|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
53-621 |
1.14e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 53 REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKfQEQNETFQASRAKMAEGLALALARKD 132
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA-QAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 133 QEwSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDARTRELNRT 212
Cdd:COG1196 313 EL-EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 213 QEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKV 292
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 293 ITHLQEKVIFLEKRLEQNLSGEDHVQELLKEktvAEQNLEDTR-QQLLAARNSHTKALYLLETRVKDLERSLQAAEEQLS 371
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEAD---YEGFLEGVKaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 372 QSRNVVADQEAqiQKLITTNQENSLSQQQVLALEQHCRERIHALEAQIEALEQTRVADQIASEQGMLQLQQENVALKESR 451
Cdd:COG1196 549 QNIVVEDDEVA--AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 452 NECEHsLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQL 531
Cdd:COG1196 627 LVAAR-LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 532 EKGHSSALLQMHKLQRELEALKtckaqeampattgedclpLQGQEPLVISKAMQNSEYELPAAEGTPNGEVGAsDLKQLQ 611
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALE------------------EQLEAEREELLEELLEEEELLEEEALEELPEPP-DLEELE 766
|
570
....*....|
gi 1907143872 612 KEKQDLEQQL 621
Cdd:COG1196 767 RELERLEREI 776
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-549 |
1.35e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.60 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 225 DLNERLEELQRHCSTLEeqRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLE 304
Cdd:COG1196 217 ELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 305 KRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQI 384
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 385 QKLITTNQENSLSQQQVLALEQHCRERIHALEAQIEALEQtrvaDQIASEQGMLQLQQENVALKESRNECEHSLQHHQLE 464
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE----RLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 465 LKKLKDEwsqreivsvaMAQALEEVRKQREEFQQQATELTAIIEEKNQslcEKDEALLQKEQELRQLEKGHSSALLQMHK 544
Cdd:COG1196 451 EAELEEE----------EEALLELLAELLEEAALLEAALAELLEELAE---AAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
....*
gi 1907143872 545 LQREL 549
Cdd:COG1196 518 GLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-504 |
6.90e-15 |
|
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: 78.95 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 151 SQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDARTRELNRTQEELVTSNQLSSDLNERL 230
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 231 EELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKRLEQN 310
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 311 lsgEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKalylLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITT 390
Cdd:TIGR02168 830 ---ERRIAATERRLEDLEEQIEELSEDIESLAAEIEE----LEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 391 NQENSLSQQQVLALEQHCRERIHALEAQIEALEQTR--VADQIASEQGM-LQLQQENVALKE-SRNECEHSLQHHQLELK 466
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGLEVRIdnLQERLSEEYSLtLEEAEALENKIEdDEEEARRRLKRLENKIK 982
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907143872 467 KLKDewsqreiVSVAMAQALEEVRKQREEFQQQATELT 504
Cdd:TIGR02168 983 ELGP-------VNLAAIEEYEELKERYDFLTAQKEDLT 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-422 |
8.96e-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: 72.40 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 121 AEGLALALARKDQEWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQ 200
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 201 ELDARTRELNRTQEELVTsnqlssdLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQ 280
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEE-------LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 281 KVTAETQEKEKVITHLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLL-------- 352
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLrseleels 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 353 ------ETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITT-NQENSLSQQQVLAL-------EQHCRERIHALEAQ 418
Cdd:TIGR02168 901 eelrelESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALenkieddEEEARRRLKRLENK 980
|
....
gi 1907143872 419 IEAL 422
Cdd:TIGR02168 981 IKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-441 |
1.38e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 139 MEQLEKDK------RFLTSQLQEVKNQSLSLfqKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDARTRELNRT 212
Cdd:COG1196 202 LEPLERQAekaeryRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 213 QEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKV 292
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 293 ITHLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVKDLERSLQAAEEQLSQ 372
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143872 373 SRNVVADQEAQIQKLITTNQENSLSQQQVLALEQHCRERIHALEAQIEALEQTRVADQIASEQGMLQLQ 441
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Grip |
smart00755 |
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245; |
683-728 |
4.58e-12 |
|
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
Pssm-ID: 197860 Cd Length: 46 Bit Score: 61.08 E-value: 4.58e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907143872 683 EINFEYLKHVVLKFMSCRESEAFHLIKAVSVLLNFSQEEENMLKET 728
Cdd:smart00755 1 EANFEYLKNVLLQFLTLRESERETLLPVISTVLQLSPEEMQKLLEV 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-640 |
6.81e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 59 QLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALE--KHQDSSM-RKFQEQNETFQASRAKMAEglalaLARKDQEW 135
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEelRLEVSELeEEIEELQKELYALANEISR-----LEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 136 SEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDARTRELNRTQEE 215
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 216 LVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVvlEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITH 295
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 296 LQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQ---QLLAARNSHTKALYLLETRVKDLERSLQAAEEQLSQ 372
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGG 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 373 SRN-VVADQEAQIQKLITTNQENSLSQQQVLALEQHCRERIHALEAQIEA--------------------------LEQT 425
Cdd:TIGR02168 546 RLQaVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsylLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 426 RVADQIASEQGMLQLQQENV--------------ALKESRNECEHSLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRK 491
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRK 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 492 QREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSSALLQMHKLQRELEALKTCKAQEAMPATTGEDCLP 571
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907143872 572 LQGQEPLVISKAMQNSEYELPAAEG---TPNGEVG--ASDLKQLQKEKQDLEQQLIEKNKIMKQMQQRMLELKK 640
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAeltLLNEEAAnlRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-533 |
7.66e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 201 ELDARTRELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLtaskagaEHKIVVLEQKEQELQAIIQQHSIDLQ 280
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-------RLEVSELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 281 KVTAETQEKEKVITHLQEKVIFLEKRLEQNLSGEDHVQELLKEKtvaEQNLEDTRQQLLAARNSHTKALYLLEtrvkDLE 360
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL---EEKLEELKEELESLEAELEELEAELE----ELE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 361 RSLQAAEEQLSQSRNVVADQEAQIQKLittnqenslsqqqvlaleqhcRERIHALEAQIEALEQTRVadqiaseqgmlQL 440
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASL---------------------NNEIERLEARLERLEDRRE-----------RL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 441 QQENVALKESRNECEHSLQHHQLELKKlkdewsqreivsvamaQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEA 520
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELE----------------EELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330
....*....|...
gi 1907143872 521 LLQKEQELRQLEK 533
Cdd:TIGR02168 484 LAQLQARLDSLER 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-375 |
1.24e-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: 62.00 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 42 GDDFASDGSSSREDLS--SQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEkhqdssmrkfQEQNETFQASRAK 119
Cdd:TIGR02168 652 GDLVRPGGVITGGSAKtnSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE----------ELEEELEQLRKEL 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 120 MAEGLALALARKD-QEWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKM 198
Cdd:TIGR02168 722 EELSRQISALRKDlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 199 EQELDARTRELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSID 278
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 279 LQKVTAETQEKEKVITHLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALY-LLETRVK 357
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeEAEALEN 961
|
330
....*....|....*...
gi 1907143872 358 DLERSLQAAEEQLSQSRN 375
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLEN 979
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
228-554 |
2.21e-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: 61.24 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 228 ERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQ----ELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFL 303
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKEAIERQLASLEEELEKLTEEISEL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 304 EKRLEQNLSGEDHVQELLKEKTVAEQNledtrqQLLAARNSHTKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQ 383
Cdd:TIGR02169 264 EKRLEEIEQLLEELNKKIKDLGEEEQL------RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 384 IQKLITTNQENSLSQQQVLALEQHCRERIHALEAQIEALEqtrvADQIASEQGMLQLQQENVALKESRNEcehslqhHQL 463
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD----KEFAETRDELKDYREKLEKLKREINE-------LKR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 464 ELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSSALLQMH 543
Cdd:TIGR02169 407 ELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS 486
|
330
....*....|.
gi 1907143872 544 KLQRELEALKT 554
Cdd:TIGR02169 487 KLQRELAEAEA 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
319-552 |
4.24e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 319 ELLKEKTVAEQNLEDTRQQLLAARnshtKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQENSLSQ 398
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELR----KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 399 QQVLALEQHCRERIHALEAQIEALEQTRVADQIASEQGMLQLQQENVALKESRNEcehslqhhqleLKKLKDEWSQREIV 478
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-----------LTLLNEEAANLRER 825
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907143872 479 SVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSSALLQMHKLQRELEAL 552
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-387 |
6.66e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 53 REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQD----------SSMRKFQEQNETFQASRAKMAe 122
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAElrelelallvLRLEELREELEELQEELKEAE- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 123 glalalarkdqewsEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQEL 202
Cdd:TIGR02168 253 --------------EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 203 DARTRELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKV 282
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 283 TAETQEKEKVITHLQEKVifleKRLEQNLSGEDHVQELLKEKTVAEQ--NLEDTRQQLLAARNSHTKALYLLETRVKDLE 360
Cdd:TIGR02168 399 NNEIERLEARLERLEDRR----ERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEEAE 474
|
330 340
....*....|....*....|....*..
gi 1907143872 361 RSLQAAEEQLSQSRNVVADQEAQIQKL 387
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENL 501
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
311-621 |
7.55e-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: 59.31 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 311 LSGEDHVQELLKEKTVAEQNLEDTRQQLLAARN---SHTKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKL 387
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 388 ITTNQENSLSQQQVLALEQHCRERIHALEAQIEALEQTrvadqiASEQGMLQLQQENVALKESRNECEHSLQHHQLELKK 467
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR------LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 468 LKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSSALLQMHKLQR 547
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907143872 548 ELEALKTCKAQEAMPATTGEDCLPLQGQEplviskamqNSEYELPAAEGTPNGEVGAsDLKQLQKEKQDLEQQL 621
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEE---------LSEIEDPKGEDEEIPEEEL-SLEDVQAELQRVEEEI 967
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
62-728 |
1.18e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 62 RRNEQIRKLEARLSDyAEQVRNLQKIKEKLEIalEKHQDSSMRKFQEQNETFQASRAKMAEGLALALARKDQEWSEKMEQ 141
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKD-AEEAKKAEEERNNEEI--RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 142 LEKdkrfltsqLQEVKNQSlslfQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKME---QELDARTRELNRTQEELVT 218
Cdd:PTZ00121 1301 KKK--------ADEAKKKA----EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaakAEAEAAADEAEAAEEKAEA 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 219 SNQLSSDLNERLEELQRHCstlEEQRDHLTASKAGAEHKIVVLEQKEQELQaiiQQHSIDLQKVTAETQEKEKVITHLQE 298
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKA---EEKKKADEAKKKAEEDKKKADELKKAAAA---KKKADEAKKKAEEKKKADEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 299 --KVIFLEKRLEQNLSGEDhvqelLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVKDLErsLQAAEEQLSQSRNV 376
Cdd:PTZ00121 1443 akKADEAKKKAEEAKKAEE-----AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKKKADEA 1515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 377 VADQEAQIQKLITTNQENSLSQQQVLALEQHCRERIHALEAQIEALEQTRVADQIASEQGMLQLQQENVALKESRNECEH 456
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE 1595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 457 SLQHHQLELKKLKDEWSQREIVSVAMAQAL---EEVRKQREEFQQQATELTAIIEE----------KNQSLCEKDEALLQ 523
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAEElkkaeeenkiKAAEEAKKAEEDKK 1675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 524 KEQELRQLEKGHSSALLQMHKLQRELEALKTCKAQEAMPATTGEDCLPLQGQEPLVISKAMQNSEYELPAAEGTPNGEVG 603
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 604 ASDLKQLQKEKQDLEQQLIEKNKIMKQMQQRMLELKKTLQKELKIRPDSELFEVREKTGPEipnmapsvtNNTDLTDARE 683
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE---------GNLVINDSKE 1826
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1907143872 684 INFEYLKHVVL-KFMSCRESEAF--HLIKAVSVLLNFSQEEENMLKET 728
Cdd:PTZ00121 1827 MEDSAIKEVADsKNMQLEEADAFekHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
62-558 |
1.24e-08 |
|
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: 58.83 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 62 RRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQASRAKMAEG-LALALARKDQEWSEKME 140
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRdLQGQLAHAKKQQELQQR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 141 QLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQeiskvKHMLLKKEECLGKMEQELDARTRELNRTQEELVTSN 220
Cdd:TIGR00618 439 YAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT-----KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 221 QLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKV 300
Cdd:TIGR00618 514 NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 301 IFLEKRLEQNLSGEDHVQELLKEKTVaEQNLEDTRQQLLAARNSHTKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQ 380
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLR-KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 381 EAQIQKLITTNQENSLSQQQVLALE--QHCRERIHALEAQIEALEQTRVADQIASEQGMLQLQQENVALKESRNECEHSL 458
Cdd:TIGR00618 673 ELLASRQLALQKMQSEKEQLTYWKEmlAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQA 752
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 459 QHHQLELKKLKDEWSQREIVSVAMAQALEEV-------RKQREEFQQQATELTAIIEEK----NQSLCEKDEALLQKEQE 527
Cdd:TIGR00618 753 RTVLKARTEAHFNNNEEVTAALQTGAELSHLaaeiqffNRLREEDTHLLKTLEAEIGQEipsdEDILNLQCETLVQEEEQ 832
|
490 500 510
....*....|....*....|....*....|.
gi 1907143872 528 LRQLEKGHSSALLQMHKLQRELEALKTCKAQ 558
Cdd:TIGR00618 833 FLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-644 |
2.24e-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: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 52 SREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQASRAKmaeglalaLARK 131
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS--------LERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 132 DQEWSEKMEQLEKDKRFLTSQLQEVKNQslslfqkRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDARTRELNR 211
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAE-------IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 212 TQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAiiqqhsiDLQKVTAETQEKEK 291
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE-------EKEDKALEIKKQEW 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 292 VITHLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVK----------DLER 361
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgSVGE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 362 SLQAAEEQLSQSR--NVVADQEAQIQKLITTNQENSLSQQQVLALEQHCRER---------------------------- 411
Cdd:TIGR02169 536 RYATAIEVAAGNRlnNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERrdlsilsedgvigfavdlvefdpkyepa 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 412 ----------IHALEAQIEALEQTRV-------------------------ADQIASEQGMLQLQQENVALKESRNECEH 456
Cdd:TIGR02169 616 fkyvfgdtlvVEDIEAARRLMGKYRMvtlegelfeksgamtggsraprggiLFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 457 SLQHHQLELKKLKDEWSQREivsvamaQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHS 536
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDAS-------RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 537 SALLQMHKLQRELEALKTCKAQEAMPATTGEdclpLQGQEPLV--ISKAMQNSEYELPAAEgtpngevgaSDLKQLQKEK 614
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAE----LSKLEEEVsrIEARLREIEQKLNRLT---------LEKEYLEKEI 835
|
650 660 670
....*....|....*....|....*....|
gi 1907143872 615 QDLEQQLIEKNKIMKQMQQRMLELKKTLQK 644
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
58-554 |
3.43e-08 |
|
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: 56.95 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 58 SQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQdSSMRKFQEQNETFQASRAKMAEGLalalarkdQEWSE 137
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT-TEISNTQTQLNQLKDEQNKIKKQL--------SEKQK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 138 KMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEidELEGFQQQEISKVKHMLLKKEECLGKMEQELDARTRELNRTQEELV 217
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 218 TSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQ 297
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 298 EKVIFLEKRLEqNLSGEDHVQELLKEktvaeqNLEDTRQQllaarnshtkalylLETRVKDLERSLQAAEEQLSQSRNVV 377
Cdd:TIGR04523 433 ETIIKNNSEIK-DLTNQDSVKELIIK------NLDNTRES--------------LETQLKVLSRSINKIKQNLEQKQKEL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 378 ADQEAQIQKLittNQENSLSQQQVLALEQhcreRIHALEAQIEALEQTRvadqiaseqgmLQLQQENVALKESRNECEHS 457
Cdd:TIGR04523 492 KSKEKELKKL---NEEKKELEEKVKDLTK----KISSLKEKIEKLESEK-----------KEKESKISDLEDELNKDDFE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 458 LQHHQLELKKLKdewSQREIVSvaMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSS 537
Cdd:TIGR04523 554 LKKENLEKEIDE---KNKEIEE--LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
490
....*....|....*..
gi 1907143872 538 ALLQMHKLQRELEALKT 554
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQ 645
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
68-428 |
3.58e-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: 57.39 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 68 RKLEARLSDYAEQVRNLQKIKEKLEIALEKHQ--DSSMRKFQEQNETFQASRAKMAEGLALALARKDQEWSEKM---EQL 142
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIErlDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLkekEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 143 EKDKRFLTSQLQEVKNQSLSLFQKRDEI-DELEgfqqqEISKVKHMLLKKEECLGkmEQELDARTRELNRTQEELVTSNQ 221
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELeKRLE-----EIEQLLEELNKKIKDLG--EEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 222 LSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVI 301
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 302 FLEKRLEQNLSGEDHVQ----ELLKEKTVAEQNLEDTRQQLLAARNSHTKalylLETRVKDLERSLQAAEEQLSQSRNVV 377
Cdd:TIGR02169 389 DYREKLEKLKREINELKreldRLQEELQRLSEELADLNAAIAGIEAKINE----LEEEKEDKALEIKKQEWKLEQLAADL 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907143872 378 ADQEAQIQKLITTNQENSlsqqqvlaleqhcrERIHALEAQIEALEQTRVA 428
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVE--------------KELSKLQRELAEAEAQARA 501
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-536 |
3.84e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.05 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 24 RIPRSVSKESVASMG----ADSGDDFASDGSSSREDLSSQLLRRNE----QIRKLEARLSDYAEQVRNLQKIKEKLEIAL 95
Cdd:pfam15921 268 RIEQLISEHEVEITGltekASSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKIEEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 96 EKH---QDSSMRKFQEQNETFQASRAKMAEGLALALARKDQEWSEKMEQLEKDKRFLTSQLqevkNQSLSLFQKRDEIDE 172
Cdd:pfam15921 348 EKQlvlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDT----GNSITIDHLRRELDD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 173 legfQQQEISKVKHML-LKKEECLGKMEQELDA-------------------RTRELNRTQEELVTSNQLSSDLNERleE 232
Cdd:pfam15921 424 ----RNMEVQRLEALLkAMKSECQGQMERQMAAiqgkneslekvssltaqleSTKEMLRKVVEELTAKKMTLESSER--T 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 233 LQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAI------IQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKR 306
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLknegdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 307 LEQN--LSGEDHVQELLKEKTVAEQNLEdtRQQLLAARNSHTKALYLLETRVKDLE----RSLQAAEEQLSQSRNVVADQ 380
Cdd:pfam15921 578 VGQHgrTAGAMQVEKAQLEKEINDRRLE--LQEFKILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKDIKQER 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 381 EAQIQKLITTNQE-NSLSQQQVLaLEQHCRERIHALE------------AQIEaLEQTR-------------------VA 428
Cdd:pfam15921 656 DQLLNEVKTSRNElNSLSEDYEV-LKRNFRNKSEEMEtttnklkmqlksAQSE-LEQTRntlksmegsdghamkvamgMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 429 DQIASEQGMLQLQQENVALKESRNECEHSLQHHQLELK-KLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTAII 507
Cdd:pfam15921 734 KQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKnKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
570 580
....*....|....*....|....*....
gi 1907143872 508 EEKNQSLCEKDEALLQKEQELRQLEKGHS 536
Cdd:pfam15921 814 DKASLQFAECQDIIQRQEQESVRLKLQHT 842
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
328-554 |
8.12e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 328 EQNLEDTRQQLLAARNshtkalyLLETRVKDLERSLQAAEEQLS--QSRNVVADQEAQIQklITTNQENSLSQQQVLAle 405
Cdd:COG3206 163 EQNLELRREEARKALE-------FLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAK--LLLQQLSELESQLAEA-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 406 qhcRERIHALEAQIEALEQtrvadQIASEQGMLQLQQENVALKESRNEcehsLQHHQLELKKLKDEWSQReivSVAMAQA 485
Cdd:COG3206 232 ---RAELAEAEARLAALRA-----QLGSGPDALPELLQSPVIQQLRAQ----LAELEAELAELSARYTPN---HPDVIAL 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143872 486 LEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSSALLQMHKLQRELEALKT 554
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| GRIP |
pfam01465 |
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ... |
683-725 |
1.28e-07 |
|
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.
Pssm-ID: 460221 [Multi-domain] Cd Length: 44 Bit Score: 48.50 E-value: 1.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1907143872 683 EINFEYLKHVVLKFMSCRE-SEAFHLIKAVSVLLNFSQEEENML 725
Cdd:pfam01465 1 GANLEYLKNVLLQFLESKEsSERKQLLPVIATLLKFSPEEEQKI 44
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
322-575 |
2.35e-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: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 322 KEKTVAEQNLEDTRQQLLAARnshtKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLittNQENSLSQQQV 401
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL---EAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 402 LALEQHCRERIHALEAQIEALEQTRVADQIaseqgMLQLQQENVALKESRNE-CEHSLQHHQLELKKLKDEWSQREIVSV 480
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPL-----ALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 481 AMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSSALLQMHKLQRELEALKTCKAQEA 560
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
250
....*....|....*
gi 1907143872 561 MPATTGEDCLPLQGQ 575
Cdd:COG4942 248 FAALKGKLPWPVSGR 262
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
52-333 |
3.09e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 52 SREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQD---SSMRKFQEQNETFQASRAKMAEgLALAL 128
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELKE-LEARI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 129 ARKDQEWSEKMEQLEKDKRFLT-SQLQEVKNQSLSLfqkRDEIDELEGfQQQEISKVKHMLLKKEECLGKMEQELDARTR 207
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEARLShSRIPEIQAELSKL---EEEVSRIEA-RLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 208 EL----NRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVT 283
Cdd:TIGR02169 844 DLkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907143872 284 AETQEKEKVITHLQEKVIFLEKRLEQNLSGEDhVQELLKEKTVAEQNLED 333
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRALEP 972
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
56-528 |
3.83e-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: 53.87 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 56 LSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNEtfqasrakmaeglalaLARKDQEW 135
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND----------------LKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 136 SEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQ---QQEISKVKHMLLKKEECLGKMEQELDARTRELNRT 212
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 213 QEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLE-QKEQ----ELQAIIQQHSIDLQKVTAETQ 287
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnQKEQdwnkELKSELKNQEKKLEEIQNQIS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 288 EKEKVITHLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVKDLERSLQAAE 367
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 368 EQLSQSRNVVADQEAQIQKLittNQENSLSQQQVLALEqhcrERIHALEAQIEALEQTRVadqiaseqgmlQLQQENVAL 447
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERL---KETIIKNNSEIKDLT----NQDSVKELIIKNLDNTRE-----------SLETQLKVL 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 448 KESRNECEHSLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQE 527
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
.
gi 1907143872 528 L 528
Cdd:TIGR04523 554 L 554
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
70-659 |
4.03e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 70 LEARLSDYAEQVRNLQKIKEKLEIALEKHQ---DSSMRKFQEQNETFQASRAKMAEglalALARKDQEWSEKMEQLEKDK 146
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfylRQSVIDLQTKLQEMQMERDAMAD----IRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 147 RFLTSQ--LQE--VKNQSLSLFQKRDEIDELEGFQQQeiskVKHMLLKKEECLGKMEQELDARTRELNRTqeelvtsnqL 222
Cdd:pfam15921 152 HELEAAkcLKEdmLEDSNTQIEQLRKMMLSHEGVLQE----IRSILVDFEEASGKKIYEHDSMSTMHFRS---------L 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 223 SSDLNERLEELQRHCSTLEEQ----RDHLTASKAGAEHKI-VVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQ 297
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRifpvEDQLEALKSESQNKIeLLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 298 EKV-IFLEKRLEQNLSGEDHVQEllkektvaeqnLEDTRQQLlaaRNSHTKALYLLETRVKDLERSLQAAEEQLSQSRnV 376
Cdd:pfam15921 299 SQLeIIQEQARNQNSMYMRQLSD-----------LESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEAR-T 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 377 VADQEAQiqklittNQENSLSQQQVLALEQHCRERIHALEA-QIEALEQTRVADQIASEQGMLQLQQENVA-------LK 448
Cdd:pfam15921 364 ERDQFSQ-------ESGNLDDQLQKLLADLHKREKELSLEKeQNKRLWDRDTGNSITIDHLRRELDDRNMEvqrlealLK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 449 ESRNECEHSLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTA---IIEEKNQSLCEKDEALLQKE 525
Cdd:pfam15921 437 AMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESserTVSDLTASLQEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 526 QELRQLEKGHSSALLQMHKLQRELEALKTCKAQeampattgEDCLPLQGQEPLVISKAMQNSEYELPAAEGTPNGEVGAs 605
Cdd:pfam15921 517 AEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE--------CEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGA- 587
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1907143872 606 dlkqlqkekqdleqQLIEKNKIMKQMQQRMLELkktlqKELKIRPDSELFEVRE 659
Cdd:pfam15921 588 --------------MQVEKAQLEKEINDRRLEL-----QEFKILKDKKDAKIRE 622
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
314-643 |
4.80e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 314 EDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKalyLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQE 393
Cdd:TIGR02169 186 IERLDLIIDEKRQQLERLRREREKAERYQALLKE---KREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 394 NslsQQQVLALEQhcreRIHALEAQIEAL---EQTRVADQIASEQGMLQLQQENVALKESRnecehsLQHHQLELKKLKD 470
Cdd:TIGR02169 263 L---EKRLEEIEQ----LLEELNKKIKDLgeeEQLRVKEKIGELEAEIASLERSIAEKERE------LEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 471 EWSQREIVSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSSALLQMHKLQRELE 550
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 551 ALKTCKAQEAMPATTGEDCLPLQGQEPLVISKAMQNSEYELPAAEGtpNGEVGASDLKQLQKEKQDLEQQLIEKNKIMKQ 630
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW--KLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
330
....*....|...
gi 1907143872 631 MQQRMLELKKTLQ 643
Cdd:TIGR02169 488 LQRELAEAEAQAR 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
158-560 |
6.51e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 158 NQSLSLFQKRDEIDELEgfqqqeiSKVKHmllkkeECLGKMEQELDARTRELNRTQEELVTSNQLSSDLNERL---EELQ 234
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKE-------EKDLH------ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLeehEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 235 RHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKRLEQnlsge 314
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE----- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 315 dhVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKL------I 388
Cdd:PRK02224 326 --LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELrerfgdA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 389 TTNQENSLSQQQVLALEqhcRERIHALEAQIEALEQTrVADQIASEQGMLQLQQ--------ENVALKESRNECEHSLQH 460
Cdd:PRK02224 404 PVDLGNAEDFLEELREE---RDELREREAELEATLRT-ARERVEEAEALLEAGKcpecgqpvEGSPHVETIEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 461 HQLELKKLKDEWSQREiVSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLE----KGHS 536
Cdd:PRK02224 480 LEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEaeaeEKRE 558
|
410 420
....*....|....*....|....
gi 1907143872 537 SALLQMHKLQRELEALKTCKAQEA 560
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLA 582
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
192-532 |
7.71e-07 |
|
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: 53.03 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 192 EECLGKMEQELDARtRELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQ----RDHLTaskagaehkivvLEQKEQE 267
Cdd:COG3096 278 NERRELSERALELR-RELFGARRQLAEEQYRLVEMARELEELSARESDLEQDyqaaSDHLN------------LVQTALR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 268 LQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKRLE--------------------------------------- 308
Cdd:COG3096 345 QQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEaaeeevdslksqladyqqaldvqqtraiqyqqavqalek 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 309 -QNLSG---------EDHVQELLKEKTVAEQNLEDTRQQLL---AARNSHTKALYLLETRVKDLERS--LQAAEEQLSQS 373
Cdd:COG3096 425 aRALCGlpdltpenaEDYLAAFRAKEQQATEEVLELEQKLSvadAARRQFEKAYELVCKIAGEVERSqaWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 374 RnvvaDQEAQIQklittnQENSLsQQQVLALEQHCRERiHALEAQIEALEQ---TRVADQIASEQGMLQLQQENVALKES 450
Cdd:COG3096 505 R----SQQALAQ------RLQQL-RAQLAELEQRLRQQ-QNAERLLEEFCQrigQQLDAAEELEELLAELEAQLEELEEQ 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 451 RNECEH---SLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTA----IIEEKNQSLCEKDEALLQ 523
Cdd:COG3096 573 AAEAVEqrsELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAamqqLLEREREATVERDELAAR 652
|
....*....
gi 1907143872 524 KEQELRQLE 532
Cdd:COG3096 653 KQALESQIE 661
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
324-644 |
1.05e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 324 KTVAEQNLEDTRQQLlaarNSHTKALYLLETRVKDLERSLQAAEEQLSQSrnvvaDQEAQIQKLITTNQENSL------S 397
Cdd:TIGR02168 174 RKETERKLERTRENL----DRLEDILNELERQLKSLERQAEKAERYKELK-----AELRELELALLVLRLEELreeleeL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 398 QQQVLALEQHCRERIHALEAQIEALEQTRVADQIASEQgMLQLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQREI 477
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE-IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 478 VSVAMAQALEE-------VRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSSALLQMHKLQRELE 550
Cdd:TIGR02168 324 QLEELESKLDElaeelaeLEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 551 ALKTCKAQEampattgEDCLPLQGQEPLVISKAMQNSEYELPAAEGTPNGEVgasdLKQLQKEKQDLEQQLIEKNKIMKQ 630
Cdd:TIGR02168 404 RLEARLERL-------EDRRERLQQEIEELLKKLEEAELKELQAELEELEEE----LEELQEELERLEEALEELREELEE 472
|
330
....*....|....
gi 1907143872 631 MQQRMLELKKTLQK 644
Cdd:TIGR02168 473 AEQALDAAERELAQ 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
315-551 |
1.26e-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: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 315 DHVQELLKEKTVAEQNLEDTRQQ--LLAARNSHTKALYLLETRVKDLER-----SLQAAEEQLSQSRNVVADQEAQIQKL 387
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQieLLEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 388 ittnqenslsQQQVLALEQhcreRIHALEAQIEALEQtrvadQIASEQG--MLQLQQENVALKESRNECEHSLQ--HHQL 463
Cdd:COG4913 308 ----------EAELERLEA----RLDALREELDELEA-----QIRGNGGdrLEQLEREIERLERELEERERRRArlEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 464 ELKKLKDEWSQREIVSV--AMAQALEEVRKQREEFQQQATELTAIIEEKNqslcekdEALLQKEQELRQLEKGHSSALLQ 541
Cdd:COG4913 369 AALGLPLPASAEEFAALraEAAALLEALEEELEALEEALAEAEAALRDLR-------RELRELEAEIASLERRKSNIPAR 441
|
250
....*....|
gi 1907143872 542 MHKLQRELEA 551
Cdd:COG4913 442 LLALRDALAE 451
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
127-533 |
1.36e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 127 ALARKDQEWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEgfqqQEISKVKHmllKKEEClgkmeqeldART 206
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLE----AEIEDLRE---TIAET---------ERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 207 RElnrtqeelvtsnqlssDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAET 286
Cdd:PRK02224 274 RE----------------ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 287 QEKEKVITHLQEKVIFLEKRLEQnlsGEDHVQELLKEKTVAEQNLEDTRQQLLAARN---SHTKALYLLETRVKDLERSL 363
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEE---LREEAAELESELEEAREAVEDRREEIEELEEeieELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 364 QAAEEQLSQSRNVVADQEAQIQklittNQENSLSQQQVLALEQHCRERIHALE--AQIEALEQTRV-ADQIASEQGMLQL 440
Cdd:PRK02224 415 EELREERDELREREAELEATLR-----TARERVEEAEALLEAGKCPECGQPVEgsPHVETIEEDRErVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 441 QQENVALKESRNEcehSLQHHQLELKKLKDewsQREIVSVAMAQA---LEEVRKQREEFQQQATELTAIIEEKNQSLCEK 517
Cdd:PRK02224 490 EVEEVEERLERAE---DLVEAEDRIERLEE---RREDLEELIAERretIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
410
....*....|....*.
gi 1907143872 518 DEALLQKEQELRQLEK 533
Cdd:PRK02224 564 EEEAEEAREEVAELNS 579
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
226-552 |
1.81e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 226 LNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEK 305
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 306 RLEQNLSGEDHVQELLKEKTVAEQNLEDTrqqllaarnshtkalyLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQ 385
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNDLEAR----------------LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 386 KLittnqenSLSQQQVLALEQHCRERIHALEAQIEALEQTRVADQIASEQGMLQLQQENVALKESRNecehslqhhqlEL 465
Cdd:TIGR02169 823 RL-------TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES-----------RL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 466 KKLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKEQElrqlekghSSALLQMHKL 545
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI--------PEEELSLEDV 956
|
....*..
gi 1907143872 546 QRELEAL 552
Cdd:TIGR02169 957 QAELQRV 963
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
51-644 |
3.17e-06 |
|
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: 50.74 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 51 SSREDLSSQLLRRNEQIRKLEARLSDYAEQvRNLQKIKEKLeIALEKHQDSSMRKFQEQNETFQASRAKMAEGLALALAR 130
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAVLEETQER-INRARKAAPL-AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 131 KDQEWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQkrdEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDARTRELN 210
Cdd:TIGR00618 334 VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR---EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 211 RTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHS---IDLQKVTAETQ 287
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQtkeQIHLQETRKKA 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 288 EKEKVITHLQEKVIFLEKRL-----EQNLSGED-----HVQELLKEKTVAEQNLEDTRQQLLAARNsHTKALYLLETRVK 357
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCihpnpARQDIDNPgpltrRMQRGEQTYAQLETSEEDVYHQLTSERK-QRASLKEQMQEIQ 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 358 DLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQEnsLSQQQVLALEQHCRERIHALEAQIEALEQTRVADQIASEQGM 437
Cdd:TIGR00618 570 QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE--AEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 438 LQLQQENVALKE-------SRNECEHSLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRKQRE---EFQQQATELTAII 507
Cdd:TIGR00618 648 LHALQLTLTQERvrehalsIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELEThieEYDREFNEIENAS 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 508 EEKNQSLCEKDEALLQKEQELRQL--EKGHSSALLQMHKLQRELEALKTCKAQEAMPATTGEDCLPLQGQEPLVISKAMQ 585
Cdd:TIGR00618 728 SSLGSDLAAREDALNQSLKELMHQarTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAE 807
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907143872 586 NSEYeLPAAEGTPNGEVgasdlKQLQKEKQDLEQQLIEKNKIMKQMQQRMLELKKTLQK 644
Cdd:TIGR00618 808 IGQE-IPSDEDILNLQC-----ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
125-323 |
3.49e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 125 ALALARKDQEWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDA 204
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 205 RTRELNRTQEELVT------------------SNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQ 266
Cdd:COG4942 95 LRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907143872 267 ELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKRLEQNLSGEDHVQELLKE 323
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
129-398 |
3.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 129 ARKDQEWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKvkhmllkkeeclgkmeQELDARTRE 208
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV----------------ASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 209 LNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQhsidlqkvtAETQE 288
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA---------AEDLA 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 289 KEKVITHLQEKVifleKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHtKALYLLETRvkDLERSLQAAEE 368
Cdd:COG4913 744 RLELRALLEERF----AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETA--DLDADLESLPE 816
|
250 260 270
....*....|....*....|....*....|....
gi 1907143872 369 QLSQSRNVVAD----QEAQIQKLITTNQENSLSQ 398
Cdd:COG4913 817 YLALLDRLEEDglpeYEERFKELLNENSIEFVAD 850
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
149-576 |
3.65e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 149 LTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKhmllkkeeclGKMEQELDARTRELNRTQEELVTSNQLSSDLNE 228
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDR----------EQWERQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 229 RLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQkeqelqaiiqqhsiDLQKVTAETQEKEKVITHLQEKViflEKRLE 308
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEE--------------DIKTLTQRVLERETELERMKERA---KKAGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 309 QNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKAlyllETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLI 388
Cdd:pfam07888 165 QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQR----DTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 389 TTNQENSLSQQQVLALEQHCRERIHALEAQIEALEQTRVAdqiaSEQGMLQLQQENVALKESR----NECEHSLQHHQLE 464
Cdd:pfam07888 241 SLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQ----AAQLTLQLADASLALREGRarwaQERETLQQSAEAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 465 LKK--------------LKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTAIIEeknqslcekdeaLLQKEQELRQ 530
Cdd:pfam07888 317 KDRieklsaelqrleerLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLR------------VAQKEKEQLQ 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907143872 531 LEKghSSALLQMHKLQRELEALKTCKAQEAMPATTGEDCLPLQGQE 576
Cdd:pfam07888 385 AEK--QELLEYIRQLEQRLETVADAKWSEAALTSTERPDSPLSDSE 428
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
196-532 |
5.03e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 196 GKMEQELDARtRELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQ----RDHLTASKAGaehkivvLEQKEQelqai 271
Cdd:PRK04863 283 VHLEEALELR-RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDyqaaSDHLNLVQTA-------LRQQEK----- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 272 IQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKRLEQnlsgedhvqellkektvAEQNLEDTRQQLlaarNSHTKALYL 351
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEADEQQEENEARAEA-----------------AEEEVDELKSQL----ADYQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 352 LETRVKDLERSLQAAEE--QLSQSRNVVAD------QEAQIQKLITTNQENSLSQQQVL---ALEQHCR--ERIHALEAQ 418
Cdd:PRK04863 409 QQTRAIQYQQAVQALERakQLCGLPDLTADnaedwlEEFQAKEQEATEELLSLEQKLSVaqaAHSQFEQayQLVRKIAGE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 419 IEALEQTRVADQIASEQGMLQLQQENV-ALKESRNECEHSLQHHQlELKKLKDEWSQREIVSVAMAqaleevrkqrEEFQ 497
Cdd:PRK04863 489 VSRSEAWDVARELLRRLREQRHLAEQLqQLRMRLSELEQRLRQQQ-RAERLLAEFCKRLGKNLDDE----------DELE 557
|
330 340 350
....*....|....*....|....*....|....*
gi 1907143872 498 QQATELTAIIEEKNQSLCEKDEALLQKEQELRQLE 532
Cdd:PRK04863 558 QLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
274-531 |
7.22e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 274 QHSID-LQKVTAETQEKEKVITHLQEKVIFLEKRLEQNLSGEDHVQEL------LKEKTVAEQNLEDTRQQLLAARNShT 346
Cdd:PRK11281 42 QAQLDaLNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLaqapakLRQAQAELEALKDDNDEETRETLS-T 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 347 KALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQ---IQKLITTNQENSlsqQQVlaleqhcRERIHALEAQIEALE 423
Cdd:PRK11281 121 LSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperAQAALYANSQRL---QQI-------RNLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 424 QTRVaDQIASEQGMLQLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQREIvsvamaQALEEV--RKQREEFQQQAT 501
Cdd:PRK11281 191 PSQR-VLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQL------QLLQEAinSKRLTLSEKTVQ 263
|
250 260 270
....*....|....*....|....*....|.
gi 1907143872 502 EltAIIEEKNQSLceKDEALLQKEQEL-RQL 531
Cdd:PRK11281 264 E--AQSQDEAARI--QANPLVAQELEInLQL 290
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-553 |
7.86e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 54 EDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEialekHQDSSMRKFQEQNETFqasrakmaeglaLALARKDQ 133
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-----EKVKELKELKEKAEEY------------IKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 134 EWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQ---QQEISKVKHMLLKKEECLGKMEQELDARTRELN 210
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelEKRLEELEERHELYEEAKAKKEELERLKKRLTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 211 RTQEElvtsnqlssdLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQA-----------IIQQHSIDL 279
Cdd:PRK03918 384 LTPEK----------LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKEL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 280 -QKVTAETQEKEKVITHLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQnLEDTRQQL----LAARNSHTKALYLLET 354
Cdd:PRK03918 454 lEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLkkynLEELEKKAEEYEKLKE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 355 RVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQENSLSQQQvlaLEQHCRERIHALEAQIEALEqtrvadqiase 434
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE---LEELGFESVEELEERLKELE----------- 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 435 qgmlQLQQENVALKESRNECEHSLQhhqlELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTaiIEEKNQSL 514
Cdd:PRK03918 599 ----PFYNEYLELKDAEKELEREEK----ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE--YEELREEY 668
|
490 500 510
....*....|....*....|....*....|....*....
gi 1907143872 515 CEKDEALLQKEQELRQLEKGHSSALLQMHKLQRELEALK 553
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
65-553 |
8.94e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 65 EQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQASRAKMAEGLALALARKDQEWSEKMEQLEK 144
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 145 dkrfLTSQLQEVKNQSLSLFQKRDEIDELEgfqqqeiskvkhmllkkEECLGKMEQELDARTRELNRTQEELVTSNQLSS 224
Cdd:COG4717 151 ----LEERLEELRELEEELEELEAELAELQ-----------------EELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 225 DLNERLEELQRHCSTLEEQRDHLTASKAgAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEK------VITHLQE 298
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELE-AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagvlflVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 299 KVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQL---LAARNSHTKALYLLETRVKDLERSLQAAEEQLSQSRN 375
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 376 vvadqEAQIQKLITTNQENSLSQqqvlaLEQHCR--ERIHALEAQIEALEQtrvadqiaseqgmlqlqqenvALKESRNE 453
Cdd:COG4717 369 -----EQEIAALLAEAGVEDEEE-----LRAALEqaEEYQELKEELEELEE---------------------QLEELLGE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 454 CEHSLQHHQLElkKLKDEWSQREivsvamaQALEEVRKQREEFQQQATELTAIIE--EKNQSLCEKDEALLQKEQELRQL 531
Cdd:COG4717 418 LEELLEALDEE--ELEEELEELE-------EELEELEEELEELREELAELEAELEqlEEDGELAELLQELEELKAELREL 488
|
490 500
....*....|....*....|..
gi 1907143872 532 EKGHSSALLQMHKLQRELEALK 553
Cdd:COG4717 489 AEEWAALKLALELLEEAREEYR 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
148-375 |
1.21e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 148 FLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKhmllKKEECLGKMEQELDARTRELNRTQEELVTSNQLSSDLN 227
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEK----ALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 228 ERLEELQRhcsTLEEQRDHL-----TASKAGAEHKIVVLEQKEQELQAIIQQHSidLQKVTAETQEKEKVITHLQEKVIF 302
Cdd:COG4942 90 KEIAELRA---ELEAQKEELaellrALYRLGRQPPLALLLSPEDFLDAVRRLQY--LKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907143872 303 LEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAA----RNSHTKALYLLETRVKDLERSLQAAEEQLSQSRN 375
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARlekeLAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
314-443 |
1.43e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.92 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 314 EDHVQELLKEKTVAEQNLEDTRQQLLAARNshtkalyllETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQE 393
Cdd:COG3524 176 EDAVRFAEEEVERAEERLRDAREALLAFRN---------RNGILDPEATAEALLQLIATLEGQLAELEAELAALRSYLSP 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907143872 394 NSlSQQQVLaleqhcRERIHALEAQIEAlEQTRVAD--------QIASEQGMLQLQQE 443
Cdd:COG3524 247 NS-PQVRQL------RRRIAALEKQIAA-ERARLTGasggdslaSLLAEYERLELERE 296
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
55-509 |
2.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 55 DLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKhqdssMRKFQEQNETFQASRAKMAEGLALALARKD-- 132
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR-----LEELEERHELYEEAKAKKEELERLKKRLTGlt 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 133 -QEWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDE----IDELEGfqqqeiSKVKHMLLKKEECLGKMEQELDARTR 207
Cdd:PRK03918 386 pEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKElkkaIEELKK------AKGKCPVCGRELTEEHRKELLEEYTA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 208 ELNRTQEELVTSNQLSSDLNERLEELQrhcSTLEEQRDhLTASKAGAEHkivvLEQKEQELQaiiqqhSIDLQKVTAETQ 287
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELE---KVLKKESE-LIKLKELAEQ----LKELEEKLK------KYNLEELEKKAE 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 288 EKEKvithLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLlaaRNSHTKALYLLETRVKDLERSLQAAE 367
Cdd:PRK03918 526 EYEK----LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEL---AELLKELEELGFESVEELEERLKELE 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 368 E------QLSQSRNVVADQEAQIQKLITTNQENSLSQQQVLALEQHCRERIHALEAQIEALEQTRVADQiaseqgMLQLQ 441
Cdd:PRK03918 599 PfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREE------YLELS 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907143872 442 QENVALKESRNECEHSLQHHQLELKKLKDEWSQREIVSVAMaQALEEVRKQREEFQQQATELTAIIEE 509
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVKKYKALLKE 739
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
146-299 |
3.40e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 146 KRFLTSQLQEVKNQSLSLFQkrDEIDELEGFQQQEISKVKHMLLKKEEclgKMEQELDARTRELNRTQEELvtsNQLSSD 225
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRN---EFEKELRERRNELQKLEKRL---LQKEEN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907143872 226 LNERLEELQRHCSTLEEQRDHLtaskagaEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQE--KEKVITHLQEK 299
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKEL-------EQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE 166
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
167-388 |
5.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 167 RDEIDELEGFQQqEISKVKhmllKKEECLgkmeQELDARTRELNRTQEELVTSNQLSSDLN-----ERLEELQRHCSTLE 241
Cdd:COG4913 231 VEHFDDLERAHE-ALEDAR----EQIELL----EPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 242 EQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHS-IDLQKVTAETQEKEKVITHLQEKVIFLEKRLEQ-NLSGEDHVQE 319
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAlGLPLPASAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143872 320 LLKEKTVAEQNLEDTRQQLLAARNshtkALYLLETRVKDLERSLQAAE---EQLSQSRNVVADQEAQIQKLI 388
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEE----ALAEAEAALRDLRRELRELEaeiASLERRKSNIPARLLALRDAL 449
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
138-435 |
6.16e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 138 KMEQLEKDKRFLTSQLQevknQSLSLFQKRDEID-ELEGFQQQ------EISKVKHML--LKKEE-----------CLGK 197
Cdd:PRK11281 50 KQKLLEAEDKLVQQDLE----QTLALLDKIDRQKeETEQLKQQlaqapaKLRQAQAELeaLKDDNdeetretlstlSLRQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 198 MEQELDARTRELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAG--AEHKIVVLEQKEQeLQAiiQQH 275
Cdd:PRK11281 126 LESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGgkVGGKALRPSQRVL-LQA--EQA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 276 SIDLQkvtaetqekekviTHLQekviflekrlEQNLSGEDHVQELLK----EKTVAEQNLEDTRQQLLAARNShtKALYL 351
Cdd:PRK11281 203 LLNAQ-------------NDLQ----------RKSLEGNTQLQDLLQkqrdYLTARIQRLEHQLQLLQEAINS--KRLTL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 352 LETRVKDLERSLQAAEeqlSQSRNVVAdQEAQI-----QKLI-TTNQENSLSQQ-----QVL-ALEQHCRerihALEAQI 419
Cdd:PRK11281 258 SEKTVQEAQSQDEAAR---IQANPLVA-QELEInlqlsQRLLkATEKLNTLTQQnlrvkNWLdRLTQSER----NIKEQI 329
|
330
....*....|....*.
gi 1907143872 420 EALEQTRVADQIASEQ 435
Cdd:PRK11281 330 SVLKGSLLLSRILYQQ 345
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
53-446 |
7.49e-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: 46.48 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 53 REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQASRAKMAE-GLALA---- 127
Cdd:COG3096 845 RSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQhGKALAqlep 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 128 LARKDQEWSEKMEQLEKDKRFLTSQLQEVKNQslsLFQKRDEIDELEGFQQQEiskvkhmllkkeeclgkmEQELDARTR 207
Cdd:COG3096 925 LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQ---IFALSEVVQRRPHFSYED------------------AVGLLGENS 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 208 ELN-RTQEELVTSNQLSSDLNERLEELQRHCStleEQRDHLTASKAGAEHKIVVLEQKEQELQAI-IQQHSIDLQKVTAE 285
Cdd:COG3096 984 DLNeKLRARLEQAEEARREAREQLRQAQAQYS---QYNQVLASLKSSRDAKQQTLQELEQELEELgVQADAEAEERARIR 1060
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 286 TQEKEKVITHLQEKVIFLEKRLEQNLSGEDHVQELLKEktvAEQNLEDTRQQLLAARNSHTKALYL-----LETRVKDLE 360
Cdd:COG3096 1061 RDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRK---AERDYKQEREQVVQAKAGWCAVLRLardndVERRLHRRE 1137
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 361 RSLQAAEEQLSQS-------RNVVADQEAqIQKLITTNQENSLSQQQV---LALEQHCRERIHALEAQ----IEALEQ-- 424
Cdd:COG3096 1138 LAYLSADELRSMSdkalgalRLAVADNEH-LRDALRLSEDPRRPERKVqfyIAVYQHLRERIRQDIIRtddpVEAIEQme 1216
|
410 420
....*....|....*....|....*
gi 1907143872 425 ---TRVADQIASEQGMLQLQQENVA 446
Cdd:COG3096 1217 ielARLTEELTSREQKLAISSESVA 1241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
228-495 |
8.31e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 228 ERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQ--HSIDLQKVTAETQEkekvithlqekvifLEK 305
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYswDEIDVASAEREIAE--------------LEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 306 RLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKalylLETRVKDLERSLQAAEEQLSQSRNVVADQ----- 380
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGR----LEKELEQAEEELDELQDRLEAAEDLARLElrall 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 381 EAQIQKLITTNQENSLSQQQVLALEQHcRERIHALEAQIEALEQT-------RVADQIASEQGMLQLQQENVALKESRne 453
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERIDAL-RARLNRAEEELERAMRAfnrewpaETADLDADLESLPEYLALLDRLEEDG-- 828
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907143872 454 cehsLQHHQLELKKLKDEWSQREIV--SVAMAQALEEVRKQREE 495
Cdd:COG4913 829 ----LPEYEERFKELLNENSIEFVAdlLSKLRRAIREIKERIDP 868
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
112-342 |
9.57e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 112 TFQASRAKMAEGLALALARKDQEWS--EKMEQLEKDKRFLTSQLQEVKNQ------SLSLFQKRDEIDELEGFQQQEISK 183
Cdd:COG3206 141 SYTSPDPELAAAVANALAEAYLEQNleLRREEARKALEFLEEQLPELRKEleeaeaALEEFRQKNGLVDLSEEAKLLLQQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 184 VKHMllkkEECLGKMEQELDARTRELNRTQEELVTSNQLSSDL--NERLEELQRHCSTLEEQRDHLTAsKAGAEH-KIVV 260
Cdd:COG3206 221 LSEL----ESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSA-RYTPNHpDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 261 LEQKEQELQAIIQQ------HSIDLQKVTAETQEKEkvithLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDT 334
Cdd:COG3206 296 LRAQIAALRAQLQQeaqrilASLEAELEALQAREAS-----LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
....*...
gi 1907143872 335 RQQLLAAR 342
Cdd:COG3206 371 LQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-520 |
9.99e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 247 LTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKRLeqnlsgedhvqellkektv 326
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 327 aeQNLEDTRQQllaarnshtkalylLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQENSL----SQQQVL 402
Cdd:COG4942 72 --RALEQELAA--------------LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLlspeDFLDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 403 ALEQHCRERIHALEAQIEALEQTRVadqiaseqgmlQLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQREIVSVAM 482
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLA-----------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907143872 483 AQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEA 520
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
167-475 |
1.00e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 167 RDEIDELEGFQQQEISKVKHMLLKKE-ECLGKMEQELDARTRELNrtQEELVTSNQLSSDLNERlEELQRHCSTLEeqrd 245
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQlEDLVGMIQNAEKNILLLN--QARLQALEDLEKILTEK-EALQGKINILE---- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 246 hLTASKAGAEHKIVVLEQKEQElqaIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKrlEQNLSGEDHVQeLLKEKT 325
Cdd:PLN02939 177 -MRLSETDARIKLAAQEKIHVE---ILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLK--EENMLLKDDIQ-FLKAEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 326 VAEQNLEDTRQQLLAARNshtkalyLLETRVKDLERSLQAAEEQLSQSR----NVVADQEAQIQKLI--TTNQenslSQQ 399
Cdd:PLN02939 250 IEVAETEERVFKLEKERS-------LLDASLRELESKFIVAQEDVSKLSplqyDCWWEKVENLQDLLdrATNQ----VEK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 400 QVLALEQH--CRERIHALEaqiEALEQTRVAdQIASEqgMLQLQQENVALKESRNEC------------EHSLQHHQLEL 465
Cdd:PLN02939 319 AALVLDQNqdLRDKVDKLE---ASLKEANVS-KFSSY--KVELLQQKLKLLEERLQAsdheihsyiqlyQESIKEFQDTL 392
|
330
....*....|
gi 1907143872 466 KKLKDEWSQR 475
Cdd:PLN02939 393 SKLKEESKKR 402
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-535 |
1.11e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 51 SSREDLSSQLLRRNEQIR-------KLEARLSDYAEQVRNLQKIKEKLE------IALEKHQDSSMRKFQEQNETFQASR 117
Cdd:PRK02224 213 SELAELDEEIERYEEQREqaretrdEADEVLEEHEERREELETLEAEIEdlretiAETEREREELAEEVRDLRERLEELE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 118 AKMAEGLA-LALARKDQE-WSEKMEQLEKDKRFLTSQLQEVKnQSLSLFQK-----RDEIDELEGFQQqeiskvkhmllK 190
Cdd:PRK02224 293 EERDDLLAeAGLDDADAEaVEARREELEDRDEELRDRLEECR-VAAQAHNEeaeslREDADDLEERAE-----------E 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 191 KEECLGKMEQELDARTRELNRTQEELvtsnqlsSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQA 270
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEI-------EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 271 IIQqhsiDLQKVTAETQEkekvithLQEKVIFLEkrLEQNLSGEDHVqELLKEKTVAEQNLEDTRQQL------LAARNS 344
Cdd:PRK02224 434 TLR----TARERVEEAEA-------LLEAGKCPE--CGQPVEGSPHV-ETIEEDRERVEELEAELEDLeeeveeVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 345 HTKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQE--NSLSQQQVLALEQH-----CRERIHALEA 417
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEleAEAEEKREAAAEAEeeaeeAREEVAELNS 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 418 QIEALEQTRvaDQIASEQGMLQLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQR--EIVSVAMAQALEEVRKQR-- 493
Cdd:PRK02224 580 KLAELKERI--ESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERkrELEAEFDEARIEEAREDKer 657
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1907143872 494 -EEFQQQATELTAIIEEKNQSLCEKDEALLQKEQELRQLEKGH 535
Cdd:PRK02224 658 aEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR 700
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
60-344 |
1.14e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 60 LLRRNEQIRKLEARLSDYAEQVRNLQK-------IKEKLEIALEKHQDSSMRKFqeqNETFQASraKMAEGL-ALALARK 131
Cdd:COG5022 798 KLQPLLSLLGSRKEYRSYLACIIKLQKtikrekkLRETEEVEFSLKAEVLIQKF---GRSLKAK--KRFSLLkKETIYLQ 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 132 DQEWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQK---------RDEIDELEgFQQQEISKVKHMLLK--------KEEC 194
Cdd:COG5022 873 SAQRVELAERQLQELKIDVKSISSLKLVNLELESEiielkkslsSDLIENLE-FKTELIARLKKLLNNidleegpsIEYV 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 195 LGKMEQELDARTRELNRTQEE----LVTSNQLSSDLNERLEELQRHCSTLEE---QRDHLTASKAGAEHKIVVLEQKEQE 267
Cdd:COG5022 952 KLPELNKLHEVESKLKETSEEyedlLKKSTILVREGNKANSELKNFKKELAElskQYGALQESTKQLKELPVEVAELQSA 1031
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 268 LQAIIQQHSI-----DLQKVTAETQEKEKViTHLQEKVIFLEKRLEQNLSGEDHVQELL--KEKTVAEQNLEDTRQQLLA 340
Cdd:COG5022 1032 SKIISSESTElsilkPLQKLKGLLLLENNQ-LQARYKALKLRRENSLLDDKQLYQLESTenLLKTINVKDLEVTNRNLVK 1110
|
....
gi 1907143872 341 ARNS 344
Cdd:COG5022 1111 PANV 1114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
58-650 |
1.16e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 58 SQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQAsrakmaEGLALALARKDQEWSE 137
Cdd:TIGR00618 146 VVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS------QLLTLCTPCMPDTYHE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 138 KMEQLEKDKRFLTSQLQEVKnQSLSLFQKRDEIDELEGFQQQEISKVKhmllkkeeclgKMEQELDARTRELNRTQEELV 217
Cdd:TIGR00618 220 RKQVLEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLKKQQLLKQLR-----------ARIEELRAQEAVLEETQERIN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 218 TSNQLssdlnERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAiiQQHSIDLQKVTAET-QEKEKVITHL 296
Cdd:TIGR00618 288 RARKA-----APLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTlHSQEIHIRDA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 297 QEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRvKDLERSLQAAEEQLSQSRNV 376
Cdd:TIGR00618 361 HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKKQQELQQRY 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 377 VADQEAQIQKLITtnqenslSQQQVLALEQHCRERIHALEAQIEALEQ--TRVADQIASEQGMLQLQQENVALKESRneC 454
Cdd:TIGR00618 440 AELCAAAITCTAQ-------CEKLEKIHLQESAQSLKEREQQLQTKEQihLQETRKKAVVLARLLELQEEPCPLCGS--C 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 455 EHSLQHHQL---------ELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATEL---TAIIEEKNQSLCEKDEALL 522
Cdd:TIGR00618 511 IHPNPARQDidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqqsFSILTQCDNRSKEDIPNLQ 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 523 QKEQELRQLEKGHSSALLQMHKLQRELEALKTCKAQEAMPATTGEDCLPLQGQEPLVISKAMQNSEYELPAAEGTPNGEV 602
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL 670
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1907143872 603 GASDLKQLQKEKQDLEQQLIEKNKIMKQMQQRMLELKKTLQKELKIRP 650
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDR 718
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
54-556 |
1.35e-04 |
|
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: 45.55 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 54 EDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEialekhqdSSMRKFQEQNETFQASRAKMaeglalalarkdq 133
Cdd:pfam01576 232 AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELE--------AQISELQEDLESERAARNKA------------- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 134 ewsekmeqlEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDAR-TRELNRT 212
Cdd:pfam01576 291 ---------EKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKhTQALEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 213 QEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSID-------LQKVTAE 285
Cdd:pfam01576 362 TEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQraelaekLSKLQSE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 286 TQEKEKVITHLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVKDLERSLQA 365
Cdd:pfam01576 442 LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLST 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 366 AEEQLSQSRNVVADQEAQIQKLITTNQEnslSQQQVLALEQHCRERihalEAQIEALEQTRVADQIASEQGMLQLQQEN- 444
Cdd:pfam01576 522 LQAQLSDMKKKLEEDAGTLEALEEGKKR---LQRELEALTQQLEEK----AAAYDKLEKTKNRLQQELDDLLVDLDHQRq 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 445 --VALKESRNECEHSLQHHQLELKKLKDEWSQ-------REIVSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLC 515
Cdd:pfam01576 595 lvSNLEKKQKKFDQMLAEEKAISARYAEERDRaeaeareKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKD 674
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1907143872 516 EKDEALLQKEQELRQLEKGHSSALLQMHKLQRELEALKTCK 556
Cdd:pfam01576 675 DVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
51-423 |
1.50e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 51 SSREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQASRAKMAEGLALALAR 130
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 131 KDQEwsEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECL----------GKMEQ 200
Cdd:COG1196 459 EALL--ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligVEAAY 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 201 ELDARTRELNRTQEELVTSNQLSSDLNERLEE----------LQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQA 270
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 271 IIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALY 350
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 351 LLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQENSLSQQQVLALE-----------QHCRERIHALEAQI 419
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdlEELERELERLEREI 776
|
....
gi 1907143872 420 EALE 423
Cdd:COG1196 777 EALG 780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-458 |
1.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 254 AEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQekviflekRLEQNLSGEDHVQELLKEktvaeqnLED 333
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ--------RLAEYSWDEIDVASAERE-------IAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 334 TRQQLLAARNSHTKalylletrvkdlersLQAAEEQLSQSRNVVADQEAQIQKLITTNQENSLSQQQVLALEQHCRERIH 413
Cdd:COG4913 673 LEAELERLDASSDD---------------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907143872 414 ALEAQIEALEQTRVADQIASEQG-------MLQLQQENVALKESRNECEHSL 458
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGdaverelRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
68-531 |
2.21e-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: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 68 RKLEARLSDYAEQVRNLQKIKEKLEIALEKHQdsSMRKFQEQNETFQASRAKMAEGLALALA-------RKDQEWSEKME 140
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIE--LLEPIRELAERYAAARERLAELEYLRAAlrlwfaqRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 141 QLEKDKRFLTSQLQEVKNQslsLFQKRDEIDELEGfQQQEISKVKHMLLKKEecLGKMEQELDARTRELNRTQEEL---- 216
Cdd:COG4913 299 ELRAELARLEAELERLEAR---LDALREELDELEA-QIRGNGGDRLEQLERE--IERLERELEERERRRARLEALLaalg 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 217 VTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQ----------QHSIDLQKVTAE- 285
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrksnipARLLALRDALAEa 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 286 ------------------TQEK------EKVI-----------------------THLQEKVIF--LEKRLEQNLSGEDH 316
Cdd:COG4913 453 lgldeaelpfvgelievrPEEErwrgaiERVLggfaltllvppehyaaalrwvnrLHLRGRLVYerVRTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 317 VQELLKEKTVAEQNLEDTRQQLLAARNS------------HTKAL------------------------YLL----ETRV 356
Cdd:COG4913 533 PDSLAGKLDFKPHPFRAWLEAELGRRFDyvcvdspeelrrHPRAItragqvkgngtrhekddrrrirsrYVLgfdnRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 357 KDLERSLQAAEEQLSQSRNVVADQEAQIQKLitTNQENSLSQQQVLALEQ----HCRERIHALEAQIEALEQT-----RV 427
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDAL--QERREALQRLAEYSWDEidvaSAEREIAELEAELERLDASsddlaAL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 428 ADQIAS-EQGMLQLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQRE-IVSVAMAQALEEvRKQREEFQQQATELTA 505
Cdd:COG4913 691 EEQLEElEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEE-RFAAALGDAVERELRE 769
|
570 580
....*....|....*....|....*.
gi 1907143872 506 IIEEKNQSLcekDEALLQKEQELRQL 531
Cdd:COG4913 770 NLEERIDAL---RARLNRAEEELERA 792
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
207-621 |
3.05e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 207 RELNRTQEELVTSNQLSSDLN-ERLEELQRHCSTLEEQRDH---LTASKAGAEHKIVVLEQKEQELQAIIQQHS--IDLQ 280
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEklLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 281 KVTAETQEKEKVITHLQEKVIFLEKRLEQnlsgedhVQELLKEKTVAEQNLEDTRQQLLAARNSHT----KALYLLETRV 356
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEE-------LRELEEELEELEAELAELQEELEELLEQLSlateEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 357 KDLERSLQAAEEQLSQSRNVVADQEAQIQKL----ITTNQENSLSQQQVLALEQHCRERIHALEAQIEALEQTRVADQIA 432
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLenelEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 433 SEQ----GMLQLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQQQATELTAIIE 508
Cdd:COG4717 282 VLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 509 EKNQSLCEK------DEALLQKEQELRQLEKghssALLQMHKLQRELEALktckaQEAMPATTGEDCLPLQGQEPLVISK 582
Cdd:COG4717 362 ELQLEELEQeiaallAEAGVEDEEELRAALE----QAEEYQELKEELEEL-----EEQLEELLGELEELLEALDEEELEE 432
|
410 420 430
....*....|....*....|....*....|....*....
gi 1907143872 583 AMQNSEYELPAAEgtpngevgaSDLKQLQKEKQDLEQQL 621
Cdd:COG4717 433 ELEELEEELEELE---------EELEELREELAELEAEL 462
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
53-244 |
4.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 53 REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDssmrkfQEQNETFQASRAKMAEGLALALArkd 132
Cdd:COG4942 57 LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE------ELAELLRALYRLGRQPPLALLLS--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 133 qewSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDARTRELNRT 212
Cdd:COG4942 128 ---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARL 204
|
170 180 190
....*....|....*....|....*....|..
gi 1907143872 213 QEELVTSNQLSSDLNERLEELQRHCSTLEEQR 244
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
50-274 |
4.13e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 50 SSSREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQdssmRKFQEQNETFQASRAKmaeglalaLA 129
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA----RRIRALEQELAALEAE--------LA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 130 RKDQEWSEKMEQLEKDKRFLTSQLQEVknqslslfQKRDEIDELE-GFQQQEISKVKHMLlkkeECLGKMEQELDARTRE 208
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRAL--------YRLGRQPPLAlLLSPEDFLDAVRRL----QYLKYLAPARREQAEE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907143872 209 LNRTQEELvtsNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQ 274
Cdd:COG4942 155 LRADLAEL---AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
56-554 |
4.56e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 56 LSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLeiaLEKHQDSSMRKFQEQNETFQ-----ASRAKMAEGLALALAR 130
Cdd:PRK01156 247 LEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH---MKIINDPVYKNRNYINDYFKykndiENKKQILSNIDAEINK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 131 KDqEWSEKMEQLEKDKrfltSQLQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELDARTRELN 210
Cdd:PRK01156 324 YH-AIIKKLSVLQKDY----NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 211 RTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQK-----------EQELQAIIQQHSIDL 279
Cdd:PRK01156 399 IQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgEEKSNHIINHYNEKK 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 280 QKVTAETQEKEKVITHLQEKVIFLEKRLEQNLSGEdhvqellKEKTVAEQN-LEDTRQQLLAARNShtkalyllETRVKD 358
Cdd:PRK01156 479 SRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE-------INKSINEYNkIESARADLEDIKIK--------INELKD 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 359 LERSLQAAEEQLSQSRNVVADQEaqiqkliTTNQENSLSQQQVLALEQHcRERIHALEAQIEALEQtrvadqiaseqgml 438
Cdd:PRK01156 544 KHDKYEEIKNRYKSLKLEDLDSK-------RTSWLNALAVISLIDIETN-RSRSNEIKKQLNDLES-------------- 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 439 QLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQREivsvAMAQALEEVRKQREEFQQQATELTAIIEEKNqslcEKD 518
Cdd:PRK01156 602 RLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQ----ENKILIEKLRGKIDNYKKQIAEIDSIIPDLK----EIT 673
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907143872 519 EALLQKEQELRQLEKGHSSALLQMHKLQRELEALKT 554
Cdd:PRK01156 674 SRINDIEDNLKKSRKALDDAKANRARLESTIEILRT 709
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
304-552 |
5.17e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 304 EKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQLLAARNSHT---------KALYLLETRVKDLERSLQAAEEQLSQSR 374
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLavafeadpeAELRQLNRRRVELERALADHESQEQQQR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 375 NVVADQEAQIQKLittnqeNSLSQQQVLALEQHCRERIHALEAQIEALEQT--------RVADQIASEQGMLQLQQENVA 446
Cdd:PRK04863 865 SQLEQAKEGLSAL------NRLLPRLNLLADETLADRVEEIREQLDEAEEAkrfvqqhgNALAQLEPIVSVLQSDPEQFE 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 447 -LKESRNECEHSLQHHQLELKKLKdewsqrEIVSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQSLCEKDEALLQKE 525
Cdd:PRK04863 939 qLKQDYQQAQQTQRDAKQQAFALT------EVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQ 1012
|
250 260 270
....*....|....*....|....*....|....
gi 1907143872 526 QELRQLEKGHSS------ALLQMHK-LQRELEAL 552
Cdd:PRK04863 1013 AQLAQYNQVLASlkssydAKRQMLQeLKQELQDL 1046
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
388-563 |
6.22e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.47 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 388 ITTNQENSLSQQQVLALEQHCRERihaleaqieaLEQTRVADQIASEQG---MLQLQQENVALKESRNecehslqhhqle 464
Cdd:PTZ00491 659 ITTKSQEAAARHQAELLEQEARGR----------LERQKMHDKAKAEEQrtkLLELQAESAAVESSGQ------------ 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 465 lkklkdewsqreivSVAMAQALEEVRKQREEFQQQATELTAIIEEKNQslcekdEALLQKEQELRQLEKGHSSALLQM-H 543
Cdd:PTZ00491 717 --------------SRAEALAEAEARLIEAEAEVEQAELRAKALRIEA------EAELEKLRKRQELELEYEQAQNELeI 776
|
170 180
....*....|....*....|
gi 1907143872 544 KLQRELEALKTCKAQEAMPA 563
Cdd:PTZ00491 777 AKAKELADIEATKFERIVEA 796
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
410-660 |
1.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 410 ERIHALEAQIEALEQTRVADQIASEQ-----GMLQLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQREIVSV--AM 482
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQiellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELraEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 483 AQALEEVRKQREEFQQQATELTAIIEEKNQSlceKDEALLQKEQELRQLEKghssallQMHKLQRELEAL-KTCKAQEAM 561
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGN---GGDRLEQLEREIERLER-------ELEERERRRARLeALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 562 PATTGEDCLPLQGQEPLV------ISKAMQNSEYELpaaegtpngevgASDLKQLQKEKQDLEQQL--IEKNKimKQMQQ 633
Cdd:COG4913 375 LPASAEEFAALRAEAAALlealeeELEALEEALAEA------------EAALRDLRRELRELEAEIasLERRK--SNIPA 440
|
250 260 270
....*....|....*....|....*....|..
gi 1907143872 634 RMLELKKTLQKELKIRPDS-----ELFEVREK 660
Cdd:COG4913 441 RLLALRDALAEALGLDEAElpfvgELIEVRPE 472
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
54-493 |
1.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 54 EDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQ-DSSMRKFQEQNETFQASRAKMAEgLALALARKD 132
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAlEAELAELPERLEELEERLEELRE-LEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 133 QEWSEKMEQLEKDKRFLTsqlQEVKNQSLSLFQKRDEIDELEGFQQQEISKVKHMLLKKEECLGKMEQELdARTRELNRT 212
Cdd:COG4717 170 AELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-EAAALEERL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 213 QEELVTSNQLSSDLnERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKV 292
Cdd:COG4717 246 KEARLLLLIAAALL-ALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 293 ITHLQEKVIFLEKRLEQNLSGEDHVQELLKEktvaeqnLEDTRQQLLAARNSHTKALYLLETRVKDLE--RSLQAAEEQL 370
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLRE-------AEELEEELQLEELEQEIAALLAEAGVEDEEelRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 371 SQSRNVVADQEAQIQklittNQENSLSQQQVLALEQHCRERIHALEAQIEALEQTRvaDQIASEQGMLQLQQENVALKES 450
Cdd:COG4717 398 QELKEELEELEEQLE-----ELLGELEELLEALDEEELEEELEELEEELEELEEEL--EELREELAELEAELEQLEEDGE 470
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907143872 451 RNECEHSLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRKQR 493
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
72-660 |
1.93e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 72 ARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNETFQAsrakmaEGLALALARKDQewseKMEQLEKDKRFLTS 151
Cdd:pfam10174 185 RRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKT------KALQTVIEMKDT----KISSLERNIRDLED 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 152 QLQEVK-NQSLSLFQKRDEIDELEGFQqqeiSKVKHMLLKkeecLGKMEQELDARTRELNRTQEELVTSNQLSSDLNERL 230
Cdd:pfam10174 255 EVQMLKtNGLLHTEDREEEIKQMEVYK----SHSKFMKNK----IDQLKQELSKKESELLALQTKLETLTNQNSDCKQHI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 231 EELQRHCsTLEEQRDHLTASKAGA-----EHKIVVLEQKEQELQAIIQQHSIDlqkvTAETQEKEKVITHLQEKVIFLEK 305
Cdd:pfam10174 327 EVLKESL-TAKEQRAAILQTEVDAlrlrlEEKESFLNKKTKQLQDLTEEKSTL----AGEIRDLKDMLDVKERKINVLQK 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 306 RLEqnlsgedHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIq 385
Cdd:pfam10174 402 KIE-------NLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESL- 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 386 klittNQENSLSQQQVLALEQHCRER-IHALEAQIEALEQTRVADQIASEQGMLQLQQENVALKESRNECEHSLQHHQLE 464
Cdd:pfam10174 474 -----KKENKDLKEKVSALQPELTEKeSSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 465 LKKLKDEWSQReivsvamAQALE-EVRKQREEFQQQATELTAIIEEKNQSLCEKDEallqKEQELRQLEkghsSALLQMH 543
Cdd:pfam10174 549 AVRTNPEINDR-------IRLLEqEVARYKEESGKAQAEVERLLGILREVENEKND----KDKKIAELE----SLTLRQM 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 544 KLQRELEALKTCKAQEAMPATTGEDCLPLQGQEPLVISKAMQNSEYELPAAEGTpngevgASDLKQLQKEKQDLEQQLIE 623
Cdd:pfam10174 614 KEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKT------RQELDATKARLSSTQQSLAE 687
|
570 580 590
....*....|....*....|....*....|....*..
gi 1907143872 624 KNKIMKQMQQrmlELKKTLQKELKIRPDSELFEVREK 660
Cdd:pfam10174 688 KDGHLTNLRA---ERRKQLEEILEMKQEALLAAISEK 721
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
432-559 |
2.03e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.39 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 432 ASEQGMLQLQQENVALK-ESRNECEHSLQHHQLELKKLKDEwsqreivsvAMAQALEEVRKQREEFQ-------QQATEL 503
Cdd:PRK00106 32 AAELTLLNAEQEAVNLRgKAERDAEHIKKTAKRESKALKKE---------LLLEAKEEARKYREEIEqefkserQELKQI 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907143872 504 TAIIEEKNQSLCEKDEALLQKEQELRQLEKGHSSALLQMHKLQRELEALKTCKAQE 559
Cdd:PRK00106 103 ESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAE 158
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
44-685 |
2.10e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 44 DFASDGSSSREDLSSQLLRRNEQIRKLEarlSDYAEQVRnlqKIKEKLEIALEKHQDSSMRKFQEQNETFQASRAKMAEG 123
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTE---TGKAEEAR---KAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 124 LALALARKDQEWSEKMEQLEKDKRFLTSQLQEvknqslslfqkrdeidelEGFQQQEISKVKHMllKKEECLGKMEQEld 203
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAKKAEAARKAE------------------EVRKAEELRKAEDA--RKAEAARKAEEE-- 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 204 ARTRELNRTQEElvtsnqlssdlnERLEELQRhcsTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQkvt 283
Cdd:PTZ00121 1212 RKAEEARKAEDA------------KKAEAVKK---AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK--- 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 284 AETQEKEKVITHLQEKviflEKRLEQNLSGEDHVQELLKEKTVAEQNLEDTRQQllaARNSHTKAlyllETRVKDLERSL 363
Cdd:PTZ00121 1274 AEEARKADELKKAEEK----KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK---AEEAKKKA----DAAKKKAEEAK 1342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 364 QAAEEQLSQSRNVVADQEAQIQKLITTNQENSLSQQQVLALEQHCRERIHALEAQIEALEQTRVADQIASEQGMLQLQQE 443
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 444 NVALKESRNECEHSLQhhQLELKKLKDEWSQReivsVAMAQALEEVRKQREEfQQQATELTAIIEEKNQS--LCEKDEAL 521
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKK--KAEEAKKADEAKKK----AEEAKKAEEAKKKAEE-AKKADEAKKKAEEAKKAdeAKKKAEEA 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 522 LQKEQELRQLEKGHSSA-LLQMHKLQRELEALKTC----KAQEAMPATTGEDCLPLQGQEPLVISKAMQNSEYELPAAEG 596
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKAdEAKKAEEAKKADEAKKAeeakKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 597 TPNGEVGASDLKQLQKEKQDLEQQLIEKNKIMKQMQQRMLELKKTLQKELKIRPdselfEVREKTGPEIPNMAPSVTNNT 676
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE-----EEKKKVEQLKKKEAEEKKKAE 1650
|
....*....
gi 1907143872 677 DLTDAREIN 685
Cdd:PTZ00121 1651 ELKKAEEEN 1659
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
178-500 |
2.29e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 178 QQEISKVKHMLLKKEECLGKMEQELDARTRELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHK 257
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 258 IVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKRLeQNLSGEDHVQELLKEKTVAEQNLEDTRQQ 337
Cdd:COG4372 124 RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL-QALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 338 LLAARNSHTKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQENSLSQQQVLALEQHCRERIHALEA 417
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 418 QIEALEQTRVADQIASEQGMLQLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQ 497
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362
|
...
gi 1907143872 498 QQA 500
Cdd:COG4372 363 AEA 365
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
228-552 |
4.70e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.71 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 228 ERLEELQRHCSTLEE------------QRDHLTASKAGAEHKIVVLEQK-EQELQAIIQQhsidLQKVTAETQEKEKVIT 294
Cdd:COG3096 785 KRLEELRAERDELAEqyakasfdvqklQRLHQAFSQFVGGHLAVAFAPDpEAELAALRQR----RSELERELAQHRAQEQ 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 295 HLQEKVIFLEKRLEQnLSGEDHVQELLKEKTVAEQnLEDTRQQLLAArnshtkalylletrvkdlerslQAAEEQLSQSR 374
Cdd:COG3096 861 QLRQQLDQLKEQLQL-LNKLLPQANLLADETLADR-LEELREELDAA----------------------QEAQAFIQQHG 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 375 NVVADQEAQIQKLITTNQENSLSQQQVLALEQhcreRIHALEAQIEALE---QTRVADQIASEQGMLQLQQE-NVALKES 450
Cdd:COG3096 917 KALAQLEPLVAVLQSDPEQFEQLQADYLQAKE----QQRRLKQQIFALSevvQRRPHFSYEDAVGLLGENSDlNEKLRAR 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 451 RNECEHSLQHHQLELKKLKDEWSQREIVSVAMAQALEEVRKQREEFQQ--QATELTAIIEEKNQSLCEKDE---ALLQKE 525
Cdd:COG3096 993 LEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQelEELGVQADAEAEERARIRRDElheELSQNR 1072
|
330 340
....*....|....*....|....*..
gi 1907143872 526 QELRQLEKGHSSALLQMHKLQRELEAL 552
Cdd:COG3096 1073 SRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
208-393 |
5.11e-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: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 208 ELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQ 287
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 288 EKEKVITHLQekVIFLEKRLEQNLSG-------EDHVQELLKEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVKDLE 360
Cdd:COG3883 97 RSGGSVSYLD--VLLGSESFSDFLDRlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190
....*....|....*....|....*....|...
gi 1907143872 361 RSLQAAEEQLSQSRNVVADQEAQIQKLITTNQE 393
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
42-281 |
5.52e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 42 GDDFASDGSSS-REDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKL---EIALEKHQDSSMRKFQEQNETFQASR 117
Cdd:PRK01156 459 GTTLGEEKSNHiINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeseEINKSINEYNKIESARADLEDIKIKI 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 118 AKMAEGLALALARKDQEWSEKMEQLEKDKRFLTSQLQEVKNQSLSLFQKRDE-----IDELEGFQQQEISKVKHMLLKKE 192
Cdd:PRK01156 539 NELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNeikkqLNDLESRLQEIEIGFPDDKSYID 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 193 ECLGKMEQELDARTRELNRTQEELVTSNQLS--------------------SDLNERLEELQRHCSTLEEQRDHLTASKA 252
Cdd:PRK01156 619 KSIREIENEANNLNNKYNEIQENKILIEKLRgkidnykkqiaeidsiipdlKEITSRINDIEDNLKKSRKALDDAKANRA 698
|
250 260
....*....|....*....|....*....
gi 1907143872 253 GAEHKIVVLEQKEQELQAIIQQHSIDLQK 281
Cdd:PRK01156 699 RLESTIEILRTRINELSDRINDINETLES 727
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
242-453 |
6.22e-03 |
|
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: 39.75 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 242 EQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSIDLQKVTAETQEKEKVITHLQEKVIFLEKRLEQNlsgEDHVQELL 321
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 322 KEKTVAEQNLEDTRQQLLAARNSHTKALYLLETRVKDLERSLQAAEEQLSQSRNVVADQEAQIQKLITTNQENSLSQQQV 401
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907143872 402 LALEQHCRERIHALEAQIEalEQTRVADQIASEQGmlQLQQENVALKESRNE 453
Cdd:COG4942 177 EALLAELEEERAALEALKA--ERQKLLARLEKELA--ELAAELAELQQEAEE 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-259 |
6.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 49 GSSSREdlssQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEKLEIALEKHQDSSMRKFQEQNetfqasrakmaeglALAL 128
Cdd:COG4913 605 GFDNRA----KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--------------VASA 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 129 ARKDQEWSEKMEQLEKDkrflTSQLQEVKnqslslfqkrDEIDELEGfQQQEISKVKHMLLKKEeclGKMEQELDARTRE 208
Cdd:COG4913 667 EREIAELEAELERLDAS----SDDLAALE----------EQLEELEA-ELEELEEELDELKGEI---GRLEKELEQAEEE 728
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907143872 209 LNRTQEELVT-----SNQLSSDLNERLEEL------QRHCSTLEEQRDHLTASKAGAEHKIV 259
Cdd:COG4913 729 LDELQDRLEAaedlaRLELRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEEELE 790
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
133-297 |
6.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 133 QEWSEKMEQLEKDKRfltsqlqevknqslslfQKRDEIDELEGFQQQEISKVKhmllKKEECLGKMEQELDARTRELNRT 212
Cdd:PRK12704 64 EEIHKLRNEFEKELR-----------------ERRNELQKLEKRLLQKEENLD----RKLELLEKREEELEKKEKELEQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 213 QEEL-VTSNQLSSDLNERLEELQRHCStleeqrdhLTASKAgaehKIVVLEQKEQELQAIIQQH---SIDLQKVTAETQE 288
Cdd:PRK12704 123 QQELeKKEEELEELIEEQLQELERISG--------LTAEEA----KEILLEKVEEEARHEAAVLikeIEEEAKEEADKKA 190
|
....*....
gi 1907143872 289 KEKVITHLQ 297
Cdd:PRK12704 191 KEILAQAIQ 199
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
199-557 |
8.17e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 199 EQELDARTRELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAIIQQHSID 278
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 279 LQ----KVTAETQEKEKVITHLQEkvifLEKRLEQNlsgEDHVQELLKEKTVAE---QNLEDTRQQLLAARNSHTKALYL 351
Cdd:pfam01576 84 LEeeeeRSQQLQNEKKKMQQHIQD----LEEQLDEE---EAARQKLQLEKVTTEakiKKLEEDILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 352 LETRVKDLERSLQAAEEQ---LSQSRN----VVADQEAQIQKLITTNQENSLSQQQVLALEQHCRERIHALEAQIEALE- 423
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKaksLSKLKNkheaMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 424 ------------QTRVADQIAS-----------EQGMLQLQQENVALKESRNECEHSLQHHQLELKKLKDEWSQreivSV 480
Cdd:pfam01576 237 qlakkeeelqaaLARLEEETAQknnalkkirelEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELED----TL 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907143872 481 AMAQALEEVRKQREefqQQATELTAIIEEKNQSlcekdeallqKEQELRQLEKGHSSALlqmHKLQRELEALKTCKA 557
Cdd:pfam01576 313 DTTAAQQELRSKRE---QEVTELKKALEEETRS----------HEAQLQEMRQKHTQAL---EELTEQLEQAKRNKA 373
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
39-423 |
9.83e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 39 ADSGDDFASDGSSSREDLSSQLLRRNEQIRKLEARLSDYAEQVRNLQKIKEkleiALEKHQDSSMRKFQEQNETFQASRA 118
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE----ELREERDELREREAELEATLRTARE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 119 KMAEGLALALARK------DQEWSEKMEQLEKDkrfltsqlqevknqslslfqkRDEIDELEgfqqQEISKVKHMLLKKE 192
Cdd:PRK02224 441 RVEEAEALLEAGKcpecgqPVEGSPHVETIEED---------------------RERVEELE----AELEDLEEEVEEVE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 193 ECLGKMEqELDARTRELNRTQEELVTSNQLSSDLNERLEELQRHCSTLEEQRDHLTASKAGAEHKIVVLEQKEQELQAII 272
Cdd:PRK02224 496 ERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907143872 273 QQHSIDLQKVTAETQEKEKVIThLQEKVIFLEKRLEQnlsgedhvqelLKEKTVAEQNLEDTRQQLLAARNSHTKAL--Y 350
Cdd:PRK02224 575 AELNSKLAELKERIESLERIRT-LLAAIADAEDEIER-----------LREKREALAELNDERRERLAEKRERKRELeaE 642
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907143872 351 LLETRVKDLERSLQAAEEQLSQSRNVVADQEAQ---IQKLITTnQENSLSQQQVLaleqhcRERIHALEAQIEALE 423
Cdd:PRK02224 643 FDEARIEEAREDKERAEEYLEQVEEKLDELREErddLQAEIGA-VENELEELEEL------RERREALENRVEALE 711
|
|
| |
