
gi 1907204915 625 LEELVLSEMNSPSRTQ 640
Cdd:TIGR02169 393 KLEKLKREINELKREL 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
240-441 |
1.21e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 240 IEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQrqgerLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALR 319
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEK-----EEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 320 TSLAALEQIQtaKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEslrANSRLLEQLQEIGQEKEQLTQDL 399
Cdd:COG4717 123 KLLQLLPLYQ--ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907204915 400 QEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKE 441
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
7-473 |
1.27e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 7 EEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKAL-SKSKKAQEVEVLLSENEMLQAKLHSQ 85
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELaELEEELEELEEELEELEEELEEAEEE 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 86 EEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEgvpgaagahvdgELLRLQAENTALQKNMAALQERYGKEAVRPSAVG 165
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAE------------ELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 166 EGQGDppgdvlptpLAPMPLAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQ 245
Cdd:COG1196 421 EELEE---------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 246 RKEADLKAQLARTQKLQQELEAANQSLA---------ELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgLLAENS 316
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE-YLKAAK 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 317 ALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELM----------------------------------- 361
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYyvlgdtllgrtlvaarleaalrravtlagrlrevt 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 362 GQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKE 441
Cdd:COG1196 651 LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQL 730
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1907204915 442 LLGVRARYERELREL----------------HEDKKRQEEELRGQIRE 473
Cdd:COG1196 731 EAEREELLEELLEEEelleeealeelpeppdLEELERELERLEREIEA 778
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
223-493 |
1.50e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 223 CRLQTEK-ETLFNDSRNKIEELQQRKEA--DLKAQLARTQKLQQELEAANQSLAELRDqRQGERLEHAAALRALQDQVSS 299
Cdd:PRK02224 473 DRERVEElEAELEDLEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERRE-TIEEKRERAEELRERAAELEA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 300 QSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLrEQTSELASELQHRQAEYEELMGQKDDLNSQlqeslraNS 379
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAEL-------ND 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 380 RLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEElgavrlrHEKELLGVRARYERELRELhed 459
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELRE-------ERDDLQAEIGAVENELEEL--- 693
|
250 260 270
....*....|....*....|....*....|....
gi 1907204915 460 kkrqeEELRGQIREEKARTRELENLQHTVEELQA 493
Cdd:PRK02224 694 -----EELRERREALENRVEALEALYDEAEELES 722
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
268-495 |
1.63e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 268 ANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSlaaleqiqtaktQELNMLREQTSELA 347
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 348 SELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLE--QLQEIGQEKEQLTQDLQEARksaekrkvmldelamETLQEKS 425
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELS---------------ARYTPNH 290
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907204915 426 ----QHKEELGAVRLRHEKELLGVRARYERELRELhedkKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 495
Cdd:COG3206 291 pdviALRAQIAALRAQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
193-609 |
1.63e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 193 EMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQR----KEADLKAQLARTQKLQQELEAA 268
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyqELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 269 NQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELAS 348
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 349 ELQhRQAEYEELMGQKDDLNSQ-LQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSqH 427
Cdd:COG4717 235 ELE-AAALEERLKEARLLLLIAaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP-A 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 428 KEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARtRELENLQHTVEEL--QAQVHSMDGAKGWF 505
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-LQLEELEQEIAALlaEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 506 ERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKD---EELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRI 582
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|....*..
gi 1907204915 583 LEKKgsAVLKDLKRQLHLERKRADKLQ 609
Cdd:COG4717 472 AELL--QELEELKAELRELAEEWAALK 496
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
240-408 |
1.85e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 240 IEELQQRKEADLKAQLA----RTQKLQQELEAANQSLAELR--------DQRQGERLEHAAALRALQDQVSSQSADAQ-- 305
Cdd:COG3206 162 LEQNLELRREEARKALEfleeQLPELRKELEEAEAALEEFRqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEar 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 306 -EQVEGLLAENSALRTSLAALEQIQTAKTQeLNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLE- 383
Cdd:COG3206 242 lAALRAQLGSGPDALPELLQSPVIQQLRAQ-LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEa 320
|
170 180
....*....|....*....|....*
gi 1907204915 384 QLQEIGQEKEQLTQDLQEARKSAEK 408
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAE 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
321-588 |
2.48e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 321 SLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQ 400
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 401 EARKSAEKRKVMLDELaMETLQEKSQHKEELGAVRLRHEKELLgVRARYereLRELHEDKKRQEEELRGQIREEKARTRE 480
Cdd:COG4942 94 ELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAV-RRLQY---LKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 481 LENLQHTVEELQAQVhsmdgakgwferrlkeaeeslqQQQQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQEERD 560
Cdd:COG4942 169 LEAERAELEALLAEL----------------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250 260
....*....|....*....|....*...
gi 1907204915 561 GHVKTISNLKQEVKDTVDGQRILEKKGS 588
Cdd:COG4942 227 ALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
235-495 |
2.64e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 235 DSRNKIEELQQRKEA---DLKAQLARTQKLQQELEAANQSLA----ELRDQRQGERLEhaAALRALQDQVSSQ---SADA 304
Cdd:PRK04863 297 TSRRQLAAEQYRLVEmarELAELNEAESDLEQDYQAASDHLNlvqtALRQQEKIERYQ--ADLEELEERLEEQnevVEEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 305 QEQVEGLLAENSA-------LRTSLA----ALEQIQT------------AKTQELNMLREQTSELASELQHR-QAEYEEL 360
Cdd:PRK04863 375 DEQQEENEARAEAaeeevdeLKSQLAdyqqALDVQQTraiqyqqavqalERAKQLCGLPDLTADNAEDWLEEfQAKEQEA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 361 MGQKDDLNSQLQESLRANSR------------------------------------LLEQLQEIGQEKEQLTQDLQEARk 404
Cdd:PRK04863 455 TEELLSLEQKLSVAQAAHSQfeqayqlvrkiagevsrseawdvarellrrlreqrhLAEQLQQLRMRLSELEQRLRQQQ- 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 405 SAEKrkvMLDELAMEtLQEKSQHKEELGAVRLRHEKELLGVRArYERELRELHEDKKRQEEELRGQIREEKARTRELENL 484
Cdd:PRK04863 534 RAER---LLAEFCKR-LGKNLDDEDELEQLQEELEARLESLSE-SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAA 608
|
330
....*....|.
gi 1907204915 485 QHTVEELQAQV 495
Cdd:PRK04863 609 QDALARLREQS 619
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
239-457 |
3.95e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 239 KIEEL-QQRKEADLKA-----QLARTQKLQQELEAAN-QSLAELRDQRQgERLEHAAALRALQDQVSSQSADAQEQVEGL 311
Cdd:PHA02562 175 KIRELnQQIQTLDMKIdhiqqQIKTYNKNIEEQRKKNgENIARKQNKYD-ELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 312 LAENSALRTSLAALE-QIQTAK---------------TQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESL 375
Cdd:PHA02562 254 SAALNKLNTAAAKIKsKIEQFQkvikmyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 376 RANSRLLEQLQEIGQEKeqltQDLQEARKSAEKRKVMLDELAMETLqeksQHKEELGAVRlRHEKELLGVRARYERELRE 455
Cdd:PHA02562 334 EQSKKLLELKNKISTNK----QSLITLVDKAKKVKAAIEELQAEFV----DNAEELAKLQ-DELDKIVKTKSELVKEKYH 404
|
..
gi 1907204915 456 LH 457
Cdd:PHA02562 405 RG 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
211-615 |
5.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 211 LSEKLKKKQESFCRLQTEKETLFNDSRNKIEE---LQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQG-ERLEH 286
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEelkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 287 AAALRALQDQVSSQSADAQEQVEGL---LAENSALRTSLAALEQIQTAKTQELNMLREQTS-ELASELQHRQAEYEELMG 362
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 363 QKddlnSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEL 442
Cdd:COG4717 207 RL----AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 443 LGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQH--------TVEELQAQVHSMDGAKGWFERRLKEAEE 514
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalglppdlSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 515 SLQQQQQEQEETL-KLCREEHAAELKGKDEELQNvREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKkgsavLKD 593
Cdd:COG4717 363 LQLEELEQEIAALlAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEELEEE-----LEE 436
|
410 420
....*....|....*....|..
gi 1907204915 594 LKRQLHLERKRADKLQERLQEI 615
Cdd:COG4717 437 LEEELEELEEELEELREELAEL 458
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
237-494 |
6.51e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.56 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 237 RNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQ-----------RQGERLEHAAALRALQDQVSSQSADAQ 305
Cdd:pfam05667 242 KRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSfsgssttdtglTKGSRFTHTEKLQFTNEAPAATSSPPT 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 306 EQVEgllaensalrtslaaLEQIQTAKTQELNMLREQTSELASELQhrqaEYEELMGQKDDLNSQLQESLRANSRLLEQL 385
Cdd:pfam05667 322 KVET---------------EEELQQQREEELEELQEQLEDLESSIQ----ELEKEIKKLESSIKQVEEELEELKEQNEEL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 386 QEIGQEKEQLTQDLQEARKSAEKRKVMLDELAmETLQEKSQHKEElgavrlrHEKELLgvrARYeRELRELHEDKKRQEE 465
Cdd:pfam05667 383 EKQYKVKKKTLDLLPDAEENIAKLQALVDASA-QRLVELAGQWEK-------HRVPLI---EEY-RALKEAKSNKEDESQ 450
|
250 260
....*....|....*....|....*....
gi 1907204915 466 ELRGQIREEKARTRELENLQHTVEELQAQ 494
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKEELYKQ 479
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-377 |
6.53e-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: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 180 LAPMPLAEVELKWEMEREEKKLLWEQLQglELSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQ 259
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIA--ELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 260 KLQQELEAANQSLAELRD---------QRQG-----------------------------ERLEHAAALRALQDQVSSQS 301
Cdd:COG4942 87 ELEKEIAELRAELEAQKEelaellralYRLGrqpplalllspedfldavrrlqylkylapARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907204915 302 ADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRA 377
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
240-503 |
1.41e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 240 IEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRdqrqgERLEHAAALRalqdqvsSQSADAQEQVEGLLAENSALR 319
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLE-----KEVKELEELK-------EEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 320 TSLAALEQIQTAKTQELNMLREQTSELaSELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDL 399
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 400 QEARKSAEKRKVMLDELamETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTR 479
Cdd:PRK03918 338 ERLEELKKKLKELEKRL--EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260
....*....|....*....|....
gi 1907204915 480 ELENlqhTVEELQAQVHSMDGAKG 503
Cdd:PRK03918 416 ELKK---EIKELKKAIEELKKAKG 436
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
213-430 |
2.11e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 44.71 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 213 EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRA 292
Cdd:pfam03528 11 AELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAVATVSENT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 293 LQDQVSSQSADAQEQVegllaensalrTSLAALEQiQTAKTQELNMLREQTSELASELQHRQAEYEElmgqKDDLNSQLQ 372
Cdd:pfam03528 91 KQEAIDEVKSQWQEEV-----------ASLQAIMK-ETVREYEVQFHRRLEQERAQWNQYRESAERE----IADLRRRLS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 373 EslransrlleqlqeiGQEKEQLTQDLQEARKSAEKRK--VMLDELAMETLQEKSQHKEE 430
Cdd:pfam03528 155 E---------------GQEEENLEDEMKKAQEDAEKLRsvVMPMEKEIAALKAKLTEAED 199
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
230-426 |
2.59e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 230 ETLFNDSRNKIEELQQrKEADLKAQLArtqKLQQELEAANQSLAELRDQRQGERlEHAAALRALQDQVSSQSADAQEQVE 309
Cdd:COG3883 15 DPQIQAKQKELSELQA-ELEAAQAELD---ALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 310 GLLAENSALRTSLAALEQIQTAKTQE--------LNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRL 381
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907204915 382 LEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQ 426
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
255-426 |
2.80e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 255 LARTQKLQQELEAANQ---SLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALE--QIQ 329
Cdd:PRK10929 119 LEKSRQAQQEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELElaQLS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 330 TAKTQELNMLR-----EQTSELASELQ--------HRQAEYEE-------LMGQKDDLNSQLQESLRAN---SRLLEQ-- 384
Cdd:PRK10929 199 ANNRQELARLRselakKRSQQLDAYLQalrnqlnsQRQREAERalestelLAEQSGDLPKSIVAQFKINrelSQALNQqa 278
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907204915 385 --LQEIGQEKEQLTQDLQEARKsaekrkvmldelAMETLQEKSQ 426
Cdd:PRK10929 279 qrMDLIASQQRQAASQTLQVRQ------------ALNTLREQSQ 310
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
187-290 |
3.12e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 187 EVELKWEMEREEKKLLWEQlqglELSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQrKEADLKAQLARTQKLQQELE 266
Cdd:PRK12704 57 EALLEAKEEIHKLRNEFEK----ELRERRNELQKLEKRLLQKEENL----DRKLELLEK-REEELEKKEKELEQKQQELE 127
|
90 100
....*....|....*....|....
gi 1907204915 267 AANQSLAELRDQRQgERLEHAAAL 290
Cdd:PRK12704 128 KKEEELEELIEEQL-QELERISGL 150
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
186-459 |
3.29e-04 |
|
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: 44.67 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 186 AEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSrnkieelqQRKEADLKAQLARTQKLQQEL 265
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA--------EERLAKLEAEIDKLLAEIEEL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 266 EAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgllaENSALRTSLAALeqiqtakTQELNMLREQTSE 345
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKL-------KREINELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 346 LASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELametlqEKS 425
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV------EKE 484
|
250 260 270
....*....|....*....|....*....|....
gi 1907204915 426 QHKEELGAVRLRHEKELLGVRARYERELRELHED 459
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
373-615 |
4.31e-04 |
|
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: 44.29 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 373 ESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYErE 452
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE-K 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 453 LRELHEDKKRQEEELRGQIREEKARTRELEN-----LQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETL 527
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 528 klcreEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADK 607
Cdd:TIGR02169 336 -----AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
....*...
gi 1907204915 608 LQERLQEI 615
Cdd:TIGR02169 411 LQEELQRL 418
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
185-589 |
4.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 185 LAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEaDLKAQLARTQKLQQE 264
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 265 LEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLA----ALEQIQTAKT------- 333
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKelkkAIEELKKAKGkcpvcgr 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 334 -----QELNMLREQTSELA---SELQHRQAEYEELMGQKDDLNSQL--QESLRANSRLLEQLQEIGQE-KEQLTQDLQEA 402
Cdd:PRK03918 444 elteeHRKELLEEYTAELKrieKELKEIEEKERKLRKELRELEKVLkkESELIKLKELAEQLKELEEKlKKYNLEELEKK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 403 RKSAEKRKVMLDELAME--TLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIRE------- 473
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKElepfyne 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 474 -------EKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEELQ 546
Cdd:PRK03918 604 ylelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELE 683
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907204915 547 NVREQLQQAQeerdghvKTISNLKQEVKDTVDGQRILEKKGSA 589
Cdd:PRK03918 684 ELEKRREEIK-------KTLEKLKEELEEREKAKKELEKLEKA 719
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
189-498 |
4.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 189 ELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK---EADLKAQLARTQKLQQEL 265
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLaelEEELEEAQEELEELEEEL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 266 EAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSE 345
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 346 LASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARkSAEKRKVMLDELAMETLQEKS 425
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE-LEQEIAALLAEAGVEDEEELR 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 426 QHkeelgAVRLRHEKELLGVRARYERELREL---------HEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVH 496
Cdd:COG4717 389 AA-----LEQAEEYQELKEELEELEEQLEELlgeleelleALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
..
gi 1907204915 497 SM 498
Cdd:COG4717 464 QL 465
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8-493 |
5.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 8 EEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAqkalskSKKAQEVEVLLSENEMLQAKLHSQEE 87
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL------EEKEERLEELKKKLKELEKRLEELEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 88 DFRLQNstlmaefsklcsQLEQLELENRQLKEGVPGAAGAHVDGELLRLQAENTALQKNMAALQERYG----KEAVRPSA 163
Cdd:PRK03918 360 RHELYE------------EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGelkkEIKELKKA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 164 VGEgqgdppgdvLPTPLAPMPLAEVELKwemEREEKKLLWEQLQGLELSEKLKKKQESFCRlqteketlfnDSRNKIEEL 243
Cdd:PRK03918 428 IEE---------LKKAKGKCPVCGRELT---EEHRKELLEEYTAELKRIEKELKEIEEKER----------KLRKELREL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 244 qqRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLA 323
Cdd:PRK03918 486 --EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 324 ALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEsLRANSRLLEQLQEigqEKEQLTQDLQEAR 403
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKE-LEREEKELKKLEE---ELDKAFEELAETE 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 404 KSAEKRKVMLDELAMETLQEKSQHKEELgavRLRHEKELLGVRARYErELRELHEDKKRQEEELRGQIREEKARTRELEN 483
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEEYEELREE---YLELSRELAGLRAELE-ELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
490
....*....|
gi 1907204915 484 LQHTVEELQA 493
Cdd:PRK03918 716 LEKALERVEE 725
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
185-620 |
6.12e-04 |
|
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: 43.80 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 185 LAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRlQTEKETLFNDSRNKIEELQQRKEADLKAQLA-RTQKLQQ 263
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRAR-KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRsRAKLLMK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 264 ELEAANQSlAELRDQRQGERLEHAaalralQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQT 343
Cdd:TIGR00618 330 RAAHVKQQ-SSIEEQRRLLQTLHS------QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 344 SELASE---LQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMET 420
Cdd:TIGR00618 403 DILQREqatIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 421 LQEKSQHKEElGAVRLRHEKEllgvraRYERELRELHEDKKRQeeelrgQIREEKARTRELENLQHTVEELQAQVHSMDG 500
Cdd:TIGR00618 483 LQETRKKAVV-LARLLELQEE------PCPLCGSCIHPNPARQ------DIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 501 aKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQ 580
Cdd:TIGR00618 550 -QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907204915 581 RILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSK 620
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR 668
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
211-327 |
6.83e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 211 LSEKLKKKQESFCRLQTEKETL---FNDSRNKIEELQQRKeADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHA 287
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELadlLSLERQGNQDLQDSV-ANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907204915 288 AALRAlQDQVSSQsadAQEQVEGLLAENSALRTSLAALEQ 327
Cdd:PRK09039 123 QELDS-EKQVSAR---ALAQVELLNQQIAALRRQLAALEA 158
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
337-627 |
8.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 337 NMLRE-QTSELASELQhrqAEYEELMGQKDDLnsqlqESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDE 415
Cdd:COG4913 216 YMLEEpDTFEAADALV---EHFDDLERAHEAL-----EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 416 LAMETLQEKSQhkeelgavRLRHEKELLGVRaryERELRELHEDKKRQEEELRGQIREEKarTRELENLQHTVEELQAQV 495
Cdd:COG4913 288 RRLELLEAELE--------ELRAELARLEAE---LERLEARLDALREELDELEAQIRGNG--GDRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 496 hsmdgakgwfERRLKEaeeslqqqqqeqeetlklcREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKD 575
Cdd:COG4913 355 ----------EERERR-------------------RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907204915 576 TVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEE 627
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDE 457
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-411 |
8.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 210 ELSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRqGERLEHAAA 289
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDAL-QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-GERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 290 LRALQDQVSS--QSADAQEQVEGLLAENSALRTSLAALEQIQTAKtQELNMLREQTSELASELQHRQAEYEElmgQKDDL 367
Cdd:COG3883 98 SGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEA---AKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907204915 368 NSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKV 411
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
241-474 |
1.02e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 241 EELQQRKEaDLKAQLARTQKLQQELEAANQSLAEL--------RDQRQGERLEHA------------AALRALQDQVSSQ 300
Cdd:COG3096 889 ETLADRLE-ELREELDAAQEAQAFIQQHGKALAQLeplvavlqSDPEQFEQLQADylqakeqqrrlkQQIFALSEVVQRR 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 301 SADAQEQVEGLLAENSALRTSL-AALEQIQTAKTQELNMLREQTSELASELQHRQAeyeelmgqkddlnsqLQESLRANS 379
Cdd:COG3096 968 PHFSYEDAVGLLGENSDLNEKLrARLEQAEEARREAREQLRQAQAQYSQYNQVLAS---------------LKSSRDAKQ 1032
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 380 rllEQLQEIGQEKEQL-TQDLQEARKSAEKRKVMLDELAMETLQEKSQhkeelgavrlrhekeLLGVRARYERELRELHE 458
Cdd:COG3096 1033 ---QTLQELEQELEELgVQADAEAEERARIRRDELHEELSQNRSRRSQ---------------LEKQLTRCEAEMDSLQK 1094
|
250
....*....|....*.
gi 1907204915 459 DKKRQEEELRgQIREE 474
Cdd:COG3096 1095 RLRKAERDYK-QEREQ 1109
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
186-610 |
1.03e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 186 AEVELKWEMEREEKKLLWEQLQG--------------------LELSEKLKKKQESFCRLQTEKETLFNDSRNKIEEL-- 243
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNniekmilafeelrvqaenarLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLli 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 244 ----QQRKEADLKAQLARTQ----KLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSAdaqeqveglLAEN 315
Cdd:pfam05483 248 qiteKENKMKDLTFLLEESRdkanQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA---------LEED 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 316 SALRT-SLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKddlnsqlQESLRANSrllEQLQEIGQEKEQ 394
Cdd:pfam05483 319 LQIATkTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTE-------QQRLEKNE---DQLKIITMELQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 395 LTQDLQEARKSAEKRKVMLDELAM-----ETLQEKSQHKEELGAVRLRHEKELLGVRARYERELREL----------HED 459
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKilaedEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLeiqltaiktsEEH 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 460 KKRQEEELRGQIREEKARTRELENlqhTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELK 539
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKNIELTA---HCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907204915 540 GKDeELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQE 610
Cdd:pfam05483 546 LRD-ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
264-715 |
1.08e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 264 ELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgllaENSALRTSLAALEQIQTAKTQELNMLREQT 343
Cdd:pfam05557 31 ELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAE----LNRLKKKYLEALNKKLNEKESQLADAREVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 344 SELASELQHRQaeyEELMGQKDDLNSQLQESLRANSRLlEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMEtLQE 423
Cdd:pfam05557 107 SCLKNELSELR---RQIQRAELELQSTNSELEELQERL-DLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFE-IQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 424 KSQHKEELGAVRLRhekelLGVRARYERELRELHEDKKRqeeelrgqireekartreLENLQHTVEELQAQVHSMdgakg 503
Cdd:pfam05557 182 QEQDSEIVKNSKSE-----LARIPELEKELERLREHNKH------------------LNENIENKLLLKEEVEDL----- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 504 wfERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEEL-----QNVREQLQQAQEERDGHVKTISNLKQEVKDTVD 578
Cdd:pfam05557 234 --KRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 579 GQRILEKKGSAVLKDLKrQLHLERKRADKLQERLQ-EILTNSKSRTGLEELVLS---EMN----SPSRTQTGDSSSVSSF 650
Cdd:pfam05557 312 ARRELEQELAQYLKKIE-DLNKKLKRHKALVRRLQrRVLLLTKERDGYRAILESydkELTmsnySPQLLERIEEAEDMTQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 651 SY---------------REILKEKESSAIPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKWMLEEKVKHLEVS 715
Cdd:pfam05557 391 KMqahneemeaqlsvaeEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEME 470
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
3-632 |
1.11e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 3 QALSEEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFsKAQKALSKSK-------KAQEVEVLLSEN 75
Cdd:pfam15921 198 EASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQL-EALKSESQNKielllqqHQDRIEQLISEH 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 76 EM------------------LQAKLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEGVPGAAgAHVDGELLRLQ 137
Cdd:pfam15921 277 EVeitgltekassarsqansIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKI-EELEKQLVLAN 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 138 AENTALQKNmaalQERYGKEAvrpsavgeGQGDppgDVLPTPLAPMPLAEVELkwEMEREEKKLLWEQLQGLELSEKLKK 217
Cdd:pfam15921 356 SELTEARTE----RDQFSQES--------GNLD---DQLQKLLADLHKREKEL--SLEKEQNKRLWDRDTGNSITIDHLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 218 KQESFCRLQTEK-ETLFNDSRNKIEELQQRKEADLKAQ---LARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRAL 293
Cdd:pfam15921 419 RELDDRNMEVQRlEALLKAMKSECQGQMERQMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTV 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 294 QDQVSSQSaDAQEQVEGLLAENSALRTSLaaleqiqTAKTQELNMLREQtselASELQHRQAEYEEL---MGQKDDLNSQ 370
Cdd:pfam15921 499 SDLTASLQ-EKERAIEATNAEITKLRSRV-------DLKLQELQHLKNE----GDHLRNVQTECEALklqMAEKDKVIEI 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 371 LQESLRANSRLLEQ----LQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKE-ELGAVRLrhekellgV 445
Cdd:pfam15921 567 LRQQIENMTQLVGQhgrtAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlELEKVKL--------V 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 446 RARYEReLRELHEDKKRQEEELRgqirEEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEaeeslqqqqqeqee 525
Cdd:pfam15921 639 NAGSER-LRAVKDIKQERDQLLN----EVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKM-------------- 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 526 tlklcreehaaELKGKDEELQNVREQLqQAQEERDGH-VKTISNLKQEV---KDTVDGQRILEKKGSAVLKDLKRQLHLE 601
Cdd:pfam15921 700 -----------QLKSAQSELEQTRNTL-KSMEGSDGHaMKVAMGMQKQItakRGQIDALQSKIQFLEEAMTNANKEKHFL 767
|
650 660 670
....*....|....*....|....*....|.
gi 1907204915 602 RKRADKLQERLQEILTNSKSRTGLEELVLSE 632
Cdd:pfam15921 768 KEEKNKLSQELSTVATEKNKMAGELEVLRSQ 798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7-394 |
1.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 7 EEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLD--KEFSKAQKALSK--------SKKAQEVEVLLSENE 76
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAElperleelEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 77 MLQAKLHSQEEDFR--LQNSTLMAE--FSKLCSQLEQLELENRQLKEGVpgaAGAHVDGELLRLQAENTALQKNMAALQE 152
Cdd:COG4717 167 ELEAELAELQEELEelLEQLSLATEeeLQDLAEELEELQQRLAELEEEL---EEAQEELEELEEELEQLENELEAAALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 153 RYGKEAVRPSAVG-----EGQGDPPGD--------------VLPTPLAPMPLAEVELKWEMEREEKKLLWEQLQGLELSE 213
Cdd:COG4717 244 RLKEARLLLLIAAallalLGLGGSLLSliltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 214 KLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQEL--EAANQSLAELRD--QRQGERLEHAAA 289
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaEAGVEDEEELRAalEQAEEYQELKEE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 290 LRALQDQVSSQSADAQEQVEGLLAENsaLRTSLAALEQIQTAKTQELNMLREQTSELASELQH--RQAEYEELMGQKDDL 367
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEEL 481
|
410 420 430
....*....|....*....|....*....|...
gi 1907204915 368 NSQLQE------SLRANSRLLEQLQEIGQEKEQ 394
Cdd:COG4717 482 KAELRElaeewaALKLALELLEEAREEYREERL 514
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
195-483 |
1.21e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 195 EREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQlartQKLQQELEAANQSLAE 274
Cdd:pfam02463 740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ----EEELRALEEELKEEAE 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 275 LRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREqtsELASELQHRQ 354
Cdd:pfam02463 816 LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ---KLKDELESKE 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 355 AEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAV 434
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL 972
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907204915 435 RLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELEN 483
Cdd:pfam02463 973 GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
185-615 |
1.27e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 185 LAEVELKWEMEREEKKLLWEQLQGLELS------------------EKLKKKQESFCRLQTEKETlFNDSRNKIEELqqr 246
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERieelkkeieeleekvkelKELKEKAEEYIKLSEFYEE-YLDELREIEKR--- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 247 kEADLKAQLARTQKLQQELEAANQSLAELRD-----QRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENsaLRTS 321
Cdd:PRK03918 316 -LSRLEEEINGIEERIKELEEKEERLEELKKklkelEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 322 LAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDD---LNSQLQESLRAN--SRLLEQLQEIGQEKEQLT 396
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvCGRELTEEHRKEllEEYTAELKRIEKELKEIE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 397 QDLQEARKSAEK-RKVMLDELAMETLQEKSQHKEELgavrlrhEKELLGVRARYERELRELHEDKKRQEEELRGQIREEK 475
Cdd:PRK03918 473 EKERKLRKELRElEKVLKKESELIKLKELAEQLKEL-------EEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 476 ARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHaAELKGKDEELQNVREQLQQA 555
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKL 624
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907204915 556 QEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLE--------RKRADKLQERLQEI 615
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLElsrelaglRAELEELEKRREEI 692
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
190-498 |
1.42e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.52 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 190 LKWEMEREEKKLLWEQLQGL-----ELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQE 264
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLhfgykSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 265 LEAANqslaelrdqrqgerlehAAALRALQDQVSSQSADaQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTS 344
Cdd:pfam12128 324 LEALE-----------------DQHGAFLDADIETAAAD-QEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 345 E-----LASELQHRQAEYEELMGQKDDLNSQLQESLRA-NSRLLEQLQEIGQEKEQLTQDLQEArksaekrKVMLDELAM 418
Cdd:pfam12128 386 EqnnrdIAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGEL-------KLRLNQATA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 419 --ETLQEKSQHKEELGAVRLRHEKEllgvRARYERELRELHEDKKRQEEELRgQIREEKARTRELEN-LQHTVEELQAQV 495
Cdd:pfam12128 459 tpELLLQLENFDERIERAREEQEAA----NAEVERLQSELRQARKRRDQASE-ALRQASRRLEERQSaLDELELQLFPQA 533
|
...
gi 1907204915 496 HSM 498
Cdd:pfam12128 534 GTL 536
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
229-597 |
1.45e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 229 KETLFNDSRNKIEELQQR------------------KEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAAL 290
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMmlshegvlqeirsilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 291 RALQDQVSSQSADAQEQVEGLLAENSalrtslAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQ 370
Cdd:pfam15921 241 FPVEDQLEALKSESQNKIELLLQQHQ------DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 371 LQESLRANSRLLEQLQEIGQEKEQLTQDLQEarkSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARyE 450
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRMYEDKIE---ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKR-E 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 451 RELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDG-AKGWFERRLKEAEESLQQQQQEQEETlkl 529
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSeCQGQMERQMAAIQGKNESLEKVSSLT--- 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907204915 530 creehaAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTvdgQRILEKKGSAVLK-----DLKRQ 597
Cdd:pfam15921 468 ------AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK---ERAIEATNAEITKlrsrvDLKLQ 531
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-713 |
1.54e-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: 42.36 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 8 EEFQRMQTQLLELRTnnYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKskKAQEVEVLLSENEMLQAKLHSQEE 87
Cdd:TIGR02169 211 ERYQALLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISE--LEKRLEEIEQLLEELNKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 88 DFRLQNSTLMAEFSKLCSQLE-QLELENRQLKEgvpgaagahVDGELLRLQAENTALQKNMAALQERYGKEAVRPSAVGE 166
Cdd:TIGR02169 287 EEQLRVKEKIGELEAEIASLErSIAEKERELED---------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 167 gQGDPPGDVLPTPLAPmpLAEVELKWEMEREEKKLLWEQLQglELSEKLKKKQESFCRLQTEKETLFNDSRNkIEELQQR 246
Cdd:TIGR02169 358 -EYAELKEELEDLRAE--LEEVDKEFAETRDELKDYREKLE--KLKREINELKRELDRLQEELQRLSEELAD-LNAAIAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 247 KEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAaLRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALE 326
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD-LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 327 QIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQ-------KDDLNSQ-----LQE------------SLRANSRLL 382
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNrlnnvvvEDDAVAKeaielLKRrkagratflplnKMRDERRDL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 383 EQLQEIGQEKEQLtqDLQEARKSAEK--RKVMLDELAMETLQEKSQHKEELGAVRLrhEKELL---GVRARYERELRELH 457
Cdd:TIGR02169 591 SILSEDGVIGFAV--DLVEFDPKYEPafKYVFGDTLVVEDIEAARRLMGKYRMVTL--EGELFeksGAMTGGSRAPRGGI 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 458 EDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLkEAEESLQQQQQEQEETLKLCREEHAAE 537
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-GEIEKEIEQLEQEEEKLKERLEELEED 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 538 LKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDtvdgqrILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILT 617
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 618 NSKSRTGLEELVLSEMNspsrtqtgdsssvSSFSYREILKEKESSAiparslssspqaqpPRPAELSDEEVAELFQRLAE 697
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQ-------------ELQEQRIDLKEQIKSI--------------EKEIENLNGKKEELEEELEE 872
|
730
....*....|....*.
gi 1907204915 698 TQQEKWMLEEKVKHLE 713
Cdd:TIGR02169 873 LEAALRDLESRLGDLK 888
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
188-443 |
1.69e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 188 VELKWEMEREEKKLlwEQLQGLELSEKLKKKQESfcrlqTEKETLFNDSRnKIEELQQRKEADLKAQLARTQKLQQELEA 267
Cdd:COG5022 832 LRETEEVEFSLKAE--VLIQKFGRSLKAKKRFSL-----LKKETIYLQSA-QRVELAERQLQELKIDVKSISSLKLVNLE 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 268 ANQSLAELRDQRQGE-------RLEHAAALRALQD--QVSSQSA---DAQEQVEGLLAENSALRTSlaaleqiqtakTQE 335
Cdd:COG5022 904 LESEIIELKKSLSSDlienlefKTELIARLKKLLNniDLEEGPSieyVKLPELNKLHEVESKLKET-----------SEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 336 LNMLREQTSELASELQHRQaeyEELMGQKDDLNSQL--QESLRANSRLLEQLQEIGQEKEQLTQDLQEARkSAEKRKVML 413
Cdd:COG5022 973 YEDLLKKSTILVREGNKAN---SELKNFKKELAELSkqYGALQESTKQLKELPVEVAELQSASKIISSES-TELSILKPL 1048
|
250 260 270
....*....|....*....|....*....|
gi 1907204915 414 DELAMETLQEKSQHKEELGAVRLRHEKELL 443
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRRENSLL 1078
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
208-305 |
1.99e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 41.63 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 208 GLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQ------QRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQ- 280
Cdd:PRK06975 341 GYALNRKVDRLDQELVQRQQANDAQTAELRVKTEQAQasvhqlDSQFAQLDGKLADAQSAQQALEQQYQDLSRNRDDWMi 420
|
90 100 110
....*....|....*....|....*....|...
gi 1907204915 281 ---GERLEHAAALRALQDQVSS-----QSADAQ 305
Cdd:PRK06975 421 aevEQMLSSASQQLQLTGNVQLalialQNADAR 453
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
245-508 |
2.18e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.21 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 245 QRKEADLKAQLARTQKLQQELEAANQSLA-ELRDQRqgerlehaAALRALQDQVssqsADAQEQVEGLLAENSALRTSLA 323
Cdd:pfam19220 82 EGELEELVARLAKLEAALREAEAAKEELRiELRDKT--------AQAEALERQL----AAETEQNRALEEENKALREEAQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 324 ALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEslraNSRLLEQLQEIGQEKEQLTQDLQEAR 403
Cdd:pfam19220 150 AAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAE----LETQLDATRARLRALEGQLAAEQAER 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 404 KSAEKRKvmldELAMETLQ-EKSQHKEELGAVRLRH---EKELLGVRARyereLRELHEDKKRQEEELRGQIREEKARTR 479
Cdd:pfam19220 226 ERAEAQL----EEAVEAHRaERASLRMKLEALTARAaatEQLLAEARNQ----LRDRDEAIRAAERRLKEASIERDTLER 297
|
250 260
....*....|....*....|....*....
gi 1907204915 480 ELENLQHTVEELQAQVHSMDGAKGWFERR 508
Cdd:pfam19220 298 RLAGLEADLERRTQQFQEMQRARAELEER 326
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
228-510 |
2.60e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 228 EKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQgerlehaaALRALQDQVSSQSADAQEQ 307
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE--------QLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 308 VEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQE 387
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 388 IGQEKEQLTQDLQ-----EARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKR 462
Cdd:COG4372 162 LQEELAALEQELQalseaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907204915 463 QEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLK 510
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
198-615 |
3.07e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 198 EKKLLWEQLQGLELSEKLKKKQESFcrlqTEKETLFNDSRNKIEELQQRKEaDLKAQLartQKLQQELEAANQSLAELRD 277
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEI----NEKTTEISNTQTQLNQLKDEQN-KIKKQL---SEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 278 QRQgerlEHAAALRALQDQ--------VSSQSADAQEQVEGL---LAEN----SALRTSLAALEQIQTAKTQELNMLREQ 342
Cdd:TIGR04523 289 QLN----QLKSEISDLNNQkeqdwnkeLKSELKNQEKKLEEIqnqISQNnkiiSQLNEQISQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 343 TSELASELQHRQAEYEE-------LMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDE 415
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSykqeiknLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 416 LAMETLQEKSQHKeELGAVRLRHEKELlgvrARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 495
Cdd:TIGR04523 445 LTNQDSVKELIIK-NLDNTRESLETQL----KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 496 HSMdgakgwferrlkeaeeslqqqqQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQ--EERDGHVKTISNLKQEV 573
Cdd:TIGR04523 520 SSL----------------------KEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQ 577
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1907204915 574 KDTVDGQRILE---KKGSAVLKDLKRQLHLERKRADKLQERLQEI 615
Cdd:TIGR04523 578 KSLKKKQEEKQeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
236-415 |
3.24e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 236 SRNKIEELQQRKEADLKAQLARTQKLQQEL------------EAANQSLAELRDQRQGERLEHAAA---LRALQDQVSSQ 300
Cdd:PRK11448 51 ALLGIYEPPCENQHDLLRRLGKEGFLPDEIldvfhklrkignKAVHEFHGDHREALMGLKLAFRLAvwfHRTYGKDWDFK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 301 SADAQEQVEgllaensalrtSLAALEQIQtaktQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSR 380
Cdd:PRK11448 131 PGPFVPPED-----------PENLLHALQ----QEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQE 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907204915 381 LLEQLQEIGQEKEQLTQDLQEARKSAEKR---KVMLDE 415
Cdd:PRK11448 196 LEAQLEQLQEKAAETSQERKQKRKEITDQaakRLELSE 233
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
262-399 |
3.41e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 262 QQELEAANQSLAELRDQRQGERlehaaalralqdqvsSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLRE 341
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLER---------------QGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907204915 342 QTSELASELQHRQAEYEELMGQKDDLNSQ---LQESLRANSRLLEQLQEIGQEKEQLTQDL 399
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQiaaLRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-485 |
4.11e-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: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 294 QDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQE 373
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 374 SLRANSRL---------------LEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDelamETLQEKSQHKEELGAVRlrh 438
Cdd:COG3883 98 SGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELE----AKLAELEALKAELEAAK--- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907204915 439 eKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQ 485
Cdd:COG3883 171 -AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
193-407 |
4.88e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 193 EMEREEKKllwEQL-QGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQS 271
Cdd:pfam17380 384 QMERQQKN---ERVrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQ 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 272 LAELRDQRQGERLEHAAALralqDQVSSQSADAQEQVEGLLAENSALRTSlAALEQIQTAKTQELNMLREQTSeLASELQ 351
Cdd:pfam17380 461 QVERLRQQEEERKRKKLEL----EKEKRDRKRAEEQRRKILEKELEERKQ-AMIEEERKRKLLEKEMEERQKA-IYEEER 534
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907204915 352 HRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAE 407
Cdd:pfam17380 535 RREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
185-384 |
5.10e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 185 LAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKetlfNDSRNKIEELQQRKEADLKA-----QLARTQ 259
Cdd:COG3206 191 LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL----AEAEARLAALRAQLGSGPDAlpellQSPVIQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 260 KLQQELEAANQSLAELRdQRQGE--------RLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQiqta 331
Cdd:COG3206 267 QLRAQLAELEAELAELS-ARYTPnhpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA---- 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907204915 332 KTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLrANSRLLEQ 384
Cdd:COG3206 342 RLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV-GNVRVIDP 393
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-606 |
5.36e-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: 40.44 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 7 EEEFQRMQTQLLELRTNNYQLSDELRKNGVELSSLRQKVAYLDKEFSKAQKALSKSKKA-----QEVEVLLSENEMLQA- 80
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKleklkREINELKRELDRLQEe 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 81 --KLHSQEEDFRLQNSTLMAEFSKLCSQLEQLELENRQLKEGVPGAAG--AHVDGELLRLQAENTALQKNMAALQERYGK 156
Cdd:TIGR02169 415 lqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 157 EAVRPSAVGEGQGD--PPGDVLPTPLAPM-----PLAEVELKW--------------------EMEREEKKLLWEQLQGL 209
Cdd:TIGR02169 495 AEAQARASEERVRGgrAVEEVLKASIQGVhgtvaQLGSVGERYataievaagnrlnnvvveddAVAKEAIELLKRRKAGR 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 210 ELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQkLQQELEAANQSLAELR-DQRQGERLE--- 285
Cdd:TIGR02169 575 ATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTL-VVEDIEAARRLMGKYRmVTLEGELFEksg 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 286 -----HAAALRALQDQVS--SQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYE 358
Cdd:TIGR02169 654 amtggSRAPRGGILFSRSepAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 359 ELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmlDELAMETLQEKSQHKEELGAVRLRH 438
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRI 810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 439 EKELLGVRARYERE--LRELHEDKKRQEEELRGQIREEKA-RTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEaees 515
Cdd:TIGR02169 811 EARLREIEQKLNRLtlEKEYLEKEIQELQEQRIDLKEQIKsIEKEIENLNGKKEELEEELEELEAALRDLESRLGD---- 886
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 516 lqqqqqeqeetLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLK 595
Cdd:TIGR02169 887 -----------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED 955
|
650
....*....|.
gi 1907204915 596 RQLHLERKRAD 606
Cdd:TIGR02169 956 VQAELQRVEEE 966
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
291-559 |
5.55e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 291 RALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASElQHRQAEYEELMGQKDDLNSQ 370
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 371 LQESLR---ANSRLLEQLQ-EIGQEKEQLTQDLQEARK-----SAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKE 441
Cdd:pfam17380 366 RQEEIAmeiSRMRELERLQmERQQKNERVRQELEAARKvkileEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 442 LLGVRARYERELRELHEDKKRQEEELR----GQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQ 517
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERkrkkLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER 525
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907204915 518 QQQQEQEETLKLCREEHAAELKGkdEELQNVREQLQQAQEER 559
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEM--EERRRIQEQMRKATEER 565
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
187-431 |
5.57e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 187 EVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELE 266
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 267 AANQSLAELRDQrqgerLEHAAALRALQDQVSSQSADAQEQVEGllaENSALRTSLAALEQIQTAKTQELNMLREQTSEL 346
Cdd:TIGR00618 698 MLAQCQTLLREL-----ETHIEEYDREFNEIENASSSLGSDLAA---REDALNQSLKELMHQARTVLKARTEAHFNNNEE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 347 ASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQ--------LQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAM 418
Cdd:TIGR00618 770 VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEigqeipsdEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH 849
|
250
....*....|....*
gi 1907204915 419 ETLQ--EKSQHKEEL 431
Cdd:TIGR00618 850 QLLKyeECSKQLAQL 864
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
210-394 |
6.72e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 210 ELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQqrkeadlkaqlARTQKLQQELEAANQSLAELRDQRQGERLEHAAA 289
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME-----------TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 290 LRAlqdqvssqSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNS 369
Cdd:pfam15921 726 MKV--------AMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
170 180 190
....*....|....*....|....*....|....*
gi 1907204915 370 Q----------LQESLRANSRLLEQLQEIGQEKEQ 394
Cdd:pfam15921 798 QerrlkekvanMEVALDKASLQFAECQDIIQRQEQ 832
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
233-388 |
7.62e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 233 FNDSRNKIEELQQRKEADLKAQLARTQKLQ-QELEAAnqsLAELRDQRQGERLEHAAALRALQDQVSSQS----ADAQEQ 307
Cdd:COG2433 345 YDAYKNKFERVEKKVPPDVDRDEVKARVIRgLSIEEA---LEELIEKELPEEEPEAEREKEHEERELTEEeeeiRRLEEQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 308 VEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELA---SELQHRQAEYEELmgqKDDLNsQLQESLRANSRLLEQ 384
Cdd:COG2433 422 VERLEAEVEELEAELEEKDERIERLERELSEARSEERREIrkdREISRLDREIERL---ERELE-EERERIEELKRKLER 497
|
....
gi 1907204915 385 LQEI 388
Cdd:COG2433 498 LKEL 501
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
238-489 |
8.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 238 NKIEELQQRKE--ADLKAQLA-RTQKLQQELEAANQ----------------SLAELRDQRQgERLEHAAALRALQDQVS 298
Cdd:PRK04863 786 KRIEQLRAEREelAERYATLSfDVQKLQRLHQAFSRfigshlavafeadpeaELRQLNRRRV-ELERALADHESQEQQQR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 299 SQSADAQEQVEGL---------LAENS------ALRTSLAALEQIQ----------TAKTQELNMLREQTSELAS-ELQH 352
Cdd:PRK04863 865 SQLEQAKEGLSALnrllprlnlLADETladrveEIREQLDEAEEAKrfvqqhgnalAQLEPIVSVLQSDPEQFEQlKQDY 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 353 RQAE------------------------YEE---LMGQKDDLNSQLQESLR----ANSRLLEQLQEIGQEKEQLTQDLQE 401
Cdd:PRK04863 945 QQAQqtqrdakqqafaltevvqrrahfsYEDaaeMLAKNSDLNEKLRQRLEqaeqERTRAREQLRQAQAQLAQYNQVLAS 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 402 ARKSAEKRKVMLDELAMEtLQEKSQHKEELGAVRLRHEKELLGVRARYERELR-ELHEDKKRQEEELRGQIREEKARTRE 480
Cdd:PRK04863 1025 LKSSYDAKRQMLQELKQE-LQDLGVPADSGAEERARARRDELHARLSANRSRRnQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
....*....
gi 1907204915 481 LENLQHTVE 489
Cdd:PRK04863 1104 YHEMREQVV 1112
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
209-510 |
8.31e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 209 LELSEKLKKKQESFCRLQTEKEtlfnDSRNKIEELQQRKEaDLKAQLArtqKLQQELEAA-------NQSLAELRDQRQg 281
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQE----ENEARAEAAEEEVD-ELKSQLA---DYQQALDVQqtraiqyQQAVQALERAKQ- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 282 erLEHAAALRA--LQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIqtAKTQEL------NMLREQTSELASELQHR 353
Cdd:PRK04863 429 --LCGLPDLTAdnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF--EQAYQLvrkiagEVSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 354 QAEYEELMGQKDDLNSQLQE---SLRANSRLLEQLQEIGQ----------EKEQLTQDLQEARKSAEKRKVMLDELAMET 420
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSEleqRLRQQQRAERLLAEFCKrlgknlddedELEQLQEELEARLESLSESVSEARERRMAL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907204915 421 LQEKSQHKEELGAVRLRhEKELLGVRARYEReLRELH----EDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVH 496
Cdd:PRK04863 585 RQQLEQLQARIQRLAAR-APAWLAAQDALAR-LREQSgeefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
330
....*....|....
gi 1907204915 497 SMDGAKGWFERRLK 510
Cdd:PRK04863 663 RLSQPGGSEDPRLN 676
|
|
| |
