|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-485 |
3.02e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 49 DLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEG--DVE 126
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERrrELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 127 ALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGEN 206
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 207 QMLQSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQ 286
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 287 DADVSGASLQSELAHSLEDGDQGQSAEARGDTPTTRSPKTREVSSPQPSP-PEESLEPPKKRTSLSPAEILEEKEAEVAK 365
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 366 LQDEISLQQAELQS-------LREELQRQKELRAQEDPGEALHSALSDRDEAVNKALELSLELNRVSLERDSLYRELLRA 438
Cdd:COG1196 556 DEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1622916188 439 IRQKVALTQELEAWQDDMQVVIGQQLRSQRQKELNAAASSSTPRRAA 485
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-386 |
2.04e-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: 70.09 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 53 QLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAE---WEARAVELEGDVEALR 129
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 130 AQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQ---ELQRELDTLRGQCQAQALAGAELRTRLESLQGEN 206
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 207 QMLQSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQ 286
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 287 DADVSGASLQSELAHSLEDGDQGQSAEARGDTPTTRSPKTREVSSPQPSPPEESLEPPKKRTSLSPAEILEEKE-AEVAK 365
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEyEELKE 1000
|
330 340
....*....|....*....|.
gi 1622916188 366 LQDEISLQQAELQSLREELQR 386
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
74-453 |
4.33e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 74 RNEELRRQLETLSAQHLEREERLQQENHELRRgLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSEL 153
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 154 SeqnlRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGQGR 233
Cdd:COG1196 298 A----RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 234 LQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQDADVSGASLQSELAHSLEDGDQGQSAE 313
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 314 ARgdtpttrspktrevsspqpsppeesleppkkRTSLSPAEILEEKEAEVAKLQDEISLQQAELQSLREELQRQKELRAQ 393
Cdd:COG1196 454 LE-------------------------------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 394 EDPGEALHSALSDRDEAVNKALELSLELNRVSLERDSLYRELLRAIRQKVALTQELEAWQ 453
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
56-479 |
4.46e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 56 QKEKDLLLAAELGKMLLERNEELRRQLETLsAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALR------ 129
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAEL-EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellael 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 130 AQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQML 209
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 210 QSRRQDL-------EAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEE 282
Cdd:COG1196 378 EEELEELaeelleaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 283 SRLQDADVSGASLQSELAHSLEDGDQGQSAEARGDTPTTRSPKTREVSSPQPSPPEESLEPPKKRTSLSPAEILEEKEAE 362
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 363 VAKLQDEISLQQAELQSLREELQRQKELRAQEDPGEA---LHSALSDRDEAVNKALELSLELNRVSLERDSLYRELLRAI 439
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622916188 440 RQKVALTQELEAWQDDMQVVIGQQLRSQRQKELNAAASSS 479
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-425 |
5.25e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 76 EELRRQLETLSAQhLEREERLQQENHELRrglAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSE 155
Cdd:TIGR02168 196 NELERQLKSLERQ-AEKAERYKELKAELR---ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 156 QNLR---LSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIrglrEEVEKGQG 232
Cdd:TIGR02168 272 LRLEvseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL----AELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 233 RLQTTHEELLLLRRERREHNLELERARSEAEEalsALRRLQRRVSELEEESRLQDADVSGA-SLQSELAHSLEDGDQGQS 311
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEE---QLETLRSKVAQLELQIASLNNEIERLeARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 312 AEARGDTPTTRSPKTREVSSpqpsppeesleppKKRTSLSPAEILEEKEAEVAKLQDEISLQQAELQSLREELQRqkeLR 391
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEE-------------LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ---LQ 488
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622916188 392 AQEDPGEALHSALSDRDEAV----NKALELSLELNRVS 425
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVkallKNQSGLSGILGVLS 526
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-385 |
9.36e-11 |
|
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: 64.70 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 70 MLLERNEELRRQLETLsaqhLEREERLQQENHELRRGLA---ARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRER 146
Cdd:TIGR02169 678 RLRERLEGLKRELSSL----QSELRRIENRLDELSQELSdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 147 ARALSELSEQNLRLSQQLAQASQTE---------------QELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQS 211
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEealndlearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 212 RRQ-------DLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELE---- 280
Cdd:TIGR02169 834 EIQelqeqriDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqie 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 281 -EESRLQDADVSGASLQSELAHSLEdgdqgqsaeargdtpttrsPKTREVSSPQPSPPEESLEPPKKR-----TSLSPAE 354
Cdd:TIGR02169 914 kKRKRLSELKAKLEALEEELSEIED-------------------PKGEDEEIPEEELSLEDVQAELQRveeeiRALEPVN 974
|
330 340 350
....*....|....*....|....*....|..
gi 1622916188 355 ILEEKE-AEVAKLQDEISLQQAELQSLREELQ 385
Cdd:TIGR02169 975 MLAIQEyEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-295 |
1.38e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 71 LLERNEELRRQLETLSAQhlerEERLQQENHELRRGLAARGAEWEaravELEGDVEALRAQLGEQRSEQQDSGREraraL 150
Cdd:TIGR02168 230 LVLRLEELREELEELQEE----LKEAEEELEELTAELQELEEKLE----ELRLEVSELEEEIEELQKELYALANE----I 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 151 SELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKG 230
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622916188 231 QGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQDADVSGASL 295
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-316 |
5.10e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 53 QLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRgLAARGAEWEARAVELEGDVEALRAQL 132
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA-LANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 133 GEQRSEQQDSGRERARALSELSEqnlrLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSR 212
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAE----LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 213 RQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNL-----ELERARSEAEEALSALRRLQRRVSELEEESR--- 284
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkelqaELEELEEELEELQEELERLEEALEELREELEeae 474
|
250 260 270
....*....|....*....|....*....|....
gi 1622916188 285 --LQDADVSGASLQSELAhSLEDGDQGQSAEARG 316
Cdd:TIGR02168 475 qaLDAAERELAQLQARLD-SLERLQENLEGFSEG 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-235 |
1.22e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 50 LALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQqenhELRRGLAARGAEWEARA---VELEGDVE 126
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRskvAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 127 ALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSqqlaqaSQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGEN 206
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
170 180
....*....|....*....|....*....
gi 1622916188 207 QMLQSRRQDLEAQIRGLREEVEKGQGRLQ 235
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
61-295 |
2.21e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 61 LLLAAELGKMLLERNEELRRQLETLSAQhLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQ 140
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQE-IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 141 DSGRERARALSELSEQNLRLSQQLAQA--------------SQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGEN 206
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 207 QMLQSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQ 286
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*....
gi 1622916188 287 DADVSGASL 295
Cdd:COG4942 247 GFAALKGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
53-234 |
5.69e-07 |
|
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: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 53 QLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELR-RGLAARGAEWEARAVELE---GDVEAL 128
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDassDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 129 RAQLGEQRSEQQDSGRERARALSELSeqnlRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAElrTRLESLQGENQM 208
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIG----RLEKELEQAEEELDELQDRLEAAEDLARLELRALLE--ERFAAALGDAVE 764
|
170 180
....*....|....*....|....*.
gi 1622916188 209 LQSRRQdLEAQIRGLREEVEKGQGRL 234
Cdd:COG4913 765 RELREN-LEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
76-386 |
3.02e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 76 EELRRQLETLSAQ--HLEREERLQQENHELR-RGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSE 152
Cdd:TIGR02169 194 DEKRQQLERLRREreKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 153 LSEQNLRLSqqlAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGQG 232
Cdd:TIGR02169 274 LEELNKKIK---DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 233 RLQTTHEELLLLRRerrehnlELERARSEAEEALSALRRLQRRVSELEEEsrLQDADVSGASLQSELAHSLEDGDQ--GQ 310
Cdd:TIGR02169 351 RRDKLTEEYAELKE-------ELEDLRAELEEVDKEFAETRDELKDYREK--LEKLKREINELKRELDRLQEELQRlsEE 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916188 311 SAEARGDTPTTRSPKTrEVSSPQPSPPEESLEPPKKRTSLspAEILEEKEAEVAKLQDEISLQQAELQSLREELQR 386
Cdd:TIGR02169 422 LADLNAAIAGIEAKIN-ELEEEKEDKALEIKKQEWKLEQL--AADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
37-265 |
6.04e-06 |
|
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: 48.61 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 37 FLGGGPGPEEPEDLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRgLAARGAEWEA 116
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 117 RAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELR 196
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622916188 197 TRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEA 265
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
73-402 |
1.11e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 73 ERNEELRRQLETLSAQ------HLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRS---EQQDSG 143
Cdd:PRK02224 384 EEIEELEEEIEELRERfgdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecGQPVEG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 144 RERARALSELSEQNLRLSQQLAQASQTEQELQRELDtlrgqcqaQALAGAELRTRLESLQgenqmlqSRRQDLEAQIRGL 223
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE--------RAEDLVEAEDRIERLE-------ERREDLEELIAER 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 224 REEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQDADVSGASLQSELAHSL 303
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEI 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 304 ED-----GDQGQSAEARGDTPTTRSPKTREVSSPQPSPPEESLEPPKKRTSLSPAEI---LEEKEAEVAKLQDEISLQQA 375
Cdd:PRK02224 609 ERlrekrEALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVeekLDELREERDDLQAEIGAVEN 688
|
330 340
....*....|....*....|....*..
gi 1622916188 376 ELQSLREELQRQKELRAQEDPGEALHS 402
Cdd:PRK02224 689 ELEELEELRERREALENRVEALEALYD 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
29-267 |
1.68e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 29 FVLERRDSFLGGGPGPEEPEDL------ALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHE 102
Cdd:COG4913 216 YMLEEPDTFEAADALVEHFDDLeraheaLEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 103 LRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERaraLSELSEQNLRLSQQLAQASQTEQELQRELDTLR 182
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR---LEQLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 183 GQCQAQALAGAELRTRLESLQGEnqmLQSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEA 262
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEA---LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
....*
gi 1622916188 263 EEALS 267
Cdd:COG4913 450 AEALG 454
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
92-223 |
2.25e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 92 REERLQQENHELRRGLAARGAEwEARAVELEGDVEALRAQLGEQRSEQ---QDSGRERARALSELSEQNLRLSQQLAQAS 168
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLSLE-RQGNQDLQDSVANLRASLSAAEAERsrlQALLAELAGAGAAAEGRAGELAQELDSEK 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622916188 169 QTEQELQRELDTLRGQCqaqalagAELRTRLESLQGENQMLQSRRQDLEAQIRGL 223
Cdd:PRK09039 130 QVSARALAQVELLNQQI-------AALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-282 |
2.99e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 108 AARGAEWEARAVELEGDVEALRAQLG--EQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQReLDTLRGQC 185
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELER-LDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 186 QAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEkgqgRLQTTHEELLLLRRERREHNLELERARSEAEEA 265
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD----ELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170
....*....|....*...
gi 1622916188 266 LSALRR-LQRRVSELEEE 282
Cdd:COG4913 764 ERELREnLEERIDALRAR 781
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
55-233 |
3.16e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 55 QQKEKDLLLAAELGKMLLERNEELRRQLETLsaqhlEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLgE 134
Cdd:PRK04863 495 WDVARELLRRLREQRHLAEQLQQLRMRLSEL-----EQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL-E 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 135 QRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQ 214
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERD 648
|
170
....*....|....*....
gi 1622916188 215 DLEAQIRGLREEVEKGQGR 233
Cdd:PRK04863 649 ELAARKQALDEEIERLSQP 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
78-457 |
6.87e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 78 LRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQrSEQQDSGRERARALSELSEQN 157
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA-DEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 158 LRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGQGRLQTT 237
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 238 HEELLLLRRERREH--------------NLELERARSEAEEALSALRRLQRRVSELEEesRLQDADVSGASLQSELAHSL 303
Cdd:PRK02224 341 NEEAESLREDADDLeeraeelreeaaelESELEEAREAVEDRREEIEELEEEIEELRE--RFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 304 EDGDqgqsaEARGDTPTTRSpkTREVSSPQPSPPEESLEPPKKRTSLSP------AEILEEKEAEVAKLQDEISLQQAEL 377
Cdd:PRK02224 419 EERD-----ELREREAELEA--TLRTARERVEEAEALLEAGKCPECGQPvegsphVETIEEDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 378 QSLREELQRQKELRAQEDPGEALhsalsdrdEAVNKALELSLELNRVSLERDSLYRELLRAirQKVALTQELEAWQDDMQ 457
Cdd:PRK02224 492 EEVEERLERAEDLVEAEDRIERL--------EERREDLEELIAERRETIEEKRERAEELRE--RAAELEAEAEEKREAAA 561
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
149-419 |
7.70e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 45.23 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 149 ALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAqalagaeLRTRLESLQGENQMLQSRRQDLEAQIRGLREEVE 228
Cdd:pfam09726 396 ALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERS-------LKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 229 KGQGRLQttheellllrrerrehnlELERARSEAEEALSAlrrlQRRVSELEEESrlqdadvsgaslqselahsledgdq 308
Cdd:pfam09726 469 QLEKRLK------------------AEQEARASAEKQLAE----EKKRKKEEEAT------------------------- 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 309 gqSAEARGDTPTTRSPKTrevsspqpsppeESLEPPKKrtslspaeileEKEAEVAKLQDEISLQQAELQSLREELQRQK 388
Cdd:pfam09726 502 --AARAVALAAASRGECT------------ESLKQRKR-----------ELESEIKKLTHDIKLKEEQIRELEIKVQELR 556
|
250 260 270
....*....|....*....|....*....|.
gi 1622916188 389 ELRAQEDPGEALHSALSDRDEAvNKALELSL 419
Cdd:pfam09726 557 KYKESEKDTEVLMSALSAMQDK-NQHLENSL 586
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
56-236 |
7.81e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 56 QKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAArgaeweARAVELEGDVEALRAQLGEQ 135
Cdd:COG3206 202 RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA------LPELLQSPVIQQLRAQLAEL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 136 RseqqdsgRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQAlagAELRTRLESLQGENQMLQSRRQD 215
Cdd:COG3206 276 E-------AELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL---EALQAREASLQAQLAQLEARLAE 345
|
170 180
....*....|....*....|....
gi 1622916188 216 L---EAQIRGLREEVEKGQGRLQT 236
Cdd:COG3206 346 LpelEAELRRLEREVEVARELYES 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
79-282 |
7.83e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 79 RRQLETLSAQHLEREERLqqenhelrrglaargAEWEARAVELEGDVEALRAQlgeqrseqqdsgRERARALSELSEQNL 158
Cdd:COG4913 609 RAKLAALEAELAELEEEL---------------AEAEERLEALEAELDALQER------------REALQRLAEYSWDEI 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 159 RLSQQLAQASQTEQELQR------ELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEkgqg 232
Cdd:COG4913 662 DVASAEREIAELEAELERldassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE---- 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622916188 233 RLQTTHEELLLLRRERREHNLELERARSEAEEALSA-LRRLQRRVSELEEE 282
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEErIDALRARLNRAEEE 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
143-305 |
8.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 143 GRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQA-QALAG-AELRTRLESLQGENQMLQSRRQDLEA-- 218
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEySWDEIDVASAEREIAELEAELERLDAss 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 219 -QIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVS-----ELEEESRLQDADVSG 292
Cdd:COG4913 685 dDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGDAVE 764
|
170
....*....|...
gi 1622916188 293 ASLQSELAHSLED 305
Cdd:COG4913 765 RELRENLEERIDA 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-386 |
1.10e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 50 LALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQ----QENHELRRGLAARGAEWEARAVELEGDV 125
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 126 EALRAQLGEQRSEQQDsgRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGE 205
Cdd:COG1196 541 EAALAAALQNIVVEDD--EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 206 NQMLQSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRL 285
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 286 QDADVSGASLQSELAHSLEDGDQGQSAEARGdtpttrspktrevsspqpsppEESLEPPKKRTSLSPAEILEEKEAEVAK 365
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQ---------------------LEAEREELLEELLEEEELLEEEALEELP 757
|
330 340
....*....|....*....|.
gi 1622916188 366 LQDEISLQQAELQSLREELQR 386
Cdd:COG1196 758 EPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-454 |
1.19e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 165 AQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLL 244
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 245 RRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQDADVSGASLQSELAHSledgdqgQSAEARGDTPTTRsp 324
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-------ALDELRAELTLLN-- 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 325 ktrevsspqpsppeesleppkkRTSLSPAEILEEKEAEVAKLQDEISLQQAELQSLREELQR-QKELRAQEDPGEALHSA 403
Cdd:TIGR02168 817 ----------------------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlAAEIEELEELIEELESE 874
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622916188 404 LsdrDEAVNKALELSLELNRVSLERDSLYRELLRAIRQKVALTQELEAWQD 454
Cdd:TIGR02168 875 L---EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
49-176 |
1.20e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.27 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 49 DLALQLQQKEKDLLlAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRR--GLAARGAEWEARAVELEGDVE 126
Cdd:COG1566 80 DLQAALAQAEAQLA-AAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqALYKKGAVSQQELDEARAALD 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622916188 127 ALRAQLGEQRSeQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQR 176
Cdd:COG1566 159 AAQAQLEAAQA-QLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-398 |
1.80e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 51 ALQLQQKEKDLLLAAELGKMLLE--RNEELRRQletlsAQHLEREERLQQENHELRRGLAARGAEWEAR-AVELEGDVEA 127
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEakKADEAKKK-----AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkADEAKKKAEE 1494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 128 LRAQLGEQR--SEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQ-ELQRELDTLRgqcQAQALAGAELRTRLESLQG 204
Cdd:PTZ00121 1495 AKKKADEAKkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaEEKKKADELK---KAEELKKAEEKKKAEEAKK 1571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 205 --ENQMLQSRRQDLEAQIRGLReeVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEE 282
Cdd:PTZ00121 1572 aeEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 283 SRLQDADVSGASLQSELAHSLEDgDQGQSAEARgdtpttrspKTREVSSPQPSPPEESLEPPKKRTSLSPAEILEEKEAE 362
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEE-DKKKAEEAK---------KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAE 1719
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622916188 363 VAKLQDEISLQQAELQSLREELQRQKELRAQEDPGE 398
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
73-393 |
2.36e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 73 ERNEELRRQLETLSAQHLEREERLQQENHELRRGLAA-RGAEWEARAVElegDVEALRAQLGEQR--SEQQDSGRERARA 149
Cdd:PRK04863 307 YRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAlRQQEKIERYQA---DLEELEERLEEQNevVEEADEQQEENEA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 150 LSELSEQN-LRLSQQLA-----------QASQTEQELQReLDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLE 217
Cdd:PRK04863 384 RAEAAEEEvDELKSQLAdyqqaldvqqtRAIQYQQAVQA-LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 218 AQIRglreevekgqgrlqttheellllrrerrehnlELERARSEAEEALSALRRLQRRVS---------ELEEESRLQDA 288
Cdd:PRK04863 463 QKLS--------------------------------VAQAAHSQFEQAYQLVRKIAGEVSrseawdvarELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 289 -DVSGASLQSELAHSLEDGDQGQSAEARGDTPTTRSPKtrevsspqpsppeesleppkkrtSLSPAEILEEKEAEVAKLQ 367
Cdd:PRK04863 511 lAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGK-----------------------NLDDEDELEQLQEELEARL 567
|
330 340
....*....|....*....|....*..
gi 1622916188 368 DEISLQQAELQSLREELQRQ-KELRAQ 393
Cdd:PRK04863 568 ESLSESVSEARERRMALRQQlEQLQAR 594
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
81-233 |
3.01e-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: 43.79 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 81 QLETLSAQHLEREERLQQENHELRRG-----LAARGAEWEARAVELE------GDVEALRAQLGEQRSEQQDSGRERARA 149
Cdd:COG3096 479 ELVCKIAGEVERSQAWQTARELLRRYrsqqaLAQRLQQLRAQLAELEqrlrqqQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 150 LSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQ---AQALAGAELRTRLESLQGE-NQMLQSRRQDLEAQIRGLRE 225
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelaARAPAWLAAQDALERLREQsGEALADSQEVTAAMQQLLER 638
|
....*...
gi 1622916188 226 EVEKGQGR 233
Cdd:COG3096 639 EREATVER 646
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
134-300 |
4.52e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 134 EQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAG--AELRTRLESLQGENQMLQS 211
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 212 R---RQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLE-LERARSEAEEALSALRRLQRRVSELEEESRLQD 287
Cdd:COG4717 154 RleeLRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEeLEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170
....*....|...
gi 1622916188 288 ADVSGASLQSELA 300
Cdd:COG4717 234 NELEAAALEERLK 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
70-457 |
4.60e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 70 MLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELegdvEALRAQLGEQRSEQQDSGRERARA 149
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 150 lsELSEQNLRLSQQLAQASQTEQELQRELDTLRgqcqAQALAGAELRTRLESLQGEnqmLQSRRQDLEAQIRGLREEVEK 229
Cdd:COG4717 122 --EKLLQLLPLYQELEALEAELAELPERLEELE----ERLEELRELEEELEELEAE---LAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 230 gqgRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQDADVSGASLQSELAHSLEDGDQG 309
Cdd:COG4717 193 ---ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 310 QSAEARGDTPTTRSPKTREVSSPQPSPPEESLEPPKKRTSLSPAEILEEKE--AEVAKLQDEISLQQAELQSLREELQRQ 387
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 388 KELRAQEDpgEALHSALSDRDEAVNKALelsleLNRVSLERDSLYRELLRAIRQKVALTQELEAWQDDMQ 457
Cdd:COG4717 350 QELLREAE--ELEEELQLEELEQEIAAL-----LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE 412
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
97-282 |
7.67e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 97 QQENHELRRGLAARGAEW-EARAVELEGDVEALRAQLGEQRSEQQ--DSGRERARALSELSEqnlrLSQQLAQASQTEQE 173
Cdd:COG3206 162 LEQNLELRREEARKALEFlEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE----LESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 174 LQRELDTLRGQCQAQALAGAE---------LRTRLESLQGENQMLQSR-------RQDLEAQIRGLREEVEKGQGRLQTT 237
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEllqspviqqLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622916188 238 HEELLLLRRERREhnlELERARSEAEEALSALRRLQRRVSELEEE 282
Cdd:COG3206 318 LEAELEALQAREA---SLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
76-508 |
8.42e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 76 EELRRQLETLS-----AQHLEREERLQQENHELRRGLAARGAE-----WEARAVELEGDVEALRAQLGEQRSEQQDSGRE 145
Cdd:COG4913 245 EDAREQIELLEpirelAERYAAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 146 RARALSELSEQNL----RLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQM----LQSRRQDLE 217
Cdd:COG4913 325 LDELEAQIRGNGGdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAlleaLEEELEALE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 218 AQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALS----------------------------AL 269
Cdd:COG4913 405 EALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGldeaelpfvgelievrpeeerwrgaierVL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 270 R-----------------------RLQRRVSELEEESRLQDADVSGAS------------------LQSELAHSLE---- 304
Cdd:COG4913 485 GgfaltllvppehyaaalrwvnrlHLRGRLVYERVRTGLPDPERPRLDpdslagkldfkphpfrawLEAELGRRFDyvcv 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 305 DGDQGQSAEARGDTPT--TRSPKTREVSSPQPSPPEESLeppkkrTSLSPAEILEEKEAEVAKLQDEIS----------L 372
Cdd:COG4913 565 DSPEELRRHPRAITRAgqVKGNGTRHEKDDRRRIRSRYV------LGFDNRAKLAALEAELAELEEELAeaeerlealeA 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 373 QQAELQSLREELQRQKELRAQEDPGEALHSALSDRDEAVNKALELSLELNRVSLERDSLYRELLRAIRQKVALTQELEAW 452
Cdd:COG4913 639 ELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRL 718
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916188 453 QDDMQVVIGQQLRSQRQKELNAAASSSTPR-RAAPRFSLRLGPGPAGGFLSNLFRRT 508
Cdd:COG4913 719 EKELEQAEEELDELQDRLEAAEDLARLELRaLLEERFAAALGDAVERELRENLEERI 775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-394 |
8.51e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 51 ALQLQQKEKDLLLAAELGKMLLE--RNEELRRQLE-TLSAQHLERE-ERLQQENHELRRGLAARGAEWEARAVELEGDVE 126
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEakKADEAKKKAEeAKKADEAKKKaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 127 ALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGEN 206
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 207 QM-LQSRRQDLEAQIRG--LREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSAlRRLQRRVSELEEES 283
Cdd:PTZ00121 1606 KMkAEEAKKAEEAKIKAeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-EEDKKKAEEAKKAE 1684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 284 RLQDADVSGASLQSELAHSLEDGDQGQSAEARGDTPTTRSPKTREVSSPQPSPPEEslEPPKKRTSlspAEILEEKEAEV 363
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE--EDKKKAEE---AKKDEEEKKKI 1759
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622916188 364 AKLQDEISLQQAELQS-----LREELQRQKELRAQE 394
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKekeavIEEELDEEDEKRRME 1795
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
145-449 |
1.06e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 145 ERARALSELSEQNLRLSQQ----LAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQI 220
Cdd:pfam10174 447 EKERIIERLKEQREREDRErleeLESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 221 RGLREEVEKGQGRLQTTHEELLLLRR----ERREHNLELE--RARSEAEEALSALRRLQRRVSELEEESRLQDADVSGAS 294
Cdd:pfam10174 527 EQKKEECSKLENQLKKAHNAEEAVRTnpeiNDRIRLLEQEvaRYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 295 L--------QSELAHSLEDGDQGQSAEARGDTPTTRSPKTREVSSPQPSPPEESLEPPKKRTSlspaeILEEKEAEVAKL 366
Cdd:pfam10174 607 SltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQ-----ELDATKARLSST 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 367 QDEISLQQAELQSLREELQRQKElRAQEDPGEALHSALSDRDEAVnKALELSlelnrvSLERDSLYRELLRAIRQKVALT 446
Cdd:pfam10174 682 QQSLAEKDGHLTNLRAERRKQLE-EILEMKQEALLAAISEKDANI-ALLELS------SSKKKKTQEEVMALKREKDRLV 753
|
...
gi 1622916188 447 QEL 449
Cdd:pfam10174 754 HQL 756
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
58-416 |
1.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 58 EKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEwEARAVELEGDVEALRAQLGEQRS 137
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE-DAKRVEIARKAEDARKAEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 138 EQQDSGRERARALSELSEQNLRLSQQLAQASQTEQ-ELQRELDTLRgqcQAQALAGAELRTRLESLQGENQmlQSRRQDl 216
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKaEEERKAEEAR---KAEDAKKAEAVKKAEEAKKDAE--EAKKAE- 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 217 eaQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERA--RSEAEEALSALRRlqRRVSELE---EESRLQDAdvs 291
Cdd:PTZ00121 1247 --EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAeeKKKADEAKKAEEK--KKADEAKkkaEEAKKADE--- 1319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 292 gASLQSELAHSLEDGDQGQSAEARGDTPTTRSPKTREVSSPQPSPPEESLEPPKKRTSLSPAEILEEKEAEVAKlQDEIS 371
Cdd:PTZ00121 1320 -AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-ADEAK 1397
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622916188 372 LQQAELQSLREELQRQKELRAQEDPGEALHSALSDRDEAVNKALE 416
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
76-433 |
1.73e-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: 41.26 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 76 EELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQ----QDSG-------- 143
Cdd:pfam15921 302 EIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERdqfsQESGnlddqlqk 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 144 -----RERARALSELSEQNLRLSQQLAQASQTEQELQRELD--------------TLRGQCQAQalagaeLRTRLESLQG 204
Cdd:pfam15921 382 lladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmevqrleallkAMKSECQGQ------MERQMAAIQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 205 ENQMLQ---SRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNlELERARSEAEEALSALR-RLQRRVSELE 280
Cdd:pfam15921 456 KNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ-EKERAIEATNAEITKLRsRVDLKLQELQ 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 281 ----EESRLQDADVSGASLQSELA----------HSLEDGDQ--GQSAEARGDTPTTRSPKTREVSSPQpsppeeslepp 344
Cdd:pfam15921 535 hlknEGDHLRNVQTECEALKLQMAekdkvieilrQQIENMTQlvGQHGRTAGAMQVEKAQLEKEINDRR----------- 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 345 kkrtslspaeiLEEKEAEVAKLQDEISLQQAELQSLREELQRQKELRAQEDPGEALHSALSDRDEAVNKALELSLELNRV 424
Cdd:pfam15921 604 -----------LELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL 672
|
....*....
gi 1622916188 425 SLERDSLYR 433
Cdd:pfam15921 673 SEDYEVLKR 681
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
73-291 |
1.78e-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: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 73 ERNEELRRQLETLSAQHLEREERLQ--QENHELrRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARAL 150
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEefRQKNGL-VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 151 SELSEqnLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGE-NQMLQSRRQDLEAQIRGLREEVEK 229
Cdd:COG3206 254 DALPE--LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622916188 230 GQGRLQTTHEELLLLRRERRehnlELERARSEAEEALSALRRLQRRVSELEEESRLQDADVS 291
Cdd:COG3206 332 LQAQLAQLEARLAELPELEA----ELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-417 |
1.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 74 RNEELRRQLETLSAQHLEREERLQQENHElRRGLAARGAEwEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSEL 153
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEAARKAEEE-RKAEEARKAE-DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 154 SEQNLRLSQQLAQASqtEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMlQSRRQDLEAQIRGLREEVEKGQGR 233
Cdd:PTZ00121 1261 RMAHFARRQAAIKAE--EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKK 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 234 LQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQDADVSGASLQSELAHSLEDGDQGQSAE 313
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 314 ARGDTPTTRSPKTREVSSPQPSPPEesleppKKRTSLSPAEILEEKEAEVAKLQDEISLQQAELQSLREELQRQKELRAQ 393
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEE------AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
330 340
....*....|....*....|....
gi 1622916188 394 EDPGEALHSALSDRDEAVNKALEL 417
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
49-390 |
2.46e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 49 DLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAAR---GAEWEARAVELEGDV 125
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRrdlGEELEALKTELEDTL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 126 EALRAQlGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQA-SQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQG 204
Cdd:pfam01576 313 DTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMRQKhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 205 ENQMLQSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEE--- 281
Cdd:pfam01576 392 ELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESqlq 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 282 --ESRLQDADVSGASLQSELaHSLEDgDQGQSAEARGDTPTTRSPKTREVSSPQPSPPE------------ESLEPPKKR 347
Cdd:pfam01576 472 dtQELLQEETRQKLNLSTRL-RQLED-ERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDmkkkleedagtlEALEEGKKR 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622916188 348 ---TSLSPAEILEEKEAEVAKLQDEISLQQAELQSLREELQRQKEL 390
Cdd:pfam01576 550 lqrELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQL 595
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
73-228 |
2.63e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 73 ERNEELRRQLETLSAQHLEREERLQ----QENHELRRGLAARgaewearavelegDVEALRAQLGEQRSEQQDSGRERAR 148
Cdd:PRK11281 80 EETEQLKQQLAQAPAKLRQAQAELEalkdDNDEETRETLSTL-------------SLRQLESRLAQTLDQLQNAQNDLAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 149 ALSELSEQNLRLSQ---QLAQASQTEQELQRELD-----------TLRGQCQA-QALAGAELRTRLESLQGENQM---LQ 210
Cdd:PRK11281 147 YNSQLVSLQTQPERaqaALYANSQRLQQIRNLLKggkvggkalrpSQRVLLQAeQALLNAQNDLQRKSLEGNTQLqdlLQ 226
|
170
....*....|....*...
gi 1622916188 211 SRRQDLEAQIRGLREEVE 228
Cdd:PRK11281 227 KQRDYLTARIQRLEHQLQ 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-229 |
3.13e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 50 LALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALR 129
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 130 AQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTE---QELQRELDTLRGQCQA------QALAG-AELRTRL 199
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdlEELERELERLEREIEAlgpvnlLAIEEyEELEERY 797
|
170 180 190
....*....|....*....|....*....|
gi 1622916188 200 ESLQGENQMLQSRRQDLEAQIRGLREEVEK 229
Cdd:COG1196 798 DFLSEQREDLEEARETLEEAIEEIDRETRE 827
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
77-411 |
3.52e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 77 ELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQdsgreraRALSELSEQ 156
Cdd:pfam15921 253 ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYM-------RQLSDLEST 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 157 NLRLSQQLAQASQTEQELQRELDtlrgqcQAQALAGAElrtrLESLQGENQMLQSRRQDLEAQIRGLREEVEKGQGRLQT 236
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELE------KQLVLANSE----LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 237 THEELLLLRRERREHNLELERARSEAEEALSALRRLQRRV----SELEEESRLQDADVSGASLQSELAHSLEDGDQGQSA 312
Cdd:pfam15921 396 EKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLkamkSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 313 EARGDTPTTRSPK-TREVSSPQPSPPEESLEPPKKrtslspaeILEEKEAEVAKLQDEISLQQAELQSLREElqrQKELR 391
Cdd:pfam15921 476 MLRKVVEELTAKKmTLESSERTVSDLTASLQEKER--------AIEATNAEITKLRSRVDLKLQELQHLKNE---GDHLR 544
|
330 340
....*....|....*....|
gi 1622916188 392 AQEDPGEALHSALSDRDEAV 411
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVI 564
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
73-237 |
3.59e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 73 ERNEELRRQLETLSAQHLEREERLQ--QENHELRRGLAARGAewearAVELEGDVEALRAQLGEQRSEQQdsgreraRAL 150
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQklQRLHQAFSRFIGSHL-----AVAFEADPEAELRQLNRRRVELE-------RAL 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 151 SELSEQNLRLSQQLAQASQTEQELQR---------------ELDTLRGQCQAQALAGAELRT---RLESLQGENQMLQSR 212
Cdd:PRK04863 854 ADHESQEQQQRSQLEQAKEGLSALNRllprlnlladetladRVEEIREQLDEAEEAKRFVQQhgnALAQLEPIVSVLQSD 933
|
170 180
....*....|....*....|....*
gi 1622916188 213 RQDLEAqirgLREEVEKGQGRLQTT 237
Cdd:PRK04863 934 PEQFEQ----LKQDYQQAQQTQRDA 954
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
71-479 |
3.67e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 39.89 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 71 LLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARAL 150
Cdd:COG5278 122 ELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 151 SELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKG 230
Cdd:COG5278 202 ALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 231 QGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQDADVSGASLQSELAHSLEDGDQGQ 310
Cdd:COG5278 282 ALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 311 SAEARGDTPTTRSPKTREVSSPQPSPPEESLEPPKKRTSLSPAEILEEKEAEVAKLQDEISLQQAELQSLREELQRQKEL 390
Cdd:COG5278 362 AEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 391 RAQEDPGEALHSALSDRDEAVNKALELSLELNRVSLERDSLYRELLRAIRQKVALTQELEAWQDDMQVVIGQQLRSQRQK 470
Cdd:COG5278 442 LAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAAL 521
|
....*....
gi 1622916188 471 ELNAAASSS 479
Cdd:COG5278 522 AAALASAEL 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-280 |
3.82e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 50 LALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALR 129
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 130 AQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRLESLQGENQML 209
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622916188 210 QSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSA------LRRLQRRVSELE 280
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLeelereLERLEREIEALG 780
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
155-287 |
6.57e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.12 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 155 EQNLRLSQQLAQASQTEQELQRELDTLRGQCQAQA------LAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVE 228
Cdd:PRK11281 80 EETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETretlstLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622916188 229 KGQG-------RLQTTHEELLLLRRERREHNLELeRARSEAEEALSALRRLQRRvSELEEESRLQD 287
Cdd:PRK11281 160 RAQAalyansqRLQQIRNLLKGGKVGGKALRPSQ-RVLLQAEQALLNAQNDLQR-KSLEGNTQLQD 223
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-417 |
7.20e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 74 RNEELRRQLETLSAQHLEREERLQQEN-----HELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERAR 148
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIARKAEdarkaEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 149 ALSELSEQNLRLSQ-QLAQASQTEQELQRELDTLRGQCQAQALAGAELrTRLESLQGENQMLQSRRQDleaQIRGlREEV 227
Cdd:PTZ00121 1215 EEARKAEDAKKAEAvKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM-AHFARRQAAIKAEEARKAD---ELKK-AEEK 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 228 EKGQGRLQTTHEELLLLRRERREHNLELERARSEAEEALSALRRLQRRVSELEEESRLQDADVSGASLQSELAHSLEDGD 307
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 308 QGQSAEARGDTPTTRSpKTREVSSPQPSpPEESLEPPKKRTSLSPAEiLEEKEAEVAKLQDEISLQQAELQSLREELQRQ 387
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKK-KAEEKKKADEA-KKKAEEDKKKADELKKAA-AAKKKADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
330 340 350
....*....|....*....|....*....|
gi 1622916188 388 KELRAQEDPGEALHSALSDRDEAvNKALEL 417
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEA-KKADEA 1475
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
120-429 |
7.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 120 ELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEqnlrLSQQLAQASQTEQELQRELDTLRGQCQAQALAGAELRTRL 199
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 200 ESLQGENQMLQSRRQDLEAQIRGLREEVEKGQGRLQTTHEELLLLRRERREHNLELER-ARSEAEEALSALRRLQRRVSE 278
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 279 LEEEsrLQDADVSGASLQSELAHSLEDGDQGQSAEARGDTPTTRSPKTREVSSPQPSPPEESLEPPKKRTSLSPAEILEE 358
Cdd:COG4372 198 KEEE--LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEE 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622916188 359 KEAEVAKLQDEISLQQAELQSLREELQRQKELRAQEDPGEALHSALSDRDEAVNKALELSLELNRVSLERD 429
Cdd:COG4372 276 EELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
287-390 |
9.91e-03 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 38.34 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 287 DADVSGASlQSELAHSLEDGDQGQSAEARGDTPTTRS--PKTREVSSPQPSPPEESLEPPKKRTSLSPA---------EI 355
Cdd:PTZ00421 369 DEYFSGGN-AEPLVYDMSAVFDGTSPELMGASALSPSgkPRHSGVSVPASTSAMTHSFDDNTSKHADPCamgvkrmdeGI 447
|
90 100 110
....*....|....*....|....*....|....*
gi 1622916188 356 LEEKEAEVAKLQDEISLQQAELQSLREELQRQKEL 390
Cdd:PTZ00421 448 LDERLGRLQALSEKLRTQHEEIKRCREALQKKESI 482
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
62-183 |
9.99e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 38.74 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622916188 62 LLAAELGkmLLERNEELRRQL--------ETLSAQHLEREERLQQENHELRrglAARGAEWEARAVELEGDVEALRAQLG 133
Cdd:PRK11281 196 LLQAEQA--LLNAQNDLQRKSlegntqlqDLLQKQRDYLTARIQRLEHQLQ---LLQEAINSKRLTLSEKTVQEAQSQDE 270
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622916188 134 EQRSE-----QQDSGRERA---------RALSELSEQNLRLSQQLAQASQTEQELQRELDTLRG 183
Cdd:PRK11281 271 AARIQanplvAQELEINLQlsqrllkatEKLNTLTQQNLRVKNWLDRLTQSERNIKEQISVLKG 334
|
|
| |
