|
Name |
Accession |
Description |
Interval |
E-value |
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
746-860 |
7.42e-46 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 159.63 E-value: 7.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 746 SVSTVAAGPSVQVVERMSTTIRRLESERAAFKDEIVRLTAQRDEARQEVVELMREVEEKRKCDQRIQELEATVEQLDQRY 825
Cdd:pfam12325 1 SVSTSGAGPSVQLVERLSSTIRRLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRY 80
|
90 100 110
....*....|....*....|....*....|....*
gi 240279359 826 QTTLEMLGEKSELVEELKADISDLKKIYRELVDST 860
Cdd:pfam12325 81 ETTLELLGEKSEEVEELKADVEDLKEMYREQVQQL 115
|
|
| TMF_DNA_bd |
pfam12329 |
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA ... |
271-344 |
8.53e-21 |
|
TATA element modulatory factor 1 DNA binding; This is the middle region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes that contains at its N-terminal section a number of leucine zippers that could potentially form coiled coil structures.. The whole proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells.
Pssm-ID: 372049 [Multi-domain] Cd Length: 74 Bit Score: 86.98 E-value: 8.53e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240279359 271 GSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAE 344
Cdd:pfam12329 1 SSLEKLLKEKDEQIAQLMEEGEKLSKKELKLNNTIKKLRAKNKELEKEIAELKKKLEKLEKELENLEERLKRAE 74
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
302-616 |
2.67e-16 |
|
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: 83.95 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 302 RATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAeiaeQKALERLN-SVSKAEKQLETATAEREASNATITD 380
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL----RKELEELSrQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 381 LKSQLARA-VSRAEAAERKARMEATEAE-KRQIAELRDDLSSAKIEREISEE---KLRREIRDLKEGIEREKERARIREI 455
Cdd:TIGR02168 752 LSKELTELeAEIEELEERLEEAEEELAEaEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 456 ELRGEQSVLESKMESLRSRAEEVSSSAtgESHAKLLRQIEVLQTQYAVASEnwhgiegsliaRLTAVETERDELERREGD 535
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLA--AEIEELEELIEELESELEALLN-----------ERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 536 LRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLvvkQDLAKQKEAELTLIQRLEEERA 615
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL---EEAEALENKIEDDEEEARRRLK 975
|
.
gi 240279359 616 R 616
Cdd:TIGR02168 976 R 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-616 |
1.43e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 321 ETKKRLEKVEKDLVNAEDRVS-----------QAEIAEQ-----------KALERLNSVSKAEKQLETATAEREASNATI 378
Cdd:COG1196 176 EAERKLEATEENLERLEDILGelerqleplerQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 379 TDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRReiRDLKEGIEREKERARIREIELR 458
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR--RELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 459 GEQSVLESKMESLRSRAEEVSSSAtgESHAKLLRQIEVLQTQYAVASENWHGIEGSLIARLTAVETERDELERREGDLRR 538
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAE--AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240279359 539 KAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERAR 616
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
219-633 |
1.22e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 219 AQMRADHEMSELRWQEELHAYVERIDALQSKLK-YLAKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKLSKT 297
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEeLEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 298 ELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAEREASNAT 377
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 378 ITDLKSQLARAVSRAEAAERKAR---------MEATEAEKRQIAELRDDLSSAKIEREISEE------------------ 430
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAarllllleaEADYEGFLEGVKAALLLAGLRGLAGAVAVLigveaayeaaleaalaaa 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 431 ---KLRREIRDLKEGIEREKERA-------RIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQ 500
Cdd:COG1196 548 lqnIVVEDDEVAAAAIEYLKAAKagratflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 501 YAVASENWHGIEGSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTR 580
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 240279359 581 KLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARRPSSPFLQEPP 633
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-623 |
1.35e-13 |
|
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: 75.09 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 321 ETKKRLEKVEKDLVNAEDRVSQAEiaeqKALERLnsvskaEKQLETATAEREasnatITDLKSQLARAVSRAEAAERKAR 400
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELE----RQLKSL------ERQAEKAERYKE-----LKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 401 MEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDLkegiEREKERARIREIELRGEQSVLESKMESLRSRAEEVSS 480
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL----EEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 481 S--ATGESHAKLLRQIEVLQTQYAVASENWHGIEG---SLIARLTAVETERDELERREGDL-------RRKAREASLKAK 548
Cdd:TIGR02168 317 QleELEAQLEELESKLDELAEELAELEEKLEELKEeleSLEAELEELEAELEELESRLEELeeqletlRSKVAQLELQIA 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240279359 549 KVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTkaENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
302-586 |
1.84e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 74.72 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 302 RATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAED-RVSQAEIAEQKALERLNSVSKAEKQLETATAEREASNATITD 380
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 381 LKSQLARAVSRAEAAER--------------------KARMEATEAE----KRQIAELRDDLSSAKIEREISEEKLRREI 436
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQlleelnkkikdlgeeeqlrvKEKIGELEAEiaslERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 437 RDlKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSA--TGESHAKLLRQIEVLQTQYAVASENWHGIEGS 514
Cdd:TIGR02169 336 AE-IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaeTRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240279359 515 LIARLTAVETERDELERREGD---LRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAE 586
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKineLEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
276-624 |
3.82e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 276 KLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLN 355
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 356 SVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELRD-----DLSSAKIEREISEE 430
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaeaeEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 431 KLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHA---------KLLRQIEVLQTQY 501
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEeaeleeeeeALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 502 AVASENWHGIEGSLIARLTAVETERDELERREGDLR-RKAREASLKAKKVEGELENSRAVIQEIERNLEASkqEIQNLTR 580
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA--LAAALQN 550
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 240279359 581 KLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARRP 624
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-623 |
5.83e-13 |
|
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: 73.17 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 346 AEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLaravSRAEAAERKARMEATEAEkRQIAELRDDLSSAKIER 425
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL----EELEEELEQLRKELEELS-RQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 426 EISEEKLRREIRDLKEGIEREKERARIREiELRGEQSVLESKMESLRSRAEEVSssatgESHAKLLRQIEVLQTQYAVAS 505
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLK-----EELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 506 ENWHgiegSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEI---------- 575
Cdd:TIGR02168 817 EEAA----NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERasleealall 892
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 240279359 576 ----QNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:TIGR02168 893 rselEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-614 |
1.02e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 215 EEAMAQMRADHEMSELRwQEELHAYVERIDALQSKLKYLAKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKL 294
Cdd:COG1196 383 ELAEELLEALRAAAELA-AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 295 SKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNS---------VSKAEKQLE 365
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgavavligvEAAYEAALE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 366 TATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIA------------------ELRDDLSSAKIEREI 427
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALaaalargaigaavdlvasDLREADARYYVLGDT 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 428 SEEKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVASEN 507
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 508 WHGIEGSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKL----- 582
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIealgp 781
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 240279359 583 -----------TKAENDFLVV-KQDLAKQKEAELTLIQRLEEER 614
Cdd:COG1196 782 vnllaieeyeeLEERYDFLSEqREDLEEARETLEEAIEEIDRET 825
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-623 |
1.72e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 215 EEAMAQMRADHEMSELRWQEELHA-YVERIDALQSKLKYLAKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQK 293
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEElAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 294 LSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAE------IAEQKALERLNSVSKAEKQLETA 367
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarllllLEAEADYEGFLEGVKAALLLAGL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 368 TAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDLKEGIEREK 447
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 448 ERARIREiELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVASENWHGIEGSLIARLTAVETERD 527
Cdd:COG1196 600 AVDLVAS-DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 528 ELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQN-LTRKLTKAENDFLVVKQDLAKQKEAELTL 606
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEqLEAEREELLEELLEEEELLEEEALEELPE 758
|
410
....*....|....*..
gi 240279359 607 IQRLEEERARWQELARR 623
Cdd:COG1196 759 PPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
215-623 |
2.18e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 215 EEAMAQMRADHEMSELRW---QEELHAYVERIDALQSKLKYLA-KEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEE 290
Cdd:COG1196 266 EAELEELRLELEELELELeeaQAEEYELLAELARLEQDIARLEeRRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 291 GQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAE 370
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 371 REASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELR--------DDLSSAKIEREISEEKLRREIRDLKEG 442
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEeaalleaaLAELLEELAEAAARLLLLLEAEADYEG 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 443 IER-------------------------EKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVL 497
Cdd:COG1196 506 FLEgvkaalllaglrglagavavligveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 498 QTQYAVASENWHGIEGSLIARLTAVETER-----DELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASK 572
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARyyvlgDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 240279359 573 QEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
240-631 |
2.37e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 240 VERIDALQSKLKYLAKEAAESAKNAAASAEAGSLEKKLLE--KDEQIANLMEEGQKLSktELDHRATIKKLrqsiAESAK 317
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKAD--EAKKKAEEAKK----AEEAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 318 SQAETKKRLEKVEKdlvNAEDRvSQAEIAEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAER 397
Cdd:PTZ00121 1464 KKAEEAKKADEAKK---KAEEA-KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 398 KARMEATEAEK-RQIAELRDDLSSAKIEREISEEKlRREIRDLKEGIEREKERARIREIELRGEQSVLES-----KMESL 471
Cdd:PTZ00121 1540 KKAEEKKKADElKKAEELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeakKAEEA 1618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 472 RSRAEEVSSSATGESHAKLLRQI---EVLQTQYAVASENWHGIEGSLIARLTAVETERDELERREGDLRRKAREASLKAK 548
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKeaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 549 KVEGELENSRAVIQEIERNLEASK--QEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARRPSS 626
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKkaEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
....*
gi 240279359 627 PFLQE 631
Cdd:PTZ00121 1779 AVIEE 1783
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
215-623 |
5.90e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 215 EEAMAQMRADHEMSELRWQEELHAYVERIDALQSKLKYLAKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKL 294
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 295 SKTELDHRATIKK----LRQSIAESAKSQAETKKRLEKVEK--DLVNAEDRVSQAEIAEQKALERLNS---VSKAEKQLE 365
Cdd:PTZ00121 1379 KADAAKKKAEEKKkadeAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKK 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 366 TATAEREASNATITDLKSQLARAVSRAEAAERKA---RMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDLKEG 442
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAeeaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 443 IEREKERARIREIELRGEQSVLESKMESLRSRAEEvSSSATGESHAKLLRQIEVlqtqyavasenwhgiegsliARLTAV 522
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE-EDKNMALRKAEEAKKAEE--------------------ARIEEV 1597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 523 ETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQeiqnlTRKLTKAENDFLVVKQDLAKQKEA 602
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-----AEELKKAEEENKIKAAEEAKKAEE 1672
|
410 420
....*....|....*....|....*
gi 240279359 603 ELTLIQRL----EEERARWQELARR 623
Cdd:PTZ00121 1673 DKKKAEEAkkaeEDEKKAAEALKKE 1697
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
308-501 |
7.31e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 62.73 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 308 LRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQ-------AEIAEQKALErLNSVSKAEKQLETATAEREASNATITD 380
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglVDLSEEAKLL-LQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 381 LKSQLARAVSRAEAAERKARMEATEAE----KRQIAELRDDLS-------SAKIEREISEEKLRREIRDLKEGIEREKER 449
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQlaelEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 240279359 450 ARIREIELRGEQSVLESKMESLRSRAEEVsssatgeshAKLLRQIEVLQTQY 501
Cdd:COG3206 325 LQAREASLQAQLAQLEARLAELPELEAEL---------RRLEREVEVARELY 367
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
241-623 |
1.81e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 241 ERIDALQSKLKYLAKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQA 320
Cdd:PRK03918 259 EKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 321 ---ETKKRLEKVEKDLVNAEDRVSQAEIAEQKaLERLNSVSK----------------AEKQLETATAEREASNATITDL 381
Cdd:PRK03918 339 rleELKKKLKELEKRLEELEERHELYEEAKAK-KEELERLKKrltgltpeklekeleeLEKAKEEIEEEISKITARIGEL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 382 KS---QLARAVSRAEAAERKA---RMEATEAEKRQI-----AELRDdLSSAKIEREISEEKLRREIRDLKegIEREKERA 450
Cdd:PRK03918 418 KKeikELKKAIEELKKAKGKCpvcGRELTEEHRKELleeytAELKR-IEKELKEIEEKERKLRKELRELE--KVLKKESE 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 451 RIREIELRGEQSVLESKMESLRsrAEEVSSSAtgESHAKLLRQIEVLQTQYAVASENWHGIEGsLIARLTAVETERDELE 530
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKKYN--LEELEKKA--EEYEKLKEKLIKLKGEIKSLKKELEKLEE-LKKKLAELEKKLDELE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 531 RREGDLRRKAREASLKA-KKVEGELENSRAVIQEIERnLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKeaeltliQR 609
Cdd:PRK03918 570 EELAELLKELEELGFESvEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELAETE-------KR 641
|
410
....*....|....
gi 240279359 610 LEEERARWQELARR 623
Cdd:PRK03918 642 LEELRKELEELEKK 655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-850 |
2.52e-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: 61.23 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 314 ESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKA-LERLNS-VSKAEKQLETATAEREASNATITDLKSQLARAVSR 391
Cdd:TIGR02168 203 KSLERQAEKAERYKELKAELRELELALLVLRLEELREeLEELQEeLKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 392 AEAAERK-----ARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRR----------EIRDLKEGIEREKERARIREIE 456
Cdd:TIGR02168 283 IEELQKElyalaNEISRLEQQKQILRERLANLERQLEELEAQLEELESkldelaeelaELEEKLEELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 457 LRGEQSVLESKMESLRSRAEEVSSSAtgeshAKLLRQIEVLQTQYAVASenwhgiegsliARLTAVETERDELERREGDL 536
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLETLRSKV-----AQLELQIASLNNEIERLE-----------ARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 537 RRKAREAslKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQDLAkQKEAELTLIQRLEE---- 612
Cdd:TIGR02168 427 LKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA-QLQARLDSLERLQEnleg 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 613 --ERARWQELARRPSSPFLqePPTGSPITFNRKQTA------GPDPTRPMSDRALSRRS--SSIPPALFSELTTPPYQNH 682
Cdd:TIGR02168 504 fsEGVKALLKNQSGLSGIL--GVLSELISVDEGYEAaieaalGGRLQAVVVENLNAAKKaiAFLKQNELGRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 683 FSPTNSNPQQPRITPSHEFSGDLTHAQTYEPE-----EYFNGMSTPVTPSAQGT---HTLTHHSRGV---NDIISVSTVA 751
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalSYLLGGVLVVDDLDNALelaKKLRPGYRIVtldGDLVRPGGVI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 752 AGPSVQ----VVERmSTTIRRLESERAAFKDEIVRLTAQRDEARQEVVELMREVEEKRK--------------------- 806
Cdd:TIGR02168 662 TGGSAKtnssILER-RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrqisalrkdlarlea 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 240279359 807 ----CDQRIQELEATVEQLDQRYQTTLEMLGEKSEL-------VEELKADISDLK 850
Cdd:TIGR02168 741 eveqLEERIAQLSKELTELEAEIEELEERLEEAEEElaeaeaeIEELEAQIEQLK 795
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
233-623 |
2.92e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 233 QEELHAYVERIDALQSKLKYLAKEAAE---SAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKLSKTELD---HRATIK 306
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKlekLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEleeLEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 307 KLRQSIAESAKS-QAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLEtATAEREASNATITDLKSQL 385
Cdd:COG4717 174 ELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERLKEARLLL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 386 ----------ARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDL-KEGIEREKERARIRE 454
Cdd:COG4717 253 liaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELeEEELEELLAALGLPP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 455 IELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVASENwhgiegSLIARLTAVEtERDELERREG 534
Cdd:COG4717 333 DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAE-EYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 535 DLRRK--AREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFlvvkQDLAKQKEAElTLIQRLEE 612
Cdd:COG4717 406 ELEEQleELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL----EQLEEDGELA-ELLQELEE 480
|
410
....*....|.
gi 240279359 613 ERARWQELARR 623
Cdd:COG4717 481 LKAELRELAEE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-575 |
3.35e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 301 HRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQ-KALERLNSVSKAEKqLETATAEREASNATIT 379
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlKELEEKLKKYNLEE-LEKKAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 380 DLKSQLARAVSRAE-AAERKARMEATEAEKRQIAELRDDL----------SSAKIEREISE-EKLRR---EIRDLKEGIE 444
Cdd:PRK03918 536 KLKGEIKSLKKELEkLEELKKKLAELEKKLDELEEELAELlkeleelgfeSVEELEERLKElEPFYNeylELKDAEKELE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 445 REKERARIREIEL---RGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAvasenwhgiegSLIARLTA 521
Cdd:PRK03918 616 REEKELKKLEEELdkaFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELA-----------GLRAELEE 684
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 240279359 522 VETERDELERREGDLRRKAREASLKAKKVEgELENSRAVIQEIERNLEASKQEI 575
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKALERVEELREKVKKYKALL 737
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
233-621 |
4.18e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 233 QEELHAYVERIDALQSKLKYLAKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKLSKTELD---HRATIKKLR 309
Cdd:COG4717 97 LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEEleeLEAELAELQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 310 QSIAESAKS-QAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLEtATAEREASNATITDLKSQL--- 385
Cdd:COG4717 177 EELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAALEERLKEARLLLlia 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 386 -------ARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDL-KEGIEREKERARIREIEL 457
Cdd:COG4717 256 aallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELeEEELEELLAALGLPPDLS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 458 RGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVASENwhgiegSLIARLTAVEtERDELERREGDLR 537
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAE-EYQELKEELEELE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 538 RK--AREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQD--LAKQKEAELTLIQRLEEE 613
Cdd:COG4717 409 EQleELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELREL 488
|
....*...
gi 240279359 614 RARWQELA 621
Cdd:COG4717 489 AEEWAALK 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
274-601 |
4.60e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 274 EKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEiaeqkalER 353
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-------EL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 354 LNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKAR----MEATEAEKRQIAELRDDLSSAKIEREISE 429
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkeLKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 430 EKLRREIRDLKEGI-EREKERARIREI-----ELRGEQSVLESKME------SLRSRAEEVSSSATGESHAKLLRQIEVL 497
Cdd:PRK03918 317 SRLEEEINGIEERIkELEEKEERLEELkkklkELEKRLEELEERHElyeeakAKKEELERLKKRLTGLTPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 498 QTqyavasenwhgiegsliaRLTAVETERDELERREGDL------RRKAREASLKAKKV------EGELENSRAVIQEIE 565
Cdd:PRK03918 397 EK------------------AKEEIEEEISKITARIGELkkeikeLKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYT 458
|
330 340 350
....*....|....*....|....*....|....*.
gi 240279359 566 RNLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKE 601
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
273-569 |
5.84e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 273 LEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSI-AESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKAL 351
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 352 ERLnsvSKAEKQLETATAEREASNATITDLKSQlaRAVSRAEAAERKARMEATEAEKRQI----AELRDDLSSAKIEREi 427
Cdd:TIGR02169 322 ERL---AKLEAEIDKLLAEIEELEREIEEERKR--RDKLTEEYAELKEELEDLRAELEEVdkefAETRDELKDYREKLE- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 428 seeKLRREIRDLKEGIER---EKERARIREIELRGEQSVLESKMESLRSRAEEVsssatGESHAKLLRQIEVLQTQYAVA 504
Cdd:TIGR02169 396 ---KLKREINELKRELDRlqeELQRLSEELADLNAAIAGIEAKINELEEEKEDK-----ALEIKKQEWKLEQLAADLSKY 467
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240279359 505 SEnwhgiegsliaRLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLE 569
Cdd:TIGR02169 468 EQ-----------ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-623 |
8.36e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 203 VTEPTETSTDDYEEAMAQMRADHEMSELRWQEELHAYVERIDALQSKLKYLAKEAAESAKNAAASAEAGSLEKKLLEKDE 282
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 283 QIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRvsqAEIAEQKALERLNSVSKAEK 362
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 363 QLETATAEREASNATITDLKSqlARAVSRAEAAERKARMEATEA-EKRQIAELRDDLSSAKIEREIseEKLRREIRDLKE 441
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAeEKKKADEAKKKAEEAKKADEA--KKKAEEAKKAEE 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 442 GIEREKERARIREIELRGEQSV----LESKMESLRSRAEEVSSSATGESHAKLLRQIEvlqtQYAVASENWHGIEGSLIA 517
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE----EAKKADEAKKAEEAKKAD 1537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 518 RLTAVETERDELERREGDLRRKAREA-SLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQDL 596
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
410 420
....*....|....*....|....*..
gi 240279359 597 AKQKEAELtliQRLEEERARWQELARR 623
Cdd:PTZ00121 1618 AKIKAEEL---KKAEEEKKKVEQLKKK 1641
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
275-850 |
1.23e-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: 58.91 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 275 KKLLEKDEQIANLMEEGQKLSKTELdhRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERL 354
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEEL--REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 355 NS----VSKAEKQLETATAEREASNATITDLKSQLARAVSRA-EAAERKARMEATEAE-KRQIAELRDDLSSAKIEREIS 428
Cdd:TIGR02168 291 YAlaneISRLEQQKQILRERLANLERQLEELEAQLEELESKLdELAEELAELEEKLEElKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 429 EEKLRreirDLKEGIEREkeRARIREIE-----LRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAV 503
Cdd:TIGR02168 371 ESRLE----ELEEQLETL--RSKVAQLElqiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 504 ASENWHGIEGSLIARLTAVETERDELErregdlrrKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLT 583
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELE--------EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 584 KAENDFLVVKQDLAKQKEAELTLIQRLEEeraRWQELARRPSSPFLQEpptgspITFNRKQTAG---------PDPTRPM 654
Cdd:TIGR02168 517 GLSGILGVLSELISVDEGYEAAIEAALGG---RLQAVVVENLNAAKKA------IAFLKQNELGrvtflpldsIKGTEIQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 655 SDRALSRRSSSIPPALFSELTT--PPYQNHFSP-----------TNSNPQQPRITPSHEF---SGDLTH---AQTYEPEE 715
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKDLVKfdPKLRKALSYllggvlvvddlDNALELAKKLRPGYRIvtlDGDLVRpggVITGGSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 716 YFNGM------------------------STPVTPSAQGTHTLTHHSRGVNDIISVSTVAAGPSVQVVERMSTTIRRLES 771
Cdd:TIGR02168 668 TNSSIlerrreieeleekieeleekiaelEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240279359 772 ERAAFKDEIVRLTAQRDEARQEVVELMREVEEkrkCDQRIQELEATVEQLDQRYQTTLEMLGEKSELVEELKADISDLK 850
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-490 |
1.65e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 272 SLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVS--QAEIAEQK 349
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAelRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 350 AL--ERLNSVSKAEKQLETATAEReASNATITDLKSQLARAVSRAeaaeRKARMEATEAEKRQIAELRDDLSSAKIEREI 427
Cdd:COG4942 104 EElaELLRALYRLGRQPPLALLLS-PEDFLDAVRRLQYLKYLAPA----RREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240279359 428 SEEKLRREIRDLKE----------GIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKL 490
Cdd:COG4942 179 LLAELEEERAALEAlkaerqkllaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
272-620 |
2.06e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 272 SLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSI----AESAKSQAETK---KRLEKVEKDLVNAEDRVSQAE 344
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERddllAEAGLDDADAEaveARREELEDRDEELRDRLEECR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 345 IAEQKALERLNSVSKAEKQLET---------ATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELR 415
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEEraeelreeaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 416 DDLSSAKIEREISEEKLRREIRDLKEGIErekERARIREI--------------------ELRGEQSVLESKMESLRSRA 475
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVE---EAEALLEAgkcpecgqpvegsphvetieEDRERVEELEAELEDLEEEV 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 476 EEVSSS-ATGESHAKLLRQIEVLQTQYAVASEnwhgiegsLIA----RLTAVETERDELERREGDLRRKAREASLKAKKV 550
Cdd:PRK02224 492 EEVEERlERAEDLVEAEDRIERLEERREDLEE--------LIAerreTIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 551 EGELENSRAVIQEIERNLEASKQEIQNLTRkltkaendflvVKQDLAKQKEAELTlIQRLEEERARWQEL 620
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLER-----------IRTLLAAIADAEDE-IERLREKREALAEL 621
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
306-586 |
2.37e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 306 KKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLnsvSKAEKQLETATAEREASNATITDLKSQL 385
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI---GEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 386 -----ARAVSRAEAAERKARMEATEAekrQIAELRDDLssAKIEREISEEK---LRREIRDLKEgiEREKERARIREIEL 457
Cdd:TIGR02169 747 ssleqEIENVKSELKELEARIEELEE---DLHKLEEAL--NDLEARLSHSRipeIQAELSKLEE--EVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 458 RGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAvasenwhgiegSLIARLTAVETERDELERREGDLR 537
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-----------ELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 240279359 538 RKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAE 586
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
214-547 |
2.67e-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: 57.77 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 214 YEEAMAQMRADH---EMSELRWQEELHAYVERIDALQSKLKYLAKEAAESAKNAAAsaeagsLEKKLLEKDEQIANLMEE 290
Cdd:TIGR02169 672 EPAELQRLRERLeglKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ------LEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 291 GQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKAL------------ERLNSVS 358
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEvsriearlreieQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 359 KAEKQLETATAEREASNATITDLKSQLARAV--SRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREI 436
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 437 RDLKEGIEREKERARIREIELrgeQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIE-VLQTQYAVASENWHGIE--- 512
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKL---EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQrVEEEIRALEPVNMLAIQeye 982
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 240279359 513 ------GSLIARLTAVETERDELERREGDLRRKAREASLKA 547
Cdd:TIGR02169 983 evlkrlDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
355-628 |
5.70e-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: 55.93 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 355 NSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKArmeatEAEKRQIAELRDDLssAKIEREISEekLRR 434
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-----AALARRIRALEQEL--AALEAELAE--LEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 435 EIRDLKEGIEREKER--ARIREIELRGEQSVLESKMESlrsraeevsssatgESHAKLLRQIEVLQTqyavasenwhgIE 512
Cdd:COG4942 91 EIAELRAELEAQKEElaELLRALYRLGRQPPLALLLSP--------------EDFLDAVRRLQYLKY-----------LA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 513 GSLIARLTAVETERDELERREGDLRRKAREaslkakkvegeLENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVV 592
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELEAERAE-----------LEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
250 260 270
....*....|....*....|....*....|....*.
gi 240279359 593 KQDLAKQKEAELTLIQRLEEERARwqELARRPSSPF 628
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAA--AAERTPAAGF 248
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
327-638 |
1.42e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 327 EKVEKDLVNAEDRV-SQAEIAEQKAL-ERLNSVSKAEKQ----LETATAEREASNATITDLKSQLAravsraEAAERKAR 400
Cdd:PRK02224 179 ERVLSDQRGSLDQLkAQIEEKEEKDLhERLNGLESELAEldeeIERYEEQREQARETRDEADEVLE------EHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 401 MEATEAEkrqIAELRDDLSSAKIEREiseeKLRREIRDLKEGIE--REKERARIREIEL-RGEQSVLESKMESLRSRAEE 477
Cdd:PRK02224 253 LETLEAE---IEDLRETIAETERERE----ELAEEVRDLRERLEelEEERDDLLAEAGLdDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 478 VSssatgeshakllrqiEVLQTQYAVASENWHGIEGsliarltavETER-DELERREGDLRRKAREASLKAKKVEGELEN 556
Cdd:PRK02224 326 LR---------------DRLEECRVAAQAHNEEAES---------LREDaDDLEERAEELREEAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 557 SRAVIQEIERNLEASKQEIQNLTRKLTKAE--NDFLVVKQDLAKQKEAEL-TLIQRLEEERARWQELARRPSSPFLQEPP 633
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEdfLEELREERDELREREAELeATLRTARERVEEAEALLEAGKCPECGQPV 461
|
....*
gi 240279359 634 TGSPI 638
Cdd:PRK02224 462 EGSPH 466
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
274-619 |
2.73e-07 |
|
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: 54.41 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 274 EKKLLEK--DEQIANLMEEGQK---LSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVS--QAEIA 346
Cdd:pfam01576 153 ERKLLEEriSEFTSNLAEEEEKaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAelQAQIA 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 347 EQKAlerlnSVSKAEKQLETA-------TAEREASNATITDLKSQLARAVSRAEaAERKARMEAtEAEKRQIA------- 412
Cdd:pfam01576 233 ELRA-----QLAKKEEELQAAlarleeeTAQKNNALKKIRELEAQISELQEDLE-SERAARNKA-EKQRRDLGeelealk 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 413 -ELRDDLSSAKIEREIsEEKLRREIRDLKEGIEREKERARIREIELRGEQSvleSKMESLRSRAEEVSSSATGESHAKLL 491
Cdd:pfam01576 306 tELEDTLDTTAAQQEL-RSKREQEVTELKKALEEETRSHEAQLQEMRQKHT---QALEELTEQLEQAKRNKANLEKAKQA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 492 RQIEVLQTQYAVASENWHGIEGSliARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEAS 571
Cdd:pfam01576 382 LESENAELQAELRTLQQAKQDSE--HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 240279359 572 KQEIQNLTRKLTKAENdflvVKQDLAKQKEAELTLIQRLEEERARWQE 619
Cdd:pfam01576 460 SKDVSSLESQLQDTQE----LLQEETRQKLNLSTRLRQLEDERNSLQE 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
233-453 |
3.16e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 233 QEELHAYVERIDALQSKLKYLAKEAAesaknaaasaeagSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSI 312
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEK-------------ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 313 AESAKSQAETKKRLEKVEKDLVNAEDR------VSQAEIAE-QKALERLNSVSKA-EKQLETATAEREASNATITDLKSQ 384
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDaVRRLQYLKYLAPArREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240279359 385 LAR-AVSRAEAAERKARMEATEAEKRQ-IAELRDDLSSAKIEREISEEKlRREIRDLKEGIEREKERARIR 453
Cdd:COG4942 173 RAElEALLAELEEERAALEALKAERQKlLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
370-626 |
3.75e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 370 EREASNATITDLKSQLARaVSRAEAAERKARmeateaEKR----QIAELRDDLSSAKIEREISEEkLRREIRDlkEGIER 445
Cdd:COG4913 219 EEPDTFEAADALVEHFDD-LERAHEALEDAR------EQIellePIRELAERYAAARERLAELEY-LRAALRL--WFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 446 EKERARIREIELRGEQSVLESKMESLRSRAEEvsssatgeshakLLRQIEVLQTQYAvasenwhGIEGSLIARLtavETE 525
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDA------------LREELDELEAQIR-------GNGGDRLEQL---ERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 526 RDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAelt 605
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE--- 423
|
250 260
....*....|....*....|.
gi 240279359 606 liqrLEEERARwqeLARRPSS 626
Cdd:COG4913 424 ----LEAEIAS---LERRKSN 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
305-619 |
3.87e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 305 IKKLRQSIAESAKSQAETK----KRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAEREASNATITD 380
Cdd:COG4717 48 LERLEKEADELFKPQGRKPelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 381 LKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDLKEGIE-------REKERARIR 453
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeelqdlaEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 454 EIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQ----------IEVLQTQYAVASENWHGIEGSLIARLTAVE 523
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 524 TERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKaendfLVVKQDLAKQKEAE 603
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE-----LQELLREAEELEEE 362
|
330
....*....|....*.
gi 240279359 604 LTLIQRLEEERARWQE 619
Cdd:COG4717 363 LQLEELEQEIAALLAE 378
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
272-612 |
6.44e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 272 SLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAE--IAEQK 349
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEkqLNQLK 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 350 A-LERLNS-------------VSKAEKQLETATAEREASNATITDLKSQLARAVSraeaaERKARMEATEAEKRQIAELR 415
Cdd:TIGR04523 295 SeISDLNNqkeqdwnkelkseLKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-----ELTNSESENSEKQRELEEKQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 416 DDLSsaKIEREISE-----EKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKME------SLRSRAEEVSSSATG 484
Cdd:TIGR04523 370 NEIE--KLKKENQSykqeiKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKeierlkETIIKNNSEIKDLTN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 485 ESHAK-------------LLRQIEVLQTQYAVASENWHGIE----------GSLIARLTAVETERDELERREGDLRRKAR 541
Cdd:TIGR04523 448 QDSVKeliiknldntresLETQLKVLSRSINKIKQNLEQKQkelkskekelKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 542 EASLKAKKVEGEL----------------ENSRAVIQEIERNLEASKQEIQNLTRKLTKaendflvvKQDLAKQKEAE-L 604
Cdd:TIGR04523 528 KLESEKKEKESKIsdledelnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEE--------KQELIDQKEKEkK 599
|
....*...
gi 240279359 605 TLIQRLEE 612
Cdd:TIGR04523 600 DLIKEIEE 607
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
210-851 |
8.09e-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: 53.14 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 210 STDDYEEAMAQMRAdHEMSELRWQEELHAYVERIDALQSKLKYL--------AKEAAESAKNAAASAEAGSLEKKLLEKD 281
Cdd:TIGR02168 230 LVLRLEELREELEE-LQEELKEAEEELEELTAELQELEEKLEELrlevseleEEIEELQKELYALANEISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 282 EQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAE---IAEQKALERLNS-V 357
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrlEELEEQLETLRSkV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 358 SKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRReIR 437
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE-LR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 438 DLKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEV-----SSSATGESHAKLLRQIEVlQTQYAVASEN----- 507
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkallkNQSGLSGILGVLSELISV-DEGYEAAIEAalggr 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 508 --------------------------WHGIEGSLIARLTAVETERDELERREGDLRRKAR--EASLKAKKV--------- 550
Cdd:TIGR02168 547 lqavvvenlnaakkaiaflkqnelgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRKAlsyllggvl 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 551 ------------------------EGELENSRAVI---------------QEIERN---LEASKQEIQNLTRKLTKAEND 588
Cdd:TIGR02168 627 vvddldnalelakklrpgyrivtlDGDLVRPGGVItggsaktnssilerrREIEELeekIEELEEKIAELEKALAELRKE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 589 FLVVKQDLAKQKEAELTLIQRLEEERARWQELARRPSSPFLQEPPTGSPITFNRKQTAGPDPTRPMSDRALSRRSSSIpp 668
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-- 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 669 alfsELTTPPYQNHFSPTNSNPQQPRitpshEFSGDLT------HAQTYEPEEYFNGMS---TPVTPSAQGTHTLTHHSR 739
Cdd:TIGR02168 785 ----EELEAQIEQLKEELKALREALD-----ELRAELTllneeaANLRERLESLERRIAateRRLEDLEEQIEELSEDIE 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 740 GVNDIISVSTVAAGPSVQVVERMSTTIRRLESERAAFKDEIVRLTAQRDEARQEVVELMREVEEKR----KCDQRIQELE 815
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELReklaQLELRLEGLE 935
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 240279359 816 ATVEQLDQR----YQTTLEMLGEKSELVE----ELKADISDLKK 851
Cdd:TIGR02168 936 VRIDNLQERlseeYSLTLEEAEALENKIEddeeEARRRLKRLEN 979
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
275-612 |
8.48e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.13 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 275 KKLLEKDEQIANLMEEGQKLSKTELDHRAT-IKKLRQSIA-ESAKSQAETK---KRLE------KVEKDLVNAEDrvSQA 343
Cdd:TIGR01612 1361 KKIIDEVKEYTKEIEENNKNIKDELDKSEKlIKKIKDDINlEECKSKIESTlddKDIDecikkiKELKNHILSEE--SNI 1438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 344 EIAEQKALERLNSVSKAEKQLETATAERE------ASNAT------ITDLKSQLARAVSRAEAAERKARM-----EATEA 406
Cdd:TIGR01612 1439 DTYFKNADENNENVLLLFKNIEMADNKSQhilkikKDNATndhdfnINELKEHIDKSKGCKDEADKNAKAieknkELFEQ 1518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 407 EKRQIAELRDDLSSAKIEREISEEK-----LRREIRDLKEGIEREKERArireielrgEQSVLESKMESLRSRAEEVSSS 481
Cdd:TIGR01612 1519 YKKDVTELLNKYSALAIKNKFAKTKkdseiIIKEIKDAHKKFILEAEKS---------EQKIKEIKKEKFRIEDDAAKND 1589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 482 ATGESHAKLLRQIEVLQTQYAVASENWHGIEGSLiarltaveTERDELERREGDLRRKAREASLKAKKVE-GELENSRAV 560
Cdd:TIGR01612 1590 KSNKAAIDIQLSLENFENKFLKISDIKKKINDCL--------KETESIEKKISSFSIDSQDTELKENGDNlNSLQEFLES 1661
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 240279359 561 IQEIERNLEASKQEIQNLTRKLTKAENDflvVKQdlaKQKEAELTLIQRLEE 612
Cdd:TIGR01612 1662 LKDQKKNIEDKKKELDELDSEIEKIEID---VDQ---HKKNYEIGIIEKIKE 1707
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
300-586 |
1.48e-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: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 300 DHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNsVSKAEKQLETATAER---EASNA 376
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELerlDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 377 TITDLKSQLARAVSRAEAAERKArmeatEAEKRQIAELRDDLSSAkiereiseEKLRREIRDLKEGIEREKERARIREIE 456
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEEL-----DELKGEIGRLEKELEQA--------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 457 LRGEQSVLESKMESLRSRAEEVSSSATGEsHAKLLRQIEVLQTQYavaSENWHGIEGSLIARLTAVETERDELERREGD- 535
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIDALRAR-LNRAEEELERAMRAF---NREWPAETADLDADLESLPEYLALLDRLEEDg 828
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 240279359 536 -LRRKAREASLKAKKVEGELENsraVIQEIERNLEASKQEIQNLTRKLTKAE 586
Cdd:COG4913 829 lPEYEERFKELLNENSIEFVAD---LLSKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
331-563 |
1.52e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 331 KDLVNAEDRVSQAEiAEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQ 410
Cdd:COG4913 235 DDLERAHEALEDAR-EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 411 IAELRDDLssakierEISEEKLRREIR----DLKEGIEREKERARIREIELRGEQSVLESKMESLrsraeEVSSSATGES 486
Cdd:COG4913 314 LEARLDAL-------REELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAAL-----GLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 487 HAKLLRQIEVLQTQYAvasenwhgiegsliARLTAVETERDELERREGDLRRKARE-----ASLKAKK--VEGELENSRA 559
Cdd:COG4913 382 FAALRAEAAALLEALE--------------EELEALEEALAEAEAALRDLRRELREleaeiASLERRKsnIPARLLALRD 447
|
....
gi 240279359 560 VIQE 563
Cdd:COG4913 448 ALAE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
233-615 |
2.65e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 233 QEELHAYVERIDALQSKLKYLAKEAAESAknaaasaeagSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSI 312
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLE----------KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 313 AESAKSQAETK---KRLEKVEKD----------LVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAEREASNATIT 379
Cdd:PRK03918 269 EELKKEIEELEekvKELKELKEKaeeyiklsefYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 380 DLKSQLARAVSRAEAAErkaRMEATEAEKRQIAELRDDLSSAKIEREISE-EKLRREIRDlkegiEREKERARIREIELR 458
Cdd:PRK03918 349 ELEKRLEELEERHELYE---EAKAKKEELERLKKRLTGLTPEKLEKELEElEKAKEEIEE-----EISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 459 GEQsvLESKMESLRSRAEE--VSSSATGESHakllrqievlqtqyavasenwhgiEGSLIARLTA----VETERDELERR 532
Cdd:PRK03918 421 IKE--LKKAIEELKKAKGKcpVCGRELTEEH------------------------RKELLEEYTAelkrIEKELKEIEEK 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 533 EGDLRRKAREAS---------LKAKKVEGELENSRAVIQEIE-RNLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEA 602
Cdd:PRK03918 475 ERKLRKELRELEkvlkkeselIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
410
....*....|....*....
gi 240279359 603 ELTL------IQRLEEERA 615
Cdd:PRK03918 555 KKKLaelekkLDELEEELA 573
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
348-856 |
3.59e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 348 QKALERLNSVSKAEKQLETATAERE------ASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSA 421
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIEllepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 422 KIEREIseekLRREIRDLKEgiEREKERARIREIELRGEQSvLESKMESLRSRAEEVSssatgESHAKLLRQIEVLQTQY 501
Cdd:COG4913 308 EAELER----LEARLDALRE--ELDELEAQIRGNGGDRLEQ-LEREIERLERELEERE-----RRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 502 AVASENWHGIEGSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQnltRK 581
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA---EA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 582 LTKAENDFLVVkqdlakqkeAELtlIQRLEEERaRWQELARRPSSPF----LQEP-------------PTGSPITFNRKQ 644
Cdd:COG4913 453 LGLDEAELPFV---------GEL--IEVRPEEE-RWRGAIERVLGGFaltlLVPPehyaaalrwvnrlHLRGRLVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 645 TAGPDPTRPmsdrALSRRSssippaLFSELTTPPyqnhfsptnsNPQQPRItpSHEFSGDLTHAQTYEPEEyFNGMSTPV 724
Cdd:COG4913 521 TGLPDPERP----RLDPDS------LAGKLDFKP----------HPFRAWL--EAELGRRFDYVCVDSPEE-LRRHPRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 725 TPSAQGTHTLTHHSRGVND------IISVSTVAAgpsvqvvermsttIRRLESERAAFKDEIVRLTAQRDEARQEvvelM 798
Cdd:COG4913 578 TRAGQVKGNGTRHEKDDRRrirsryVLGFDNRAK-------------LAALEAELAELEEELAEAEERLEALEAE----L 640
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 240279359 799 REVEEKRKCDQRIQELEATveqlDQRYQTTLEMLGEKSELVEELKADISDLKKIYREL 856
Cdd:COG4913 641 DALQERREALQRLAEYSWD----EIDVASAEREIAELEAELERLDASSDDLAALEEQL 694
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
279-576 |
3.95e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 279 EKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAE-SAKSQAETKKRLEKVEKDLVNAEDRVSQAEiAEQKALERLNSV 357
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRlFDEKQSEKDKKNKALAERKDSANERLNSLE-AQLKQLDKKHQA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 358 SKAEKQ---LETATAEREASNATITDLKSQLARAVSRAEAAE--RKARMEATEAE-KRQIAELRDDlssakierEISEEK 431
Cdd:pfam12128 701 WLEEQKeqkREARTEKQAYWQVVEGALDAQLALLKAAIAARRsgAKAELKALETWyKRDLASLGVD--------PDVIAK 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 432 LRREIRDLKEGIER-EKERARIREIElRGEQSVLESKMESLRSRAEEVSSSATgESHAKLLRQIEVLQTQYAVASENWHG 510
Cdd:pfam12128 773 LKREIRTLERKIERiAVRRQEVLRYF-DWYQETWLQRRPRLATQLSNIERAIS-ELQQQLARLIADTKLRRAKLEMERKA 850
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 240279359 511 IEGSLIaRLTAVETERDELERREGDLRRKAREASLkakkvEGELENSRAVIQEIERNLEASKQEIQ 576
Cdd:pfam12128 851 SEKQQV-RLSENLRGLRCEMSKLATLKEDANSEQA-----QGSIGERLAQLEDLKLKRDYLSESVK 910
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
275-650 |
6.44e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 50.01 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 275 KKLLEKDEQIANLmEEGQKLS--KTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEiaeqkale 352
Cdd:NF033838 75 QKSLDKRKHTQNV-ALNKKLSdiKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEAT-------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 353 rlNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQiAELRDDLSSAKIEREISEEKL 432
Cdd:NF033838 146 --KKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPR-DEEKIKQAKAKVESKKAEATR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 433 RREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEvssSATGESHAKLLRQIEVLQTQYAVASENWHGIE 512
Cdd:NF033838 223 LEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKR---GVLGEPATPDKKENDAKSSDSSVGEETLPSPS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 513 GSLIARLTAVETERDELERREGDLRRKARE--ASLKAKKVEGELENSRAVIQEIErnLEASKQEiqnltrklTKAENDFL 590
Cdd:NF033838 300 LKPEKKVAEAEKKVEEAKKKAKDQKEEDRRnyPTNTYKTLELEIAESDVKVKEAE--LELVKEE--------AKEPRNEE 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240279359 591 VVKQDLAK--QKEAELTLIQRLEEERARWQELARRPSSPF--LQEPPTGSPITFNRKQTAGPDP 650
Cdd:NF033838 370 KIKQAKAKveSKKAEATRLEKIKTDRKKAEEEAKRKAAEEdkVKEKPAEQPQPAPAPQPEKPAP 433
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
305-454 |
7.49e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 305 IKKLRQSIAESAKSQAETKKRLEKVEKdlvNAEDRVSQAEIAEQKALERLnSVSKAEKQLETATAEREAsnatitdlKSQ 384
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIA---QANREAEEAELEQEREIETA-RIAEAEAELAKKKAEERR--------EAE 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 385 LARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRdlkEGIEREKERARIRE 454
Cdd:COG2268 259 TARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVR---KPAEAEKQAAEAEA 325
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
215-595 |
9.67e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 215 EEAMAQMRADHEMSELRWQEELHAYVE---RIDALQSKLKYLAKEAAESAKNAAASAEAGSLEKKLLEKDEqiANLMEEG 291
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEeakKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK--ADEAKKA 1518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 292 QKLSKTELDHRATIKKLrqsiAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAER 371
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKK----ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 372 EASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDLKEGIEREKERAR 451
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 452 IREIELRGEQSVLESKMESLRSRAEEVsssatgeshakllRQIEVLQTQYAVASENWHGIEGSLIARLTAVEterdELER 531
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEA-------------KKAEELKKKEAEEKKKAEELKKAEEENKIKAE----EAKK 1737
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240279359 532 REGDLRRKAREaslkAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQD 595
Cdd:PTZ00121 1738 EAEEDKKKAEE----AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-620 |
1.06e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 231 RWQEELHAYVERIDALQSKLKYLAKEAAESAKNAAAsaeagsLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQ 310
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQR------LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 311 SIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLAR--- 387
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSvge 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 388 ----AVSRAEAAERKARMEATEAEKRQIAELrddLSSAKIERE--ISEEKLRREIRDL----KEG--------IEREKER 449
Cdd:TIGR02169 536 ryatAIEVAAGNRLNNVVVEDDAVAKEAIEL---LKRRKAGRAtfLPLNKMRDERRDLsilsEDGvigfavdlVEFDPKY 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 450 ARI-----------REIELrGEQSVLESKMESLRSRAEEVSSSATGeSHAKLLRQIEVLQTQYAVASENWHGIEG----- 513
Cdd:TIGR02169 613 EPAfkyvfgdtlvvEDIEA-ARRLMGKYRMVTLEGELFEKSGAMTG-GSRAPRGGILFSRSEPAELQRLRERLEGlkrel 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 514 -SLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVV 592
Cdd:TIGR02169 691 sSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
410 420
....*....|....*....|....*...
gi 240279359 593 KQDLAKQKEAELTLIQRLEEEraRWQEL 620
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHS--RIPEI 796
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
229-616 |
1.15e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 229 ELRWQEELHAYV-ERIDALQSKLKYL-AKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIK 306
Cdd:TIGR04523 132 QKKENKKNIDKFlTEIKKKEKELEKLnNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 307 KLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLA 386
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 387 RAVSRAEA----------AERKARMEATEAEKRQ-----------IAELRDDLSSAKIEREISE---EKLRREIRDLK-- 440
Cdd:TIGR04523 292 QLKSEISDlnnqkeqdwnKELKSELKNQEKKLEEiqnqisqnnkiISQLNEQISQLKKELTNSEsenSEKQRELEEKQne 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 441 -EGIEREKErARIREIE-LRGEQSVLESKMESLRSRAEEVSSSATG--ESHAKLLRQIEVLQTQYAVASENwhgIEgSLI 516
Cdd:TIGR04523 372 iEKLKKENQ-SYKQEIKnLESQINDLESKIQNQEKLNQQKDEQIKKlqQEKELLEKEIERLKETIIKNNSE---IK-DLT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 517 ARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENsraviqeIERNLEASKQEIQNLTRKLTKAENDFlvvkQDL 596
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEKV----KDL 515
|
410 420
....*....|....*....|
gi 240279359 597 AKQKEAELTLIQRLEEERAR 616
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKE 535
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
311-544 |
1.69e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 311 SIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAEREASNA--TITDLKSQLARA 388
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTARELlrRYRSQQALAQRL 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 389 VS-RAEAAERKARMEATEAEKRQIAELrDDLSSAKIEREISEEKLRREIRDLKEGIEREKERARIREIELRGEQSVLESK 467
Cdd:COG3096 515 QQlRAQLAELEQRLRQQQNAERLLEEF-CQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 468 MESLRSRAeevssSATGESHAKLLRqievLQTQYAVASENWHGIEG---SLIARLTAVETERDELERREGDLRRKAREAS 544
Cdd:COG3096 594 IKELAARA-----PAWLAAQDALER----LREQSGEALADSQEVTAamqQLLEREREATVERDELAARKQALESQIERLS 664
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
241-441 |
2.05e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 241 ERIDALQSKLKYLAKEAAESAKNAAASaeagsleKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAEsaksqa 320
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEAL-------EAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAE------ 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 321 etKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETataEREASNATITDLKSQLARAVS------RAEA 394
Cdd:COG4913 677 --LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAAEDlarlelRALL 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 240279359 395 AERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDLKE 441
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
274-623 |
2.25e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 274 EKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAE--IAEQK-- 349
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalLEAGKcp 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 350 --------------ALERLNSVSKAEKQLETATAEREasnatitDLKSQLARAVSRAEAAERKARMEateaEKRQIAELR 415
Cdd:PRK02224 456 ecgqpvegsphvetIEEDRERVEELEAELEDLEEEVE-------EVEERLERAEDLVEAEDRIERLE----ERREDLEEL 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 416 ddlssakiereiseeklrreIRDLKEGIEREKERARireiELRGEQSVLESKMESLRSRAEEVSSSAtgESHAKLLRQIE 495
Cdd:PRK02224 525 --------------------IAERRETIEEKRERAE----ELRERAAELEAEAEEKREAAAEAEEEA--EEAREEVAELN 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 496 VLQTQYAVASENWHGIEGSLiARLTAVETERDEL-ERREG-----DLRR-KAREASLKAKKVEGELENSRavIQEIERNL 568
Cdd:PRK02224 579 SKLAELKERIESLERIRTLL-AAIADAEDEIERLrEKREAlaelnDERReRLAEKRERKRELEAEFDEAR--IEEAREDK 655
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 240279359 569 EASKQEIQNLTRKLTKAENDflvvKQDLAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREE----RDDLQAEIGAVENELEELEELRERREALENR 706
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
264-586 |
2.95e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 264 AAASAEAGSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQA 343
Cdd:PTZ00121 1202 AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 344 EIAEQKALERLNSVSKAEKQLETATAEREASNATITD-LKSQLARAVSRAEAAERKA--RMEATEAEKRQIAELRDDLSS 420
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADeAKKKAEEAKKKADAAKKKAeeAKKAAEAAKAEAEAAADEAEA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 421 AKIEREISEEKLRREIRDLKEGIEREKERARIREIELRGEQ-----------SVLESKMESLRSRAEEVSSSATGESHAK 489
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkkkadelkkaAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 490 LLRQIEVL--QTQYAVASENwhgiegsliARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERN 567
Cdd:PTZ00121 1442 EAKKADEAkkKAEEAKKAEE---------AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
330
....*....|....*....
gi 240279359 568 LEASKQEIQNLTRKLTKAE 586
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAE 1531
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
396-616 |
3.88e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 396 ERKARMEATEAEKRQIAELRDDLSS--AKIEREISE-EKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLR 472
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREelEKLEKEVKElEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 473 SRAEEVSSSATGESHAKLLRQIEVLQTQYAVASENWHGIEGSLIARLTAVETERDELERREGDLRrkareaslKAKKVEG 552
Cdd:PRK03918 277 ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE--------ELKKKLK 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240279359 553 ELENSRAVIQEIERNLEASKQ---EIQNLTRKLTKAENDFLVVKQDLAKQKEAELTL-IQRLEEERAR 616
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKEEIEEeISKITARIGE 416
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
276-443 |
5.07e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 276 KLLEKDEQIANLMEEGQKLskteldhRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLN 355
Cdd:COG1579 11 DLQELDSELDRLEHRLKEL-------PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 356 SVSKA------EKQLETATAEREASNATITDLKSQLARAVSR-----AEAAERKARMEATEAE-KRQIAELRDDLSSAKI 423
Cdd:COG1579 84 NVRNNkeyealQKEIESLKRRISDLEDEILELMERIEELEEElaeleAELAELEAELEEKKAElDEELAELEAELEELEA 163
|
170 180
....*....|....*....|
gi 240279359 424 EREISEEKLRREIRDLKEGI 443
Cdd:COG1579 164 EREELAAKIPPELLALYERI 183
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
271-409 |
6.91e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 271 GSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKV---------EKDLVNAEDRVS 341
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240279359 342 QAEIAEQKALERLnsvSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKR 409
Cdd:COG1579 107 DLEDEILELMERI---EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
380-623 |
7.38e-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: 46.76 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 380 DLKSQLARAVSRAEAAERKARMEATEAEKR------QIAELRDDLSSAKIEREISEEKLRR-------EIRDLKEGIERE 446
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQlvqangELEKASREETFARTALKNARLDLRRlfdekqsEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 447 KERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVASENWHGIEGSLIARLTAVETER 526
Cdd:pfam12128 677 KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWY 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 527 DElerregdlrrkareaSLKAKKVEGElensraviqeierNLEASKQEIQNLTRKLTKAEND--------------FLVV 592
Cdd:pfam12128 757 KR---------------DLASLGVDPD-------------VIAKLKREIRTLERKIERIAVRrqevlryfdwyqetWLQR 808
|
250 260 270
....*....|....*....|....*....|.
gi 240279359 593 KQDLAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:pfam12128 809 RPRLATQLSNIERAISELQQQLARLIADTKL 839
|
|
| PilO |
COG3167 |
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures]; |
785-849 |
7.74e-05 |
|
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
Pssm-ID: 442400 [Multi-domain] Cd Length: 202 Bit Score: 44.55 E-value: 7.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240279359 785 AQRDEARQEVVELMREVEEKRKCDQRIQELEATVEQLDQRYQTTLEMLGEKSElVEELKADISDL 849
Cdd:COG3167 46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELEQQLGELLKQLPSKAE-VPALLDDISQA 109
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
398-623 |
7.81e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 398 KARMEATEAEKRQIAELRDDLSSAKIEREISEEKL-RREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRS--- 473
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLkEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEllr 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 474 --RAEEVSSSATGESHAKLLRQIEVLQTQYAVASENWHGIEGSLIARLTAVETERDELERREGDLRRKAREASLKAKKVE 551
Cdd:pfam02463 248 deQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240279359 552 GELENSRAVIQEIE-------RNLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:pfam02463 328 KELKKEKEEIEELEkelkeleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
271-620 |
7.87e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 271 GSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLE---KVEKDLVNAEDRVSQAEIAE 347
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLadrVQEAQDKINEELKLLKQKID 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 348 QKALERLNSVSKAEKQLETA-------TAEREASNATITDLKSQLARAVSRAEAAERKARMEA-TEAEKRQIAELRDDLS 419
Cdd:pfam02463 747 EEEEEEEKSRLKKEEKEEEKselslkeKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEElKEEAELLEEEQLLIEQ 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 420 SAKIEREISEEKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQT 499
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 500 QYAVASENWHGIEGSLIARLTAVETERDELERRegdlrrkareaSLKAKKVEGELENSRAVIQEIERNLEasKQEIQNLT 579
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEE-----------LLLEEADEKEKEENNKEEEEERNKRL--LLAKEELG 973
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 240279359 580 RKLTKAENDFlvvkQDLAKQKEAELTLIQRLEEERARWQEL 620
Cdd:pfam02463 974 KVNLMAIEEF----EEKEERYNKDELEKERLEEEKKKLIRA 1010
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
283-436 |
8.21e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 283 QIANLMEEGQKLSKTELDHRATIKKLRQSIAEsAKSQAETKKRLEKVEKD-----------------LVNAEDRVSQAEI 345
Cdd:PHA02562 235 EIEELTDELLNLVMDIEDPSAALNKLNTAAAK-IKSKIEQFQKVIKMYEKggvcptctqqisegpdrITKIKDKLKELQH 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 346 AEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAErkARMEATEAE----KRQIAELRDDLSSA 421
Cdd:PHA02562 314 SLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK--AAIEELQAEfvdnAEELAKLQDELDKI 391
|
170
....*....|....*.
gi 240279359 422 KIER-EISEEKLRREI 436
Cdd:PHA02562 392 VKTKsELVKEKYHRGI 407
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
279-551 |
1.37e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 279 EKDEQIANLMEEgqkLSKTELDHRATIKKLrqsiaESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVS 358
Cdd:PRK02224 472 EDRERVEELEAE---LEDLEEEVEEVEERL-----ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 359 KAEKQLETATAEREASNAtitdlKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSS-AKIEREISEEKLRREIR 437
Cdd:PRK02224 544 ERAAELEAEAEEKREAAA-----EAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiADAEDEIERLREKREAL 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 438 DLKEGIEREK---ERARIREIELRGEQSVLEsKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVASE-------- 506
Cdd:PRK02224 619 AELNDERRERlaeKRERKRELEAEFDEARIE-EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEleeleelr 697
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 240279359 507 NWHGIEGSLIARLTAVETERDELERREGDLRrkareASLKAKKVE 551
Cdd:PRK02224 698 ERREALENRVEALEALYDEAEELESMYGDLR-----AELRQRNVE 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
233-445 |
1.37e-04 |
|
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: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 233 QEELHAYVERIDALQSKLKYLAKEAAESAKNAAASAEA---GSLEKKLLEKDEQIANLMEEGQKLS--KTELDH-RATIK 306
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSDDLAalEEQLEElEAELE 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 307 KLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALE-------RLNSVSKAEKQL-ETATAEREASNATI 378
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRalleerfAAALGDAVERELrENLEERIDALRARL 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 379 TDLKSQLARAVSR------AEAAERKARMEATEA--------EKRQIAELRDDLSSAKIEREISE-----EKLRREIRDL 439
Cdd:COG4913 783 NRAEEELERAMRAfnrewpAETADLDADLESLPEylalldrlEEDGLPEYEERFKELLNENSIEFvadllSKLRRAIREI 862
|
....*.
gi 240279359 440 KEGIER 445
Cdd:COG4913 863 KERIDP 868
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
307-623 |
1.42e-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: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 307 KLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQ----------LETATAEREASNA 376
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQqekieryqedLEELTERLEEQEE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 377 TITDLKSQLARAVSRAEAAErkarmEATEAEKRQIAELR---DDLSSAKIEREISEEKLRR-----EIRDLK-EGIEREK 447
Cdd:COG3096 369 VVEEAAEQLAEAEARLEAAE-----EEVDSLKSQLADYQqalDVQQTRAIQYQQAVQALEKaralcGLPDLTpENAEDYL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 448 ERARIREIELRGEQSVLESKM--------------ESLRSRAEEVSSSATGESHAKLLRQIEVLQtqyavasenwhgieg 513
Cdd:COG3096 444 AAFRAKEQQATEEVLELEQKLsvadaarrqfekayELVCKIAGEVERSQAWQTARELLRRYRSQQ--------------- 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 514 SLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSraviQEIERNLEASKQEIQNLTrkltkaendflvvk 593
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA----EELEELLAELEAQLEELE-------------- 570
|
330 340 350
....*....|....*....|....*....|
gi 240279359 594 QDLAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAAR 600
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
312-481 |
1.51e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 312 IAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAeqkalerlnsVSKAEKQLETATAEREASNATITDLKSQLARAVSr 391
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTE----------LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 392 aeAAERKARMEATEAEKRQIAELRDDLSSAKIEREiseeKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESL 471
Cdd:COG1579 88 --NKEYEALQKEIESLKRRISDLEDEILELMERIE----ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|
gi 240279359 472 RSRAEEVSSS 481
Cdd:COG1579 162 EAEREELAAK 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-623 |
2.52e-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: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 407 EKRQIAELRDDLSSAKIEREiseEKLRREIRDLKEGIEREKERA-RIREIELRGEQ---SVLESKMESLRSRAEEVSSSA 482
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRL---EDILNELERQLKSLERQAEKAeRYKELKAELRElelALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 483 tgeshAKLLRQIEVLQTQYAVASEnwhgiegsliaRLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQ 562
Cdd:TIGR02168 249 -----KEAEEELEELTAELQELEE-----------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240279359 563 EIERNLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-451 |
2.56e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 273 LEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAksqaetKKRLEKVEKDLVNAEDRVSQAEiaeqKALE 352
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERE----RRRA 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 353 RLnsvskaEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEkRQIAELRDDLssakiereiseEKL 432
Cdd:COG4913 363 RL------EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE-AALRDLRREL-----------REL 424
|
170 180
....*....|....*....|..
gi 240279359 433 RREIRDLKEG---IEREKERAR 451
Cdd:COG4913 425 EAEIASLERRksnIPARLLALR 446
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
274-577 |
3.03e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 274 EKKLLEKDEQIANLMEEGQKLSKTELDHRATIkklrqsIAESAKSQAETKKRLEKVEKDLVNAE-DRVSQAEIAEQkaLE 352
Cdd:pfam17380 304 EKEEKAREVERRRKLEEAEKARQAEMDRQAAI------YAEQERMAMERERELERIRQEERKRElERIRQEEIAME--IS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 353 RLnsvskaeKQLETATAEREASNatitdlksqlARAVSRAEAAERKARMEatEAEKRQIAELRDDLSSAKIEReisEEKL 432
Cdd:pfam17380 376 RM-------RELERLQMERQQKN----------ERVRQELEAARKVKILE--EERQRKIQQQKVEMEQIRAEQ---EEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 433 RREIRDLKEGIEREKERARIREIELRGEQSVL-----ESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVASEN 507
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQQQVERLrqqeeERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEER 513
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240279359 508 WHGI-EGSLIARLTAVETERdelERREGDLRRKAREASLKAKKVEGELENS---RAVIQEIERNLEASKQEIQN 577
Cdd:pfam17380 514 KRKLlEKEMEERQKAIYEEE---RRREAEEERRKQQEMEERRRIQEQMRKAteeRSRLEAMEREREMMRQIVES 584
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
323-443 |
3.32e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 323 KKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSV-SKAEKQLETATAEREA-SNATITDLKSQLARAVSRAEAAERKAR 400
Cdd:COG0711 30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEArAEAAEIIAEARKEAEAiAEEAKAEAEAEAERIIAQAEAEIEQER 109
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 240279359 401 MEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDLKEGI 443
Cdd:COG0711 110 AKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
233-610 |
3.40e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 233 QEELHAYVERIDALQSKLKylAKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSI 312
Cdd:pfam07111 305 RSLLNRWREKVFALMVQLK--AQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMEL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 313 AESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNsvsKAEKQLETATAEREASNATITDLKSQLARAVS-- 390
Cdd:pfam07111 383 SRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVE---QAVARIPSLSNRLSYAVRKVHTIKGLMARKVAla 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 391 --RAEAAERKARMEATEAE-KRQIAELRDDLSSAKIEREISEEKLRREIRDLKEgiEREKERARIREIELRGEQSvLESK 467
Cdd:pfam07111 460 qlRQESCPPPPPAPPVDADlSLELEQLREERNRLDAELQLSAHLIQQEVGRARE--QGEAERQQLSEVAQQLEQE-LQRA 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 468 MESLRSRAEEVSSSATGESH----AKLLRQiEVLQTQYAVASenwhgiegSLIARLTAVETE-RDEL---ERREGDLRRK 539
Cdd:pfam07111 537 QESLASVGQQLEVARQGQQEsteeAASLRQ-ELTQQQEIYGQ--------ALQEKVAEVETRlREQLsdtKRRLNEARRE 607
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240279359 540 AREASLKAKKVEGELENSRAVIQEIER-NLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRL 610
Cdd:pfam07111 608 QAKAVVSLRQIQHRATQEKERNQELRRlQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRL 679
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
358-497 |
3.65e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 358 SKAEKQLETAtaEREAsnatitdlKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREir 437
Cdd:PRK12704 27 KIAEAKIKEA--EEEA--------KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 438 dlKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSssatgESHAKLLRQIEVL 497
Cdd:PRK12704 95 --EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELE-----ELIEEQLQELERI 147
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
408-612 |
3.75e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 408 KRQIAELRDDLSSAK--IEREIseEKLRREIRDLKEGIEREKERARIreIELRGEQSVLESKMESLRSRAEEVSSSAtge 485
Cdd:COG3206 163 EQNLELRREEARKALefLEEQL--PELRKELEEAEAALEEFRQKNGL--VDLSEEAKLLLQQLSELESQLAEARAEL--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 486 shAKLLRQIEVLQTQYAVASENWHGIEGSliARLTAVETERDELERREGDLRR------------KAREASLKA------ 547
Cdd:COG3206 236 --AEAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSArytpnhpdvialRAQIAALRAqlqqea 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240279359 548 KKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEE 612
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
303-595 |
4.15e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.13 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 303 ATIKKLRQSIAESAKSQAETKKRLEKVEKDLV-NAEDRVSQA--EIAEQKALERLNSVSKAEKQLETATAEREASNATIT 379
Cdd:pfam15964 238 SQVKSLRKDLAESQKTCEDLKERLKHKESLVAaSTSSRVGGLclKCAQHEAVLAQTHTNVHMQTIERLTKERDDLMSALV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 380 DLKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREIS--EEKLRREIRDLKEGIEREKERARIreiEL 457
Cdd:pfam15964 318 SVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELErqKERLEKELASQQEKRAQEKEALRK---EM 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 458 RGEQSVLESKMESLRSRAEEVSSSATGESHAK--LLRQIEVLQTQYAVASENWHGIEGSLIARLTAVETERDELERREGD 535
Cdd:pfam15964 395 KKEREELGATMLALSQNVAQLEAQVEKVTREKnsLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHRE 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 240279359 536 LRRKA-REASLKAKKVEG---ELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQD 595
Cdd:pfam15964 475 YRTKTgRQLEIKDQEIEKlglELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLE 538
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
320-589 |
4.26e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 320 AETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLetATAEREASNATITDLKSQLARAvSRAEAAERKA 399
Cdd:PRK04863 840 RQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRL--NLLADETLADRVEEIREQLDEA-EEAKRFVQQH 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 400 RMEATEAEK---------RQIAELRDDLSSAKIEREiseeKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMES 470
Cdd:PRK04863 917 GNALAQLEPivsvlqsdpEQFEQLKQDYQQAQQTQR----DAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQ 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 471 LRSRAEEVSSSATGEshaklLRQIEVLQTQYavasenwHGIEGSLIARLTAVETERDELERREGDLRRKARE-----ASL 545
Cdd:PRK04863 993 RLEQAEQERTRAREQ-----LRQAQAQLAQY-------NQVLASLKSSYDAKRQMLQELKQELQDLGVPADSgaeerARA 1060
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 240279359 546 KAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDF 589
Cdd:PRK04863 1061 RRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDY 1104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-851 |
5.34e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 277 LLEKDEQIANlmEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEkvEKDLVNAEDRVSQAEIAEQKAlerlnS 356
Cdd:PRK02224 189 LDQLKAQIEE--KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRD--EADEVLEEHEERREELETLEA-----E 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 357 VSKAEKQLETATAEREASNATITDLKSQLARAvsRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREI 436
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEEL--EEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 437 RDLKEGIEREKERARIRE---IELRGEQSVLESKMESLRSRAEEVSSsatgeshakllrQIEVLQTQYAVASENWHGIEg 513
Cdd:PRK02224 338 QAHNEEAESLREDADDLEeraEELREEAAELESELEEAREAVEDRRE------------EIEELEEEIEELRERFGDAP- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 514 sliARLTAVETERDELERREGDLRrkAREASLKAkkvegELENSRAVIQEIERNLEASK-----QEIQNLTRKLTKAEND 588
Cdd:PRK02224 405 ---VDLGNAEDFLEELREERDELR--EREAELEA-----TLRTARERVEEAEALLEAGKcpecgQPVEGSPHVETIEEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 589 FLVVK--QDLAKQKEAELTLIQRLEEERArWQELARRPSSpfLQEpptgspitfnrkqtagpdpTRPMSDRALSRRSSSI 666
Cdd:PRK02224 475 ERVEEleAELEDLEEEVEEVEERLERAED-LVEAEDRIER--LEE-------------------RREDLEELIAERRETI 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 667 ppalfselttppyqnhfsptnsNPQQPRITPSHEFSGDL-THAQTYEPEeyfngmstpvtpsAQGTHTLTHHSRGVNDII 745
Cdd:PRK02224 533 ----------------------EEKRERAEELRERAAELeAEAEEKREA-------------AAEAEEEAEEAREEVAEL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 746 SVSTVAAGPSVQVVERmsttIRRLESERAAFKDEIVRLTAQRdEARQEVVELMRE-VEEKRkcdQRIQELEAT-----VE 819
Cdd:PRK02224 578 NSKLAELKERIESLER----IRTLLAAIADAEDEIERLREKR-EALAELNDERRErLAEKR---ERKRELEAEfdearIE 649
|
570 580 590
....*....|....*....|....*....|..
gi 240279359 820 QLDQRYQTTLEMLGEKSELVEELKADISDLKK 851
Cdd:PRK02224 650 EAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
277-606 |
5.43e-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: 43.56 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 277 LLEKDEQIANLMEEGQKLS----KTELDHRATIKKLRQSIAESAKSQAETKKRLEKvekDLVNAEDRVSQAEIAEQKALE 352
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQdenlKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE---DLQIATKTICQLTEEKEAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 353 RLNsvsKAEKQLETATAEREASNATITDLksqLARAVSRAEAAERKARMEATEAEKRQiAELrDDLSSAKIEREISEEKL 432
Cdd:pfam05483 339 ELN---KAKAAHSFVVTEFEATTCSLEEL---LRTEQQRLEKNEDQLKIITMELQKKS-SEL-EEMTKFKNNKEVELEEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 433 RREIRDLKEGIEREKERARIREiELRGEQSVLESKMESLRSRAE--EVSSSATGESHAKLLRQIEVLQTQyaVASENWHG 510
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAE-ELKGKEQELIFLLQAREKEIHdlEIQLTAIKTSEEHYLKEVEDLKTE--LEKEKLKN 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 511 IEgsLIARLTAVETERDELERREGDLR---RKAREASLKAKKVEGELENSRAVIQEIERNL--------EASKQEIQNLT 579
Cdd:pfam05483 488 IE--LTAHCDKLLLENKELTQEASDMTlelKKHQEDIINCKKQEERMLKQIENLEEKEMNLrdelesvrEEFIQKGDEVK 565
|
330 340
....*....|....*....|....*..
gi 240279359 580 RKLTKAENDFLVVKQDLAKQKEAELTL 606
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKIL 592
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
397-626 |
6.44e-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: 43.52 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 397 RKARMEATEAEKRQ------IAELRDDLSSAKIEREISEE--KLRREIRDL--------KEGIEREKERARIREIELRGE 460
Cdd:TIGR02169 173 EKALEELEEVEENIerldliIDEKRQQLERLRREREKAERyqALLKEKREYegyellkeKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 461 QSVLESKMESLRSRAEEVsssatgeshAKLLRQIEvlqtqyavasenwHGIEGSLIARLTAVETERDELERREGDLRRKA 540
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEI---------EQLLEELN-------------KKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 541 REASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKaendflvVKQDLAKQKEAELTLIQRLEEERARWQEL 620
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK-------LTEEYAELKEELEDLRAELEEVDKEFAET 383
|
....*.
gi 240279359 621 ARRPSS 626
Cdd:TIGR02169 384 RDELKD 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
272-488 |
6.48e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 272 SLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKD-------------LVNAE- 337
Cdd:COG3883 34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrsggsvsyldvLLGSEs 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 338 -----DRVSQAEIAEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEA--AERKARMEATEAEKRQ 410
Cdd:COG3883 114 fsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAqqAEQEALLAQLSAEEAA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240279359 411 IAELRDDLSSAKIEREiSEEKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHA 488
Cdd:COG3883 194 AEAQLAELEAELAAAE-AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
274-578 |
7.23e-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: 43.09 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 274 EKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALER 353
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 354 LNSV----SKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKarmeaTEAEKRQIAELRDDLSSAK-----IE 424
Cdd:TIGR04523 414 IKKLqqekELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKIKqnleqKQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 425 REISE-----EKLRREIRDLKEGI---EREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATgeshaKLLRQIEV 496
Cdd:TIGR04523 489 KELKSkekelKKLNEEKKELEEKVkdlTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK-----KENLEKEI 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 497 LQTQYAVasENWHGIEGSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRA---VIQEIERNLEASKQ 573
Cdd:TIGR04523 564 DEKNKEI--EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKeneKLSSIIKNIKSKKN 641
|
....*
gi 240279359 574 EIQNL 578
Cdd:TIGR04523 642 KLKQE 646
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
397-615 |
8.11e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.99 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 397 RKARMEATEAEKRqIAELRDDLSSAKIEREISEEKLRREIRDLKEGIEREKERA--RIREIElrGEQSVLESKMESLRSR 474
Cdd:PRK05771 46 RKLRSLLTKLSEA-LDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIekEIKELE--EEISELENEIKELEQE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 475 AEEVSSSATGESHAKLLRQIEVLQTQYAVASENwHGIEGSLIARLTAVETERDE----------LERREGDLRRKAREAS 544
Cdd:PRK05771 123 IERLEPWGNFDLDLSLLLGFKYVSVFVGTVPED-KLEELKLESDVENVEYISTDkgyvyvvvvvLKELSDEVEEELKKLG 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240279359 545 LKAKKVEgELENSRAVIQEIERNLEASKQEIQNLTRKL----TKAENDFLVVKQDLAKQKEAELTLIQRLEEERA 615
Cdd:PRK05771 202 FERLELE-EEGTPSELIREIKEELEEIEKERESLLEELkelaKKYLEELLALYEYLEIELERAEALSKFLKTDKT 275
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
244-623 |
8.66e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 244 DALQSKLKYLAKEAAESAknaaasaeagslEKKLLekdeqIANLMEEGQKLSKTElDHRATIKKLRQSIAESAKSQAETK 323
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEA------------EDKLV-----QQDLEQTLALLDKID-RQKEETEQLKQQLAQAPAKLRQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 324 KRLEKVEKDLVNaedrvsqaeiAEQKALERLnSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEaaerKARMEA 403
Cdd:PRK11281 101 AELEALKDDNDE----------ETRETLSTL-SLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE----RAQAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 404 TEAEKRqIAELRDDLSSAKiereISEEKLRREIRDLkegierekerarireieLRGEQSVLESKMESLRsraeevsssat 483
Cdd:PRK11281 166 YANSQR-LQQIRNLLKGGK----VGGKALRPSQRVL-----------------LQAEQALLNAQNDLQR----------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 484 geshaKLLRQIEVLQTQYavasenwhgiegsliarltavETERDELerregdlrrkareaSLKAKKVEGELENSRAVIQe 563
Cdd:PRK11281 213 -----KSLEGNTQLQDLL---------------------QKQRDYL--------------TARIQRLEHQLQLLQEAIN- 251
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240279359 564 iERNLEASKQEIQNLT--RKLTKAENDFLVvkqdlAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:PRK11281 252 -SKRLTLSEKTVQEAQsqDEAARIQANPLV-----AQELEINLQLSQRLLKATEKLNTLTQQ 307
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
292-450 |
9.13e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 292 QKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAER 371
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240279359 372 EASNAtitdlKSQLARAVSRAEAaerKARMEATEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDLKEGIEREKERA 450
Cdd:TIGR02794 137 EAEAE-----RKAKEEAAKQAEE---EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAA 207
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-581 |
9.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 229 ELRWQEELHAYVERIDALQSKLKYLAKEAAESAKNAAASAEAGSL-EKKLLEKDEQIANlmEEGQKLSKTELDHRATIKK 307
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKK 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 308 lrqSIAESAKSQAETKKRLEKV----EKDLVNAEDRVSQAEIAEQKAlERLNSVSKAEKQLETATAEREASNATITDLKS 383
Cdd:PTZ00121 1634 ---KVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKA-EEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 384 QLARAVSRAEAA-----ERKARME----ATEAEKRQIAELRDDLSSAK--IEREISEEKLRREIRDLKEGIERE--KERA 450
Cdd:PTZ00121 1710 KEAEEKKKAEELkkaeeENKIKAEeakkEAEEDKKKAEEAKKDEEEKKkiAHLKKEEEKKAEEIRKEKEAVIEEelDEED 1789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 451 RIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVASE---------NWHGIEGSLIARLTA 521
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEadafekhkfNKNNENGEDGNKEAD 1869
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240279359 522 VETERDELERREGDLRRKAREASLKAKKVEGELENSRA-------------VIQEIERNLEASKQEIQNLTRK 581
Cdd:PTZ00121 1870 FNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMagknndiiddkldKDEYIKRDAEETREEIIKISKK 1942
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
760-856 |
9.69e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 760 ERMSTTIRRLESERAAFKDEIVRLTAQRDEARQEVVELMREVEEKRK----CDQRIQELEATVEQLDQRYQTTLEMLGEK 835
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiarLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100
....*....|....*....|.
gi 240279359 836 SELVEELKADISDLKKIYREL 856
Cdd:COG1196 336 EEELEELEEELEEAEEELEEA 356
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
313-623 |
1.05e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 313 AESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALER-LNSVSKAE--------KQLETATAEREASNATITDLKS 383
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERkAEEARKAEdakkaeavKKAEEAKKDAEEAKKAEEERNN 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 384 QLARAVSRAEAAERKARMEATEAEKRQIAelrDDLSSAKIEREISEEKLRREIRDLKEGIEREKERARIREIELRGEQSv 463
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKA---DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA- 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 464 lESKMESLRSRAEEVSSSAtgeshakllrqiEVLQTQYAVASENWHGIEgsliARLTAVETERDELERREGDLRRKAREA 543
Cdd:PTZ00121 1328 -KKKADAAKKKAEEAKKAA------------EAAKAEAEAAADEAEAAE----EKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 544 SlKAKKVEGELENSRAVIQEIERNLEASKQ--EIQNLTRKLTKAENdflvVKQDLAKQKEAEltLIQRLEEERARWQELA 621
Cdd:PTZ00121 1391 K-KADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKADE----AKKKAEEAKKAD--EAKKKAEEAKKAEEAK 1463
|
..
gi 240279359 622 RR 623
Cdd:PTZ00121 1464 KK 1465
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
215-613 |
1.18e-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: 42.65 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 215 EEAMAQMRADHEM---------SELRWQEELHAYVERIDALQSKLKYLAKEAAESAKNAAASAEAgSLEKKLLEKDEQIA 285
Cdd:TIGR00618 232 REALQQTQQSHAYltqkreaqeEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLA-AHIKAVTQIEQQAQ 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 286 NLMEEGQ---KLSKTELDHRATIKKLRQSIAESAKSQA--------------ETKKRLEKVEKDLVNAEDRVSQAEIAEQ 348
Cdd:TIGR00618 311 RIHTELQskmRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhsqeihirdaheVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 349 kALERLNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKR-QIAELRDDLSSAKIEREI 427
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTaQCEKLEKIHLQESAQSLK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 428 SEEKLRREIRDLKEGIEREKERARIREIELRGEQSVLEskmESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVASEN 507
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLC---GSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 508 WHGIEGSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAEN 587
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
410 420
....*....|....*....|....*...
gi 240279359 588 DFLVVKQDLAKQKE--AELTLIQRLEEE 613
Cdd:TIGR00618 627 LQDVRLHLQQCSQElaLKLTALHALQLT 654
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
320-601 |
1.60e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 320 AETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQL-----ETATAEREASNATITDLKSQLARAVSRAEA 394
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlladETLADRLEELREELDAAQEAQAFIQQHGKA 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 395 AERKARMEAT-EAEKRQIAELRDDLSSAKIEREiseeKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRS 473
Cdd:COG3096 919 LAQLEPLVAVlQSDPEQFEQLQADYLQAKEQQR----RLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNEKLRARLE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 474 RAEEVSSSATgeshakllRQIEVLQTQYAVASENWHGIEGSLIAR---LTAVETERDELE-RREGDLRRKAREaslKAKK 549
Cdd:COG3096 995 QAEEARREAR--------EQLRQAQAQYSQYNQVLASLKSSRDAKqqtLQELEQELEELGvQADAEAEERARI---RRDE 1063
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 240279359 550 VEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKE 601
Cdd:COG3096 1064 LHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKA 1115
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
249-565 |
1.67e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 249 KLKYLAKEAAESAKNAAASAEagsLEKKLLEKDEQ--IANLMEEGQKLSKTELDHRATIKKLRQSIAESAKsQAETKKRL 326
Cdd:pfam02463 201 KLKEQAKKALEYYQLKEKLEL---EEEYLLYLDYLklNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLA-QVLKENKE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 327 EKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEA 406
Cdd:pfam02463 277 EEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 407 EKRQIAELRDDLSSAKIEREISEEKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGES 486
Cdd:pfam02463 357 EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 487 HAKLLRQIEVLQTQYAVASENWHGIEGSLIARLTAVETERDEL-----ERREGDLRRKAREASLKAKKVEGELENSRAVI 561
Cdd:pfam02463 437 ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLvklqeQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
|
....
gi 240279359 562 QEIE 565
Cdd:pfam02463 517 KDGV 520
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
345-647 |
1.73e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 345 IAEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLaRAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIE 424
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGY-KSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 425 REISEEKLRREIRDLKEGIEREKERARIREiELRGEQSVLESKME-SLRSRAEEVSssatgESHAKLLRQIEVLQTQY-- 501
Cdd:pfam12128 306 LNGELSAADAAVAKDRSELEALEDQHGAFL-DADIETAAADQEQLpSWQSELENLE-----ERLKALTGKHQDVTAKYnr 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 502 ---AVASENWHGIEG---------SLIARLTAVetERDELERREGDLR-------RKAREASLKAKKVEGELE---NSRA 559
Cdd:pfam12128 380 rrsKIKEQNNRDIAGikdklakirEARDRQLAV--AEDDLQALESELReqleagkLEFNEEEYRLKSRLGELKlrlNQAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 560 VIQEIERNLEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARRPSSPFLQ-EPPTGSPI 638
Cdd:pfam12128 458 ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLL 537
|
....*....
gi 240279359 639 TFNRKQTAG 647
Cdd:pfam12128 538 HFLRKEAPD 546
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
306-450 |
2.13e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 306 KKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALErlnsvskAEKQLETATAEREASNATITDLKSQL 385
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAL-------KQKQAEEAAAKAAAAAKAKAEAEAKR 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240279359 386 ARAVSRAEAAERKARMEAtEAEKRQIAELRDDLSSAKIEREISEEKLRREIRDLKEGIEREKERA 450
Cdd:PRK09510 156 AAAAAKKAAAEAKKKAEA-EAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-619 |
2.23e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 229 ELRWQEELHAYVERIDALQSKLKyLAKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKL 308
Cdd:TIGR00606 497 ETLKKEVKSLQNEKADLDRKLRK-LDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 309 RQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKA----------EKQLETATAEREASNATI 378
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsqdeESDLERLKEEIEKSSKQR 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 379 TDLKSQLARAVSRAEAAERKA--------RMEATEAEKRQ-IAELRDDLSSAKIEREISE------EKLRREIRDLKEGI 443
Cdd:TIGR00606 656 AMLAGATAVYSQFITQLTDENqsccpvcqRVFQTEAELQEfISDLQSKLRLAPDKLKSTEselkkkEKRRDEMLGLAPGR 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 444 EREKERARIREIELRGEQSVLESKMESLRSRAEEVSS-----SATGESHAKLLRQIEVLQTQYAVASENWHGIEGsliar 518
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgtiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQ----- 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 519 lTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQE-------------------------------IERN 567
Cdd:TIGR00606 811 -QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDqqeqiqhlksktnelkseklqigtnlqrrqqFEEQ 889
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 240279359 568 LEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQE 619
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD 941
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
210-479 |
2.29e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 210 STDDYEEAMAQMRADHEMSELRwQEELHAYVERIDALQSKLKYLAKEAAESAKNAAASAEAgslEKKLLEKDEQIANLME 289
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAER---RETIEEKRERAEELRE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 290 EGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAED-RVSQAEIAE-QKALERLNSVSKAEKQLETA 367
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERiRTLLAAIADaEDEIERLREKREALAELNDE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 368 TAEReasnatitdlksqlaravsRAEAAERKARMEATEAEKRqIAELRDDLSSAKIEREISEEKLR--REIRD--LKE-- 441
Cdd:PRK02224 625 RRER-------------------LAEKRERKRELEAEFDEAR-IEEAREDKERAEEYLEQVEEKLDelREERDdlQAEig 684
|
250 260 270
....*....|....*....|....*....|....*...
gi 240279359 442 GIEREKERARireiELRGEQSVLESKMESLRSRAEEVS 479
Cdd:PRK02224 685 AVENELEELE----ELRERREALENRVEALEALYDEAE 718
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
302-476 |
2.30e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.19 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 302 RATIKKLRQSIAESAKSQAETKKRLEKVEKDlvnAEDRVSQAEIA-----EQKALERLNSVSKAEKQLETATAEREASNA 376
Cdd:COG1842 36 EEDLVEARQALAQVIANQKRLERQLEELEAE---AEKWEEKARLAlekgrEDLAREALERKAELEAQAEALEAQLAQLEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 377 TITDLKSQLARA--------------VSRAEAAErkarmeATEAEKRQIAELRDDLSSAKIEReiseeklrreirdLKEG 442
Cdd:COG1842 113 QVEKLKEALRQLeskleelkakkdtlKARAKAAK------AQEKVNEALSGIDSDDATSALER-------------MEEK 173
|
170 180 190
....*....|....*....|....*....|....
gi 240279359 443 IEREKERARIREiELRGEQSvLESKMESLRSRAE 476
Cdd:COG1842 174 IEEMEARAEAAA-ELAAGDS-LDDELAELEADSE 205
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
300-465 |
2.36e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.43 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 300 DHRATIKKLRQSIAESAKSQAETKKRLEKVEKDlvnAEDRVSQAEIA-----EQKALERLNSVSKAEKQLETATAEREAS 374
Cdd:pfam04012 33 DMQSELVKARQALAQTIARQKQLERRLEQQTEQ---AKKLEEKAQAAltkgnEELAREALAEKKSLEKQAEALETQLAQQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 375 NATITDLKSQLARAVSRAEAAERKARMEATEaEKRQIAELRDDLSSAKIEREISEEKLRReirdLKEGIEREKERARIRE 454
Cdd:pfam04012 110 RSAVEQLRKQLAALETKIQQLKAKKNLLKAR-LKAAKAQEAVQTSLGSLSTSSATDSFER----IEEKIEEREARADAAA 184
|
170
....*....|.
gi 240279359 455 iELRGEQSVLE 465
Cdd:pfam04012 185 -ELASAVDLDA 194
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
291-399 |
2.46e-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: 41.74 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 291 GQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLvnaEDRVSQAEIAEQKALERLNSVSKAEKQLETAT-- 368
Cdd:NF012221 1670 GKQLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDI---DDAKADAEKRKDDALAKQNEAQQAESDANAAAnd 1746
|
90 100 110
....*....|....*....|....*....|....*
gi 240279359 369 ----AEREASNAtitdlKSQLARAVSRAEAAERKA 399
Cdd:NF012221 1747 aqsrGEQDASAA-----ENKANQAQADAKGAKQDE 1776
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
272-613 |
2.62e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 272 SLEKKLLEKDEQIANLMEEgqklskteldhratIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKAL 351
Cdd:TIGR04523 128 KLEKQKKENKKNIDKFLTE--------------IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 352 ERLNSVSKAEKQLETATAEREASNATITDLKSQlaravsraeaaeRKARMEATEAEKRQIAELRDDLSSAKIEREISEEK 431
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNKSLESQISELKKQ------------NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 432 LRREIRDLKEGIeREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYavaSENWHGI 511
Cdd:TIGR04523 262 QNKIKKQLSEKQ-KELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQI---SQNNKII 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 512 EgSLIARLTAVETERDELERREGDLRRkareaslkakkvegELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLV 591
Cdd:TIGR04523 338 S-QLNEQISQLKKELTNSESENSEKQR--------------ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
330 340
....*....|....*....|..
gi 240279359 592 VKQdLAKQKEAEltlIQRLEEE 613
Cdd:TIGR04523 403 QEK-LNQQKDEQ---IKKLQQE 420
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
513-623 |
2.72e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 513 GSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASK---------QEIQNLTRKLT 583
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLKRRIS 106
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 240279359 584 KAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARR 623
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| PHA01972 |
PHA01972 |
structural protein |
273-451 |
3.21e-03 |
|
structural protein
Pssm-ID: 222842 Cd Length: 828 Bit Score: 41.06 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 273 LEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKkRLEKVEKDLVNAED---------RVSQA 343
Cdd:PHA01972 1 MPQKCVEAVAQAAGRQLTADEIKGIEDRIKEAMRSVARKDPKGWKEESIAK-RFYKTDADLARQELvhdaikkkkRVALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 344 EIAEQKALERLNSVSKAEKQLET------ATAEREASNATITDLKSQLARAVSRAEAAE-RKARMEATEAEKRQIA--EL 414
Cdd:PHA01972 80 IAKQAEATKKINEVLTADKDPAAallgmlSRDPNEEAKFLSVEQRINATRDVSKAKISDfMAALDPTTRQIFAGIAtgER 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 240279359 415 RDDLSSAKIEREISeeklrREIRDLKEGIEREKERAR 451
Cdd:PHA01972 160 RFDKAQQRLLDDIV-----HELYGRQTGNADAKKAAK 191
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
275-588 |
3.31e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 275 KKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVE--KD----LVNAEDRVSQAEIAEQ 348
Cdd:pfam05622 59 KKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEAQalKDemdiLRESSDKVKKLEATVE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 349 ---KALERLNSVSKAEKQLEtataEReasNATITDLKSQLARAVSRAEAAERKarmeaTEAEKRQIAELRDDLSsakiER 425
Cdd:pfam05622 139 tykKKLEDLGDLRRQVKLLE----ER---NAEYMQRTLQLEEELKKANALRGQ-----LETYKRQVQELHGKLS----EE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 426 EISEEKLRREIRDLKEGIE---REKERARI-----REI--ELRGEQSvleSKMESLRSRAEEVSSSATGESHAKLLRQIE 495
Cdd:pfam05622 203 SKKADKLEFEYKKLEEKLEalqKEKERLIIerdtlRETneELRCAQL---QQAELSQADALLSPSSDPGDNLAAEIMPAE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 496 VLQTQYAVASEN---WHGIEGSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEAS- 571
Cdd:pfam05622 280 IREKLIRLQHENkmlRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSs 359
|
330
....*....|....*....
gi 240279359 572 --KQEIQNLTRKLTKAEND 588
Cdd:pfam05622 360 llKQKLEEHLEKLHEAQSE 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
766-858 |
3.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 766 IRRLESERAAFKDEIVRLTAQRDEARQEVVELMREVEEKRkcDQRIQELEATVEQLDQRYQTTLEMLGEKSELVEELKAD 845
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNG--GDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
90
....*....|...
gi 240279359 846 ISDLKKIYRELVD 858
Cdd:COG4913 375 LPASAEEFAALRA 387
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
273-489 |
3.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 273 LEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRqsiaESAKSQAETKKRLEKVE-KDLVNAEDRVSQAEIAEQKAL 351
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD----ELEEELAELLKELEELGfESVEELEERLKELEPFYNEYL 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 352 ERLNSVSKAE---KQLETATAEREASNATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREIS 428
Cdd:PRK03918 606 ELKDAEKELEreeKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEEL 685
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240279359 429 EEKLRREIRDLKEGIEREKERARIREiELRGEQSVLEsKMESLRSRAEEVSSSATGESHAK 489
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKK-ELEKLEKALE-RVEELREKVKKYKALLKERALSK 744
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
770-856 |
3.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 770 ESERAAFKDEIVRLTAQRDEARQEVVELMREVEEKrkcDQRIQELEATVEQLDQRYQTTLemlgEKSELVEELKADISDL 849
Cdd:COG2433 405 ERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK---DERIERLERELSEARSEERREI----RKDREISRLDREIERL 477
|
....*..
gi 240279359 850 KKIYREL 856
Cdd:COG2433 478 ERELEEE 484
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
241-462 |
4.14e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 241 ERIDALQSKLKYLAKEAAESAKNAAASAEAGSLEKKLLEKDEQIANLMEEGQKLSKTEldhraTIKKLRQSIAEsAKSQA 320
Cdd:PRK10929 45 EIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNM-----STDALEQEILQ-VSSQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 321 ETKKRLEKVEKDLVNA-EDRVSQaeIAEQKalerlnsvSKAEKQLETATAEREASNATITDLkSQLARAVSRAEAAERKA 399
Cdd:PRK10929 119 LEKSRQAQQEQDRAREiSDSLSQ--LPQQQ--------TEARRQLNEIERRLQTLGTPNTPL-AQAQLTALQAESAALKA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 400 RMEATE-----AEKRQ-IAELRDDLSSAKIER-EISEEKLRREIRDLKegiEREKERArIREIELRGEQS 462
Cdd:PRK10929 188 LVDELElaqlsANNRQeLARLRSELAKKRSQQlDAYLQALRNQLNSQR---QREAERA-LESTELLAEQS 253
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
346-554 |
4.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 346 AEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAErkarmEATEAEKRQIAELRDDLSSAKIER 425
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAK-----TELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 426 EISEEKLrREIRDLKE--GIEREKErarireiELRGEQSVLESKMeslrsraeevsssatgeshAKLLRQIEVLQTQYAV 503
Cdd:COG1579 76 KKYEEQL-GNVRNNKEyeALQKEIE-------SLKRRISDLEDEI-------------------LELMERIEELEEELAE 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 240279359 504 ASENWHGIEGSLIARLTAVETERDELERREGDLRRKAREAslkAKKVEGEL 554
Cdd:COG1579 129 LEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL---AAKIPPEL 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
492-631 |
4.82e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 492 RQIEVLQTQYAVASENWHGIEgsliARLTAVETERDELERREGDLRR--KAREASLKAKKVEGELENSRAVIQEIERN-- 567
Cdd:COG4913 610 AKLAALEAELAELEEELAEAE----ERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASsd 685
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240279359 568 -LEASKQEIQNLTRKLTKAENDFLVVKQD---LAKQKEAELTLIQRLEEERARWQELARRPSSPFLQE 631
Cdd:COG4913 686 dLAALEEQLEELEAELEELEEELDELKGEigrLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
272-594 |
4.88e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 272 SLEKKLLEKDEQIANLMEEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKAL 351
Cdd:COG4372 49 QLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 352 ERLNSVSKAEKQLETATAEREasnATITDLKSQLARAVSRAEAAERKARMEATEAEKRQIAELRDDLSSAKIEREISEEK 431
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAERE---EELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 432 LRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSSSATGESHAKLLRQIEVLQTQYAVasENWHGI 511
Cdd:COG4372 206 EKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE--LEIAAL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 512 EGSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLV 591
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
...
gi 240279359 592 VKQ 594
Cdd:COG4372 364 EAG 366
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
312-439 |
5.17e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 39.63 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 312 IAESA-KSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLNSVSKAEKQLET---ATAEREASNA-TITDLKSQLA 386
Cdd:pfam00261 107 IAEEAdRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEAseeKASEREDKYEeQIRFLTEKLK 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 240279359 387 RAVSRAEAAERKA-RMEateaekRQIAELRDDLSSAKIEREISEEKLRREIRDL 439
Cdd:pfam00261 187 EAETRAEFAERSVqKLE------KEVDRLEDELEAEKEKYKAISEELDQTLAEL 234
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
273-542 |
5.30e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.38 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 273 LEKKLLEKDEQIANL---MEEGQKLSK--TELDHR----ATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQA 343
Cdd:NF033838 130 FKKDTLEPGKKVAEAtkkVEEAEKKAKdqKEEDRRnyptNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 344 EI---AEQKALERLNSVSKAEKQletatAEREASNATITDLKSQLARAVSRAEAAERKARME-------ATEAEKRQIAE 413
Cdd:NF033838 210 KAkveSKKAEATRLEKIKTDREK-----AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKrgvlgepATPDKKENDAK 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 414 LRDDL--------SSAKIEREISE-----EKLRREIRDLKEGIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSS 480
Cdd:NF033838 285 SSDSSvgeetlpsPSLKPEKKVAEaekkvEEAKKKAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAKE 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240279359 481 SATGEshakllrqiEVLQTQYAVASENwhgiegsliARLTAVETERDELERREGDLRRKARE 542
Cdd:NF033838 365 PRNEE---------KIKQAKAKVESKK---------AEATRLEKIKTDRKKAEEEAKRKAAE 408
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
323-439 |
5.82e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 37.80 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 323 KKRLEKVEKDLVNAEDRVSQAEIAEQkalerlnsvsKAEKQLETATAEREAsnatitdlksQLARAVSRAEAAERKARME 402
Cdd:cd06503 29 DEREEKIAESLEEAEKAKEEAEELLA----------EYEEKLAEARAEAQE----------IIEEARKEAEKIKEEILAE 88
|
90 100 110
....*....|....*....|....*....|....*..
gi 240279359 403 ATEAEKRQIAELRDDLSSakiEREISEEKLRREIRDL 439
Cdd:cd06503 89 AKEEAERILEQAKAEIEQ---EKEKALAELRKEVADL 122
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
518-613 |
6.11e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 518 RLTAVETERDELERREGDLRRKAREASLKAKKVEGELENSRAVIQEIERNLEASKQEIQNLTRKLTKAENDFLVVK---- 593
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnke 90
|
90 100
....*....|....*....|.
gi 240279359 594 -QDLAKQKEAELTLIQRLEEE 613
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDE 111
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
410-759 |
6.75e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 410 QIAELRDDLSSAKIEREISEEKLRReirdlkegIEREKERARIREIELRGEQSVLESKMESLRSRAEEVSssatgeshAK 489
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDA--------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE--------AE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 490 LLRQIEVLQTQYAVASENwhGIEGSLIARLTAVETERDELERRE--GDLRRKAREASLKAKKVEGELENSRAVIQEIERN 567
Cdd:COG3883 81 IEERREELGERARALYRS--GGSVSYLDVLLGSESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 568 LEASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRLEEERARWQELARRPSSPFLQEPPTGSPITFNRKQTAG 647
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 648 PDPTRPMSDRALSRRSSSIPPALFSELTTPPYQNHFSPTNSNPQQPRITPSHEFSGDLTHAQTYEPEEYFNGMSTPVTPS 727
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGG 318
|
330 340 350
....*....|....*....|....*....|..
gi 240279359 728 AQGTHTLTHHSRGVNDIISVSTVAAGPSVQVV 759
Cdd:COG3883 319 AGAVVGGASAGGGGGSGGGGGSSGGGSGGGGG 350
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
425-619 |
7.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 425 REISEEKLRREIRDLkegierEKERARIREIELRgEQSVLESKMESLRSRAEEvsssatgesHAKLLRQIEVLQTQYAva 504
Cdd:COG4717 44 RAMLLERLEKEADEL------FKPQGRKPELNLK-ELKELEEELKEAEEKEEE---------YAELQEELEELEEELE-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 505 senwhgiegSLIARLTAVETERDELERREGDLRRKAREASLKAKKVEG-----ELENSRAVIQEIERNLEASKQEIQNLT 579
Cdd:COG4717 106 ---------ELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELperleELEERLEELRELEEELEELEAELAELQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 240279359 580 RKLTKAENDFLVVK----QDLAKQKEAELTLIQRLEEERARWQE 619
Cdd:COG4717 177 EELEELLEQLSLATeeelQDLAEELEELQQRLAELEEELEEAQE 220
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
301-465 |
7.72e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 40.00 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 301 HRATIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAEDRVSQAEIAEQKALERLN-SVSKAekqLETATAEREASNATIT 379
Cdd:PTZ00491 596 HKNSAKIIRQAVFGSNDETGEVRDSLRFPANNLVITNVDVQSVEPVDERTRDSLQkSVQLA---IEITTKSQEAAARHQA 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 380 DLKSQLARA-------VSRAEAAERK-------ARMEATEAEKRQIAELRDDLSSAKIE--REISEEKLRREIRDLKEGI 443
Cdd:PTZ00491 673 ELLEQEARGrlerqkmHDKAKAEEQRtkllelqAESAAVESSGQSRAEALAEAEARLIEaeAEVEQAELRAKALRIEAEA 752
|
170 180
....*....|....*....|..
gi 240279359 444 EREKERARiREIELRGEQSVLE 465
Cdd:PTZ00491 753 ELEKLRKR-QELELEYEQAQNE 773
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
272-609 |
8.07e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 272 SLEKKLLEKDEQIANLMEEgqklskteldhratIKKLRQSIAESAKSQAETKKRLEKVEKDLVNAedrVSQAEIAEQKAL 351
Cdd:TIGR04523 58 NLDKNLNKDEEKINNSNNK--------------IKILEQQIKDLNDKLKKNKDKINKLNSDLSKI---NSEIKNDKEQKN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 352 ERLNSVSKAEKQLETATAEREASNATITDLKSQLarAVSRAEAAERKARMEATEAEK----RQIAELRDDLSSAKIEREI 427
Cdd:TIGR04523 121 KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL--EKLNNKYNDLKKQKEELENELnlleKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 428 SEEKLrreiRDLKEGIEREKErARIREIELRGEQSVLESKMESLRSRAEEVSS---------SATGESHAKLLRQIEVLQ 498
Cdd:TIGR04523 199 LELLL----SNLKKKIQKNKS-LESQISELKKQNNQLKDNIEKKQQEINEKTTeisntqtqlNQLKDEQNKIKKQLSEKQ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 499 TQyavaSENWHGIEGSLIARLTAVETERDELER-REGDLRRKAREaslKAKKVEGELENSRAVIQEIERNLEASKQEIQN 577
Cdd:TIGR04523 274 KE----LEQNNKKIKELEKQLNQLKSEISDLNNqKEQDWNKELKS---ELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350
....*....|....*....|....*....|..
gi 240279359 578 LTRKLTKAENDFLVVKQDLaKQKEAELTLIQR 609
Cdd:TIGR04523 347 LKKELTNSESENSEKQREL-EEKQNEIEKLKK 377
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
336-531 |
8.29e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.65 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 336 AEDRVsqaEIAEQKALERLNSVSKAEKQLETATAEREASNATITDLKSQLARAVSRAEAAERKARME-ATEA--EKRQIA 412
Cdd:COG1842 21 AEDPE---KMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDlAREAleRKAELE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 413 ELRDDLSSAKIEREISEEKLRREIRDLKEGIerekERARIREIELRGEQSVLESKmESLRSRAEEVSSSATGESHAKLLR 492
Cdd:COG1842 98 AQAEALEAQLAQLEEQVEKLKEALRQLESKL----EELKAKKDTLKARAKAAKAQ-EKVNEALSGIDSDDATSALERMEE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 240279359 493 QIEVLQTQYAVASEnwHGIEGSLIARLTAVETE---RDELER 531
Cdd:COG1842 173 KIEEMEARAEAAAE--LAAGDSLDDELAELEADsevEDELAA 212
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
766-856 |
8.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 766 IRRLESERAAFKDEIVRLTAQRDEARQEVVELMREVEEKRKCDQRIQELEATVEQLDQRYQTTLEMLGEKSELVEELKAD 845
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274
|
90
....*....|.
gi 240279359 846 ISDLKKIYREL 856
Cdd:PRK03918 275 IEELEEKVKEL 285
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
289-610 |
8.79e-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: 39.94 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 289 EEGQKLSKTELDHRATIKKLRQSIAESAKSQAETKKRLEK-------VEKDLVNAEDR-------VSQAEIAE--QKALE 352
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEElsaresdLEQDYQAASDHlnlvqtaLRQQEKIEryQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 353 RLNS--------VSKAEKQLETATAEREASNATITDLKSQLA--------------------RAVSRAEAAERKARMEAT 404
Cdd:COG3096 358 ELTErleeqeevVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqaldvqqtraiqyqqavQALEKARALCGLPDLTPE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 405 EAEKRQiAELRDDLSSAKIEREISEEKL------RRE-------IRDLKEGIEREKERARIREIELRG-EQSVLESKMES 470
Cdd:COG3096 438 NAEDYL-AAFRAKEQQATEEVLELEQKLsvadaaRRQfekayelVCKIAGEVERSQAWQTARELLRRYrSQQALAQRLQQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 471 LRSRAEEVsssatgESHAKLLRQIEVLQTQYAVASenwhgieGSLIARLTAVETERDELERREGDLRRKAREASLKAKKV 550
Cdd:COG3096 517 LRAQLAEL------EQRLRQQQNAERLLEEFCQRI-------GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSEL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 551 EGELENSRAVIQEIERN----------LE----------ASKQEIQNLTRKLTKAENDFLVVKQDLAKQKEAELTLIQRL 610
Cdd:COG3096 584 RQQLEQLRARIKELAARapawlaaqdaLErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
760-851 |
9.78e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 9.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240279359 760 ERMSTTIRRLESERAAFKDEIVRLTAQRDEARQEVVELMREVEEKRkcdQRIQELEATVEQLDQRYQTTLEMLGEKSELV 839
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ---AEEYELLAELARLEQDIARLEERRRELEERL 318
|
90
....*....|..
gi 240279359 840 EELKADISDLKK 851
Cdd:COG1196 319 EELEEELAELEE 330
|
|
|