|
Name |
Accession |
Description |
Interval |
E-value |
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
72-389 |
2.31e-18 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 85.74 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 72 RERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQ 151
Cdd:pfam13868 2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 152 VTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVgRA 231
Cdd:pfam13868 82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL-EY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 232 LQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARK-QLMNEVMNT 310
Cdd:pfam13868 161 LKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKaRQRQELQQA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116138752 311 RKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIAHQQQAREAEKEEERQEFEA 389
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGER 319
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-350 |
1.38e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 9 EERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQqfRERCEELRtklasiheK 88
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAK--------K 1490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 89 KVVEERNAQIEFNKELKRQKLVEEhlfARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEE 168
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADE---AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE 1567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 169 EARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLdlnmklvgRALQDLQDEADKKKQKREE 248
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI--------KAEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 249 MGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKL-QVQERLQRKLREQE 327
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAeELKKKEAEEKKKAE 1719
|
330 340
....*....|....*....|...
gi 116138752 328 ELALHEQRISESLKVLHQEDMED 350
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEED 1742
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-347 |
3.74e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 45 RERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIhEKKVVEERNAQIEFNKELKRQKLVEEHL---FARLWEE 121
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL-EAELEELRLELEELELELEEAQAEEYELlaeLARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 122 DRLAKERREAQEEKRQRELVQNTRlgLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREdEQEKLQKQKRRQETRSS 201
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAE--LEEELEELEEELEELEEELEEAEEELEEAEAELAEA-EEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 202 LKKAVQDKIESMQREYREDLDLNmklvgRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDI 281
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLE-----ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116138752 282 KAKKLAEKDRELALQRAARKQlmnEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQED 347
Cdd:COG1196 456 EEEEALLELLAELLEEAALLE---AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
125-396 |
1.78e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 125 AKERREAQEEKRQREL---------VQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKlQKQKRR 195
Cdd:COG1196 212 AERYRELKEELKELEAellllklreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE-EAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 196 QETRSSLKKAVQDKIESMQReyREDLDLNMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELN 275
Cdd:COG1196 291 YELLAELARLEQDIARLEER--RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 276 RLLEDIKAKKLAEKDRELALQRAARKQLMNEV-MNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARR 354
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 116138752 355 CALAEEYRNQLQMQIAHQQQAREAEKEEERQEFEAGLAANKA 396
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
55-373 |
5.79e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 55 KEKERQEFVAEKLDQQFRERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQklveehlfarlweedrlakerREAQEE 134
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQ---------------------IEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 135 KRQRELVQntrlgldaqvtsiqaqrqgarrmKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQ 214
Cdd:pfam13868 88 KRQEEYEE-----------------------KLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 215 REYREDLDLNMKLVgRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELA 294
Cdd:pfam13868 145 LEKEEEREEDERIL-EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 295 LQRAARK-QLMNEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIAHQQ 373
Cdd:pfam13868 224 REEAEKKaRQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEERE 303
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-360 |
5.99e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 9 EERRNKLRELLASEENEYfSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQF----RERCEELRTKLAS 84
Cdd:COG1196 252 EAELEELEAELAELEAEL-EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREleerLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 85 IHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEE-KRQRELVQNTRLGLDAQVTSIQAQRQGAR 163
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQLEELEEAEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 164 RMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKK 243
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 244 QKREEMGREQKIYNDYLMQRREEEKAQEKELNR--LLEDIKAKKLAEKDRELALQrAARKQLMNEVMNTRKLQVQERLQR 321
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAgaVAVLIGVEAAYEAALEAALA-AALQNIVVEDDEVAAAAIEYLKAA 569
|
330 340 350
....*....|....*....|....*....|....*....
gi 116138752 322 KLREQEELALHEQRISESLKVLHQEDMEDFARRCALAEE 360
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
9-303 |
1.50e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 9 EERRNKLRELLASEENEYFSEMQLKgETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEK 88
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYR-QELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 89 KVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEE 168
Cdd:pfam13868 130 EEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 169 eaRILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKREe 248
Cdd:pfam13868 210 --LYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM- 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 116138752 249 mgREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQL 303
Cdd:pfam13868 287 --KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-296 |
2.89e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 9 EERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEK 88
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 89 KVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEE 168
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 169 EARILEQNK---AQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQK 245
Cdd:PTZ00121 1666 EAKKAEEDKkkaEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 116138752 246 REEMGREQKIYNDYLMQRREEEKAQEkELNRLLEDIKAKKLAEKDRELALQ 296
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAE-EIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
10-366 |
4.93e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 10 ERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEKK 89
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 90 VVEERNAQIEFNKELKRQKLVEEhLFARLWEEDRLAKERREAQEEKRQRElvqntrlglDAQVTSIQAQRQGARRMKEEE 169
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADE-AKKKAEEDKKKADELKKAAAAKKKAD---------EAKKKAEEKKKADEAKKKAEE 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 170 ARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESmqreyrEDLDLNMKLVGRALQDLQDEADKKKQKREEM 249
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA------DEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 250 GREQKIYNDYLM---QRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLREQ 326
Cdd:PTZ00121 1517 KAEEAKKADEAKkaeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 116138752 327 EELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQ 366
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-312 |
5.01e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 9 EERRNKLRELLASEENEYFSEMQLKGEtieekKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRT--KLASIH 86
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAE-----EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaeEKKKAE 1567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 87 EKKVVEERNAQIEFNKELKRQ---KLVEEHLFARLWEEDRLAKERREAQEEKRQRELV---QNTRLGLDAQVTSIQAQRQ 160
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 161 GARRMKEEEARIlEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEAD 240
Cdd:PTZ00121 1648 KAEELKKAEEEN-KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116138752 241 KKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRK 312
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
38-314 |
6.24e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 38 EEKKDKMRERTKLLREKK----EKERQEFVAEKLDQQFRERCEELRTklASIHEKKVVEERNAQIEFNKELKRQKLVEEH 113
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKarqaEMDRQAAIYAEQERMAMERERELER--IRQEERKRELERIRQEEIAMEISRMRELERL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 114 LFARLWEEDRLAKERREA-----QEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQ-NKAQIKREDEQE 187
Cdd:pfam17380 384 QMERQQKNERVRQELEAArkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERvRLEEQERQQQVE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 188 KLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALqdLQDEADKKKQKREEMGREQKIYNDYLMQRREEE 267
Cdd:pfam17380 464 RLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM--IEEERKRKLLEKEMEERQKAIYEEERRREAEEE 541
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 116138752 268 KAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQ 314
Cdd:pfam17380 542 RRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-339 |
1.17e-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: 44.67 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 20 ASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKerqeFVAEKLDQQFRERCEELRTKLASIHEKKVVEERNAQIE 99
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER----YQALLKEKREYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 100 FNKElKRQKLVEEHlfarlwEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQ 179
Cdd:TIGR02169 251 EELE-KLTEEISEL------EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 180 IKREDEQ-----EKLQKQKRRQETRSSLKKAVQDKIESMQREYR------EDLDLNMKLVGRALQDLQDEADKKKQKREE 248
Cdd:TIGR02169 324 LAKLEAEidkllAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraelEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 249 MGREQkiynDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQErlQRKLREQEE 328
Cdd:TIGR02169 404 LKREL----DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE--QELYDLKEE 477
|
330
....*....|.
gi 116138752 329 LALHEQRISES 339
Cdd:TIGR02169 478 YDRVEKELSKL 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
69-342 |
5.61e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 69 QQFRERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARL------WEEDRLAKERREAQEEKRQREL-- 140
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELqeleekLEELRLEVSELEEEIEELQKELya 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 141 --------------VQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQI-----KREDEQEKLQKQKRRQETRSS 201
Cdd:TIGR02168 293 laneisrleqqkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 202 LKKAVQDKIESMQREY---REDLDLNMKLVGRA---LQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKE-- 273
Cdd:TIGR02168 373 RLEELEEQLETLRSKVaqlELQIASLNNEIERLearLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEel 452
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116138752 274 ----------LNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLREQEELALHEQRISESLKV 342
Cdd:TIGR02168 453 qeelerleeaLEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV 531
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
122-330 |
6.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 122 DRLAKERREAQEEKRQRELVQntrlGLDAQVTSIQAQRQGARRMKEEEARI------LEQNKAQIKREDEQEKLQKQKRR 195
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE----PIRELAERYAAARERLAELEYLRAALrlwfaqRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 196 QETRSSLKKAVQDKIESMQREYREDldlnmklVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELN 275
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGN-------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116138752 276 RLLEDIKAKKLAEKDRELALQRAARKQLmnevmnTRKLQVQERLQRKLREQEELA 330
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAE------AALRDLRRELRELEAEIASLE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
5-220 |
9.03e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 5 VINTEERRNKLRELLASEENEyfsEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLAS 84
Cdd:COG1196 297 LARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 85 IHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLwEEDRLAKERREAQEEKRQREL-VQNTRLGLDAQVTSIQAQRQGAR 163
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEELEELEEaLAELEEEEEEEEEALEEAAEEEA 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116138752 164 RMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYRED 220
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-370 |
1.48e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 9 EERRNKLRELLASEENEYFSEMQLKGETIEEKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEK 88
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 89 KVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAqvtsiqaqRQGARRMKEE 168
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA--------IEYLKAAKAG 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 169 EARILEQNKAQIKREDEQeklqKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQKREE 248
Cdd:COG1196 573 RATFLPLDKIRARAALAA----ALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 249 MGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLREQEE 328
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 116138752 329 LALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIA 370
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-341 |
1.66e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 87 EKKVVEERNAQIEFNK--ELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQvtsiQAQRQGARR 164
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKaeELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE----EAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 165 MKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQ 244
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 245 KREEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDIKAKKLaeKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLR 324
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK--KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
250
....*....|....*..
gi 116138752 325 EQEELALHEQRISESLK 341
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAK 1424
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
76-373 |
2.25e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 76 EELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRlakeRREAQEEKRQRELVQNTRLGLDAQVTSI 155
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRR----KLEEAEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 156 QAQRQGARRMKEEEARILEQNKAQ-------IKREDEQEKLQKQKRRQETRSSLKKAVQDKIesmQREYREDLDLNMKLV 228
Cdd:pfam17380 345 ERERELERIRQEERKRELERIRQEeiameisRMRELERLQMERQQKNERVRQELEAARKVKI---LEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 229 GRALQDLQDEADKKKQKREEMGREQKIYNdylMQRREEEKAQEKELNRLLEDIKAKKLAEKDRELALQRAA----RKQLM 304
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEERAREMER---VRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAeeqrRKILE 498
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116138752 305 NEVMNTRKLQVQERLQRKLREQEelaLHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQMQIAHQQ 373
Cdd:pfam17380 499 KELEERKQAMIEEERKRKLLEKE---MEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE 564
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
15-366 |
2.77e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 15 LRELLASEENEYFSEMQLKGETIEEKKDKMRE-------RTKLLREKKEKERQEF-VAEKLDQQFRERCEELRTKLASIH 86
Cdd:pfam02463 125 LESQGISPEAYNFLVQGGKIEIIAMMKPERRLeieeeaaGSRLKRKKKEALKKLIeETENLAELIIDLEELKLQELKLKE 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 87 EKKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMK 166
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 167 EEEARILEQNKAQIKREDEQEKLQKQK-RRQETRSSLKKAVQDKIESMQREYREDLDLNMKLVGRALQDLQDEADKKKQK 245
Cdd:pfam02463 285 EEELKLLAKEEEELKSELLKLERRKVDdEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 246 REEMGREQKIYNDYLMQRREEEKAQEKELNRLLEDikaKKLAEKDRELALQRAARKQLMNEVMNTRKLQVQERLQRKLRE 325
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL---KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 116138752 326 QEELALHEQRISESLKVLHQEDMEDFARRCALAEEYRNQLQ 366
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
121-329 |
3.62e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 121 EDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRS 200
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 201 SLKKAVQDKIES-MQREYREDLDLNMKLVGRALQDLQDEADKKKQKREEmgreqkiyndyLMQRREEEKAQEKELNRLLE 279
Cdd:COG4942 113 LYRLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-----------LAALRAELEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 116138752 280 DIKAKKlaekdRELALQRAARKQLMNEVmNTRKLQVQERLQRKLREQEEL 329
Cdd:COG4942 182 ELEEER-----AALEALKAERQKLLARL-EKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-346 |
4.20e-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: 39.67 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 53 EKKEKERQEFvaekldQQFRERCEELRTKLASIHE--KKVVEERNAQIEFNKELKRQKLVEEHLFARLWEEDRLAKERRE 130
Cdd:TIGR02169 170 RKKEKALEEL------EEVEENIERLDLIIDEKRQqlERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 131 AQEEKRQRELVQntrlgldaqvtsIQAQRQGARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQETRSSLKKAvQDKI 210
Cdd:TIGR02169 244 RQLASLEEELEK------------LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL-ERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 211 ESMQREyredldlnMKLVGRALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKELNRLLedikaKKLAEKD 290
Cdd:TIGR02169 311 AEKERE--------LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR-----AELEEVD 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 116138752 291 RELALQRAARKQLmnevmntrklqvQERLQRKLREQEELALHEQRISESLKVLHQE 346
Cdd:TIGR02169 378 KEFAETRDELKDY------------REKLEKLKREINELKRELDRLQEELQRLSEE 421
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-311 |
7.10e-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: 38.90 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 39 EKKDKMRERTKLLREKKEKERQEFVAEKLDQQFRERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEHLFARL 118
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 119 WE-EDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRqgARRMKEEEARILEQNKAQIKREDEQEKLQKQKRRQE 197
Cdd:TIGR02169 311 AEkERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 198 TRSSLKKAVQDKIESMQREYREDLDLNMKLVGR------ALQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQE 271
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEEladlnaAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 116138752 272 KELNRLLEDIKA--KKLAEKDRELALQRAARKQLMNEVMNTR 311
Cdd:TIGR02169 469 QELYDLKEEYDRveKELSKLQRELAEAEAQARASEERVRGGR 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-354 |
7.62e-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: 38.88 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 35 ETIEEKKDKMRERTKLLREKKEKERQEFVA-EKLDQQFRERCEELRTKLASIHEKKVVEERNAQIEFNKELKRQKLVEEH 113
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEElEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 114 LFARLWEEDRLAKERREAQEEKRQRELVQNTRLGLDAQVTSIQAQRQGARRMKEEEARilEQNKAQIKREDEQEKLQKQK 193
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE--EAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 194 RRQETRSSLKKAVQDKIESMQREyredldlnmklvgraLQDLQDEADKKKQKREEMGREQKIYNDYLMQRREEEKAQEKE 273
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAE---------------IEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116138752 274 LNRLLEDIKakklaEKDRELALQRAARKQlMNEVMNTRKLQVQErLQRKLREQEELALHEQRISESLKVLHQEDMEDFAR 353
Cdd:TIGR02168 903 LRELESKRS-----ELRRELEELREKLAQ-LELRLEGLEVRIDN-LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
.
gi 116138752 354 R 354
Cdd:TIGR02168 976 R 976
|
|
|