|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
211-588 |
9.01e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 211 IEELQQRKEAdLKAQlART----QKLQQELEAANQSLAELRDQRQGERLEHAAAlralqdqvssQSADAQEQVEGLLAEN 286
Cdd:COG1196 195 LGELERQLEP-LERQ-AEKaeryRELKEELKELEAELLLLKLRELEAELEELEA----------ELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 287 SALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQL 366
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 367 TQDLQEARKSAEKRKVMLDELAmETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEK 446
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAE-EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 447 ARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLcrEEHAAELKGKDEELQNVREQLQQA 526
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL--EAALAELLEELAEAAARLLLLLEA 499
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720435465 527 QEERDGHVKTISNLKQevkdtVDGQRILEKKGSAVLKDLKRqlhLERKRADKLQERLQEILT 588
Cdd:COG1196 500 EADYEGFLEGVKAALL-----LAGLRGLAGAVAVLIGVEAA---YEAALEAALAAALQNIVV 553
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
167-475 |
1.07e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 167 REEKKLLWEQLQGLELSEKLKKKQEsfcrlQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAEL 246
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEE-----LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 247 RDQRqgERLEHA-AALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQ 325
Cdd:COG1196 294 LAEL--ARLEQDiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 326 AEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAv 405
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE- 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 406 RLRHEKELLGVRARyERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGW 475
Cdd:COG1196 451 EAELEEEEEALLEL-LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-588 |
2.32e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 187 KKKQESFCRLQTEKETL--FNDSRNKIEElqQRKEADLKAQLA-RTQKLQQELEAANQSLAELRDQRQGERLEhaaALRA 263
Cdd:TIGR02168 172 ERRKETERKLERTRENLdrLEDILNELER--QLKSLERQAEKAeRYKELKAELRELELALLVLRLEELREELE---ELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 264 LQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQ 343
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 344 ESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmldelamETLQEKSQHKEELgavrlrhEKELLGVRARYere 423
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------AELEELESRLEEL-------EEQLETLRSKV--- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 424 lrelhEDKKRQEEELRGQIREEKARtreLENLQHTVEELQAQVhsmdgakgwfERRLKEAEESLQQQQQEQEETLKLCRE 503
Cdd:TIGR02168 389 -----AQLELQIASLNNEIERLEAR---LERLEDRRERLQQEI----------EELLKKLEEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 504 EHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVlkdlkRQLHLERKRADKLQERL 583
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV-----KALLKNQSGLSGILGVL 525
|
....*
gi 1720435465 584 QEILT 588
Cdd:TIGR02168 526 SELIS 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
164-603 |
3.84e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 164 EMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQ------QRKEADLKAQLARTQKLQQEL- 236
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRReleerlEELEEELAELEEELEELEEELe 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 237 EAANQS------LAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgLLAENSALRTSLAALEQIQTAKTQELNML 310
Cdd:COG1196 341 ELEEELeeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-ALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 311 REQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLD-ELAM 389
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLlLLEA 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 390 ETLQE------KSQHKEELGAVRLRHEKELLGVRARYEREL------------RELHEDKKRQEEELRGQ-------IRE 444
Cdd:COG1196 500 EADYEgflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaalqnivVEDDEVAAAAIEYLKAAkagratfLPL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 445 EKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEtlKLCREEHAAELKGKDEELQNVREQLQ 524
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR--LEAALRRAVTLAGRLREVTLEGEGGS 657
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720435465 525 QAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVLSE 603
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
159-466 |
6.63e-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: 69.70 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 159 VELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEaDLKAQLARTQKLQQELEA 238
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRK-DLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 239 ANQSLAELRDQRQGERLEHAAALRALQdQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTA-------KTQELNMLR 311
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 312 EQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDEL---A 388
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELeskR 910
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435465 389 METLQEKSQHKEELGAVRLRHEKeLLGVRARYERELRELHEDkkrqeeELRGQIREEKARTRELENLQHTVEELQAQV 466
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
224-473 |
2.48e-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: 63.24 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 224 AQLARTQKLQQELEAANQSLAELRDQRQgerlehaaalralqdQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAK 303
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA---------------ALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 304 TQELNMLREQTSELASELQHRQAEYEEL------MGQKDDLNSQL-QESLRANSRLLEQLQEIGQEKEQLTQDLQEARKS 376
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELlralyrLGRQPPLALLLsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 377 AEKRKvmldelamETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQ 456
Cdd:COG4942 162 LAALR--------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|....*..
gi 1720435465 457 HTVEELQAQVHSMDGAK 473
Cdd:COG4942 234 AEAAAAAERTPAAGFAA 250
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
162-451 |
8.04e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 162 KWEMEREEK---KLLWEQLQGLELSEKLKKKQEsfcrLQTEKETLFNDSRNKIEELQQRKEadlkaqlaRTQKLQQELEA 238
Cdd:TIGR02169 202 RLRREREKAeryQALLKEKREYEGYELLKEKEA----LERQKEAIERQLASLEEELEKLTE--------EISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 239 ANQSLAEL----RDQRQGERLEHAAALRALQDQVSS-----------------QSADAQEQVEGLLAENSALRTSL---- 293
Cdd:TIGR02169 270 IEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASlersiaekereledaeeRLAKLEAEIDKLLAEIEELEREIeeer 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 294 ---AALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDL 370
Cdd:TIGR02169 350 krrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 371 QEARKSAEKRKVMLDELAMEtLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEdKKRQEEELRGQIREEKARTR 450
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALE-IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-LQRELAEAEAQARASEERVR 507
|
.
gi 1720435465 451 E 451
Cdd:TIGR02169 508 G 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
168-703 |
1.31e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 168 EEKKLLWEQLQGLELSEKLKKKQEsfcrLQTEKETLFNDSRNKIEELQQRKEADLKAQLAR-TQKLQQELEAANQSLAEL 246
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADE----LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkADEAKKKAEEAKKKADAA 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 247 RDQRQgERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQI--QTAKTQELNMLREQTSELASELQHR 324
Cdd:PTZ00121 1335 KKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKaeEKKKADEAKKKAEEDKKKADELKKA 1413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 325 QAEYE---------ELMGQKDDLNSQLQESLRANSrlLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEK 395
Cdd:PTZ00121 1414 AAAKKkadeakkkaEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 396 SQH-KEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIR--EEKARTRELENlqhtVEELQA--QVHSMD 470
Cdd:PTZ00121 1492 AEEaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEEKKKADELKK----AEELKKaeEKKKAE 1567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 471 GAKGWFERR---LKEAEESLQQQQQEQEETLKLCREEHA--AELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVK 545
Cdd:PTZ00121 1568 EAKKAEEDKnmaLRKAEEAKKAEEARIEEVMKLYEEEKKmkAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 546 DTvDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEiltnskSRTGLEELVLSEMNSPSRTQTGDSSSVSSFSYRE 625
Cdd:PTZ00121 1648 KA-EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720435465 626 ILKEKESSAIPARSLSSSPQAQPPRPAELS-DEEVAELFQRLAETQQEKWMLEEKVKHLEVSSASMAEDLCRKSAIIET 703
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-592 |
7.18e-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: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 53 ELSSLRQKVAYLDKEFSKAQKLC-----------SQLEQLELENRQLKEGVpgaagAHVDGELLRLQAENTALQKNMAAL 121
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELeeltaelqeleEKLEELRLEVSELEEEI-----EELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 122 QERYgKEAVRPSAVGEGQgdppgdvlptplapmpLAEVELKWEMEREEKKLLWEQLQGL-ELSEKLKKKQESFCRLQTEK 200
Cdd:TIGR02168 308 RERL-ANLERQLEELEAQ----------------LEELESKLDELAEELAELEEKLEELkEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 201 ETLFNDSRNKIEELQqRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQ-DQVSSQSADAQEQV 279
Cdd:TIGR02168 371 ESRLEELEEQLETLR-SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEEL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 280 EGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRAN---SRLLEQ- 355
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilGVLSELi 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 356 -----------------LQEIGQEKEQLTQDLQEARKSAEKRKVML--------DELAMETLQEKSQHKEELG------- 403
Cdd:TIGR02168 530 svdegyeaaieaalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFlpldsikgTEIQGNDREILKNIEGFLGvakdlvk 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 404 ------------------------AVRLRHEKELLG---------VRARY----------------ERELRELHEDKKRQ 434
Cdd:TIGR02168 610 fdpklrkalsyllggvlvvddldnALELAKKLRPGYrivtldgdlVRPGGvitggsaktnssilerRREIEELEEKIEEL 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 435 EEELRgqireekARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEEtlklcREEHAAELKGKDE 514
Cdd:TIGR02168 690 EEKIA-------ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-----LEERIAQLSKELT 757
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720435465 515 ELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKS 592
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
181-380 |
8.70e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 181 ELSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAA 260
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKAL-LKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 261 LRALQDQ---------VSSQSA-DAQEQVEGLLAENSALRTSLAALEQIQT---AKTQELNMLREQTSELASELQHRQAE 327
Cdd:COG4942 110 LRALYRLgrqpplallLSPEDFlDAVRRLQYLKYLAPARREQAEELRADLAelaALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720435465 328 YEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKR 380
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
209-451 |
1.21e-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: 57.85 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 209 NKIEELQQRKEAdlkaqlartqkLQQELEAANQSLAELRDQRQgerlEHAAALRALQDQVssqsADAQEQVEGLLAENSA 288
Cdd:COG4942 20 DAAAEAEAELEQ-----------LQQEIAELEKELAALKKEEK----ALLKQLAALERRI----AALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 289 LRTSLAALEQIQTAKTQELNMLREQTSELASELQ-HRQAEYEELMGQKDDLNsQLQESLRANSRLLEQLQEIGQEKEQLT 367
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYrLGRQPPLALLLSPEDFL-DAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 368 QDLQEARKSAEKRKVMLDELametLQEKSQHKEELGAVRLRHEKELLGVRAR---YERELRELHEDKKRQEEELRGQIRE 444
Cdd:COG4942 160 AELAALRAELEAERAELEAL----LAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAE 235
|
....*..
gi 1720435465 445 EKARTRE 451
Cdd:COG4942 236 AAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
219-470 |
2.85e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 219 EADLKAQLARTQKLQQELEAANQSLAELRDQRqgERLEHAAALralqdqvssqsADAQEQVEGLLAENSALRTSLAALEQ 298
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQI--ELLEPIREL-----------AERYAAARERLAELEYLRAALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 299 iqtakTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEslransrLLEQLQEI-GQEKEQLTQDLQEARKSA 377
Cdd:COG4913 287 -----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDE-------LEAQIRGNgGDRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 378 EKRKVMLDELAmetlqeksQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQH 457
Cdd:COG4913 355 EERERRRARLE--------ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
250
....*....|...
gi 1720435465 458 TVEELQAQVHSMD 470
Cdd:COG4913 427 EIASLERRKSNIP 439
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
181-588 |
4.05e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 181 ELSEKLKKKQESFCRLQTEKETL---FNDSRNKIEELQQRKE----------ADLKAQLARTQKLQQELEAANQSLAELR 247
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELaeeVRDLRERLEELEEERDdllaeaglddADAEAVEARREELEDRDEELRDRLEECR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 248 dQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAE 327
Cdd:PRK02224 335 -VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 328 YEELMGQKDDLNSQLQEsLRANSRLLEQLQEIGQEkeqltqdLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRL 407
Cdd:PRK02224 414 LEELREERDELREREAE-LEATLRTARERVEEAEA-------LLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 408 RHEKELLGVRARYER--ELRELH------EDKKRQEEELRGQIREEKARTRE-LENLQHTVEELQAQvhsmdgAKGWFER 478
Cdd:PRK02224 486 DLEEEVEEVEERLERaeDLVEAEdrierlEERREDLEELIAERRETIEEKRErAEELRERAAELEAE------AEEKREA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 479 RLKEAEESLQQQQQ-----EQEETLKLCRE---------EHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEV 544
Cdd:PRK02224 560 AAEAEEEAEEAREEvaelnSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAELNDERRERLAEKRERKREL 639
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1720435465 545 KDTVDGQRILEKKGsavlkdlkrqlhlERKRADKLQERLQEILT 588
Cdd:PRK02224 640 EAEFDEARIEEARE-------------DKERAEEYLEQVEEKLD 670
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
160-459 |
7.81e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 160 ELKWEMEREEKKLLWEQLQGLELSEKLKKKQEsfcrlqteketLFNDSRNKIEELQQRKEAD---LKAQLARTQKLQQEL 236
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-----------RLEELEEDLSSLEQEIENVkseLKELEARIEELEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 237 EAANQSLAELRDQRQGERLEH-AAALRALQDQVSSQSADAQE---QVEGLLAENSALRTSLAALEQIQTAKTQELNMLRE 312
Cdd:TIGR02169 775 HKLEEALNDLEARLSHSRIPEiQAELSKLEEEVSRIEARLREieqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 313 QTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVM-------LD 385
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKlealeeeLS 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 386 ELAMETLQEKSQHKEELGAVRLRHEKELLGVRAR------------YERELRELHEDKKRQE--EELRGQIREekaRTRE 451
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalepvnmlaiqeYEEVLKRLDELKEKRAklEEERKAILE---RIEE 1011
|
....*...
gi 1720435465 452 LENLQHTV 459
Cdd:TIGR02169 1012 YEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-461 |
8.47e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 216 QRKEADLKAQLARtqkLQQELEAANQSLAELRDQRQgERLEHAAALRALQDQVSSQ--SADAQEQVEGLLAENSALRTSL 293
Cdd:COG4913 609 RAKLAALEAELAE---LEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWDEidVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 294 AALEQiqtaktqelnmLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEA 373
Cdd:COG4913 685 DDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 374 RKSAEKRKVMLDELAMETLQEKSQHKEELGavrlRHEKELLGVRAR---------------------YERELRELHEDK- 431
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRARLN----RAEEELERAMRAfnrewpaetadldadleslpeYLALLDRLEEDGl 829
|
250 260 270
....*....|....*....|....*....|
gi 1720435465 432 KRQEEELRGQIREEKarTRELENLQHTVEE 461
Cdd:COG4913 830 PEYEERFKELLNENS--IEFVADLLSKLRR 857
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-566 |
9.76e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 183 SEKLKKKQESfCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQS--------LAELRDQRQGER 254
Cdd:PTZ00121 1472 ADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeakkadeAKKAEEKKKADE 1550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 255 LEHAAALRALQDQVSSQSADAQEQvegllAENSALRTSlAALEQIQTAKTQELNMLREQTSELASElQHRQAEYEELMGQ 334
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEE-----DKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAE 1623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 335 K-------DDLNSQLQESLRANSRLLEQLQEigQEKEQLTQDLQEARKSAEKRKvmldelAMETLQEKSQHKEELGAVRL 407
Cdd:PTZ00121 1624 ElkkaeeeKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAEEAKKAEEDKK------KAEEAKKAEEDEKKAAEALK 1695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 408 RHEKEllgvrARYERELRELHEDKKRQEEELRgqiREEKARTRELENLQHTVEElqaqvhsmdgakgwfERRlKEAEESL 487
Cdd:PTZ00121 1696 KEAEE-----AKKAEELKKKEAEEKKKAEELK---KAEEENKIKAEEAKKEAEE---------------DKK-KAEEAKK 1751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 488 QQQQQEQEETLKLCREEHAAELKGKDEELqnVREQLQQAQEERDGHV-KTISNLKQEVKDTVDGQrileKKGSAVLKDLK 566
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVdKKIKDIFDNFANIIEGG----KEGNLVINDSK 1825
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
164-468 |
1.06e-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: 55.75 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 164 EMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSL 243
Cdd:pfam02463 194 ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 244 AELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQH 323
Cdd:pfam02463 274 NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 324 RQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELG 403
Cdd:pfam02463 354 EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720435465 404 AVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHS 468
Cdd:pfam02463 434 EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
215-591 |
1.83e-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: 55.06 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 215 QQRKEADLK-----AQLARTQKLQQELEAANQSLaelrdQRQGER----LEHAAALRALQDQVSSQSAD-AQEQVEGLLA 284
Cdd:TIGR02168 172 ERRKETERKlertrENLDRLEDILNELERQLKSL-----ERQAEKaeryKELKAELRELELALLVLRLEeLREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 285 ENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKE 364
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 365 QLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEelgavrlrhekellgvraryereLRELHEDKKRQEEELRGQIRE 444
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEE-----------------------LEAELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 445 EKARTRELENlqhTVEELQAQVHSMDgakgwferrlkeaeES----LQQQQQEQEETLKLCREEHAAELKGKDEELQNVR 520
Cdd:TIGR02168 384 LRSKVAQLEL---QIASLNNEIERLE--------------ARlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435465 521 EQLQQAQEERDGHVKTISNLKQEVkdtvdgqrileKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSK 591
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREEL-----------EEAEQALDAAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
252-592 |
3.73e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 252 GERLEHAAALRALQDQVSSQSAdaQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEEL 331
Cdd:TIGR02169 658 GSRAPRGGILFSRSEPAELQRL--RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 332 MGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmlDELAMETLQEKsqhkeelgavrlrhek 411
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEI---------------- 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 412 ellgvraryERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEaeeslqqqq 491
Cdd:TIGR02169 797 ---------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN--------- 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 492 qeqeetLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVkdtvdgqrilekkgsavlKDLKRQLHL 571
Cdd:TIGR02169 859 ------LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI------------------EELEAQIEK 914
|
330 340
....*....|....*....|.
gi 1720435465 572 ERKRADKLQERLQEILTNSKS 592
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
302-586 |
3.90e-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: 53.91 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 302 AKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEslrANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRK 381
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ---LRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 382 VMLDELAmETLQEKSQHKEELGAVRLrHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEE 461
Cdd:TIGR02168 751 QLSKELT-ELEAEIEELEERLEEAEE-ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 462 LQAQVHSMDGAKGWFERRLKEAEESlqqqqqeqeetlklcREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLK 541
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSED---------------IESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720435465 542 QEVKDTVDGQRILEKKgsavLKDLKRQLHLERKRADKLQERLQEI 586
Cdd:TIGR02168 894 SELEELSEELRELESK----RSELRRELEELREKLAQLELRLEGL 934
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
196-546 |
5.12e-07 |
|
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: 53.58 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 196 LQTEKETLFNDSRNKIEELQQRKEAdlkaqlaRTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADA 275
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQQHQD-------RIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 276 QEQVEGLLAENSALRTSLAALEQIQTAKTQElnmLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLranSRLLEQ 355
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEE---LEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL---ADLHKR 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 356 LQEIGQEKEQ----LTQDLQEARKSAEKRKvMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYE--RELRELHE 429
Cdd:pfam15921 390 EKELSLEKEQnkrlWDRDTGNSITIDHLRR-ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNEslEKVSSLTA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 430 DKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHsmdgakgwfERRLKEAEESLQQQQQEQEETLKLCREEHaaeL 509
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ---------EKERAIEATNAEITKLRSRVDLKLQELQH---L 536
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720435465 510 KGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKD 546
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEN 573
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
195-456 |
5.79e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 195 RLQTEKETLFNDSRNKIEElqqRKEADLKAQLARtqkLQQELEAANQSLAELRDQRqgerlEHAAALRALQDQVSSQSAD 274
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEE---KEEKDLHERLNG---LESELAELDEEIERYEEQR-----EQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 275 AQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAE--------------YEELMGQKDDLNS 340
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglddadaeavearREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 341 QLQ-------------ESLRANSRLLE-QLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELametlqeksqhKEELGAVR 406
Cdd:PRK02224 329 RLEecrvaaqahneeaESLREDADDLEeRAEELREEAAELESELEEAREAVEDRREEIEEL-----------EEEIEELR 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720435465 407 LRHE--KELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQ 456
Cdd:PRK02224 398 ERFGdaPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-349 |
1.27e-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: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 164 EMEREEKKLlwEQLQGL-ELSEKLKKKQESFCRLQTEKETL--FNDSR--NKIEELQQRKEADLKAQLARTQKLQQELEA 238
Cdd:COG4913 243 ALEDAREQI--ELLEPIrELAERYAAARERLAELEYLRAALrlWFAQRrlELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 239 ANQSLAELRDQRQ---GERLEHAAA-LRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQT 314
Cdd:COG4913 321 LREELDELEAQIRgngGDRLEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL 400
|
170 180 190
....*....|....*....|....*....|....*
gi 1720435465 315 SELASELQHRQAEYEELMGQKDDLNSQLqESLRAN 349
Cdd:COG4913 401 EALEEALAEAEAALRDLRRELRELEAEI-ASLERR 434
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-611 |
3.55e-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: 50.84 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 358 EIGQEKEQLTQDLQEARKSAEKRKVMLDELA--METLQEKSQHKEELGAVRLRHEkellgvraryERELRELHEDKKRQE 435
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRqqLERLRREREKAERYQALLKEKR----------EYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 436 EELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEE 515
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 516 LQNVREQLQQAQEERDGHVKTISNLKQEVKDtvdgQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTG 595
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEE----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250
....*....|....*.
gi 1720435465 596 LEELVLSEMNSPSRTQ 611
Cdd:TIGR02169 393 KLEKLKREINELKREL 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
274-454 |
5.28e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 274 DAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEY--EELMGQKDDLNSQLQEsLRANSR 351
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELER-LDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 352 LLEQLQeigqekEQLtQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHE----KELLGVRARYERELREL 427
Cdd:COG4913 686 DLAALE------EQL-EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEaaedLARLELRALLEERFAAA 758
|
170 180
....*....|....*....|....*....
gi 1720435465 428 HEDKKRQE--EELRGQIREEKARTRELEN 454
Cdd:COG4913 759 LGDAVERElrENLEERIDALRARLNRAEE 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
211-412 |
5.72e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 211 IEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQrqgerLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALR 290
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEK-----EEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 291 TSLAALEQIQtaKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEslrANSRLLEQLQEIGQEKEQLTQDL 370
Cdd:COG4717 123 KLLQLLPLYQ--ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE---LQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720435465 371 QEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKE 412
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
181-580 |
6.29e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 181 ELSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQ-----RKEADLKAQLARTQKLQQELEAANQSLAELrDQRQGERL 255
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEL-EELEEELEELEAeleelREELEKLEKLLQLLPLYQELEALEAELAEL-PERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 256 EHAAALRALQDQVSSQSADAQEQVEGLlaENSALRTSLAALEQIQTAKtQELNMLREQTSELASELQHRQAEYEELMGQK 335
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEEL--EELLEQLSLATEEELQDLA-EELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 336 DDLNSQLqESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKV------------------MLDELAMETLQEKSQ 397
Cdd:COG4717 230 EQLENEL-EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflvlgllallflllAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 398 HKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTREL--ENLQHTVEEL--QAQVHSMDGAK 473
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALlaEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 474 GWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKD---EELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDG 550
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
410 420 430
....*....|....*....|....*....|
gi 1720435465 551 QRILEKKgsAVLKDLKRQLHLERKRADKLQ 580
Cdd:COG4717 469 GELAELL--QELEELKAELRELAEEWAALK 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
194-464 |
6.68e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 194 CRLQTEK-ETLFNDSRNKIEELQQRKEA--DLKAQLARTQKLQQELEAANQSLAELRDqRQGERLEHAAALRALQDQVSS 270
Cdd:PRK02224 473 DRERVEElEAELEDLEEEVEEVEERLERaeDLVEAEDRIERLEERREDLEELIAERRE-TIEEKRERAEELRERAAELEA 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 271 QSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLrEQTSELASELQHRQAEYEELMGQKDDLNSQlqeslraNS 350
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAEL-------ND 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 351 RLLEQLQEIGQEKEQLTQDLQEARKSAEKRKvmlDELAMETLQEKSQHKEELGAVRLRHEKELLGVraryERELRELhed 430
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEARIEEARED---KERAEEYLEQVEEKLDELREERDDLQAEIGAV----ENELEEL--- 693
|
250 260 270
....*....|....*....|....*....|....
gi 1720435465 431 kkrqeEELRGQIREEKARTRELENLQHTVEELQA 464
Cdd:PRK02224 694 -----EELRERREALENRVEALEALYDEAEELES 722
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
239-466 |
9.49e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 239 ANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSlaaleqiqtaktQELNMLREQTSELA 318
Cdd:COG3206 158 AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 319 SELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLE--QLQEIGQEKEQLTQDLQEARksaekrkvmldelamETLQEKS 396
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELS---------------ARYTPNH 290
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720435465 397 ----QHKEELGAVRLRHEKELLGVRARYERELRELhedkKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 466
Cdd:COG3206 291 pdviALRAQIAALRAQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
211-379 |
1.02e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 211 IEELQQRKEADLKAQLA----RTQKLQQELEAANQSLAELR--------DQRQGERLEHAAALRALQDQVSSQSADAQ-- 276
Cdd:COG3206 162 LEQNLELRREEARKALEfleeQLPELRKELEEAEAALEEFRqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEar 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 277 -EQVEGLLAENSALRTSLAALEQIQTAKTQeLNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLE- 354
Cdd:COG3206 242 lAALRAQLGSGPDALPELLQSPVIQQLRAQ-LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEa 320
|
170 180
....*....|....*....|....*
gi 1720435465 355 QLQEIGQEKEQLTQDLQEARKSAEK 379
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAE 345
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
206-466 |
1.22e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 206 DSRNKIEELQQRKEA---DLKAQLARTQKLQQELEAANQSLA----ELRDQRQGERLEhaAALRALQDQVSSQ---SADA 275
Cdd:PRK04863 297 TSRRQLAAEQYRLVEmarELAELNEAESDLEQDYQAASDHLNlvqtALRQQEKIERYQ--ADLEELEERLEEQnevVEEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 276 QEQVEGLLAENSA-------LRTSLA----ALEQIQT------------AKTQELNMLREQTSELASELQHR-QAEYEEL 331
Cdd:PRK04863 375 DEQQEENEARAEAaeeevdeLKSQLAdyqqALDVQQTraiqyqqavqalERAKQLCGLPDLTADNAEDWLEEfQAKEQEA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 332 MGQKDDLNSQLQESLRANSR------------------------------------LLEQLQEIGQEKEQLTQDLQEARk 375
Cdd:PRK04863 455 TEELLSLEQKLSVAQAAHSQfeqayqlvrkiagevsrseawdvarellrrlreqrhLAEQLQQLRMRLSELEQRLRQQQ- 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 376 SAEKrkvMLDELAMEtLQEKSQHKEELGAVRLRHEKELLGVRArYERELRELHEDKKRQEEELRGQIREEKARTRELENL 455
Cdd:PRK04863 534 RAER---LLAEFCKR-LGKNLDDEDELEQLQEELEARLESLSE-SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAA 608
|
330
....*....|.
gi 1720435465 456 QHTVEELQAQV 466
Cdd:PRK04863 609 QDALARLREQS 619
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
288-559 |
1.23e-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: 48.22 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 288 ALRTSLAALEQIQTAKtQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLT 367
Cdd:COG4942 11 LALAAAAQADAAAEAE-AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 368 QDLQEARKSAEKRKVMLDELaMETLQEKSQHKEELGAVRLRHEKELLgVRARYereLRELHEDKKRQEEELRGQIREEKA 447
Cdd:COG4942 90 KEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAV-RRLQY---LKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 448 RTRELENLQHTVEELQAQVhsmdgakgwferrlkeaeeslqQQQQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQ 527
Cdd:COG4942 165 LRAELEAERAELEALLAEL----------------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250 260 270
....*....|....*....|....*....|..
gi 1720435465 528 EERDGHVKTISNLKQEVKDTVDGQRILEKKGS 559
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
210-428 |
1.67e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 210 KIEEL-QQRKEADLKA-----QLARTQKLQQELEAAN-QSLAELRDQRQgERLEHAAALRALQDQVSSQSADAQEQVEGL 282
Cdd:PHA02562 175 KIRELnQQIQTLDMKIdhiqqQIKTYNKNIEEQRKKNgENIARKQNKYD-ELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 283 LAENSALRTSLAALE-QIQTAK---------------TQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESL 346
Cdd:PHA02562 254 SAALNKLNTAAAKIKsKIEQFQkvikmyekggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 347 RANSRLLEQLQEIGQEKeqltQDLQEARKSAEKRKVMLDELAMETLqeksQHKEELGAVRlRHEKELLGVRARYERELRE 426
Cdd:PHA02562 334 EQSKKLLELKNKISTNK----QSLITLVDKAKKVKAAIEELQAEFV----DNAEELAKLQ-DELDKIVKTKSELVKEKYH 404
|
..
gi 1720435465 427 LH 428
Cdd:PHA02562 405 RG 406
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
52-560 |
1.77e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 52 PELSSLRQKVAYLDKEFSKAQKLCSQLEQLELENRQLKegvpgaagahvdGELLRLQAENTALQKNMAALQErygKEAVR 131
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLE------------GSKRKLEEKIRELEERIEELKK---EIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 132 PSAVGEgqgdppgdvlptplapmpLAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKI 211
Cdd:PRK03918 279 EEKVKE------------------LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 212 EELQQRKEaDLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRT 291
Cdd:PRK03918 341 EELKKKLK-ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 292 SLA----ALEQIQTAKT------------QELNMLREQTSELA---SELQHRQAEYEELMGQKDDLNSQL--QESLRANS 350
Cdd:PRK03918 420 EIKelkkAIEELKKAKGkcpvcgrelteeHRKELLEEYTAELKrieKELKEIEEKERKLRKELRELEKVLkkESELIKLK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 351 RLLEQLQEIGQE-KEQLTQDLQEARKSAEKRKVMLDELAME--TLQEKSQHKEELGAVRLRHEKELLGVRARYERELREL 427
Cdd:PRK03918 500 ELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 428 HEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCR---EE 504
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkysEE 659
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 505 HAAELKGKDEELQN----VREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSA 560
Cdd:PRK03918 660 EYEELREEYLELSRelagLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA 719
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-586 |
1.79e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 182 LSEKLKKKQESFCRLQTEKETLFNDSRNKIEE---LQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQG-ERLEH 257
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEelkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 258 AAALRALQDQVSSQSADAQEQVEGL---LAENSALRTSLAALEQIQTAKTQELNMLREQTS-ELASELQHRQAEYEELMG 333
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 334 QKddlnSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKEL 413
Cdd:COG4717 207 RL----AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 414 LGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQH--------TVEELQAQVHSMDGAKGWFERRLKEAEE 485
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalglppdlSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 486 SLQQQQQEQEETL-KLCREEHAAELKGKDEELQNvREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKkgsavLKD 564
Cdd:COG4717 363 LQLEELEQEIAALlAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDEEELEEE-----LEE 436
|
410 420
....*....|....*....|..
gi 1720435465 565 LKRQLHLERKRADKLQERLQEI 586
Cdd:COG4717 437 LEEELEELEEELEELREELAEL 458
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
160-593 |
2.59e-05 |
|
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: 47.91 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 160 ELKWEMEREEKKLLWEQLQ--GLELSEKLKKKQESF-CRLQTEKETLfnDSRNKIEELQQRKEADLKAqlaRTQKLQQEL 236
Cdd:pfam12128 434 EFNEEEYRLKSRLGELKLRlnQATATPELLLQLENFdERIERAREEQ--EAANAEVERLQSELRQARK---RRDQASEAL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 237 EAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAAlEQIQTAKTQELNM----LRE 312
Cdd:pfam12128 509 RQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDP-EVWDGSVGGELNLygvkLDL 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 313 QTSELASELQHRQAEYEELmgqkDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETL 392
Cdd:pfam12128 588 KRIDVPEWAASEEELRERL----DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQ 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 393 QEKSQHKEELGAVRLRHEKELLGVraryERELRELHEDKKRQEEELRGQIREekARTRELENLQHTVEELQAQVHSMDGA 472
Cdd:pfam12128 664 SEKDKKNKALAERKDSANERLNSL----EAQLKQLDKKHQAWLEEQKEQKRE--ARTEKQAYWQVVEGALDAQLALLKAA 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 473 KGWFERRLKEAeeslqqqqqeqeetLKLCREEHAAELKGKDEELQNV------REQLQQ--AQEERDGHVKTI------- 537
Cdd:pfam12128 738 IAARRSGAKAE--------------LKALETWYKRDLASLGVDPDVIaklkreIRTLERkiERIAVRRQEVLRyfdwyqe 803
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720435465 538 ------SNLKQEVKDTVDGQRILEKKGSAVLKDLKR---QLHLERKRADKLQERLQEILTNSKSR 593
Cdd:pfam12128 804 twlqrrPRLATQLSNIERAISELQQQLARLIADTKLrraKLEMERKASEKQQVRLSENLRGLRCE 868
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
154-591 |
2.70e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 154 MPLAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFcRLQTEKETLFNDSRNKIEELQ---------------QRK 218
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ-EEQLKKQQLLKQLRARIEELRaqeavleetqerinrARK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 219 EADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQS------------ADAQEQVEGLLAEN 286
Cdd:TIGR00618 292 AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllqtlhsqeihiRDAHEVATSIREIS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 287 S---ALRTSLAALEQIQTAKTQELNMLREQTSELASE---LQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIG 360
Cdd:TIGR00618 372 CqqhTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqatIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 361 QEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEElGAVRLRHEKEllgvraRYERELRELHEDKKRQeeelrg 440
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVV-LARLLELQEE------PCPLCGSCIHPNPARQ------ 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 441 QIREEKARTRELENLQHTVEELQAQVHSMDGaKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEELQNVR 520
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEDVYH-QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435465 521 EQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSK 591
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR 668
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
208-465 |
2.74e-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: 47.71 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 208 RNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQ-----------RQGERLEHAAALRALQDQVSSQSADAQ 276
Cdd:pfam05667 242 KRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSfsgssttdtglTKGSRFTHTEKLQFTNEAPAATSSPPT 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 277 EQVEgllaensalrtslaaLEQIQTAKTQELNMLREQTSELASELQhrqaEYEELMGQKDDLNSQLQESLRANSRLLEQL 356
Cdd:pfam05667 322 KVET---------------EEELQQQREEELEELQEQLEDLESSIQ----ELEKEIKKLESSIKQVEEELEELKEQNEEL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 357 QEIGQEKEQLTQDLQEARKSAEKRKVMLDELAmETLQEKSQHKEElgavrlrHEKELLgvrARYeRELRELHEDKKRQEE 436
Cdd:pfam05667 383 EKQYKVKKKTLDLLPDAEENIAKLQALVDASA-QRLVELAGQWEK-------HRVPLI---EEY-RALKEAKSNKEDESQ 450
|
250 260
....*....|....*....|....*....
gi 1720435465 437 ELRGQIREEKARTRELENLQHTVEELQAQ 465
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKEELYKQ 479
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
151-348 |
3.22e-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: 47.07 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 151 LAPMPLAEVELKWEMEREEKKLLWEQLQglELSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQ 230
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIA--ELEKELAALKKEEKALLKQLAAL-ERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 231 KLQQELEAANQSLAELRD---------QRQG-----------------------------ERLEHAAALRALQDQVSSQS 272
Cdd:COG4942 87 ELEKEIAELRAELEAQKEelaellralYRLGrqpplalllspedfldavrrlqylkylapARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435465 273 ADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRA 348
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
205-465 |
3.66e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 205 NDSRNKIEELQQRK--EADLKAqlartqkLQQELEAANQSLAELRDQRQgerleHAAALRALQDQVSSQSADAQEQVEGL 282
Cdd:PRK11281 39 ADVQAQLDALNKQKllEAEDKL-------VQQDLEQTLALLDKIDRQKE-----ETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 283 LAENSAL------RTSLAALEQIQTAKTQELNMLREQTSELASEL--QHRQAEyeelmgqkddlnsQLQESLRANSrllE 354
Cdd:PRK11281 107 KDDNDEEtretlsTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLvsLQTQPE-------------RAQAALYANS---Q 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 355 QLQEIGQEKEQLTQDlqEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLrheKELLGVRaryeRELRELHEDkkRQ 434
Cdd:PRK11281 171 RLQQIRNLLKGGKVG--GKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQL---QDLLQKQ----RDYLTARIQ--RL 239
|
250 260 270
....*....|....*....|....*....|.
gi 1720435465 435 EEELrgQIREEKARTRELENLQHTVEELQAQ 465
Cdd:PRK11281 240 EHQL--QLLQEAINSKRLTLSEKTVQEAQSQ 268
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
211-474 |
5.12e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 211 IEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRdqrqgERLEHAAALRalqdqvsSQSADAQEQVEGLLAENSALR 290
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLE-----KEVKELEELK-------EEIEELEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 291 TSLAALEQIQTAKTQELNMLREQTSELaSELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDL 370
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 371 QEARKSAEKRKVMLDELamETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTR 450
Cdd:PRK03918 338 ERLEELKKKLKELEKRL--EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260
....*....|....*....|....
gi 1720435465 451 ELENlqhTVEELQAQVHSMDGAKG 474
Cdd:PRK03918 416 ELKK---EIKELKKAIEELKKAKG 436
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
184-401 |
6.01e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 46.64 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 184 EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAALRA 263
Cdd:pfam03528 11 AELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKAVATVSENT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 264 LQDQVSSQSADAQEQVegllaensalrTSLAALEQiQTAKTQELNMLREQTSELASELQHRQAEYEElmgqKDDLNSQLQ 343
Cdd:pfam03528 91 KQEAIDEVKSQWQEEV-----------ASLQAIMK-ETVREYEVQFHRRLEQERAQWNQYRESAERE----IADLRRRLS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 344 EslransrlleqlqeiGQEKEQLTQDLQEARKSAEKRK--VMLDELAMETLQEKSQHKEE 401
Cdd:pfam03528 155 E---------------GQEEENLEDEMKKAQEDAEKLRsvVMPMEKEIAALKAKLTEAED 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-369 |
7.44e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 53 ELSSLRQKVAYLDKEFSKAQKLCSQLEQlELENRQLKEGVPGAAGAHVDGELLRLQAENTALQKNMAALQERYGKEAVRP 132
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSR-QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 133 SAVGEGqgdppgdvlptplapmpLAEVELKWEMEREEKKLLWEQLQglELSEKLKKKQESFCRLQTEKETLFNDSRNK-- 210
Cdd:TIGR02168 778 AEAEAE-----------------IEELEAQIEQLKEELKALREALD--ELRAELTLLNEEAANLRERLESLERRIAATer 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 211 -IEELQQRKE------ADLKAQLARTQKLQQELEAANQSLAELRDQRQgerlEHAAALRALQDQVSSQSADAQEQVEGLL 283
Cdd:TIGR02168 839 rLEDLEEQIEelsediESLAAEIEELEELIEELESELEALLNERASLE----EALALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 284 AENSALRTSLAALEQIQTAKTQELNMLREQTSELAS------------------ELQHRQA------------------E 327
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltleeaealenkieddeeEARRRLKrlenkikelgpvnlaaieE 994
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720435465 328 YEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQD 369
Cdd:TIGR02168 995 YEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKD 1036
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-397 |
7.62e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 201 ETLFNDSRNKIEELQQrKEADLKAQLArtqKLQQELEAANQSLAELRDQRQGERlEHAAALRALQDQVSSQSADAQEQVE 280
Cdd:COG3883 15 DPQIQAKQKELSELQA-ELEAAQAELD---ALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 281 GLLAENSALRTSLAALEQIQTAKTQE--------LNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRL 352
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1720435465 353 LEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQ 397
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
157-581 |
1.08e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 157 AEVELKWEMEREEKKLLWEQLQG--------------------LELSEKLKKKQESFCRLQTEKETLFNDSRNKIEEL-- 214
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNniekmilafeelrvqaenarLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLli 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 215 ----QQRKEADLKAQLARTQ----KLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSAdaqeqveglLAEN 286
Cdd:pfam05483 248 qiteKENKMKDLTFLLEESRdkanQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA---------LEED 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 287 SALRT-SLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKddlnsqlQESLRANSrllEQLQEIGQEKEQ 365
Cdd:pfam05483 319 LQIATkTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTE-------QQRLEKNE---DQLKIITMELQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 366 LTQDLQEARKSAEKRKVMLDELAM-----ETLQEKSQHKEELGAVRLRHEKELLGVRARYERELREL----------HED 430
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKilaedEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLeiqltaiktsEEH 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 431 KKRQEEELRGQIREEKARTRELENlqhTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAELK 510
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKNIELTA---HCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435465 511 GKDeELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQE 581
Cdd:pfam05483 546 LRD-ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
169-586 |
1.18e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 169 EKKLLWEQLQGLELSEKLKKKQESFcrlqTEKETLFNDSRNKIEELQQRKEaDLKAQLartQKLQQELEAANQSLAELRD 248
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEI----NEKTTEISNTQTQLNQLKDEQN-KIKKQL---SEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 249 QRQgerlEHAAALRALQDQ--------VSSQSADAQEQVEGL---LAEN----SALRTSLAALEQIQTAKTQELNMLREQ 313
Cdd:TIGR04523 289 QLN----QLKSEISDLNNQkeqdwnkeLKSELKNQEKKLEEIqnqISQNnkiiSQLNEQISQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 314 TSELASELQHRQAEYEE-------LMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDE 386
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSykqeiknLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 387 LAMETLQEKSQHKeELGAVRLRHEKELlgvrARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQV 466
Cdd:TIGR04523 445 LTNQDSVKELIIK-NLDNTRESLETQL----KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 467 HSMdgakgwferrlkeaeeslqqqqQEQEETLKLCREEHAAELKGKDEELQNVREQLQQAQ--EERDGHVKTISNLKQEV 544
Cdd:TIGR04523 520 SSL----------------------KEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQ 577
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1720435465 545 KDTVDGQRILE---KKGSAVLKDLKRQLHLERKRADKLQERLQEI 586
Cdd:TIGR04523 578 KSLKKKQEEKQeliDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
211-484 |
1.40e-04 |
|
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: 45.71 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 211 IEELQQRK---EADLKAQLARTQKLQQELEAANQSLAELR----------DQRQGERLEhaaALRALQDQVSS------Q 271
Cdd:COG3096 838 LAALRQRRselERELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanllaDETLADRLE---ELREELDAAQEaqafiqQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 272 SADAQEQVEGLLaenSALRTSLAALEQIQTAKTQ---ELNMLREQTSELASELQHRQA----EYEELMGQKDDLNSQLQE 344
Cdd:COG3096 915 HGKALAQLEPLV---AVLQSDPEQFEQLQADYLQakeQQRRLKQQIFALSEVVQRRPHfsyeDAVGLLGENSDLNEKLRA 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 345 SLR----ANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETlqeksqhkEELGaVRLRHEKEllgVRARY 420
Cdd:COG3096 992 RLEqaeeARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQEL--------EELG-VQADAEAE---ERARI 1059
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720435465 421 ERelRELHEdkkrqeeelrgQIREEKARTRELENlQHTVEELQaqvhsMDGAkgwfERRLKEAE 484
Cdd:COG3096 1060 RR--DELHE-----------ELSQNRSRRSQLEK-QLTRCEAE-----MDSL----QKRLRKAE 1100
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
157-430 |
1.48e-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: 45.44 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 157 AEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSrnkieelqQRKEADLKAQLARTQKLQQEL 236
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA--------EERLAKLEAEIDKLLAEIEEL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 237 EAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgllaENSALRTSLAALeqiqtakTQELNMLREQTSE 316
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKL-------KREINELKRELDR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 317 LASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELametlqEKS 396
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV------EKE 484
|
250 260 270
....*....|....*....|....*....|....
gi 1720435465 397 QHKEELGAVRLRHEKELLGVRARYERELRELHED 430
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
235-686 |
1.81e-04 |
|
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: 45.12 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 235 ELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgllaENSALRTSLAALEQIQTAKTQELNMLREQT 314
Cdd:pfam05557 31 ELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAE----LNRLKKKYLEALNKKLNEKESQLADAREVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 315 SELASELQHRQaeyEELMGQKDDLNSQLQESLRANSRLlEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMEtLQE 394
Cdd:pfam05557 107 SCLKNELSELR---RQIQRAELELQSTNSELEELQERL-DLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFE-IQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 395 KSQHKEELGAVRLRhekelLGVRARYERELRELHEDKKRqeeelrgqireekartreLENLQHTVEELQAQVHSMdgakg 474
Cdd:pfam05557 182 QEQDSEIVKNSKSE-----LARIPELEKELERLREHNKH------------------LNENIENKLLLKEEVEDL----- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 475 wfERRLKEAEESLQQQQQEQEETLKLCREEHAAELKGKDEEL-----QNVREQLQQAQEERDGHVKTISNLKQEVKDTVD 549
Cdd:pfam05557 234 --KRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 550 GQRILEKKGSAVLKDLKrQLHLERKRADKLQERLQ-EILTNSKSRTGLEELVLS---EMN----SPSRTQTGDSSSVSSF 621
Cdd:pfam05557 312 ARRELEQELAQYLKKIE-DLNKKLKRHKALVRRLQrRVLLLTKERDGYRAILESydkELTmsnySPQLLERIEEAEDMTQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 622 SY---------------REILKEKESSAIPARSLSSSPQAQPPRPAELSDEEVAELFQRLAETQQEKWMLEEKVKHLEVS 686
Cdd:pfam05557 391 KMqahneemeaqlsvaeEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEME 470
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
158-261 |
2.12e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 158 EVELKWEMEREEKKLLWEQlqglELSEKLKKKQESFCRLQTEKETLfndsRNKIEELQQrKEADLKAQLARTQKLQQELE 237
Cdd:PRK12704 57 EALLEAKEEIHKLRNEFEK----ELRERRNELQKLEKRLLQKEENL----DRKLELLEK-REEELEKKEKELEQKQQELE 127
|
90 100
....*....|....*....|....
gi 1720435465 238 AANQSLAELRDQRQgERLEHAAAL 261
Cdd:PRK12704 128 KKEEELEELIEEQL-QELERISGL 150
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
156-469 |
2.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 156 LAEVELKWEMEREEKKLLWEQLQGL-----ELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRK---EADLKAQLA 227
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELeeleaELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLaelEEELEEAQE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 228 RTQKLQQELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQEL 307
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 308 NMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARkSAEKRKVMLDEL 387
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE-LEQEIAALLAEA 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 388 AMETLQEKSQHkeelgAVRLRHEKELLGVRARYERELREL---------HEDKKRQEEELRGQIREEKARTRELENLQHT 458
Cdd:COG4717 380 GVEDEEELRAA-----LEQAEEYQELKEELEELEEQLEELlgeleelleALDEEELEEELEELEEELEELEEELEELREE 454
|
330
....*....|.
gi 1720435465 459 VEELQAQVHSM 469
Cdd:COG4717 455 LAELEAELEQL 465
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
344-586 |
2.36e-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: 45.06 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 344 ESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYErE 423
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE-K 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 424 LRELHEDKKRQEEELRGQIREEKARTRELEN-----LQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQQQQQEQEETL 498
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 499 klcreEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADK 578
Cdd:TIGR02169 336 -----AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
....*...
gi 1720435465 579 LQERLQEI 586
Cdd:TIGR02169 411 LQEELQRL 418
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
226-397 |
2.40e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 226 LARTQKLQQELEAANQ---SLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALE--QIQ 300
Cdd:PRK10929 119 LEKSRQAQQEQDRAREisdSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELElaQLS 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 301 TAKTQELNMLR-----EQTSELASELQ--------HRQAEYEE-------LMGQKDDLNSQLQESLRAN---SRLLEQ-- 355
Cdd:PRK10929 199 ANNRQELARLRselakKRSQQLDAYLQalrnqlnsQRQREAERalestelLAEQSGDLPKSIVAQFKINrelSQALNQqa 278
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720435465 356 --LQEIGQEKEQLTQDLQEARKsaekrkvmldelAMETLQEKSQ 397
Cdd:PRK10929 279 qrMDLIASQQRQAASQTLQVRQ------------ALNTLREQSQ 310
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-382 |
2.62e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 181 ELSEKLKKKQESFCRLQTEKETLfNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRqGERLEHAAA 260
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDAL-QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL-GERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 261 LRALQDQVSS--QSADAQEQVEGLLAENSALRTSLAALEQIQTAKtQELNMLREQTSELASELQHRQAEYEElmgQKDDL 338
Cdd:COG3883 98 SGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEA---AKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720435465 339 NSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKV 382
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
166-454 |
3.08e-04 |
|
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: 44.58 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 166 EREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQlartQKLQQELEAANQSLAE 245
Cdd:pfam02463 740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ----EEELRALEEELKEEAE 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 246 LRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREqtsELASELQHRQ 325
Cdd:pfam02463 816 LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ---KLKDELESKE 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 326 AEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAV 405
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEEL 972
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720435465 406 RLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELEN 454
Cdd:pfam02463 973 GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
200-568 |
3.53e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 200 KETLFNDSRNKIEELQQR------------------KEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAAL 261
Cdd:pfam15921 161 KEDMLEDSNTQIEQLRKMmlshegvlqeirsilvdfEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 262 RALQDQVSSQSADAQEQVEGLLAENSalrtslAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQ 341
Cdd:pfam15921 241 FPVEDQLEALKSESQNKIELLLQQHQ------DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSM 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 342 LQESLRANSRLLEQLQEIGQEKEQLTQDLQEarkSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARyE 421
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRMYEDKIE---ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKR-E 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 422 RELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDG-AKGWFERRLKEAEESLQQQQQEQEETlkl 500
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSeCQGQMERQMAAIQGKNESLEKVSSLT--- 467
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720435465 501 creehaAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKDTvdgQRILEKKGSAVLK-----DLKRQ 568
Cdd:pfam15921 468 ------AQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK---ERAIEATNAEITKlrsrvDLKLQ 531
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
182-298 |
5.40e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 182 LSEKLKKKQESFCRLQTEKETL---FNDSRNKIEELQQRKeADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHA 258
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELadlLSLERQGNQDLQDSV-ANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1720435465 259 AALRAlQDQVSSQsadAQEQVEGLLAENSALRTSLAALEQ 298
Cdd:PRK09039 123 QELDS-EKQVSAR---ALAQVELLNQQIAALRRQLAALEA 158
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
161-469 |
5.84e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.67 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 161 LKWEMEREEKKLLWEQLQGL-----ELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQE 235
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLhfgykSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 236 LEAANqslaelrdqrqgerlehAAALRALQDQVSSQSADaQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTS 315
Cdd:pfam12128 324 LEALE-----------------DQHGAFLDADIETAAAD-QEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 316 E-----LASELQHRQAEYEELMGQKDDLNSQLQESLRA-NSRLLEQLQEIGQEKEQLTQDLQEArksaekrKVMLDELAM 389
Cdd:pfam12128 386 EqnnrdIAGIKDKLAKIREARDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGEL-------KLRLNQATA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 390 --ETLQEKSQHKEELGAVRLRHEKEllgvRARYERELRELHEDKKRQEEELRgQIREEKARTRELEN-LQHTVEELQAQV 466
Cdd:pfam12128 459 tpELLLQLENFDERIERAREEQEAA----NAEVERLQSELRQARKRRDQASE-ALRQASRRLEERQSaLDELELQLFPQA 533
|
...
gi 1720435465 467 HSM 469
Cdd:pfam12128 534 GTL 536
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
308-598 |
6.32e-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: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 308 NMLRE-QTSELASELQhrqAEYEELMGQKDDLnsqlqESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDE 386
Cdd:COG4913 216 YMLEEpDTFEAADALV---EHFDDLERAHEAL-----EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 387 LAMETLQEKSQhkeelgavRLRHEKELLGVRaryERELRELHEDKKRQEEELRGQIREEKarTRELENLQHTVEELQAQV 466
Cdd:COG4913 288 RRLELLEAELE--------ELRAELARLEAE---LERLEARLDALREELDELEAQIRGNG--GDRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 467 hsmdgakgwfERRLKEaeeslqqqqqeqeetlklcREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLKQEVKD 546
Cdd:COG4913 355 ----------EERERR-------------------RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720435465 547 TVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEE 598
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDE 457
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
216-479 |
7.13e-04 |
|
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: 42.75 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 216 QRKEADLKAQLARTQKLQQELEAANQSLA-ELRDQRqgerlehaAALRALQDQVssqsADAQEQVEGLLAENSALRTSLA 294
Cdd:pfam19220 82 EGELEELVARLAKLEAALREAEAAKEELRiELRDKT--------AQAEALERQL----AAETEQNRALEEENKALREEAQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 295 ALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQEslraNSRLLEQLQEIGQEKEQLTQDLQEAR 374
Cdd:pfam19220 150 AAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAE----LETQLDATRARLRALEGQLAAEQAER 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 375 KSAEKRKvmldELAMETLQ-EKSQHKEELGAVRLRH---EKELLGVRARyereLRELHEDKKRQEEELRGQIREEKARTR 450
Cdd:pfam19220 226 ERAEAQL----EEAVEAHRaERASLRMKLEALTARAaatEQLLAEARNQ----LRDRDEAIRAAERRLKEASIERDTLER 297
|
250 260
....*....|....*....|....*....
gi 1720435465 451 ELENLQHTVEELQAQVHSMDGAKGWFERR 479
Cdd:pfam19220 298 RLAGLEADLERRTQQFQEMQRARAELEER 326
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
159-414 |
7.48e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 159 VELKWEMEREEKKLlwEQLQGLELSEKLKKKQESfcrlqTEKETLFNDSRnKIEELQQRKEADLKAQLARTQKLQQELEA 238
Cdd:COG5022 832 LRETEEVEFSLKAE--VLIQKFGRSLKAKKRFSL-----LKKETIYLQSA-QRVELAERQLQELKIDVKSISSLKLVNLE 903
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 239 ANQSLAELRDQRQGE-------RLEHAAALRALQD--QVSSQSA---DAQEQVEGLLAENSALRTSlaaleqiqtakTQE 306
Cdd:COG5022 904 LESEIIELKKSLSSDlienlefKTELIARLKKLLNniDLEEGPSieyVKLPELNKLHEVESKLKET-----------SEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 307 LNMLREQTSELASELQHRQaeyEELMGQKDDLNSQL--QESLRANSRLLEQLQEIGQEKEQLTQDLQEARkSAEKRKVML 384
Cdd:COG5022 973 YEDLLKKSTILVREGNKAN---SELKNFKKELAELSkqYGALQESTKQLKELPVEVAELQSASKIISSES-TELSILKPL 1048
|
250 260 270
....*....|....*....|....*....|
gi 1720435465 385 DELAMETLQEKSQHKEELGAVRLRHEKELL 414
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRRENSLL 1078
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
155-605 |
1.01e-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: 43.03 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 155 PLAEVELKWEMEREEKKLLWEQLQGLELSEKLKKK--QESFCRLQTEKETLFNDSRNKIEELQQRKEADlkaqlartQKL 232
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHLREALQQTQQSH--------AYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 233 QQELEAANQslaelRDQRQGERLEHAAALRALQDQVSSQSaDAQEQVEgLLAENSALRTSLAALEQIQTAKTQELNMLRE 312
Cdd:TIGR00618 246 TQKREAQEE-----QLKKQQLLKQLRARIEELRAQEAVLE-ETQERIN-RARKAAPLAAHIKAVTQIEQQAQRIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 313 QTSELASELQHRQA--EYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAME 390
Cdd:TIGR00618 319 KMRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 391 TlQEKSQHKEELGAVRLRH--EKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVHS 468
Cdd:TIGR00618 399 C-KELDILQREQATIDTRTsaFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 469 MDGAKGWFERRLKEAEESLQQQQQEQEETLKLCREEHAAE--------LKGKDEELQNVREQLQQAQEERDGHVKTISNL 540
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720435465 541 KQEVKDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVLSEMN 605
Cdd:TIGR00618 558 RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
167-603 |
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 1720435465 167 REEKKLLWEQLQglELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQ------RKEADLKAQLARTQKLQQELEAAN 240
Cdd:pfam15921 334 REAKRMYEDKIE--ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKlladlhKREKELSLEKEQNKRLWDRDTGNS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 241 QSLAELR---DQRQGERLEHAAALRAL----QDQVSSQSADAQ------EQVEGLLAENSALRTSLAALEQIQTAKTQEL 307
Cdd:pfam15921 412 ITIDHLRrelDDRNMEVQRLEALLKAMksecQGQMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 308 NMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLL---EQLQEIGQEKEQLTQDLQEARKSAEKRKVML 384
Cdd:pfam15921 492 ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEILRQQI 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 385 DEL----------AMETLQEKSQHKEELGAVRLRHeKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELEN 454
Cdd:pfam15921 572 ENMtqlvgqhgrtAGAMQVEKAQLEKEINDRRLEL-QEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 455 LQHTVEELQAQVHSMDGAKGWFERR---LKEAEESLQQQQQEQEETLKLcreehaaELKGKDEELQNVREQLqQAQEERD 531
Cdd:pfam15921 651 IKQERDQLLNEVKTSRNELNSLSEDyevLKRNFRNKSEEMETTTNKLKM-------QLKSAQSELEQTRNTL-KSMEGSD 722
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435465 532 GH-VKTISNLKQEV---KDTVDGQRILEKKGSAVLKDLKRQLHLERKRADKLQERLQEILTNSKSRTGLEELVLSE 603
Cdd:pfam15921 723 GHaMKVAMGMQKQItakRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ 798
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
265-456 |
1.25e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 265 QDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQE 344
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 345 SLRANSRL---------------LEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDelamETLQEKSQHKEELGAVRlrh 409
Cdd:COG3883 98 SGGSVSYLdvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELE----AKLAELEALKAELEAAK--- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720435465 410 eKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQ 456
Cdd:COG3883 171 -AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
184-586 |
1.40e-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: 42.31 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 184 EKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKE--------------------ADLKAQLARTQKLQQELEAANQSL 243
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEelenelnllekeklniqkniDKIKNKLLKLELLLSNLKKKIQKN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 244 AELrdqrQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQT---AKTQELNMLREQTSELASE 320
Cdd:TIGR04523 214 KSL----ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKqlsEKQKELEQNNKKIKELEKQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 321 LQHRQAEYEELMGQKD-------------------DLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRK 381
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEqdwnkelkselknqekkleEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 382 VMLDELametLQEKSQHKEELgaVRLRHEKELLgvraryERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEE 461
Cdd:TIGR04523 370 NEIEKL----KKENQSYKQEI--KNLESQINDL------ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 462 LQAQVHSMDGAKGWFERRLKEaeeslqqqqqeqeetLKLCREEHAAELKGKDEELQNVREQLQQAQEERDGHVKTISNLK 541
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKN---------------LDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1720435465 542 QEVKDtvdgqriLEKKgsavLKDLKRQLHLERKRADKLQERLQEI 586
Cdd:TIGR04523 503 EEKKE-------LEEK----VKDLTKKISSLKEKIEKLESEKKEK 536
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
210-412 |
1.52e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 210 KIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQGERLEHAAalRALQDQVSS-----QSADAQEQVEGLLA 284
Cdd:NF012221 1566 RAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEES--RAVTKELTTlaqglDALDSQATYAGESG 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 285 ENSALRTSLAALEQIQTaktqelnmlreqtsELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQeigQEKE 364
Cdd:NF012221 1644 DQWRNPFAGGLLDRVQE--------------QLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGE---QNQA 1706
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720435465 365 QLTQDLQEARKSAEKRKvmLDELAMETLQEKSQHKEELGA--VRLRHEKE 412
Cdd:NF012221 1707 NAEQDIDDAKADAEKRK--DDALAKQNEAQQAESDANAAAndAQSRGEQD 1754
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
154-360 |
1.56e-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: 42.26 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 154 MPLAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTE-KETLFNDSRNKIEELQQRKEADLKAQLARTQKL 232
Cdd:TIGR00618 655 LTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAqCQTLLRELETHIEEYDREFNEIENASSSLGSDL 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 233 QQELEAANQSLAELRDQR----------QGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQ---- 298
Cdd:TIGR00618 735 AAREDALNQSLKELMHQArtvlkarteaHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeips 814
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720435465 299 ---IQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIG 360
Cdd:TIGR00618 815 dedILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
158-402 |
2.15e-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: 41.88 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 158 EVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELE 237
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 238 AANQSLAELRDQrqgerLEHAAALRALQDQVSSQSADAQEQVEGllaENSALRTSLAALEQIQTAKTQELNMLREQTSEL 317
Cdd:TIGR00618 698 MLAQCQTLLREL-----ETHIEEYDREFNEIENASSSLGSDLAA---REDALNQSLKELMHQARTVLKARTEAHFNNNEE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 318 ASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQ--------LQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAM 389
Cdd:TIGR00618 770 VTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEigqeipsdEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH 849
|
250
....*....|....*
gi 1720435465 390 ETLQ--EKSQHKEEL 402
Cdd:TIGR00618 850 QLLKyeECSKQLAQL 864
|
|
| PRK06975 |
PRK06975 |
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed |
179-276 |
2.19e-03 |
|
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
Pssm-ID: 235899 [Multi-domain] Cd Length: 656 Bit Score: 41.63 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 179 GLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQ------QRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQ- 251
Cdd:PRK06975 341 GYALNRKVDRLDQELVQRQQANDAQTAELRVKTEQAQasvhqlDSQFAQLDGKLADAQSAQQALEQQYQDLSRNRDDWMi 420
|
90 100 110
....*....|....*....|....*....|...
gi 1720435465 252 ---GERLEHAAALRALQDQVSS-----QSADAQ 276
Cdd:PRK06975 421 aevEQMLSSASQQLQLTGNVQLalialQNADAR 453
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
181-365 |
2.47e-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: 41.64 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 181 ELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQqrkeadlkaqlARTQKLQQELEAANQSLAELRDQRQGERLEHAAA 260
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEME-----------TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 261 LRAlqdqvssqSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNS 340
Cdd:pfam15921 726 MKV--------AMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
170 180 190
....*....|....*....|....*....|....*
gi 1720435465 341 Q----------LQESLRANSRLLEQLQEIGQEKEQ 365
Cdd:pfam15921 798 QerrlkekvanMEVALDKASLQFAECQDIIQRQEQ 832
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
199-481 |
2.50e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 199 EKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQSLAELRDQRQgerlehaaALRALQDQVSSQSADAQEQ 278
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELE--------QLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 279 VEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQE 358
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 359 IGQEKEQLTQDLQ-----EARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELRELHEDKKR 433
Cdd:COG4372 162 LQEELAALEQELQalseaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720435465 434 QEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLK 481
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
233-370 |
2.79e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 233 QQELEAANQSLAELRDQRQGERlehaaalralqdqvsSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLRE 312
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLER---------------QGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435465 313 QTSELASELQHRQAEYEELMGQKDDLNSQ---LQESLRANSRLLEQLQEIGQEKEQLTQDL 370
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQiaaLRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-444 |
2.80e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 156 LAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQE 235
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 236 LEAANQSLA---------ELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEgLLAENSALRTSLAALEQIQTAKTQE 306
Cdd:COG1196 511 KAALLLAGLrglagavavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE-YLKAAKAGRATFLPLDKIRARAALA 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 307 LNMLREQTSELASELQHRQAEYEELM-----------------------------------GQKDDLNSQLQESLRANSR 351
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYyvlgdtllgrtlvaarleaalrravtlagrlrevtLEGEGGSAGGSLTGGSRRE 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 352 LLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKELLGVRARYERELREL---- 427
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEelle 749
|
330 340
....*....|....*....|....*....
gi 1720435465 428 ------------HEDKKRQEEELRGQIRE 444
Cdd:COG1196 750 eealeelpeppdLEELERELERLEREIEA 778
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
207-386 |
2.83e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 207 SRNKIEELQQRKEADLKAQLARTQKLQQEL------------EAANQSLAELRDQRQGERLEHAAA---LRALQDQVSSQ 271
Cdd:PRK11448 51 ALLGIYEPPCENQHDLLRRLGKEGFLPDEIldvfhklrkignKAVHEFHGDHREALMGLKLAFRLAvwfHRTYGKDWDFK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 272 SADAQEQVEgllaensalrtSLAALEQIQtaktQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSR 351
Cdd:PRK11448 131 PGPFVPPED-----------PENLLHALQ----QEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQE 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720435465 352 LLEQLQEIGQEKEQLTQDLQEARKSAEKR---KVMLDE 386
Cdd:PRK11448 196 LEAQLEQLQEKAAETSQERKQKRKEITDQaakRLELSE 233
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
156-355 |
3.36e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 156 LAEVELKWEMEREEKKLLWEQLQGLELSEKLKKKQESFCRLQTEKetlfNDSRNKIEELQQRKEADLKA-----QLARTQ 230
Cdd:COG3206 191 LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL----AEAEARLAALRAQLGSGPDAlpellQSPVIQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 231 KLQQELEAANQSLAELRdQRQGE--------RLEHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQiqta 302
Cdd:COG3206 267 QLRAQLAELEAELAELS-ARYTPnhpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA---- 341
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720435465 303 KTQELNMLREQTSELASELQHRQAEYEELMGQKDDLNSQLQESLrANSRLLEQ 355
Cdd:COG3206 342 RLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTV-GNVRVIDP 393
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
164-378 |
3.56e-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: 40.88 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 164 EMEREEKKllwEQL-QGLELSEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQELEAANQS 242
Cdd:pfam17380 384 QMERQQKN---ERVrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQ 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 243 LAELRDQRQGERLEHAAALralqDQVSSQSADAQEQVEGLLAENSALRTSlAALEQIQTAKTQELNMLREQTSeLASELQ 322
Cdd:pfam17380 461 QVERLRQQEEERKRKKLEL----EKEKRDRKRAEEQRRKILEKELEERKQ-AMIEEERKRKLLEKEMEERQKA-IYEEER 534
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720435465 323 HRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAE 378
Cdd:pfam17380 535 RREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
262-530 |
4.16e-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: 40.88 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 262 RALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELASElQHRQAEYEELMGQKDDLNSQ 341
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME-RERELERIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 342 LQESLR---ANSRLLEQLQ-EIGQEKEQLTQDLQEARK-----SAEKRKVMLDELAMETLQEKSQHKEELGAVRLRHEKE 412
Cdd:pfam17380 366 RQEEIAmeiSRMRELERLQmERQQKNERVRQELEAARKvkileEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 413 LLGVRARYERELRELHEDKKRQEEELR----GQIREEKARTRELENLQHTVEELQAQVHSMDGAKGWFERRLKEAEESLQ 488
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERkrkkLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER 525
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720435465 489 QQQQEQEETLKLCREEHAAELKGkdEELQNVREQLQQAQEER 530
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEM--EERRRIQEQMRKATEER 565
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
209-460 |
4.52e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 209 NKIEELQQRKE--ADLKAQLA-RTQKLQQELEAANQ----------------SLAELRDQRQgERLEHAAALRALQDQVS 269
Cdd:PRK04863 786 KRIEQLRAEREelAERYATLSfDVQKLQRLHQAFSRfigshlavafeadpeaELRQLNRRRV-ELERALADHESQEQQQR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 270 SQSADAQEQVEGL---------LAENS------ALRTSLAALEQIQ----------TAKTQELNMLREQTSELAS-ELQH 323
Cdd:PRK04863 865 SQLEQAKEGLSALnrllprlnlLADETladrveEIREQLDEAEEAKrfvqqhgnalAQLEPIVSVLQSDPEQFEQlKQDY 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 324 RQAE------------------------YEE---LMGQKDDLNSQLQESLR----ANSRLLEQLQEIGQEKEQLTQDLQE 372
Cdd:PRK04863 945 QQAQqtqrdakqqafaltevvqrrahfsYEDaaeMLAKNSDLNEKLRQRLEqaeqERTRAREQLRQAQAQLAQYNQVLAS 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 373 ARKSAEKRKVMLDELAMEtLQEKSQHKEELGAVRLRHEKELLGVRARYERELR-ELHEDKKRQEEELRGQIREEKARTRE 451
Cdd:PRK04863 1025 LKSSYDAKRQMLQELKQE-LQDLGVPADSGAEERARARRDELHARLSANRSRRnQLEKQLTFCEAEMDNLTKKLRKLERD 1103
|
....*....
gi 1720435465 452 LENLQHTVE 460
Cdd:PRK04863 1104 YHEMREQVV 1112
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
180-481 |
4.75e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 180 LELSEKLKKKQESFCRLQTEKEtlfnDSRNKIEELQQRKEaDLKAQLArtqKLQQELEAA-------NQSLAELRDQRQg 252
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQE----ENEARAEAAEEEVD-ELKSQLA---DYQQALDVQqtraiqyQQAVQALERAKQ- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 253 erLEHAAALRA--LQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIqtAKTQEL------NMLREQTSELASELQHR 324
Cdd:PRK04863 429 --LCGLPDLTAdnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF--EQAYQLvrkiagEVSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 325 QAEYEELMGQKDDLNSQLQE---SLRANSRLLEQLQEIGQ----------EKEQLTQDLQEARKSAEKRKVMLDELAMET 391
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSEleqRLRQQQRAERLLAEFCKrlgknlddedELEQLQEELEARLESLSESVSEARERRMAL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 392 LQEKSQHKEELGAVRLRhEKELLGVRARYEReLRELH----EDKKRQEEELRGQIREEKARTRELENLQHTVEELQAQVH 467
Cdd:PRK04863 585 RQQLEQLQARIQRLAAR-APAWLAAQDALAR-LREQSgeefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
330
....*....|....
gi 1720435465 468 SMDGAKGWFERRLK 481
Cdd:PRK04863 663 RLSQPGGSEDPRLN 676
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
181-481 |
6.09e-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: 40.32 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 181 ELSEKLKKKQESFCRLQTEKEtlfndsRNKIEELQQRKEAD-LKAQLArtqKLQQELEA----------ANQSLAELRDQ 249
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLA------EAEARLEAAEEEVDsLKSQLA---DYQQALDVqqtraiqyqqAVQALEKARAL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 250 RQGERL------EHAAALRALQDQVSSQSADAQEQVEGLLAENSALRTSLAALEQIQTAktqelnMLREQTSELASELQH 323
Cdd:COG3096 429 CGLPDLtpenaeDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGE------VERSQAWQTARELLR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 324 RQAEYEELMGQKDDLNSQLQESlranSRLLEQLQEIGQEKEQLTQDLQEARKSAEkrkvMLDELAME---TLQEKSQHKE 400
Cdd:COG3096 503 RYRSQQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAE----ELEELLAEleaQLEELEEQAA 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 401 ELGAVRLRHEKELLGVRARYER------ELRELHEDKKRQEEE--------------LRGQIREEKARTRELENLQHTVE 460
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKElaarapAWLAAQDALERLREQsgealadsqevtaaMQQLLEREREATVERDELAARKQ 654
|
330 340
....*....|....*....|.
gi 1720435465 461 ELQAQVHSMDGAKGWFERRLK 481
Cdd:COG3096 655 ALESQIERLSQPGGAEDPRLL 675
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
155-454 |
6.15e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 155 PLAEVELKWEMEREEKKLLwEQLQGLELsEKLKKKQESFCRLQTEKETLFNDSRNKIEELQQRKEADLKAQLARTQKLQQ 234
Cdd:COG5185 241 PESELEDLAQTSDKLEKLV-EQNTDLRL-EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 235 ELEAANQSLAELRDQRQGERLEHAAALRALQDQVSSQSADAQEQVEGLLAENsALRTSLAALEQIQtaktQELNMLREqt 314
Cdd:COG5185 319 AAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV-ELSKSSEELDSFK----DTIESTKE-- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 315 selASELQHRQAEyeelmGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAMETLQE 394
Cdd:COG5185 392 ---SLDEIPQNQR-----GYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720435465 395 KSQHKEELGAVRLRHEKELLGVRA-RYERELRELhedkKRQEEELRGQIREEKARTRELEN 454
Cdd:COG5185 464 RLEEAYDEINRSVRSKKEDLNEELtQIESRVSTL----KATLEKLRAKLERQLEGVRSKLD 520
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
205-436 |
6.34e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 205 NDSRNKIEELQQ---RKEADLKAQLARTQKLQQELEAANQSLAE----LRD-QRQGERLEH-----AAALRALQDQVSSQ 271
Cdd:PRK11637 43 SDNRDQLKSIQQdiaAKEKSVRQQQQQRASLLAQLKKQEEAISQasrkLREtQNTLNQLNKqidelNASIAKLEQQQAAQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 272 SADAQEQ------------VEGLLAENSALRTS--LAALEQIQTAKTQELNMLREQTSELA---SELQHRQAEYEELMGQ 334
Cdd:PRK11637 123 ERLLAAQldaafrqgehtgLQLILSGEESQRGEriLAYFGYLNQARQETIAELKQTREELAaqkAELEEKQSQQKTLLYE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 335 KDDLNSQLQESLRANSRLLEQLqEIGQEKEQltQDLQEARKSaEKRkvMLDELAmetlqeksqhkeelgavrlRHEKEll 414
Cdd:PRK11637 203 QQAQQQKLEQARNERKKTLTGL-ESSLQKDQ--QQLSELRAN-ESR--LRDSIA-------------------RAERE-- 255
|
250 260
....*....|....*....|..
gi 1720435465 415 gVRARYERELRELHEDKKRQEE 436
Cdd:PRK11637 256 -AKARAEREAREAARVRDKQKQ 276
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
204-359 |
6.60e-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: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 204 FNDSRNKIEELQQRKEADLKAQLARTQKLQ-QELEAAnqsLAELRDQRQGERLEHAAALRALQDQVSSQS----ADAQEQ 278
Cdd:COG2433 345 YDAYKNKFERVEKKVPPDVDRDEVKARVIRgLSIEEA---LEELIEKELPEEEPEAEREKEHEERELTEEeeeiRRLEEQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 279 VEGLLAENSALRTSLAALEQIQTAKTQELNMLREQTSELA---SELQHRQAEYEELmgqKDDLNsQLQESLRANSRLLEQ 355
Cdd:COG2433 422 VERLEAEVEELEAELEEKDERIERLERELSEARSEERREIrkdREISRLDREIERL---ERELE-EERERIEELKRKLER 497
|
....
gi 1720435465 356 LQEI 359
Cdd:COG2433 498 LKEL 501
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
205-529 |
7.90e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 205 NDSRNKIEElqqrkEADLKAQLARTQKlqqELEAANQSLAELRDqrqgERLEHAAALRALQDQVSSQSADAQEQVEGLLA 284
Cdd:PRK04863 279 NERRVHLEE-----ALELRRELYTSRR---QLAAEQYRLVEMAR----ELAELNEAESDLEQDYQAASDHLNLVQTALRQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 285 ENSALRTSlAALEQIqTAKTQELNMLREQTSELASELQHRQAEYEElmgQKDDLNSQLQESLRAnsrlLEQLQEIGQEKE 364
Cdd:PRK04863 347 QEKIERYQ-ADLEEL-EERLEEQNEVVEEADEQQEENEARAEAAEE---EVDELKSQLADYQQA----LDVQQTRAIQYQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 365 QLTQDLQEARKSAEKRKVMLDELamETLQEKSQHKEELGAVRLRHEKELLGV----RARYERELRELH--------EDKK 432
Cdd:PRK04863 418 QAVQALERAKQLCGLPDLTADNA--EDWLEEFQAKEQEATEELLSLEQKLSVaqaaHSQFEQAYQLVRkiagevsrSEAW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 433 RQEEELRGQIREEKARTRELENLQHTVEELQAQVHSMDGAkgwfeRRLKEAEESLQQQQQEQEETLKLCREEHAAELKGK 512
Cdd:PRK04863 496 DVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA-----ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESL 570
|
330 340
....*....|....*....|
gi 1720435465 513 DEELQNVREQ---LQQAQEE 529
Cdd:PRK04863 571 SESVSEARERrmaLRQQLEQ 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
313-465 |
8.75e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 313 QTSELASELQHRQAEYEELMGQKDDLNSQLQESLRANSRLLEQLQEIGQEKEQLTQDLQEARKSAEKRKVMLDELAmETL 392
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA-RAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720435465 393 QEKSQHKEELGAV-----------RLRHEKELLGVRARYERELRELHEDKKRQEEELRGQIREEKARTRELENLQHTVEE 461
Cdd:COG3883 96 YRSGGSVSYLDVLlgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
....
gi 1720435465 462 LQAQ 465
Cdd:COG3883 176 QQAE 179
|
|
| |
