|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
5-519 |
9.25e-57 |
|
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: 205.02 E-value: 9.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 5 AKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAY 84
Cdd:pfam01576 566 AAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARAL 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 85 EESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLEFNQI 164
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQAL 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 165 KAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQS 244
Cdd:pfam01576 726 KAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQA 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 245 LLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKK 324
Cdd:pfam01576 806 QMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKR 885
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 325 KMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGG 404
Cdd:pfam01576 886 RLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKF 965
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 405 KKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKVKAYKGQAEEAEER 484
Cdd:pfam01576 966 KSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEE 1045
|
490 500 510
....*....|....*....|....*....|....*
gi 386972 485 ANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 519
Cdd:pfam01576 1046 ASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-523 |
1.05e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 2 AVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 81
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 82 NAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLE- 160
Cdd:TIGR02168 372 SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEe 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 161 -------FNQIKAEIERNVAEKDEEMEQAKRNHQR------VVDSLQTSLDAETRSRNEVLRVKKKMEGDLN-------- 219
Cdd:TIGR02168 452 lqeelerLEEALEELREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGvlselisv 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 220 ------EMEIQL-----------SHANRMAAEAQKQVKS------LQSLLKDTQIQLDDAVRAN---------------- 260
Cdd:TIGR02168 532 degyeaAIEAALggrlqavvvenLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKniegflgvakdlvkfd 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 261 -----------------DDLKENIAI----------------------------VERRNNLL--QAELEELRAVVEQTER 293
Cdd:TIGR02168 612 pklrkalsyllggvlvvDDLDNALELakklrpgyrivtldgdlvrpggvitggsAKTNSSILerRREIEELEEKIEELEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 294 SRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA 373
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 374 HLERMKKNMEQTIKDLQHRLDEAeQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEED 453
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQL-KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 454 KKNLLRLQDLVNKLQLkvkaykgQAEEAEERANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 523
Cdd:TIGR02168 851 SEDIESLAAEIEELEE-------LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-525 |
5.23e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 5.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 1 EAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKL 80
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 81 KNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLE 160
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 161 FNQIKAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKmEGDLNEMEIQLSHANRMAAEAQKQVK 240
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL-LEEAALLEAALAELLEELAEAAARLL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 241 SLQSLLKDTQIQLDDAVRAND---------DLKENIAIVERRNNLLQAELEELRA--VVEQTERSRKLAEQELIETSERV 309
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALLlaglrglagAVAVLIGVEAAYEAALEAALAAALQniVVEDDEVAAAAIEYLKAAKAGRA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 310 QLLHSqntSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL 389
Cdd:COG1196 575 TFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 390 QHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVkgmRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQL 469
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 386972 470 KVKAYKGQAEEAEERANTNLSKfrkVQHELDEAEERADIAESQVNKLRAKSRDIGA 525
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEE---EALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
218-519 |
1.06e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 218 LNEMEIQLSHANRMAAEAQKqVKSLQSLLKDTQIQLddAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKL 297
Cdd:COG1196 195 LGELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 298 AEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 377
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 378 MKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKgMRKSERRIKELTYQTEEDKKNL 457
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA-EEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386972 458 LRLQDLVNKLQLKVKAYKGQAEEAEERANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 519
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
212-526 |
1.58e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 212 KKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQT 291
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 292 ERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKakkaitdaammaeeLKKEQDT 371
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--------------LESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 372 SAHLERMKKNMEQTIKDLQHRLDEAEqialkggkKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTE 451
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLA--------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386972 452 EDKKNLLRLQDLVNKLQLKVKAYKGQAEEAEERANTNLSKFR-KVQHELDEAEERADIAESQVNKLRAKSRDIGAK 526
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10-532 |
1.91e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 10 LEKTKHRLqNEIEDLMVDVER--------SNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 81
Cdd:COG1196 181 LEATEENL-ERLEDILGELERqleplerqAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 82 NAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLEF 161
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 162 NQIKAEIERnVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKS 241
Cdd:COG1196 340 EELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 242 LQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLIN 321
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 322 QKKKMD--------ADLSQLQSEVEEAVQECRNAEEKAKKAI----------------TDAAMMAEELKKEQD---TSAH 374
Cdd:COG1196 499 AEADYEgflegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaalqnivveddEVAAAAIEYLKAAKAgraTFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 375 LERMKKNmEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDK 454
Cdd:COG1196 579 LDKIRAR-AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386972 455 KNLLRLQDLVNKLQLKVKAYKGQAEEAEERANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKKMHDEE 532
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
8-491 |
2.13e-11 |
|
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: 66.74 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 8 SSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES 87
Cdd:pfam01576 373 ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 88 LEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAE 167
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 168 IErNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLK 247
Cdd:pfam01576 533 LE-EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 248 DTQIQLDDAV---------------------RANDDLKENIAIVERRNNLLQAELEELRAV-------VEQTERSRKLAE 299
Cdd:pfam01576 612 EEKAISARYAeerdraeaeareketralslaRALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknVHELERSKRALE 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 300 QELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQ-ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERM 378
Cdd:pfam01576 692 QQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQaRDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAA 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 379 KKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELtyqteedKKNLL 458
Cdd:pfam01576 772 KKKLELDLKELEAQIDAANK-GREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNL-------EAELL 843
|
490 500 510
....*....|....*....|....*....|....
gi 386972 459 RLQ-DLVNKLQLKVKAYKGQAEEAEERANTNLSK 491
Cdd:pfam01576 844 QLQeDLAASERARRQAQQERDELADEIASGASGK 877
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-512 |
3.30e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 1 EAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKL 80
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 81 KNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLE 160
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 161 FNQIKAEIErNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVK 240
Cdd:COG1196 395 AAELAAQLE-ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 241 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN----NLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQN 316
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLegvkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 317 TSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTikdlqhRLDEA 396
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL------LGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 397 EQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKVKAYKG 476
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
490 500 510
....*....|....*....|....*....|....*.
gi 386972 477 QAEEAEERANTNLSKFRKVQHELDEAEERADIAESQ 512
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-315 |
1.03e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 33 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQL 112
Cdd:TIGR02168 211 KAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 113 GEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIER------NVAEKDEEMEQAKRNH 186
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 187 QRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTqiQLDDAVRANDDLKEN 266
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEE 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 386972 267 IAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQ 315
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-402 |
3.45e-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: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 49 LAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQ 128
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 129 LEVEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAkRNHQRVVDSLQTSLDAETRSRNEVL 208
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 209 RVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVV 288
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 289 EQTERSRKLAEQELIETSERVQLLHSQNTSLI-NQKKKMDADLSQLQSEVEEAvqecrnaeEKAKKAITDAAMMA-EELK 366
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAeALENKIEDDEEEARRRLKRL--------ENKIKELGPVNLAAiEEYE 996
|
330 340 350
....*....|....*....|....*....|....*.
gi 386972 367 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALK 402
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-507 |
1.61e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 1 EAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKL 80
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 81 KNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKI----LR 156
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadeAK 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 157 AQLEFNQIKAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRvKKKMEGDLNEMEIQLSHANRMAAEAQ 236
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAK 1476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 237 KQVKSLQSlLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERV------- 309
Cdd:PTZ00121 1477 KKAEEAKK-ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdelkkae 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 310 QLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQ-ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKD 388
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 389 LQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNllrlqdlVNKLQ 468
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-------AEELK 1708
|
490 500 510
....*....|....*....|....*....|....*....
gi 386972 469 LKVKAYKGQAEEAEERANTNLSKFRKVQHELDEAEERAD 507
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
85-421 |
2.15e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 85 EESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQL----EVEKMELQSALEEAEASLEHEEGKILRAQLE 160
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 161 FNQIKAEIErnvaekdeemEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEgdlnEMEIQLSHANRMAAEAQKQVK 240
Cdd:TIGR02169 253 LEKLTEEIS----------ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG----ELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 241 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAV-------VEQTERSRKLAEQELIETSERVQLLH 313
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEledlraeLEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 314 SQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRL 393
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340
....*....|....*....|....*...
gi 386972 394 DEAEQiALKGGKKQLQKLEARVRELEGE 421
Cdd:TIGR02169 479 DRVEK-ELSKLQRELAEAEAQARASEER 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-339 |
3.24e-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: 59.69 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 1 EAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKL 80
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 81 KNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLE 160
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 161 FNQIKAEIERNVAEKdEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVK 240
Cdd:TIGR02168 847 IEELSEDIESLAAEI-EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 241 SLQSLLKDTQIQLDD-AVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRK-------LAEQELIETSERVQLL 312
Cdd:TIGR02168 926 QLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlAAIEEYEELKERYDFL 1005
|
330 340
....*....|....*....|....*..
gi 386972 313 HSQNTSLINQKKKMDADLSQLQSEVEE 339
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
144-447 |
1.03e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 144 EASLEHEEGKILRAQLEFNQIKAEIERnVAEKDEEMEQAKRNHQRVVDSLQTSLDAEtrsRNEVLRVKKKMEgdlnEMEI 223
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISAL---RKDLARLEAEVE----QLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 224 QLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELI 303
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 304 ETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNME 383
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386972 384 QTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGM--------RKSERRIKELT 447
Cdd:TIGR02168 908 SKRSELRRELEELRE-KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALenkieddeEEARRRLKRLE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
68-367 |
1.43e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 68 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDL-------TEQLGEGGKNVHELEKVRNQLEVEKMELQSAL 140
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeleelSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 141 EEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHQRvVDSLQTSLDAETRSRNEVLRVKKKMEGDLNE 220
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-LDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 221 MEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ 300
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386972 301 ELIETSERVqllhsqnTSLINQKKKMDADLSQLQSEV-EEAVQECRNAEEKAKKAITDAAMMAEELKK 367
Cdd:TIGR02168 916 ELEELREKL-------AQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
46-389 |
5.81e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 46 DKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKV 125
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 126 RNQLEVEKMELQSALEEAEASLEHEEGKILRAQLEFnqIKAEIERNVAekdeemeqakrnhqrVVDSLQTSLDAETRSRN 205
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEA---------------RLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 206 EVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaivERRNnlLQAELEELR 285
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-----ERDE--LEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 286 AVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM------DADLSQLQSEVEEAVQECRNAEEKAKKAITDAA 359
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
330 340 350
....*....|....*....|....*....|
gi 386972 360 MMAEELKKEQDTSAHLERMKKNMEQTIKDL 389
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
85-504 |
8.36e-08 |
|
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: 55.18 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 85 EESLEHLETFKRENKNLQEEISDLTEQLG--EGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQL-EF 161
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDeeEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIsEF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 162 NQIKAEIErnvaEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKS 241
Cdd:pfam01576 165 TSNLAEEE----EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 242 LQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELieTSERVQLLHSQNTSLIN 321
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL--EALKTELEDTLDTTAAQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 322 QkkkmdadlsQLQSEVEEAVQECRNAEEKAKKAitdaammaeelkkeqdTSAHLERMKKNMEQTIKDLQHRLDEAEQiAL 401
Cdd:pfam01576 319 Q---------ELRSKREQEVTELKKALEEETRS----------------HEAQLQEMRQKHTQALEELTEQLEQAKR-NK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 402 KGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKVKAYKGQAEEA 481
Cdd:pfam01576 373 ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
410 420
....*....|....*....|...
gi 386972 482 EERANTNLSKFRKVQHELDEAEE 504
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQE 475
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-527 |
3.05e-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: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 263 LKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQ 342
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 343 ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknmeqtikDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGEL 422
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQA-ELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 423 EAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKVKAYKGQAEEAEERANTNLSKFRKVQHELDEA 502
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260
....*....|....*....|....*
gi 386972 503 EERADIAESQVNKLRAKSRDIGAKK 527
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
211-432 |
3.73e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 211 KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ 290
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 291 TER--SRKLAEQELIETSERVQLLHSQNTS--LINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELK 366
Cdd:COG4942 102 QKEelAELLRALYRLGRQPPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386972 367 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQKRNAES 432
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
84-424 |
3.98e-07 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 52.77 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 84 YEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQsaleEAEASLEHEEGKILRAQLEFNQ 163
Cdd:pfam05622 140 YKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 164 IKA-------EIERNVAEKD---EEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAA 233
Cdd:pfam05622 216 LEEklealqkEKERLIIERDtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 234 EAQKQvkSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRavveqtersRKLAEQElietservqllh 313
Cdd:pfam05622 296 LGQEG--SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQ---------KALQEQG------------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 314 SQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---T 385
Cdd:pfam05622 353 SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksV 432
|
330 340 350
....*....|....*....|....*....|....*....
gi 386972 386 IKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEA 424
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
16-519 |
4.55e-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: 52.81 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 16 RLQNEIEDLMVDVERSNAAAAALDKKQRNF-DKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETF 94
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 95 KRENKNLQEEISDLTEQlgeggknvheLEKVRNQLEVEKMELQSAL---EEAEASLEHEEGKIlrAQLEFNQIKAEIERN 171
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQ----------LRKMMLSHEGVLQEIRSILvdfEEASGKKIYEHDSM--STMHFRSLGSAISKI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 172 VAEKDEEMEQAKRNHQRVVDSLQTsLDAETRSRNEVL--RVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDT 249
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 250 QIQlddavranddlkeniaiVERRNNLLQAELEELRAVVEQTERsrklaeqeliETSERVQLLHSQNTSLINQKKKMDAD 329
Cdd:pfam15921 305 QEQ-----------------ARNQNSMYMRQLSDLESTVSQLRS----------ELREAKRMYEDKIEELEKQLVLANSE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 330 LSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQ 409
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM--------EVQ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 410 KLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKVkaykgqaeEAEERANTNL 489
Cdd:pfam15921 430 RLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL--------ESSERTVSDL 501
|
490 500 510
....*....|....*....|....*....|
gi 386972 490 SKfrkvqhELDEAEERADIAESQVNKLRAK 519
Cdd:pfam15921 502 TA------SLQEKERAIEATNAEITKLRSR 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-484 |
4.81e-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: 52.76 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 202 RSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAEL 281
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 282 EELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQlqSEVEEAVQECRNAEEKAKKAITDAAMM 361
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 362 AEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELEGELEAEQKRNAESVKGMRKSER 441
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK--------EIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 386972 442 RIKELTYQTEEDKKNLLRLQDLVNKLQLKVKAYKGQAEEAEER 484
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-285 |
4.82e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 9 SLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEES-------QSELESSQKEARSLSTELFKLK 81
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqkelyalANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 82 NAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLEF 161
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 162 NQIKAEIERNvaekDEEMEQAKRNHQRvvdslqtsLDAETRSRNevlrvKKKMEGDLNEMEIQLSHANRMAAEAQKQVKS 241
Cdd:TIGR02168 396 ASLNNEIERL----EARLERLEDRRER--------LQQEIEELL-----KKLEEAELKELQAELEELEEELEELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 386972 242 LQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELR 285
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
166-525 |
5.71e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 166 AEIERNVAEKDEEMEQAKRNHQR---VVDSLQTSLDAETRSRNEVLRVKKKME-----------GDLNEMEIQLSHANRM 231
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERYQALLKekreyegyellKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 232 AAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENI-AIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQ 310
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 311 LLHSQNTSLINQKKKMDADLS-------QLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDtsaHLERMKKNME 383
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEeerkrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 384 QTIKDLQHRLDEAEQIALKGG--KKQLQKLEARVRELEGELEAEQKRnaesvkgMRKSERRIKELTYQTEEDKKNLLRLQ 461
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLK 475
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386972 462 DLVNKLQlkvkaykgqaeeaeerantnlSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGA 525
Cdd:TIGR02169 476 EEYDRVE---------------------KELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-527 |
6.28e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 211 KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQ--IQLDDAVRANDdlkenIAIVERRNNLLQAELEELRAVV 288
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAEryKELKAELRELE-----LALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 289 EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKE 368
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 369 QDTSAHLERMKKNMEQTIKDLQHRLdEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTY 448
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEEL-ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 449 QTEEDKKNLLRLQDLVNKLQ-----LKVKAYKGQAEEAEERANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 523
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
....
gi 386972 524 GAKK 527
Cdd:TIGR02168 488 QARL 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-429 |
7.79e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 104 EISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKdEEMEQAK 183
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 184 RNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLshanrmaAEAQKQVKSLQSLLKDTQIQLDDAvranddl 263
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL-------EELKEELESLEAELEELEAELEEL------- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 264 keniaivERRNNLLQAELEELRAVVEQTERSRKLAEQELIEtservqllhsqntslinqkkkMDADLSQLQSEVEEAVQE 343
Cdd:TIGR02168 371 -------ESRLEELEEQLETLRSKVAQLELQIASLNNEIER---------------------LEARLERLEDRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 344 CRNAEEKAKKAitDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELE 423
Cdd:TIGR02168 423 IEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLDSLERLQE 499
|
....*.
gi 386972 424 AEQKRN 429
Cdd:TIGR02168 500 NLEGFS 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
50-515 |
1.30e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 50 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQL 129
Cdd:PTZ00121 1202 AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 130 EVEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLR 209
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 210 VKKKMEGDlnemEIQLSHANRMAAEAQKQVKSLQSLlKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVE 289
Cdd:PTZ00121 1362 AEEKAEAA----EKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 290 QTERSRKLAEQELIETSERVQllHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAitDAAMMAEELKKEQ 369
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAK--KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA--DEAKKAAEAKKKA 1512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 370 DTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEaRVRELEGELEAEQKRNAESVKGM---------RKSE 440
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNMalrkaeeakKAEE 1591
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386972 441 RRIKELTYQTEEDKKnlLRLQDLVNKLQLKVKAYKGQAEEAEERANTNLSKF----RKVQHELDEAEERADIAESQVNK 515
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKK--MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKeaeeKKKAEELKKAEEENKIKAAEEAK 1668
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
260-468 |
2.11e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 260 NDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRK--LAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEV 337
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 338 EeAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQHRLDEAEQIALKGGKKQ 407
Cdd:COG3206 243 A-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386972 408 LQKLEARVRELEGELEAEQKRnaesVKGMRKSERRIKELTYQTEEDKKNllrLQDLVNKLQ 468
Cdd:COG3206 322 LEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE 375
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
49-505 |
4.76e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 49 LAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYE-ESLEHLETFKRENKNLQEEISDLTE-----QLGEGGKNVHEL 122
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaEDARKAEEARKAEDAKRVEIARKAEdarkaEEARKAEDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 123 EKVRNQLEVEKMELQSALEEA----EASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLD 198
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDArkaeAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 199 AETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQK--QVKSLQSLLKDTQiqlddAVRANDDLKENIAIVERRNNL 276
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeEKKKADEAKKKAE-----EAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 277 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSlinQKKKMDadlsqlqsEVEEAVQECRNAEEKAKKAIT 356
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE---AKKKAD--------AAKKKAEEKKKADEAKKKAEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 357 DAAmMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKqlqKLEARVRELEGELEAEQKRNAESVKGM 436
Cdd:PTZ00121 1403 DKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 437 RKSERRIKELTYQTEEDKKnllRLQDLVNKLQLKVKAYKG-QAEEAEERANTNLSKFRKVQHELDEAEER 505
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKK---KADEAKKAAEAKKKADEAkKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
69-521 |
5.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 69 EARSLSTELFKLKNAYEESLEhletfKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEasLE 148
Cdd:COG4913 226 AADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 149 HEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHA 228
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 229 ----NRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEN-------IAIVERRNNLLQAELEELRAVVEqteRSRKL 297
Cdd:COG4913 379 aeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALA---EALGL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 298 AEQ------ELIETSER--------VQLLHSQNTSL-------------INQKK-------------------------- 324
Cdd:COG4913 456 DEAelpfvgELIEVRPEeerwrgaiERVLGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprldpds 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 325 ---KMDADLSQLQSEVEEAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTIKDL 389
Cdd:COG4913 536 lagKLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKLAAL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 390 QHRLDEAEQiALKGGKKQLQKLEARVRELEGELEAEQK--RNAESVKGMRKSERRIKELtyqtEEDKKNLLRLQDLVNKL 467
Cdd:COG4913 616 EAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDLAAL 690
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 386972 468 QLKVKAYKGQAEEAEERANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSR 521
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
16-384 |
1.59e-05 |
|
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: 47.86 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 16 RLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFK 95
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 96 RENKNLQEEISDLTEQLGEGGKNVH-ELEKVRNQLEVEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIeRNVAE 174
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEaQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL-RTLQQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 175 KDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLD 254
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 255 DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQ 334
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT 558
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 386972 335 SEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 384
Cdd:pfam01576 559 QQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQ 608
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
68-293 |
2.25e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 68 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASL 147
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 148 EHEEGKI---LRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQ 224
Cdd:COG4942 100 EAQKEELaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386972 225 LshanrmaAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTER 293
Cdd:COG4942 180 L-------AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
73-291 |
2.42e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 73 LSTELFKLKNAYEESLEHLETFKRENK--NLQEEISDLTEQLGEggknvheLEKVRNQLEVEKMELQSALEEAEASLEHE 150
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE-------LESQLAEARAELAEAEARLAALRAQLGSG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 151 EGKI--LRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHA 228
Cdd:COG3206 253 PDALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASL 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386972 229 NRMAAEAQKQVKSLQSLlkdtQIQLddavranDDLKENIAIVERRNNLLQAELEELRAVVEQT 291
Cdd:COG3206 333 QAQLAQLEARLAELPEL----EAEL-------RRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
243-473 |
5.32e-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: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 243 QSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQ 322
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 323 KKKMDADLSQLqseveeavqeCRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI--A 400
Cdd:COG4942 99 LEAQKEELAEL----------LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386972 401 LKGGKKQLQKLEARVRELEGELEAEQKRNAESVKgmrKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKVKA 473
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
73-519 |
2.78e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 73 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEG 152
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 153 KILRAQ-------------LEFNQIKAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKK------ 213
Cdd:TIGR04523 202 LLSNLKkkiqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEleqnnk 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 214 ----MEGDLNEMEIQLSHANRMAA-----EAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEEL 284
Cdd:TIGR04523 282 kikeLEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 285 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEE 364
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 365 LKKEQDTSAHLERMKKNMEQTIKDLQHRLD-------------EAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAE 431
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 432 SVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKvKAYKGQAEEAEERANTNLSKFRKVqhelDEAEERADIAES 511
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE-KEIDEKNKEIEELKQTQKSLKKKQ----EEKQELIDQKEK 596
|
....*...
gi 386972 512 QVNKLRAK 519
Cdd:TIGR04523 597 EKKDLIKE 604
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
277-524 |
3.82e-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: 43.24 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 277 LQAELEELRAvveQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEavQECRNAEEKAKKAIT 356
Cdd:pfam01576 55 LCAEAEEMRA---RLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 357 DAAM--MAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELEGELEAEQKRNAESVK 434
Cdd:pfam01576 130 EAKIkkLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 435 GMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKVKAYKGQAEEAEERANTNLSKFRKVQHELDEAEERADIAESQVN 514
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
250
....*....|
gi 386972 515 KLRAKSRDIG 524
Cdd:pfam01576 289 KAEKQRRDLG 298
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
126-527 |
4.84e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 126 RNQLEVEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHQ-RVVDSLQTSLDAETRSR 204
Cdd:PTZ00121 1071 GLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEaRKAEDARKAEEARKAED 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 205 NEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQK--QVKSLQSLLKDTQIQLDDAVRANDDLKEnIAIVERRNNLLQAE-- 280
Cdd:PTZ00121 1151 AKRVEIARKAEDARKAEEARKAEDAKKAEAARKaeEVRKAEELRKAEDARKAEAARKAEEERK-AEEARKAEDAKKAEav 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 281 --LEELRAVVEQTERSRKLAEQELIETSERVQLLH-SQNTSLINQKKKMDADLSQLQSEVEEA-----VQECRNAEEKAK 352
Cdd:PTZ00121 1230 kkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHfARRQAAIKAEEARKADELKKAEEKKKAdeakkAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 353 KA-----ITDAAMMAEELKKEQDTSAH-LERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQ 426
Cdd:PTZ00121 1310 KAeeakkADEAKKKAEEAKKKADAAKKkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 427 KRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQlKVKAYKGQAEEAE--ERANTNLSKFRKVQHELDEAEE 504
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420
....*....|....*....|...
gi 386972 505 RADIAESQVNKLRAKSRDIGAKK 527
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKK 1491
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
269-407 |
5.26e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 269 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQEcrnAE 348
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ---AI 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 386972 349 EKAKKAITDAAMMAEELKKEQDTSAHLermkKNMEQTIKDLQHRLDEAEQIALKGGKKQ 407
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKA----HELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
234-463 |
5.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 234 EAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIA-IVERRNNL--LQAELEELRAVVEQTERSRKLAEQELIETSERVQ 310
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEeHEERREELetLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 311 LLHSQNTSLINQKKKMDAD---LSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIK 387
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD---LEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 388 DLQHRLDEAEQiALKGGKKQLQKLEARVRELEGELE--AEQKRNAESVKGMRKSER-----RIKELTYQTEEDKKNLLRL 460
Cdd:PRK02224 367 ELESELEEARE-AVEDRREEIEELEEEIEELRERFGdaPVDLGNAEDFLEELREERdelreREAELEATLRTARERVEEA 445
|
...
gi 386972 461 QDL 463
Cdd:PRK02224 446 EAL 448
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-436 |
7.28e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 1 EAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKL 80
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 81 KNAYEESLEHLETFKRENKNLQEEISDLTEQLGEggknVHELEKvrnQLEVEKMELQSALEEAEASLEH----------E 150
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDE----LREREA---ELEATLRTARERVEEAEALLEAgkcpecgqpvE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 151 EGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHQRVVDSlqtsldAETRSRNEVLRVKKKMEGDL-NEMEIQLSHAN 229
Cdd:PRK02224 463 GSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL------VEAEDRIERLEERREDLEELiAERRETIEEKR 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 230 RMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERsRKLAEQELIETSERV 309
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLREKR 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 310 QLLHSQNTSLINQKKKMDADLSQLQSEVEEA-VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKD 388
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 386972 389 LQHRLDeaeqiALKGGKKQLQKLEARVRELE---GELEAE-QKRNAESVKGM 436
Cdd:PRK02224 696 LRERRE-----ALENRVEALEALYDEAEELEsmyGDLRAElRQRNVETLERM 742
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
71-359 |
7.89e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 71 RSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHE 150
Cdd:PLN02939 138 QNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 151 EGKILRAQLEFNQIKAEierNVAEKDEemeqakrnhqrvVDSLQTSLDAETRSRNEVLRVKKK---MEGDLNEMEIQLSH 227
Cdd:PLN02939 218 GLCVHSLSKELDVLKEE---NMLLKDD------------IQFLKAELIEVAETEERVFKLEKErslLDASLRELESKFIV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 228 ANR-MAAEAQKQVKSLQSLLKDTQIQLDDAVrandDLKENIAIVERRNNLLQAELEELRAVVEQTERSRklaeqeliETS 306
Cdd:PLN02939 283 AQEdVSKLSPLQYDCWWEKVENLQDLLDRAT----NQVEKAALVLDQNQDLRDKVDKLEASLKEANVSK--------FSS 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 386972 307 ERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNA-----EEKAKKAITDAA 359
Cdd:PLN02939 351 YKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTlsklkEESKKRSLEHPA 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
255-428 |
1.47e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 255 DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAE--QELIETSERVQLLHSQNTSLINQKKKMDA---D 329
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 330 LSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQH-RLDE--AEQIALKGGKK 406
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRaLLEErfAAALGDAVERE 766
|
170 180
....*....|....*....|..
gi 386972 407 QLQKLEARVRELEGELEAEQKR 428
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEE 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
65-273 |
1.59e-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: 40.90 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 65 SSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAE 144
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 145 ASL----EHEEGKILRAQLEFNQIKAEIERnvaekdeeMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNE 220
Cdd:COG4942 111 RALyrlgRQPPLALLLSPEDFLDAVRRLQY--------LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 386972 221 MEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERR 273
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
77-505 |
1.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 77 LFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAE------ASLEHE 150
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 151 EGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHQRVvdslqTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANR 230
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 231 MAAEAQKQVKSLQSLLKdtqiQLDDAVRANDDLKENIAIVERRNNLlqaeLEELRAVVEQTERSRK-LAEQELIETSERV 309
Cdd:PRK03918 322 EINGIEERIKELEEKEE----RLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKrLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 310 QLLHSQNTSLINQKKKMDADLSQLQSEVEEAvqecRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTIKDL 389
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGRELTEE-----HRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 390 QHRLDEAEqialkggkKQLQKLEARVRELEGELEAEQK--RNAESVKGMRKSERRIKELTYQT-EEDKKNLLRLQDLVNK 466
Cdd:PRK03918 465 EKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
410 420 430
....*....|....*....|....*....|....*....
gi 386972 467 LQLKVKAYKGQAEEAEERANtnlsKFRKVQHELDEAEER 505
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
143-400 |
2.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 143 AEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEeMEQAKRNHQRVVDSLQTSLDAETRSRnevlrvkkkmegDLNEME 222
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYSWDEIDVASAER------------EIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 223 IQLSHANrmaaEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQEL 302
Cdd:COG4913 675 AELERLD----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 303 IEtsERVQLLHSQNT------SLINQKKKMDADLSQLQSEVEEAVQE-CRNAEEKAKKAITDAAMMAEELK-----KEQD 370
Cdd:COG4913 751 LE--ERFAAALGDAVerelreNLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLAlldrlEEDG 828
|
250 260 270
....*....|....*....|....*....|....
gi 386972 371 TSAHLERMK----KNMEQTIKDLQHRLDEAEQIA 400
Cdd:COG4913 829 LPEYEERFKellnENSIEFVADLLSKLRRAIREI 862
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
328-527 |
2.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 328 ADLSQLQSEVEEAvqecrnaeEKAKKAITDAAMMAEELKKEQDTSAHLERMKK-----NMEQTIKDLQHRLDEAEQiALK 402
Cdd:COG4913 235 DDLERAHEALEDA--------REQIELLEPIRELAERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRA-ELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 403 GGKKQLQKLEARVRELEGEL-EAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKV----KAYKGQ 477
Cdd:COG4913 306 RLEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaEEFAAL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 386972 478 AEEAEERANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKK 527
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1-390 |
2.36e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 1 EAVNAKCSSLEKTKHRLQNEIEDLM---VDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTEL 77
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTakkMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 78 FKLKNAYEESLEHLETFKRENKN---LQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGKI 154
Cdd:pfam15921 541 DHLRNVQTECEALKLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKI 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 155 LRAQLEFNQIKAEIERNV---AEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRM 231
Cdd:pfam15921 621 RELEARVSDLELEKVKLVnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 232 AAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVql 311
Cdd:pfam15921 701 LKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL-- 778
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386972 312 lhsqnTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAhleRMKKNMEQTIKDLQ 390
Cdd:pfam15921 779 -----STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV---RLKLQHTLDVKELQ 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-431 |
2.50e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 36 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLtEQLGEG 115
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 116 GKNVHELEKVRNQLEVEKMELQSALEEAEASLE-HEEGKILRAQLE--FNQIKAEIERNVAEKDEEMEQAKRNHQRVVDS 192
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRElEEELEELEAELAelQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 193 LQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDL----KENIA 268
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 269 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAE 348
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 349 EKAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKggkKQLQKLEARVREL 418
Cdd:COG4717 368 LEQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---EELEELEEELEEL 444
|
410
....*....|...
gi 386972 419 EGELEAEQKRNAE 431
Cdd:COG4717 445 EEELEELREELAE 457
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
215-413 |
2.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 215 EGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERS 294
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 295 RKLAE---------------QELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQEcrnAEEKAKKAITDAA 359
Cdd:COG3883 95 LYRSGgsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386972 360 MMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEA 413
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
283-484 |
2.62e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 283 ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKK---AITDAA 359
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 360 MMAEELKKE--------------QDTSAHLERMKKNMEQtIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELEGELE 423
Cdd:PHA02562 269 SKIEQFQKVikmyekggvcptctQQISEGPDRITKIKDK-LKELQHSLEKLDtaIDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386972 424 AEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDlvnKLQLKVKAYKGQAEEAEER 484
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD---ELDKIVKTKSELVKEKYHR 405
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
5-504 |
3.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 5 AKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAY 84
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEKAEEYIKLSEFY 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 85 EESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEvekmELQSALEEAEASLEHEEgKILRAQLEFNQI 164
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYE-EAKAKKEELERL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 165 KAEIERN----VAEKDEEMEQAKRNHQRVVDSLQT---SLDAETRSRNEVLRVKKKMEGD--LNEMEIQLSHANRMAAEA 235
Cdd:PRK03918 378 KKRLTGLtpekLEKELEELEKAKEEIEEEISKITArigELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEY 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 236 QKQVKSLQSLLKDTQIQLDDAvRANDDLKENIAIVERRNNLLQAELEELRAVVEQTErsrKLAEQELIETSERVQLLHSQ 315
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQLKELEEKLK---KYNLEELEKKAEEYEKLKEK 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 316 NTslinqkkKMDADLSQLQSEVEEAvqecrNAEEKAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQHRLDE 395
Cdd:PRK03918 534 LI-------KLKGEIKSLKKELEKL-----EELKKKLAELEKKLDELEEELAEL-----LKELEELGFESVEELEERLKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 396 AEQ-----IALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELtyQTEEDKKNLLRLQDLVNKLQLK 470
Cdd:PRK03918 597 LEPfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL--EKKYSEEEYEELREEYLELSRE 674
|
490 500 510
....*....|....*....|....*....|....
gi 386972 471 VKAYKGQAEEAEERANTNLSKFRKVQHELDEAEE 504
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
181-403 |
4.77e-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: 39.36 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 181 QAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRAN 260
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 261 DDLKENIAIVER------RNNLLQ--------AELEELRAVVEQTERSRKLAEQELIETSERvqlLHSQNTSLINQKKKM 326
Cdd:COG4942 100 EAQKEELAELLRalyrlgRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386972 327 DADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKG 403
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
10-501 |
5.28e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 10 LEKTKHRLQNEIEDLMVDV----ERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYE 85
Cdd:pfam15921 262 LQQHQDRIEQLISEHEVEItgltEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 86 ESLEHLEtfkrenKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSalEEAEASLEHEEGKILRAQLEFNQIk 165
Cdd:pfam15921 342 DKIEELE------KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK--REKELSLEKEQNKRLWDRDTGNSI- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 166 aeiernvaekdeemeqakrnhqrVVDSLQTSLDAETRSRNEVLRVKKKMEGDLN-EMEIQLShANRMAAEAQKQVKSLQS 244
Cdd:pfam15921 413 -----------------------TIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMA-AIQGKNESLEKVSSLTA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 245 LLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKK 324
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQT 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 325 KMDADLSQLqSEVEEAVQECRNAEEKakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGG 404
Cdd:pfam15921 549 ECEALKLQM-AEKDKVIEILRQQIEN----------MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKD 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 405 KKqLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNllrLQDLVNKLQLKVKAYKGQAEEAEER 484
Cdd:pfam15921 618 AK-IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE---LNSLSEDYEVLKRNFRNKSEEMETT 693
|
490
....*....|....*..
gi 386972 485 ANTNLSKFRKVQHELDE 501
Cdd:pfam15921 694 TNKLKMQLKSAQSELEQ 710
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
167-518 |
6.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 167 EIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLL 246
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 247 KDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 326
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 327 DADLSQLQSEVEEAVQEcrNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKK 406
Cdd:COG4372 163 QEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 407 QLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKE-LTYQTEEDKKNLLRLQDLVNKLQLKVKAYKGQAEEAEERA 485
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEiAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350
....*....|....*....|....*....|...
gi 386972 486 NTNLSKFRKVQHELDEAEERADIAESQVNKLRA 518
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
85-520 |
7.00e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 85 EESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKVRNQLEVEKMELQSALEEAEASLEHEEGkilraqlefnqi 164
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE------------ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 165 KAEIERNVAEKDEEMEQAKRNHQRVVDSLQTSLDAETRSRNEVLrvkkkmegdlnemeiqlshanrmaAEAQKQVKSLQS 244
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI------------------------EELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 245 LLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSrkLAEQELIETSERVQllHSQNTSLINQKK 324
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL--LEAGKCPECGQPVE--GSPHVETIEEDR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 325 KMDADLSQLQSEVEEAVQECRNAEEKakkaitdaammAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkgg 404
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVEERLER-----------AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRE------ 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 405 kkQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLLRLQDLVNKLQLKVKA----------Y 474
Cdd:PRK02224 538 --RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAedeierlrekR 615
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 386972 475 KGQAEEAEERANTnLSKFRKVQHELDEAEERADIAESQVNKLRAKS 520
Cdd:PRK02224 616 EALAELNDERRER-LAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
228-528 |
7.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 228 ANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSE 307
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 308 RVQllhsqntSLINQKKKMDADLSQLQSEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK 387
Cdd:COG4372 81 ELE-------ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 388 DLQHRLDEAEQIALKGGKKQLQKLEARVRELEGELEAEQKRNAESVKGMRKSERRIKELtyQTEEDKKNLLRLQDLVNKL 467
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL--PRELAEELLEAKDSLEAKL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386972 468 QLKVKAYKGQAEEAEERANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKKM 528
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
277-371 |
8.02e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 39.16 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386972 277 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQEcrnaEEKAKKAIT 356
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE----RKQKRKEIT 222
|
90
....*....|....*
gi 386972 357 DAAMMAEELkKEQDT 371
Cdd:PRK11448 223 DQAAKRLEL-SEEET 236
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
277-350 |
9.11e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 37.64 E-value: 9.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386972 277 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQSEVEEAVQECRNAEEK 350
Cdd:pfam05266 107 LLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAADKEIARLKSEAEKLEQEIQDVELE 180
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