|
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 ... |
3-512 |
2.31e-58 |
|
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: 209.26 E-value: 2.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 3 LEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 82
Cdd:pfam01576 571 LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 83 HLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIE 162
Cdd:pfam01576 651 AKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFE 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 163 RNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDT 242
Cdd:pfam01576 731 RDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 243 QIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDAD 322
Cdd:pfam01576 811 QRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEAR 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 323 LSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQ 402
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIA 970
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 403 KLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNL 482
Cdd:pfam01576 971 ALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050
|
490 500 510
....*....|....*....|....*....|
gi 386973 483 SKFRKVQHELDEAEERADIAESQVNKLRAK 512
Cdd:pfam01576 1051 AARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-519 |
1.76e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 1 SSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES 80
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 81 LEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLE------- 153
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeele 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 154 -FNQIKAEIERNVAEKDEEMEQAKRNH------LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLN-------------- 212
Cdd:TIGR02168 458 rLEEALEELREELEEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlselisvdegyea 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 213 EMEIQL-----------SHANRMAAEAQKQVKS------LQSLLKDTQIQLDDAVRAN---------------------- 253
Cdd:TIGR02168 538 AIEAALggrlqavvvenLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKniegflgvakdlvkfdpklrka 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 254 -----------DDLKENIAI----------------------------VERRNNLL--QAELEELRAVVEQTERSRKLAE 292
Cdd:TIGR02168 618 lsyllggvlvvDDLDNALELakklrpgyrivtldgdlvrpggvitggsAKTNSSILerRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 293 QELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKA-------KKAITDAAMMAEELKKEQDTS 365
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIaqlskelTELEAEIEELEERLEEAEEEL 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 366 AHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEE 445
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALRE-ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386973 446 DRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTK 519
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-519 |
3.29e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 226 AEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLL 305
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 306 HSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHR 385
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 386 LDEAEQIA------LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDK 459
Cdd:TIGR02168 840 LEDLEEQIeelsedIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386973 460 LQLKVKAYKRQAEEAEEQANTNLSKFR-KVQHELDEAEERADIAESQVNKLRAKSRDIGTK 519
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-308 |
6.58e-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: 68.54 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 26 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQL 105
Cdd:TIGR02168 211 KAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 106 GSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIER------NVAEKDEEMEQAKRNH 179
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 180 LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTqiQLDDAVRANDDLKEN 259
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEE 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 386973 260 IAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQ 308
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
119-508 |
1.58e-11 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 67.24 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 119 RKQLEAEKMELQSALEEAEASLEheegKILRAQLEFNQIKaeieRNVAEKDEEMEQAKRNhlrvVDSLQTSLDAETRSRN 198
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLD----KIDRQKEETEQLK----QQLAQAPAKLRQAQAE----LEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 199 EALRVkKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAV--------RANDDLKENIAIVERRNNLL 270
Cdd:PRK11281 119 STLSL-RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSqrlqqirnLLKGGKVGGKALRPSQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 271 QAELEELRAvveQTERSRKLAE-----QELI-----ETSERVQLLHSQNTSL---INQKKKmdadlsqlqTEVEEAVQEC 337
Cdd:PRK11281 198 QAEQALLNA---QNDLQRKSLEgntqlQDLLqkqrdYLTARIQRLEHQLQLLqeaINSKRL---------TLSEKTVQEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 338 RNAEEKAKkaITDAAMMAEELKKEQDTSAHL----ERMKKNMEQTIKdLQHRLDEA--------EQI-ALKGG------- 397
Cdd:PRK11281 266 QSQDEAAR--IQANPLVAQELEINLQLSQRLlkatEKLNTLTQQNLR-VKNWLDRLtqsernikEQIsVLKGSlllsril 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 398 KKQLQKLEArvreleneleaeqkrnAESVKGMRKserRIKEL-TYQTE--EDRKNLLRLQDLVDKLQlkvkayKRQAEEA 474
Cdd:PRK11281 343 YQQQQALPS----------------ADLIEGLAD---RIADLrLEQFEinQQRDALFQPDAYIDKLE------AGHKSEV 397
|
410 420 430
....*....|....*....|....*....|....
gi 386973 475 EEQANTNLskfrkvqheLDEAEERADIAEsQVNK 508
Cdd:PRK11281 398 TDEVRDAL---------LQLLDERRELLD-QLNK 421
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-517 |
9.60e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 3 LEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 82
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 83 HLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIE 162
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 163 RNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRsrneaLRVKKKMEGDlnemeiqlshanrmAAEAQKQVKSLQSLLKDT 242
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAAR-----LLLLLEAEAD--------------YEGFLEGVKAALLLAGLR 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 243 QIQLDDAVRANDDLKENIAIVERRNNLLQaeleelRAVVEQTERSRKLAEQELIETSERVQLLHSqntSLINQKKKMDAD 322
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAALEAALAAALQ------NIVVEDDEVAAAAIEYLKAAKAGRATFLPL---DKIRARAALAAA 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 323 LSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQ 402
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 403 KLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANtnl 482
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL--- 748
|
490 500 510
....*....|....*....|....*....|....*
gi 386973 483 skfRKVQHELDEAEERADIAESQVNKLRAKSRDIG 517
Cdd:COG1196 749 ---EEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
42-395 |
1.42e-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: 63.92 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 42 LAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQ 121
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 122 LEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHLRvVDSLQTSLDAETRSRNEAL 201
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 202 RVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVV 281
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 282 EQTERSRKLAEQELIETSERVQLLHSQNTSLI-NQKKKMDADLSQLQTEVEEAvqecrnaeEKAKKAITDAAMMA-EELK 359
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAeALENKIEDDEEEARRRLKRL--------ENKIKELGPVNLAAiEEYE 996
|
330 340 350
....*....|....*....|....*....|....*.
gi 386973 360 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALK 395
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1-484 |
1.94e-10 |
|
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: 63.66 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 1 SSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES 80
Cdd:pfam01576 373 ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 81 LEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAE 160
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 161 IErNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLK 240
Cdd:pfam01576 533 LE-EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLA 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 241 DTQIQLDDAV---------------------RANDDLKENIAIVERRNNLLQAELEELRAV-------VEQTERSRKLAE 292
Cdd:pfam01576 612 EEKAISARYAeerdraeaeareketralslaRALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknVHELERSKRALE 691
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 293 QELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQ-ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERM 371
Cdd:pfam01576 692 QQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQaRDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAA 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 372 KKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELtyqteedRKNLL 451
Cdd:pfam01576 772 KKKLELDLKELEAQIDAANK-GREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNL-------EAELL 843
|
490 500 510
....*....|....*....|....*....|....
gi 386973 452 RLQ-DLVDKLQLKVKAYKRQAEEAEEQANTNLSK 484
Cdd:pfam01576 844 QLQeDLAASERARRQAQQERDELADEIASGASGK 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
78-414 |
3.34e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 78 EESLEHLETFKRENKNLQEEISDLTEQLGssgktihELEKVRKQLEaEKMELQSALEEAEASLEHEEGKILRAQLEfnQI 157
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLE-------RLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKE--AI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 158 KAEIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETR----SRNEALRVKKKMEgdlnEMEIQLSHANRMAAEAQKQVK 233
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQLRVKEKIG----ELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 234 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAV-------VEQTERSRKLAEQELIETSERVQLLH 306
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEledlraeLEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 307 SQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRL 386
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340
....*....|....*....|....*...
gi 386973 387 DEAEQiALKGGKKQLQKLEARVRELENE 414
Cdd:TIGR02169 479 DRVEK-ELSKLQRELAEAEAQARASEER 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
4-500 |
4.58e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 4 EKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEH 83
Cdd:PTZ00121 1248 ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 84 LETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKI----LRAQLEFNQIKA 159
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkadeAKKKAEEDKKKA 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 160 EIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRvKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLl 239
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA- 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 240 KDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERV-------QLLHSQNTSL 312
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdelkkaeELKKAEEKKK 1565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 313 INQKKKMDADLSQLQTEVEEAVQ-ECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ 391
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 392 I-----------ALKGGKKQLQKLEARVRELENEL---EAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLV 457
Cdd:PTZ00121 1646 KkkaeelkkaeeENKIKAAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 386973 458 DKLQLKVKAYKRQAEEAE---EQANTNLSKFRKVQHELDEAEERAD 500
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-505 |
7.13e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 3 LEKTKHRLqNEIEDLMVDVER--------SNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 74
Cdd:COG1196 181 LEATEENL-ERLEDILGELERqleplerqAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 75 NAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEF 154
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 155 NQIKAEIE------RNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEA 228
Cdd:COG1196 340 EELEEELEeaeeelEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 229 QKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAiverRNNLLQAELEELRAvveQTERSRKLAEQELIETSERVQLLHSQ 308
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEA----ELEEEEEALLELLA---ELLEEAALLEAALAELLEELAEAAAR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 309 NTSLINQKKKMD--------ADLSQLQTEVEEAVQECRNAEEKAKKAI----------------TDAAMMAEELKKEQD- 363
Cdd:COG1196 493 LLLLLEAEADYEgflegvkaALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaalqnivveddEVAAAAIEYLKAAKAg 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 364 --TSAHLERMKKNmEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTY 441
Cdd:COG1196 573 raTFLPLDKIRAR-AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386973 442 QTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQ 505
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-332 |
1.17e-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: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 2 SLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESL 81
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 82 EHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEI 161
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 162 ERNVAEKdEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKD 241
Cdd:TIGR02168 855 ESLAAEI-EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 242 TQIQLDD-AVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRK-------LAEQELIETSERVQLLHSQNTSLI 313
Cdd:TIGR02168 934 LEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLT 1013
|
330
....*....|....*....
gi 386973 314 NQKKKMDADLSQLQTEVEE 332
Cdd:TIGR02168 1014 EAKETLEEAIEEIDREARE 1032
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
103-486 |
1.88e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 103 EQLGSSGKTIHELEKVRKQLEAEKMELQSAL---EEAEASLEHEEGKIlrAQLEFNQIKAEIERNVAEKDEEMEQAKRNH 179
Cdd:pfam15921 163 DMLEDSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEASGKKIYEHDSM--STMHFRSLGSAISKILRELDTEISYLKGRI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 180 LRVVDSLQTsLDAETRSRNEAL--RVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQlddavranddlk 257
Cdd:pfam15921 241 FPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ------------ 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 258 eniaiVERRNNLLQAELEELRAVVEQTERsrklaeqeliETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQEC 337
Cdd:pfam15921 308 -----ARNQNSMYMRQLSDLESTVSQLRS----------ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 338 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEA 417
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKSECQG 444
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386973 418 EQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKR----------QAEEAEEQANTNLSKFR 486
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtvsdltaslqEKERAIEATNAEITKLR 523
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-382 |
2.20e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 39 DKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKV 118
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 119 RKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFnqIKAEIERNVAekdeemeqakrnhlrVVDSLQTSLDAETRSRN 198
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEA---------------RLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 199 EALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaivERRNnlLQAELEELR 278
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-----ERDE--LEAQLRELE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 279 AVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM------DADLSQLQTEVEEAVQECRNAEEKAKKAITDAA 352
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
330 340 350
....*....|....*....|....*....|
gi 386973 353 MMAEELKKEQDTSAHLERMKKNMEQTIKDL 382
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
61-360 |
4.50e-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: 56.22 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 61 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEK-------MELQSAL 133
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVeqleeriAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 134 EEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHLRvVDSLQTSLDAETRSRNEALRVKKKMEGDLNE 213
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-LDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 214 MEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ 293
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386973 294 ELIETSERVqllhsqnTSLINQKKKMDADLSQLQTEV-EEAVQECRNAEEKAKKAITDAAMMAEELKK 360
Cdd:TIGR02168 916 ELEELREKL-------AQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-440 |
5.34e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 137 EASLEHEEGKILRAQLEFNQIKAEIERnVAEKDEEMEQAKRnhlrvvdSLQTSLDAETRSRNEALRVKKKMEGDLNEMEI 216
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAE-LRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 217 QLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELI 296
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 297 ETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNME 376
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386973 377 QTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGM--------RKSERRIKELT 440
Cdd:TIGR02168 908 SKRSELRRELEELRE-KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALenkieddeEEARRRLKRLE 978
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
159-511 |
1.52e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 159 AEIERNVAEKDEEMEQAKRNHLR---VVDSLQTSLDAETRSRNEALRVKKKME-----------GDLNEMEIQLSHANRM 224
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERYQALLKekreyegyellKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 225 AAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENI-AIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQ 303
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 304 LLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQ 383
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 384 HRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESvkgmrksERRIKELTYQTEEDRKNLLRLQDLVDKLQLK 463
Cdd:TIGR02169 406 RELDRLQE--------ELQRLSEELADLNAAIAGIEAKINEL-------EEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 386973 464 VKAYKRQAEEAEEqantnlsKFRKVQHELDEAEERADIAESQVNKLRA 511
Cdd:TIGR02169 471 LYDLKEEYDRVEK-------ELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
77-417 |
5.32e-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: 52.38 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 77 YEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQsaleEAEASLEHEEGKILRAQLEFNQ 156
Cdd:pfam05622 140 YKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 157 IKA-------EIERNVAEKD---EEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAA 226
Cdd:pfam05622 216 LEEklealqkEKERLIIERDtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 227 EAQKQvkSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRavveqtersRKLAEQElietservqllh 306
Cdd:pfam05622 296 LGQEG--SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQ---------KALQEQG------------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 307 SQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---T 378
Cdd:pfam05622 353 SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksV 432
|
330 340 350
....*....|....*....|....*....|....*....
gi 386973 379 IKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEA 417
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
204-512 |
5.97e-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: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 204 KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQ--IQLDDAVRANDdlkenIAIVERRNNLLQAELEELRAVV 281
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAEryKELKAELRELE-----LALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 282 EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKE 361
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 362 QDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRK---------- 431
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEA-ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnneierlea 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 432 ----SERRIKELTYQTEEDRKNLLRLQdlVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 507
Cdd:TIGR02168 408 rlerLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
....*
gi 386973 508 KLRAK 512
Cdd:TIGR02168 486 QLQAR 490
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
43-508 |
7.51e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 43 AEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL 122
Cdd:PTZ00121 1202 AEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAD 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 123 EAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALR 202
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 203 VKKKMEGDlnemEIQLSHANRMAAEAQKQVKSLQSlLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVE 282
Cdd:PTZ00121 1362 AEEKAEAA----EKKKEEAKKKADAAKKKAEEKKK-ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 283 QTERSRKLAEQELIETSERVQllHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAitDAAMMAEELKKEQ 362
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAK--KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKA--DEAKKAAEAKKKA 1512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 363 DTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEaRVRELENELEAEQKRNAESVKGMrksERRIKELTYQ 442
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNM---ALRKAEEAKK 1588
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386973 443 TEEDRknllrlQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNK 508
Cdd:PTZ00121 1589 AEEAR------IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
195-477 |
8.41e-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: 51.99 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 195 RSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAEL 274
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 275 EELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQlqTEVEEAVQECRNAEEKAKKAITDAAMM 354
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 355 AEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSER 434
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK--------EIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 386973 435 RIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQ 477
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
204-437 |
9.78e-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: 50.92 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 204 KKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ 283
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 284 TER--SRKLAEQELIETSERVQLLHSQNTS--LINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELK 359
Cdd:COG4942 102 QKEelAELLRALYRLGRQPPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386973 360 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggkKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIK 437
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAEL-----AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
92-422 |
1.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 92 KNLQEEISDLteQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNqikaeiernvaEKDEE 171
Cdd:TIGR02168 216 KELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS-----------ELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 172 MEQAKRNHLRVVdSLQTSLDAETRSRNEALRvkkKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVR 251
Cdd:TIGR02168 283 IEELQKELYALA-NEISRLEQQKQILRERLA---NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 252 ANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIEtservqllhsqntslinqkkkMDADLSQLQTEVE 331
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER---------------------LEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 332 EAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSahLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVREL 411
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELEEELEE--LQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLDSL 494
|
330
....*....|.
gi 386973 412 ENELEAEQKRN 422
Cdd:TIGR02168 495 ERLQENLEGFS 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-278 |
1.08e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 2 SLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEES-------QSELESSQKEARSLSTELFKLK 74
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqkelyalANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 75 NAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEF 154
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 155 NQIKAEIERNvaekDEEMEQAKRNHLRvvdslqtsldaeTRSRNEALRvKKKMEGDLNEMEIQLSHANRMAAEAQKQVKS 234
Cdd:TIGR02168 396 ASLNNEIERL----EARLERLEDRRER------------LQQEIEELL-KKLEEAELKELQAELEELEEELEELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 386973 235 LQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELR 278
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
76-513 |
1.40e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 76 AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEheegKILRAQLEFN 155
Cdd:PRK02224 245 EHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAE----AVEARREELE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 156 QIKAEIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEAlrvkKKMEGDLNEMEIQLSHANRMAAEAQKQVKSL 235
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEA----AELESELEEAREAVEDRREEIEELEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 236 QSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAE----QELIETSERVQLLHSQNts 311
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecGQPVEGSPHVETIEEDR-- 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 312 liNQKKKMDADLSQLQTEVEEAvqecrnaEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ 391
Cdd:PRK02224 475 --ERVEELEAELEDLEEEVEEV-------EERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 392 ialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEE---DRKNLLRLQDLVDKLQLKVKAYK 468
Cdd:PRK02224 538 --------RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLAAIADAEDEIE 609
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 386973 469 RQAEEAEEQANTN------LSKFRKVQHELDEAEERADIAESQVNKLRAKS 513
Cdd:PRK02224 610 RLREKREALAELNderrerLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
62-523 |
1.86e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 62 EARSLSTELFKLKNAYEESLEhletfKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEasLE 141
Cdd:COG4913 226 AADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 142 HEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHA 221
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 222 ----NRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEN-------IAIVERRNNLLQAELEELRAVVEqteRSRKL 290
Cdd:COG4913 379 aeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALA---EALGL 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 291 AEQ------ELIETSER--------VQLLHSQNTSL-------------INQKK-------------------------- 317
Cdd:COG4913 456 DEAelpfvgELIEVRPEeerwrgaiERVLGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprldpds 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 318 ---KMDADLSQLQTEVEEAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTIKDL 382
Cdd:COG4913 536 lagKLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKLAAL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 383 QHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELtyqtEEDRKNLLRLQDLVDKL 460
Cdd:COG4913 616 EAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDLAAL 690
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386973 461 QLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNE 523
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
78-497 |
4.43e-06 |
|
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: 49.79 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 78 EESLEHLETFKRENKNLQEEISDLTEQLgssgktiHELEKVRKQLEAEKMELQSALEEAEAS---LEHEEGKILRAQLEF 154
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQL-------DEEEAARQKLQLEKVTTEAKIKKLEEDillLEDQNSKLSKERKLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 155 NQIKAEIERNVAEKDEE---MEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQ 231
Cdd:pfam01576 158 EERISEFTSNLAEEEEKaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 232 VKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELieTSERVQLLHSQNTS 311
Cdd:pfam01576 238 LAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL--EALKTELEDTLDTT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 312 LINQKKKmdadlSQLQTEVEEavqecrnaeekAKKAITDAAMMAEelkkeqdtsAHLERMKKNMEQTIKDLQHRLDEAEQ 391
Cdd:pfam01576 316 AAQQELR-----SKREQEVTE-----------LKKALEEETRSHE---------AQLQEMRQKHTQALEELTEQLEQAKR 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 392 iALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQA 471
Cdd:pfam01576 371 -NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLL 449
|
410 420
....*....|....*....|....*.
gi 386973 472 EEAEEQANTNLSKFRKVQHELDEAEE 497
Cdd:pfam01576 450 NEAEGKNIKLSKDVSSLESQLQDTQE 475
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
253-462 |
6.60e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 253 NDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRK--LAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEV 330
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 331 EeAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQHRLDEAEQIALKGGKKQ 400
Cdd:COG3206 243 A-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386973 401 LQKLEARVRELENELEAEQKRnaesVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQL 462
Cdd:COG3206 322 LEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
257-524 |
9.26e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 257 KENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ-----------ELIETSERVQLLHSQNTSLINQKKKMDADLSQ 325
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKAERYRELKEElkeleaellllKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 326 LQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLE 405
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-ELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 406 ARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDlvdklQLKVKAYKRQAEEAEEQANTNLSKF 485
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR-----AAAELAAQLEELEEAEEALLERLER 418
|
250 260 270
....*....|....*....|....*....|....*....
gi 386973 486 RKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE 524
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
42-498 |
1.17e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 42 LAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYE-ESLEHLETFKRENKNLQEEISDLTE-----QLGSSGKTIHEL 115
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaEDARKAEEARKAEDAKRVEIARKAEdarkaEEARKAEDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 116 EKVRKQLEAEKMELQSALEEA----EASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHLRVVDSLQTSLD 191
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDArkaeAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 192 AETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQK--QVKSLQSLLKDTQiqlddAVRANDDLKENIAIVERRNNL 269
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKaeEKKKADEAKKKAE-----EAKKADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 270 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSlinQKKKMDadlsqlqtEVEEAVQECRNAEEKAKKAIT 349
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE---AKKKAD--------AAKKKAEEKKKADEAKKKAEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 350 DAAmMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKqlqKLEARVRELENELEAEQKRNAESVKGM 429
Cdd:PTZ00121 1403 DKK-KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 430 RKSERRIKELTYQTEEDRKnllRLQDLVDKLQLKVKAYK-RQAEEAEEQANTNLSKFRKVQHELDEAEER 498
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKK---KADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
29-448 |
1.23e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 29 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKR-ENKNLQEEISDLTEQLGS 107
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 108 SGKTIHELEKVRKQLEAEKM--ELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKR-NHLRVVD 184
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKaeEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKKAD 1525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 185 SLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQI-------QLDDAVRANDDLK 257
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeeaRIEEVMKLYEEEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 258 ENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQkkkmdADLSQLQTEVEEAVQEC 337
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA-----AEEAKKAEEDKKKAEEA 1680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 338 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEA 417
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
410 420 430
....*....|....*....|....*....|...
gi 386973 418 EQKRNAESVKGMRKSERR--IKELTYQTEEDRK 448
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEavIEEELDEEDEKRR 1793
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
9-377 |
1.72e-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: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 9 RLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFK 88
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQ 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 89 RENKNLQEEISDLTEQLGSSGKTIH-ELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIeRNVAE 167
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEaQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL-RTLQQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 168 KDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLD 247
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 248 DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQ 327
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT 558
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 386973 328 TEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 377
Cdd:pfam01576 559 QQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQ 608
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
61-266 |
2.14e-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: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 61 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASL 140
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 141 EHEEGKI---LRAQLEFNQ-------IKAEIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGD 210
Cdd:COG4942 100 EAQKEELaelLRALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 386973 211 LNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERR 266
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
23-514 |
2.22e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 23 RSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLknayEESLEHLETFKRENKNLQEEISDLT 102
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA----EEKKKADEAKKAEEKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 103 EQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQlefnqiKAEIERNVAEKDEEMEQAKRNHLRV 182
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE------AAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 183 vdslqtslDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSllKDTQIQLDDAVRANDDLKENIAI 262
Cdd:PTZ00121 1386 --------KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEE 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 263 VERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDadlSQLQTEVEEAVQECRNAEE 342
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD---EAKKAEEAKKADEAKKAEE 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 343 KAKkaiTDAAMMAEELKKEQDTSaHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRN 422
Cdd:PTZ00121 1533 AKK---ADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 423 AESVKGMRKSERRIKELTyQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAE---EQANTNLSKFRKVQHELDEAEERA 499
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
490
....*....|....*
gi 386973 500 DIAESQVNKLRAKSR 514
Cdd:PTZ00121 1688 KKAAEALKKEAEEAK 1702
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
236-474 |
2.49e-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: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 236 QSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQ 315
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 316 KKKMDADLSQLqteveeavqeCRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI--A 393
Cdd:COG4942 99 LEAQKEELAEL----------LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 394 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKgmrKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEE 473
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 386973 474 A 474
Cdd:COG4942 246 A 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
61-494 |
3.08e-05 |
|
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: 47.04 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 61 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQE-------------------EISDLTEQLGSSGKTIH----ELEK 117
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLEALKSESQNKIElllqqhqdrieqlisehevEITGLTEKASSARSQANsiqsQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 118 VRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHLRV------VDSLQTSLD 191
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFsqesgnLDDQLQKLL 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 192 AETRSRNEALRVKKKMEGDLNEME----IQLSHANRMAAEAQKQVKSLQSLLK----DTQIQLDDAVRANDDLKENIAIV 263
Cdd:pfam15921 384 ADLHKREKELSLEKEQNKRLWDRDtgnsITIDHLRRELDDRNMEVQRLEALLKamksECQGQMERQMAAIQGKNESLEKV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 264 ERRNNLLQAELEELRAVVEQT-------ERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQ--TEVEEAV 334
Cdd:pfam15921 464 SSLTAQLESTKEMLRKVVEELtakkmtlESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQhlKNEGDHL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 335 QECRNAEEKAKKAITDAAMMAEELKKEQD-----------TSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKqLQK 403
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK-IRE 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 404 LEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNllrLQDLVDKLQLKVKAYKRQAEEAEEQANTNLS 483
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNE---LNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
490
....*....|.
gi 386973 484 KFRKVQHELDE 494
Cdd:pfam15921 700 QLKSAQSELEQ 710
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
66-284 |
5.60e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 66 LSTELFKLKNAYEESLEHLETFKRENKnlqeeISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEG 145
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 146 KI--LRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANR 223
Cdd:COG3206 255 ALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386973 224 MAAEAQKQVKSLQSLlkdtQIQLddavranDDLKENIAIVERRNNLLQAELEELRAVVEQT 284
Cdd:COG3206 335 QLAQLEARLAELPEL----EAEL-------RRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-417 |
6.39e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 3 LEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 82
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 83 HLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIE 162
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 163 RNVAEKDEEMEQAK--------------RNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEI-------QLSHA 221
Cdd:COG1196 495 LLLEAEADYEGFLEgvkaalllaglrglAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAieylkaaKAGRA 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 222 NRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRA--------VVEQTERSRKLAEQ 293
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLeaalrravTLAGRLREVTLEGE 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 294 ELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 373
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 386973 374 NMEQTIKDLQHRLDEAEQIALKGGKKQLQKLE---ARVRELENELEA 417
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELErelERLEREIEALGP 781
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-516 |
3.87e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 3 LEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 82
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 83 HLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIE 162
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 163 RnvaeKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG------DLNEME------IQLSHANRM------ 224
Cdd:TIGR02169 480 R----VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaQLGSVGeryataIEVAAGNRLnnvvve 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 225 ----AAEAQKQVKS-------------LQSLLKDTQIQLDDAVRAN-------DDLKENIAIVERRNNLLQAELEELRAV 280
Cdd:TIGR02169 556 ddavAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFavdlvefDPKYEPAFKYVFGDTLVVEDIEAARRL 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 281 VEQ----------------------TERSRKL----AEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAV 334
Cdd:TIGR02169 636 MGKyrmvtlegelfeksgamtggsrAPRGGILfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 335 QECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEAR-----VR 409
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE-DLHKLEEALNDLEARlshsrIP 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 410 ELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQ 489
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
570 580
....*....|....*....|....*..
gi 386973 490 HELDEAEERADIAESQVNKLRAKSRDI 516
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLREL 901
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
227-458 |
5.05e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 227 EAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIA-IVERRNNL--LQAELEELRAVVEQTERSRKLAEQELIETSERVQ 303
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEeHEERREELetLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 304 LLHSQNTSLINQKKKMDAD---LSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIK 380
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADaeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD---LEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 381 DLQHRLDEAEQiALKGGKKQLQKLEARVRELENELE--AEQKRNAESVKGMRKSER-----RIKELTYQTEEDRKNLLRL 453
Cdd:PRK02224 367 ELESELEEARE-AVEDRREEIEELEEEIEELRERFGdaPVDLGNAEDFLEELREERdelreREAELEATLRTARERVEEA 445
|
....*
gi 386973 454 QDLVD 458
Cdd:PRK02224 446 EALLE 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
76-523 |
5.07e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 76 AYEESLEHLETFKRENKNLQEEISDLTEQLGSSgktihelEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFN 155
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA-------EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 156 qiKAEIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSL 235
Cdd:PTZ00121 1165 --KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 236 QsllKDTQIQLDDAVRANDDLKenIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIEtservqllhsqntslinQ 315
Cdd:PTZ00121 1243 K---KAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE-----------------E 1300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 316 KKKMDadlsqlqtEVEEAVQECRNAEEKAKKAiTDAAMMAEELKKEQdtsahlERMKKNMEQTIKDLQHRLDEAEQIALK 395
Cdd:PTZ00121 1301 KKKAD--------EAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKA------EEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 396 GGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQlKVKAYKRQAEEAE 475
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-KADEAKKKAEEAK 1444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 386973 476 --EQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNE 523
Cdd:PTZ00121 1445 kaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEE 1494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
257-522 |
5.69e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 257 KENIAIVERRNNLLQAELEELRAVVE--QTERSRKLAEQELIETSERVQLlhsqnTSLINQKKKMDADLSQLQTEVEEAV 334
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEG-----YELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 335 QEcrnaEEKAKKAITDAAMMAEELKKEQDTSAhlERMKKNMEQTIKDLQHRLDEAEqialkggkKQLQKLEARVRELENE 414
Cdd:TIGR02169 251 EE----LEKLTEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELE--------AEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 415 LEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDE 494
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260
....*....|....*....|....*...
gi 386973 495 AEERADIAESQVNKLRAKSRDIGTKGLN 522
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELAD 424
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
262-400 |
9.47e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 262 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDAdlsQLQTEVEEAVQECRNAE 341
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 386973 342 EKAKKAITDAAMMAEELKKEQDTSAHLermkKNMEQTIKDLQHRLDEAEQIALKGGKKQ 400
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKA----HELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
270-517 |
9.66e-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: 42.08 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 270 LQAELEELRAvveQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEavQECRNAEEKAKKAIT 349
Cdd:pfam01576 55 LCAEAEEMRA---RLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 350 DAAM--MAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVK 427
Cdd:pfam01576 130 EAKIkkLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 428 GMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 507
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
250
....*....|
gi 386973 508 KLRAKSRDIG 517
Cdd:pfam01576 289 KAEKQRRDLG 298
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
66-512 |
1.42e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 66 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEG 145
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 146 KILRAQ-------------LEFNQIKAEIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNE----------ALR 202
Cdd:TIGR04523 202 LLSNLKkkiqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQlsekqkeleqNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 203 VKKKMEGDLNEMEIQLSHANRMAA-----EAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEEL 277
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 278 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE 357
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 358 LKKEQDTSAHLERMKKNMEQTIKDLQHRLD-------------EAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAE 424
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 425 SVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQL-KVKAYKRQAEEAEEQANTNLSKfrkvqhELDEAEERADIAE 503
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNKEIEELKQTQKSLKK------KQEEKQELIDQKE 595
|
....*....
gi 386973 504 SQVNKLRAK 512
Cdd:TIGR04523 596 KEKKDLIKE 604
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
276-460 |
1.42e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 276 ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKK---AITDAA 352
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 353 MMAEELKKE--------------QDTSAHLERMKKNMEQtIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELENELE 416
Cdd:PHA02562 269 SKIEQFQKVikmyekggvcptctQQISEGPDRITKIKDK-LKELQHSLEKLDtaIDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 386973 417 AEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKL 460
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
314-516 |
1.97e-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: 40.52 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 314 NQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiA 393
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 394 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT----YQTEEDRKNLLRLQDLVDKLQLKVKAYKR 469
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparrEQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 386973 470 QAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 516
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
70-498 |
2.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 70 LFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAE------ASLEHE 143
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 144 EGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHLRVvdslqTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANR 223
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 224 MAAEAQKQVKSLQSLLKdtqiQLDDAVRANDDLKENIAIVERRNNLlqaeLEELRAVVEQTERSRK-LAEQELIETSERV 302
Cdd:PRK03918 322 EINGIEERIKELEEKEE----RLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKrLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 303 QLLHSQNTSLINQKKKMDADLSQLQTEVEEAvqecRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTIKDL 382
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGRELTEE-----HRKELLEEYTAELKRI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 383 QHRLDEAEqialkggkKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELTYQT-EEDRKNLLRLQDLVDK 459
Cdd:PRK03918 465 EKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
410 420 430
....*....|....*....|....*....|....*....
gi 386973 460 LQLKVKAYKRQAEEAEEQANtnlsKFRKVQHELDEAEER 498
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
248-424 |
2.53e-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: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 248 DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAE--QELIETSERVQLLHSQNTSLINQKKKMDA---D 322
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDAssdD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 323 LSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELkkeqdtsahlermkKNMEQTIKDLQHRLDEAEQIALKGGKKQLQ 402
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKEL--------------EQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180
....*....|....*....|....*...
gi 386973 403 KL------EARVRELENELEAEQKRNAE 424
Cdd:COG4913 753 ERfaaalgDAVERELRENLEERIDALRA 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-177 |
2.57e-03 |
|
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: 40.82 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 1 SSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEwkQKYEESQSELESSQKEARSLSTELFKLKNAYEES 80
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 81 LEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAE 160
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
170
....*....|....*..
gi 386973 161 IERNVAEKDEEMEQAKR 177
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSE 921
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
29-424 |
3.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 29 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLtEQLGSS 108
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 109 GKTIHELEKVRKQLEAEKMELQsALEEAEASLEHEEGKILRAQLEFNQIKAEIERNVAEKDEEMEQAKRNHLRVVDSLQT 188
Cdd:COG4717 128 LPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 189 SLDAETRSRNEALRVKKKMEGDLNEMEIQLshanrMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEN--------- 259
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIltiagvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 260 ----IAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQ 335
Cdd:COG4717 282 vlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 336 ECRNAEEKAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKggkKQLQKLE 405
Cdd:COG4717 362 ELQLEELEQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---EELEELE 438
|
410
....*....|....*....
gi 386973 406 ARVRELENELEAEQKRNAE 424
Cdd:COG4717 439 EELEELEEELEELREELAE 457
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1-516 |
3.04e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 1 SSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES 80
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 81 LEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQIKAE 160
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 161 IERNVAEKDEEME-QAKRNhlRVVDSLQTSLDAETRSRNEALR-VKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSL 238
Cdd:pfam01576 308 LEDTLDTTAAQQElRSKRE--QEVTELKKALEEETRSHEAQLQeMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 239 LKDTQIQLDDAVRANDDlkeniaiVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKK 318
Cdd:pfam01576 386 NAELQAELRTLQQAKQD-------SEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 319 MDADLSQLQTEVEEAvQECRNAEEKAKKAIT--------DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAE 390
Cdd:pfam01576 459 LSKDVSSLESQLQDT-QELLQEETRQKLNLStrlrqledERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 391 QIalkggkkqLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKA---- 466
Cdd:pfam01576 538 GT--------LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKfdqm 609
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 467 ----------YKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 516
Cdd:pfam01576 610 laeekaisarYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL 669
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
325-514 |
3.29e-03 |
|
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: 40.43 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 325 QLQTEVEEAVQECRNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKL 404
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 405 EARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSK 484
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190
....*....|....*....|....*....|
gi 386973 485 FRKVQHELDEAEERADIAESQVNKLRAKSR 514
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLE 382
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
89-217 |
3.40e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 89 RENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLEFNQiKAEIERNVAEK 168
Cdd:COG2433 392 EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR-EIRKDREISRL 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 386973 169 DEEmeqakrnhlrvVDSLQTSLDaETRSRNEALRVKKKMEGDLNEMEIQ 217
Cdd:COG2433 471 DRE-----------IERLERELE-EERERIEELKRKLERLKELWKLEHS 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-295 |
3.87e-03 |
|
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: 40.05 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 2 SLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEA-RSLSTELFKLKNAYEES 80
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 81 LEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL-------EAEKMELQSALEEAEASLEheegkilRAQLE 153
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLteeyaelKEELEDLRAELEEVDKEFA-------ETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 154 FNQIKAEIErnvaEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEAlrvkKKMEGDLNEMEIQLShanrmaaEAQKQVK 233
Cdd:TIGR02169 387 LKDYREKLE----KLKREINELKRELDRLQEELQRLSEELADLNAAI----AGIEAKINELEEEKE-------DKALEIK 451
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386973 234 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRA---VVEQTERSRKLAEQEL 295
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAqarASEERVRGGRAVEEVL 516
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
270-523 |
4.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 270 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAIT 349
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 350 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGM 429
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 430 RKSERRIKELtyQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 509
Cdd:COG4372 203 AEAEKLIESL--PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250
....*....|....
gi 386973 510 RAKSRDIGTKGLNE 523
Cdd:COG4372 281 AALELEALEEAALE 294
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
208-406 |
5.04e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 208 EGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERS 287
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 288 RKLAE---------------QELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQEcrnAEEKAKKAITDAA 352
Cdd:COG3883 95 LYRSGgsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE---LEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386973 353 MMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEA 406
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
160-511 |
7.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 160 EIERNVAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLL 239
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 240 KDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 319
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 320 DADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKK 399
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 400 QLQKLEARVRELENELEAEQKRNAESVKGmRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQAN 479
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEK-DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
330 340 350
....*....|....*....|....*....|..
gi 386973 480 TNLSKFRKVQHELDEAEERADIAESQVNKLRA 511
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
61-461 |
7.50e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 61 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMeLQSALEEAEASL 140
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIER-YQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 141 EheegkilraqlEFNQIKAEIERNVAEKDEEMEQAKRNHLRVVDSL---QTSLDA-ETRS--RNEALRVKKKMEGDLNEM 214
Cdd:PRK04863 365 E-----------EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLadyQQALDVqQTRAiqYQQAVQALERAKQLCGLP 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 215 EIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaiverrnnllqaELEELRAVVEQTERSR-KLAEQ 293
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQ--------------AYQLVRKIAGEVSRSEaWDVAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 294 ELIETSERVQLLHSQNTSLINQKKKMDADLsQLQTEVEEAVQEcrnAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKK 373
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRLSELEQRL-RQQQRAERLLAE---FCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 374 N-------MEQTIKDLQHRLDEAEQIAlkggkKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEED 446
Cdd:PRK04863 576 EarerrmaLRQQLEQLQARIQRLAARA-----PAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
410
....*....|....*
gi 386973 447 RKNLLRLQDLVDKLQ 461
Cdd:PRK04863 651 AARKQALDEEIERLS 665
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10-497 |
9.19e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 10 LQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKR 89
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEE-LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 90 ENKNLQEEISDLTEQLgssgKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEgKILRAQLEFNQIKAEIERNVAEK- 168
Cdd:PRK03918 315 RLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTPEKl 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 169 DEEMEQAKRNHLRVVDSLQT------SLDAETRSRNEALRVKKKMEGD--LNEMEIQLSHANRMAAEAQKQVKSLQSLLK 240
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKitarigELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 241 DTQIQLDDAVRANDDLkENIAIVERRNNLLQAELEELRAVVEQTErsrKLAEQELIETSERVQLLHSQNTSLINQKKKMD 320
Cdd:PRK03918 470 EIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLK---KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 321 ADLSQLqteveeavqecrNAEEKAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQHRLDEAEQ-----IALK 395
Cdd:PRK03918 546 KELEKL------------EELKKKLAELEKKLDELEEELAEL-----LKELEELGFESVEELEERLKELEPfyneyLELK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 396 GGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNllRLQDLVDKLQLKVKAYKRQAEEAE 475
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELE 686
|
490 500
....*....|....*....|..
gi 386973 476 EQANTNLSKFRKVQHELDEAEE 497
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREK 708
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-177 |
9.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 3 LEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKIlaewkQKYEESQSELESSQKEARSLSTELFKLknayEESLE 82
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWDEIDVASAEREIAELEAELERL----DASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 83 HLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKMELQSALEEAEASLEHEEGKILRAQLE-------FN 155
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAaalgdavER 765
|
170 180
....*....|....*....|..
gi 386973 156 QIKAEIERNVAEKDEEMEQAKR 177
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEE 787
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
151-425 |
9.69e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 38.88 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 151 QLEFNQIKAEIERnvAEKDEEMEQAKrnhlrVVDSLQTSLDAetrsrnealrvkkkmegdLNEMEIqlshANRMAAEAQK 230
Cdd:PRK10929 22 APDEKQITQELEQ--AKAAKTPAQAE-----IVEALQSALNW------------------LEERKG----SLERAKQYQQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 231 QVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAE---LEELRAVVEQTERSRKLAE-------------QE 294
Cdd:PRK10929 73 VIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSsqlLEKSRQAQQEQDRAREISDslsqlpqqqtearRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386973 295 LIETSERVQLLHSQNTSLiNQkkkmdADLSQLQteveeavqecrnAEEKAKKAITDaammaeELKkeqdtsahLERMKKN 374
Cdd:PRK10929 153 LNEIERRLQTLGTPNTPL-AQ-----AQLTALQ------------AESAALKALVD------ELE--------LAQLSAN 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 386973 375 MEQTIKDLQHRLdeaeqialkgGKKQLQKLEARVRELENELEAEQKRNAES 425
Cdd:PRK10929 201 NRQELARLRSEL----------AKKRSQQLDAYLQALRNQLNSQRQREAER 241
|
|
| |
