|
Name |
Accession |
Description |
Interval |
E-value |
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
310-616 |
7.45e-12 |
|
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: 67.25 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 310 AEKQRMEREAKEkaeRERLAHERAEKERQEMEKREkaarEEKERLERQKIERERIERERLVREREREAKERERLERERLL 389
Cdd:pfam13868 29 AEKKRIKAEEKE---EERRLDEMMEEERERALEEE----EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 390 RERAEKERIERERIAKEREKIAKEKE-RMEKERYERERIATERERIAKERMEREKADKERQEKEQIAKEKMEKERLERER 468
Cdd:pfam13868 102 QMDEIVERIQEEDQAEAEEKLEKQRQlREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 469 IAKERERIAKERERAEKERLAREKERMERAAREKE----EREQMEGERIARERARI--AQEKERSERERLEKVRAQKERA 542
Cdd:pfam13868 182 KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQErkerQKEREEAEKKARQRQELqqAREEQIELKERRLAEEAEREEE 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2438152838 543 ALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALREKMEVEK 616
Cdd:pfam13868 262 EFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEER 335
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
300-567 |
1.13e-09 |
|
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: 60.32 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 300 KEREKMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKE 379
Cdd:pfam13868 63 KEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEW 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 380 RERLERerllreraeKERIERERIAK-EREKIAKEKERMEKERYERERIATERERIAK--ERMEREKADKER-------- 448
Cdd:pfam13868 143 KELEKE---------EEREEDERILEyLKEKAEREEEREAEREEIEEEKEREIARLRAqqEKAQDEKAERDElraklyqe 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 449 ---QEKEQIAKEKMEKERLERERIAKERE---RIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQ 522
Cdd:pfam13868 214 eqeRKERQKEREEAEKKARQRQELQQAREeqiELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR 293
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2438152838 523 EKERSERERLEKVRAQKERAALEERERAEKERLEKERIERERLKK 567
Cdd:pfam13868 294 ELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
317-622 |
2.39e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 317 REAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKERERLERERLLRERAEKE 396
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 397 RIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEKEQIAKEKMEKERLERERIAKERERI 476
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 477 AKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKERSERERLEKVRAQKERAALEERERAEKERLE 556
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2438152838 557 KERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALREKMEVEKVNKANG 622
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
395-487 |
4.02e-08 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 56.67 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 395 KERIERERIAKER-EKIAKEKERMEKERYERERiATERERIAKERMERekADKERQEKEQIAKEKMEKERLERERIAK-E 472
Cdd:PTZ00266 432 KDHAERARIEKENaHRKALEMKILEKKRIERLE-REERERLERERMER--IERERLERERLERERLERDRLERDRLDRlE 508
|
90
....*....|....*.
gi 2438152838 473 RERIAK-ERERAEKER 487
Cdd:PTZ00266 509 RERVDRlERDRLEKAR 524
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
438-536 |
5.29e-08 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 56.28 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 438 RMEREKADKERQEKEQIAKEKMEKERLERERIAKeRERIAKER-ERAEKERLAREKERMERAAREKEEREQMEGERIAR- 515
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIER-LEREERERlERERMERIERERLERERLERERLERDRLERDRLDRl 507
|
90 100
....*....|....*....|.
gi 2438152838 516 ERARIaqekERSERERLEKVR 536
Cdd:PTZ00266 508 ERERV----DRLERDRLEKAR 524
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
306-610 |
7.29e-08 |
|
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: 54.92 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 306 EKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKaaREEKERLERQKIERERIERERLVREREREAKERERLER 385
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEER--KRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 386 ERLLRERAEKERIER-ERIAKEREKIAKEKERMEKERYERERIATER-ERIAKERMEREKADKERQEKEQIAKE----KM 459
Cdd:pfam13868 110 IQEEDQAEAEEKLEKqRQLREEIDEFNEEQAEWKELEKEEEREEDERiLEYLKEKAEREEEREAEREEIEEEKEreiaRL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 460 EKERLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKERS-ERERLEKVRAQ 538
Cdd:pfam13868 190 RAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAErEEEEFERMLRK 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2438152838 539 KERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALRE 610
Cdd:pfam13868 270 QAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
300-523 |
7.62e-08 |
|
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: 54.54 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 300 KEREKMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKE 379
Cdd:pfam13868 127 QLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDEL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 380 RERLERERLLRERAEKERIERERIAKEREKIAKEkeRMEKERYERERIATERERiakERMEREKADKERQEKEQIAKEKM 459
Cdd:pfam13868 207 RAKLYQEEQERKERQKEREEAEKKARQRQELQQA--REEQIELKERRLAEEAER---EEEEFERMLRKQAEDEEIEQEEA 281
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2438152838 460 EKERLERERIAKERERIAKERERAEKErlarEKERMERAAREKEEREQMEGERIARERARIAQE 523
Cdd:pfam13868 282 EKRRMKRLEHRRELEKQIEEREEQRAA----EREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
395-509 |
5.70e-07 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 52.82 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 395 KERIERERIAKErekiAKEKERMEKERYEReriateRERIAKERMEREKAdkERQEKEQIAKEKMEKERLERERIakERE 474
Cdd:PTZ00266 437 RARIEKENAHRK----ALEMKILEKKRIER------LEREERERLERERM--ERIERERLERERLERERLERDRL--ERD 502
|
90 100 110
....*....|....*....|....*....|....*.
gi 2438152838 475 RIakerERAEKERLAR-EKERMERAAREKEEREQME 509
Cdd:PTZ00266 503 RL----DRLERERVDRlERDRLEKARRNSYFLKGME 534
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
297-613 |
2.24e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 297 RIGKEREKMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVRERERE 376
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 377 AKERERLERERLLRERAEKERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEKEQIAK 456
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 457 EKMEKERLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKERSERERLEKVR 536
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2438152838 537 AQKERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALREKME 613
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
400-612 |
2.27e-06 |
|
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: 50.30 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 400 RERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEK-----EQIAKEKMEKERLERERIAKERE 474
Cdd:pfam13868 22 KERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrqelEEQIEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 475 RIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKErSERERLEKVRAQKERAALEERERAEKER 554
Cdd:pfam13868 102 QMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEERE-EDERILEYLKEKAEREEEREAEREEIEE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2438152838 555 LEKERIERERLKKERLEKEKSAREQWeRQKNEKEREVREKELMERQKLARERALREKM 612
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDEL-RAKLYQEEQERKERQKEREEAEKKARQRQEL 237
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
219-526 |
5.85e-06 |
|
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: 48.76 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 219 KEKAEKERMEKEKVEKERMEKEKAEKERMEKEKERMEKEKAEKERMEKEKERMEKEKAEKERIGKEKERMEKEKAEKERI 298
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 299 GKEREKMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEK--REKAAREEKERLERQKIERERIERERLVRERERE 376
Cdd:pfam13868 116 AEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEylKEKAEREEEREAEREEIEEEKEREIARLRAQQEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 377 AKERERLERERLLRERAEkeriERERIAKEREKIAKEKERMEKERYERERiatERERIAKERMEREKADKERQEKEQIAK 456
Cdd:pfam13868 196 AQDEKAERDELRAKLYQE----EQERKERQKEREEAEKKARQRQELQQAR---EEQIELKERRLAEEAEREEEEFERMLR 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2438152838 457 EKMEKERLEREriAKERERIAKERERAEKERLAREKERMERAAREKEERE-QMEGERIARERARIAQEKER 526
Cdd:pfam13868 269 KQAEDEEIEQE--EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEgERLREEEAERRERIEEERQK 337
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
291-638 |
9.39e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 291 EKAEKERIGKEREKME--KVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAR-EEKERLERQKIERERIERE 367
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADeaKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaEAEAAADEAEAAEEKAEAA 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 368 RLVREREREAKERERLERERLLRERAEKERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKE 447
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 448 RQEKEQIAKEKMEKERLERERIAKERERIAKERERAE--KERLAREKERMERAAREKEEREQMEGERIARERARIAQEKE 525
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 526 RSERERLEKVRAQKERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARE 605
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
330 340 350
....*....|....*....|....*....|....*..
gi 2438152838 606 RALR----EKMEVEKVNKANGRKPNTSPPRAPPAEEK 638
Cdd:PTZ00121 1610 EEAKkaeeAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
433-504 |
8.27e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.91 E-value: 8.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2438152838 433 RIAKERmeREKADKERQEKEQIAKEKMEKERlEREriaKERERiakERERaekerlAREKERMERAAREKEE 504
Cdd:pfam03154 584 KLAKKR--EEALEKAKREAEQKAREEKEREK-EKE---KERER---ERER------EREAERAAKASSSSHE 640
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
291-638 |
9.72e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 291 EKAEKERIGKEREKMEKVKAEKQ--RMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERER 368
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKadAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 369 LVREREREAKERERLERERLLRERAEKERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKER 448
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 449 QEKEqiaKEKMEKERLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKERSE 528
Cdd:PTZ00121 1517 KAEE---AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 529 RERLEKVRAQKERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERAL 608
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
330 340 350
....*....|....*....|....*....|
gi 2438152838 609 REKMEVEKVNKANGRKPNTSPPRAPPAEEK 638
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
396-623 |
1.32e-04 |
|
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: 44.52 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 396 ERIERERIAKEREKIAKEKERMEKERYERERIATE------RERIAKERMEREKADKERQEKEQIAKEKMEKERLERERI 469
Cdd:pfam13868 42 ERRLDEMMEEERERALEEEEEKEEERKEERKRYRQeleeqiEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 470 AKERERIAKERERA----------EKERLAREKERMERAAREKEEREQM---EGERIARERARIA------QEKERSERE 530
Cdd:pfam13868 122 LEKQRQLREEIDEFneeqaewkelEKEEEREEDERILEYLKEKAEREEEreaEREEIEEEKEREIarlraqQEKAQDEKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 531 RLEKVRAQKERAALEERERAeKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALRE 610
Cdd:pfam13868 202 ERDELRAKLYQEEQERKERQ-KEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEE 280
|
250
....*....|...
gi 2438152838 611 KMEVEKVNKANGR 623
Cdd:pfam13868 281 AEKRRMKRLEHRR 293
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
303-618 |
1.67e-04 |
|
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: 44.96 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 303 EKMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKERER 382
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 383 LERERLLRERAEKERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEKEQIakEKMEKE 462
Cdd:pfam02463 743 QKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA--ELLEEE 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 463 RLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKERSERERLEKVRAQKERA 542
Cdd:pfam02463 821 QLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK 900
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2438152838 543 ALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALREKMEVEKVN 618
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVN 976
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
424-610 |
2.23e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 424 RERIATERERIAKERMEREKADKERQEKEQIAKEKMEKERLERERIAKErERIAKERERAEKERLAREKERMERAAREKE 503
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMRE-ELELEQQRRFEEIRLRKQRLEEERQRQEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 504 EREQMEGERIARERARIAQEKER---------SERERLEKVRAQKERAALEERERAEKERLEKERIERERLKKERLEKEK 574
Cdd:pfam15709 407 ERKQRLQLQAAQERARQQQEEFRrklqelqrkKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEA 486
|
170 180 190
....*....|....*....|....*....|....*.
gi 2438152838 575 SAREQWERQKNEKEREVREKELMERQKLARERALRE 610
Cdd:pfam15709 487 EEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
430-652 |
2.58e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 430 ERERIAKERMER-EKADKERQEKEQIAKEKMEKERLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQM 508
Cdd:COG3064 9 AAEAAAQERLEQaEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 509 EGERIARERARIAQEKERSERERLEKVRAQKERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKE 588
Cdd:COG3064 89 AEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2438152838 589 REVREKELMERQKLARERALREKMEVEKVNKANGRKPNTSPPRAPPAEEKPALRPEEQTSRRGR 652
Cdd:COG3064 169 AAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREA 232
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
416-531 |
2.94e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.56 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 416 RMEKERYERERIATERERIAKERMEREKADKERQEKEQIAKEKMEKERLERERIAKERERIAKERERAEKErlarEKERM 495
Cdd:pfam05672 24 REQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQE----EQERL 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 2438152838 496 ERAAREKEEREQMEGERIARERARIAQEKERSERER 531
Cdd:pfam05672 100 QKQKEEAEAKAREEAERQRQEREKIMQQEEQERLER 135
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
395-631 |
3.53e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 395 KERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEKEQiAKEKMEKERLERERIAKERE 474
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE-AEQRAAELAAEAAKKLAEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 475 RIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKERSERERLEKVRAQKERAALEERERAEKER 554
Cdd:COG3064 84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2438152838 555 LEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALREKMEVEKVNKANGRKPNTSPPR 631
Cdd:COG3064 164 AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
290-619 |
3.69e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 290 KEKAEKERIGKEREKME---KVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIER 366
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAeeaKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 367 ERLVREREREAKERERLERERLLRERAEKERIERERIAKEREKiAKEKERMEKERYERERIATERERIAKERMEREKADK 446
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 447 ERQEKEQIAK-EKMEKERLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKE 525
Cdd:PTZ00121 1602 EEEKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 526 RSERERLEKVRAQKERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARE 605
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH 1761
|
330
....*....|....
gi 2438152838 606 RALREKMEVEKVNK 619
Cdd:PTZ00121 1762 LKKEEEKKAEEIRK 1775
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
313-606 |
6.09e-04 |
|
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: 43.04 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 313 QRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKERERLERERLLRER 392
Cdd:pfam02463 141 GGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 393 AEKERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEKEQIAKEKMEKERLERERIAKE 472
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 473 RERIAKERERAEKERLAREKERMERA----AREKEEREQMEGERIARERARIAQEKERSE-RERLEKVRAQKERAALEER 547
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAekelKKEKEEIEELEKELKELEIKREAEEEEEEElEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2438152838 548 ERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARER 606
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI 439
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
458-584 |
8.01e-04 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 42.80 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 458 KMEKERLERERIAKER-ERIAKERERAEKERLarekERMERAAREKEEREQMEgeriareraRIaqEKERSERERLEKvr 536
Cdd:PTZ00266 429 RVDKDHAERARIEKENaHRKALEMKILEKKRI----ERLEREERERLERERME---------RI--ERERLERERLER-- 491
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2438152838 537 aqkeraaleereraekerlekERIERERLKKERLEK-EKSAREQWERQK 584
Cdd:PTZ00266 492 ---------------------ERLERDRLERDRLDRlERERVDRLERDR 519
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
435-534 |
8.58e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 435 AKERMEREKADKERQE-KEQIAKEKMEKERLERE-------RIAKERERIAKERERAE--KERLAREKERMERAAREKEE 504
Cdd:COG0542 400 ARVRMEIDSKPEELDElERRLEQLEIEKEALKKEqdeasfeRLAELRDELAELEEELEalKARWEAEKELIEEIQELKEE 479
|
90 100 110
....*....|....*....|....*....|
gi 2438152838 505 REQMEGERIARERARIAQEKERSERERLEK 534
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
300-609 |
1.01e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.95 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 300 KEREKMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKE 379
Cdd:COG3064 16 ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 380 RERLERERLLRERAEKERIERERiAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEKEQIAKEKM 459
Cdd:COG3064 96 EKAKAAKEAEAAAAAEKAAAAAE-KEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 460 EKERLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKERSERERLEKVRAQK 539
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 540 ERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALR 609
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAA 324
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
309-644 |
1.03e-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: 42.42 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 309 KAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAkererlererl 388
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREL----------- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 389 lreraekERIERERIAKEREKIAKEKERMEKERY-ERERIATERERIAKERMEREKADKERQEKEQIAKEKMEKERLERE 467
Cdd:pfam17380 351 -------ERIRQEERKRELERIRQEEIAMEISRMrELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 468 RIAKERERIAKERERAEKERLAREKERMERAAREKEER-EQMEGERIARERARIAQEKERSERERLEKVRAQ------KE 540
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilekelEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 541 RAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALREKMEVEKVNKA 620
Cdd:pfam17380 504 RKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVE 583
|
330 340
....*....|....*....|....
gi 2438152838 621 NGRKPNTSPPRAPPAEEKPALRPE 644
Cdd:pfam17380 584 SEKARAEYEATTPITTIKPIYRPR 607
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
301-358 |
1.30e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 42.03 E-value: 1.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2438152838 301 EREKMEKVKAEK-QRMERE--AKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQK 358
Cdd:PTZ00266 464 EREERERLERERmERIERErlERERLERERLERDRLERDRLDRLERERVDRLERDRLEKAR 524
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
297-638 |
2.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 297 RIGKEREKMEKVKAEKQRMEREAK--EKAERERLAHERAEKERQEMEKREKAAREEKErlerqkIERERIERERLVRERE 374
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDAKrvEIARKAEDARKAEEARKAEDAKKAEAARKAEE------VRKAEELRKAEDARKA 1202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 375 REAKERERLERERLLRERAEKERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEKEQI 454
Cdd:PTZ00121 1203 EAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE 1282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 455 AKEKMEKERLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQMEGERiARERARIAQEKERSERERLEK 534
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-AKKAAEAAKAEAEAAADEAEA 1361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 535 VRAQKERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALREKMEV 614
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
330 340
....*....|....*....|....
gi 2438152838 615 EKVNKANGRKPNTSPPRAPPAEEK 638
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKK 1465
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-645 |
2.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 8 DELRMIQEKMEVKRIARIALAEIRALLAKEEEEKEASWALKMKTLEAAQEQLREERRREAERVEKDEKERIEKAEKERME 87
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEE 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 88 NEKVEKERIENEKAEKERIEKEKVEEEKMEREKERMEKEKAEKERMEREKAEKEKIEKEKVEKERMEKEKVEKERMEKEK 167
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 168 AEKERMEKEKVEKERMEKEKAEKERMEKEKERMEKEKAEKERIGKEKERMEKEKAEKERMEKEKVEKERMEKEKAEKERM 247
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA 1376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 248 EKEKERMEKEKAEKERMEKEKERMEKEKAEKERIGKEKERMEKEKAEKERIGKEREKME-KVKAEKQRMEREAKEKAERE 326
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKKKAEEA 1456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 327 RLAHERAEK--ERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKERERLERERLLRERAEKERIERERIA 404
Cdd:PTZ00121 1457 KKAEEAKKKaeEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 405 KEREKIAKEKERMEKERYERERIATERERIAKERMERE-------KADKERQEKEQIAKEKMEKERLERERIAKERERIA 477
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdknmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 478 KERERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKERSERERLEKVRAQKERAALEERERAEKERLEK 557
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 558 ERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALREKMEVEKVNKANGRKPNTSPPRAPPAEE 637
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
....*...
gi 2438152838 638 KPALRPEE 645
Cdd:PTZ00121 1777 KEAVIEEE 1784
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
300-526 |
2.32e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 41.09 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 300 KEREKMEKVK----AEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVRERER 375
Cdd:PRK05035 443 QEKKKAEEAKarfeARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 376 EAKERERLERERLLRERAEKE---------RIERERIAKEREKIAKEKERMEKE-----------RYERERIATERERIA 435
Cdd:PRK05035 523 REARKAQARARQAEKQAAAAAdpkkaavaaAIARAKAKKAAQQAANAEAEEEVDpkkaavaaaiaRAKAKKAAQQAASAE 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 436 KERMEREKADKERQEKEQIAKEKMEKERLERERIAKERERIAKERERAEkerLAREKERMERAAREKEEREQMEGERIAR 515
Cdd:PRK05035 603 PEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAA---IARAKARKAAQQQANAEPEEAEDPKKAA 679
|
250
....*....|.
gi 2438152838 516 ERARIAQEKER 526
Cdd:PRK05035 680 VAAAIARAKAK 690
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
273-619 |
3.25e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 273 KEKAEKERIGKEKERMEKEKAEKERIGKEREKMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKE 352
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 353 RLERQKIERERIERERLVREREREAKERERLERERLLRERAEKERIERERIAKEREKIAKEKERMEKERYERERIATERE 432
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 433 RIAKERMER-EKADKERQEKEQIAKEKMEKERLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQMEGE 511
Cdd:PTZ00121 1616 EEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALK 1695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 512 RIARERARIAQEKERSERERLEKVRAQKERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREV 591
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
330 340
....*....|....*....|....*...
gi 2438152838 592 REKELMERQklARERALREKMEVEKVNK 619
Cdd:PTZ00121 1776 EKEAVIEEE--LDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
302-542 |
3.73e-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: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 302 REKMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKERE 381
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 382 RLERERLLRERAEKERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEKEQIAKEKMEK 461
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 462 ERLERERIAKERERIAKERERAEKERLAREKE----RMERAAREKEEREQMEGERIARERARIAQEKERSERERLEKVRA 537
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
....*
gi 2438152838 538 QKERA 542
Cdd:TIGR02168 478 DAAER 482
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
401-501 |
5.10e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 39.83 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 401 ERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERqeKEQIAKEKMEKERLERERIAKEREriaKER 480
Cdd:PRK00247 289 EQRAQYREKQKEKKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKTR--TAEKNEAKARKKEIAQKRRAAERE---INR 363
|
90 100
....*....|....*....|.
gi 2438152838 481 ERAEKERLAREKERMERAARE 501
Cdd:PRK00247 364 EARQERAAAMARARARRAAVK 384
|
|
| PLN03086 |
PLN03086 |
PRLI-interacting factor K; Provisional |
438-509 |
6.09e-03 |
|
PRLI-interacting factor K; Provisional
Pssm-ID: 178635 [Multi-domain] Cd Length: 567 Bit Score: 39.86 E-value: 6.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2438152838 438 RMEREKADKERQEKEQIAKEKMEKERLERERIAKERERIakerERAEKERlarekeRMERAAREKEEREQME 509
Cdd:PLN03086 6 RRAREKLEREQRERKQRAKLKLERERKAKEEAAKQREAI----EAAQRSR------RLDAIEAQIKADQQMQ 67
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
395-541 |
6.73e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 39.50 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 395 KERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMEREKADKERQEKEQIAKEKMEKERLERERIAKERE 474
Cdd:PRK12678 83 AAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAE 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2438152838 475 RIAKER--ERAEKERLAREKERMERAAREKEEREQMEGERIARERARIAQEKERSERERLEKVRAQKER 541
Cdd:PRK12678 163 RTEEEErdERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRR 231
|
|
| PTZ00266 |
PTZ00266 |
NIMA-related protein kinase; Provisional |
304-421 |
7.48e-03 |
|
NIMA-related protein kinase; Provisional
Pssm-ID: 173502 [Multi-domain] Cd Length: 1021 Bit Score: 39.72 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 304 KMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIEReriererlvrerereakererl 383
Cdd:PTZ00266 429 RVDKDHAERARIEKENAHRKALEMKILEKKRIERLEREERERLERERMERIERERLER---------------------- 486
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2438152838 384 erERLLRERAEKERIERERIAK-EREKIAK-EKERMEKER 421
Cdd:PTZ00266 487 --ERLERERLERDRLERDRLDRlERERVDRlERDRLEKAR 524
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
300-621 |
7.64e-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: 39.57 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 300 KEREKMEKVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKE 379
Cdd:pfam02463 714 KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 380 RERLERERLLRERAEKERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERMERekadKERQEKEQIAKEKM 459
Cdd:pfam02463 794 EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEE----LERLEEEITKEELL 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 460 EKERLERERIAKERERIAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERArIAQEKERSERERLEKVRAQK 539
Cdd:pfam02463 870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE-ILLKYEEEPEELLLEEADEK 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 540 ERAALEERERAEKERLEKERIERERLKKERLEKEKSAREQWERQKNEKEREVREKELMERQKLARERALREKMEVEKVNK 619
Cdd:pfam02463 949 EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVS 1028
|
..
gi 2438152838 620 AN 621
Cdd:pfam02463 1029 IN 1030
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
396-520 |
8.28e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 37.34 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 396 ERIERERIAKEREKIAKEKERMEKERYERERIATERERiaKERMEREKADKERQEKEQIAKEKMEKERLerERIAKERER 475
Cdd:pfam15346 17 EEAVAKRVEEELEKRKDEIEAEVERRVEEARKIMEKQV--LEELEREREAELEEERRKEEEERKKREEL--ERILEENNR 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2438152838 476 IAKERERAEKERLAREKERMERAAREKEEREQMEGERIARERARI 520
Cdd:pfam15346 93 KIEEAQRKEAEERLAMLEEQRRMKEERQRREKEEEEREKREQQKI 137
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
442-574 |
8.73e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 37.33 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 442 EKADKERQEKEQIAKEkmEKERLERERIAKERERIAKEREraEKERLAREKERMERAAREKEEREQMEGERIARERARIA 521
Cdd:pfam05672 10 EEAARILAEKRRQARE--QREREEQERLEKEEEERLRKEE--LRRRAEEERARREEEARRLEEERRREEEERQRKAEEEA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2438152838 522 QEKERSERERLEKVRAQKERAALEERERAEKERLEKERIeRERLKKERLEKEK 574
Cdd:pfam05672 86 EEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKI-MQQEEQERLERKK 137
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
307-519 |
8.74e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 38.67 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 307 KVKAEKQRMEREAKEKAERERLAHERAEKERQEMEKREKAAREEKERLERQKIERERIERERLVREREREAKERERLERE 386
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2438152838 387 RLLRERAEKERIERERIAKEREKIAKEKERMEKERYERERIATERERIAKERmEREKADKERQEKEQIAKEKMEKERLER 466
Cdd:TIGR02794 127 KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKA 205
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170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2438152838 467 ERIAKERERIAKER-ERAEKERLAREKERMERAAREKEEREQMEGERIARERAR 519
Cdd:TIGR02794 206 AAEAAAKAEAEAAAaAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGS 259
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