|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-444 |
4.25e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.02 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 193 KKADRYIEELTKERDALSLELYRNTITNEELKK-KNAELQEKLRLAESEKSEIQLNVKELKRKLERAKfllpQVQTNTLQ 271
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKaEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK----KAEEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 272 EEmwrQEEELREQEKKIRKQEEKMWRQEERLREQEGKMR------EQEEKMRRQEKRLREQEKELREQEKELREQKKLRE 345
Cdd:PTZ00121 1573 EE---DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 346 QEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEK 425
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
250
....*....|....*....
gi 749385072 426 MREEKKMQEQEKKTRDQEE 444
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEE 1748
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-478 |
8.13e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 8.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 193 KKADRYIEeLTKERDALSLELYRNTItnEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLE--RAKFLLPQVQTNTL 270
Cdd:COG1196 210 EKAERYRE-LKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEelRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 271 QEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQM 350
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 351 QEqeekmwEQEEKMREQEEkmwrQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEK 430
Cdd:COG1196 367 LL------EAEAELAEAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 749385072 431 KMQEQEKKTRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEE 478
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-533 |
8.96e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 221 EELKKKNAELQEKlrlAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEE 300
Cdd:PTZ00121 1493 EEAKKKADEAKKA---AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 301 RLREQEGKMREQE-EKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLW 379
Cdd:PTZ00121 1570 KKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 380 EQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEEKMQEEERIREREKKM 459
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749385072 460 REEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKlweQEKMQEQEEKIWEQEEKIRDQEEMWGQEKKM 533
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK---AEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
204-447 |
1.03e-11 |
|
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: 69.00 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 204 KERDALSLELYRNTITNEELKKKNAEL-QEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQEEmwrqeeELR 282
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRELERIrQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE------ERQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 283 EQEKKIRKQEEKMWRQEERLREQEgkMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQeekmwEQEE 362
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQRE--VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK-----EKRD 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 363 KMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEkMREEKKMQEQEKKTRDQ 442
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE-MEERRRIQEQMRKATEE 564
|
....*
gi 749385072 443 EEKMQ 447
Cdd:pfam17380 565 RSRLE 569
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-544 |
1.17e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 193 KKADRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQE 272
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 273 EMWRQEEELREQEKKIRKQEEKmwRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQE 352
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEK--KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 353 QEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREE--K 430
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeaK 1681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 431 KMQEQEKKtrdQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEEnmWEQEEKEWQQQRLPEQKEKLWEQEKMQEQE 510
Cdd:PTZ00121 1682 KAEEDEKK---AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE--ENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
330 340 350
....*....|....*....|....*....|....
gi 749385072 511 EKIWEQEEKIRDQEEMWGQEKKMWRQEKMREQED 544
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-545 |
2.97e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 221 EELKKKNAELQEKLRLaeSEKSEIQLNVKELKRKLERAKfllpQVQTNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEE 300
Cdd:PTZ00121 1408 DELKKAAAAKKKADEA--KKKAEEKKKADEAKKKAEEAK----KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 301 RLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLWE 380
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 381 QEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEEKMQEEERIREREKKMR 460
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 461 EEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEKIWEQEEKIRDQEEMWGQEKKMWRQ-EKM 539
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaEEL 1721
|
....*.
gi 749385072 540 REQEDV 545
Cdd:PTZ00121 1722 KKAEEE 1727
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-619 |
7.28e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 221 EELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLE---RAKFLLPQVQTNTLQEEMWRQEEELREQEKKIRKQEEKMWR 297
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 298 QEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMRE----QEEKMWR 373
Cdd:PTZ00121 1433 ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkaAEAKKKA 1512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 374 QEERLWEQEK---QMREQEQKMRDQEERMWEQderlREKEERMREQEKMWEQVEKMREEKKMQEQEKKT---RDQEEKMQ 447
Cdd:PTZ00121 1513 DEAKKAEEAKkadEAKKAEEAKKADEAKKAEE----KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNmalRKAEEAKK 1588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 448 EEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEKIWEQEEKIRDQEEMW 527
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 528 GQEKKMWRQEKMREQEDVETGGEAAGAGEADVGAGGEDAGSGAEDVGPGGEDVGAGREAAGEGGENAGAEEDvaaggEDA 607
Cdd:PTZ00121 1669 KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE-----EDK 1743
|
410
....*....|..
gi 749385072 608 GGEEDAGAGEED 619
Cdd:PTZ00121 1744 KKAEEAKKDEEE 1755
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-546 |
9.15e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 221 EELKKKNAELQEKLRLaeSEKSEIQLNVKELKRKLERAKF---LLPQVQTNTLQEEMWRQEEELREQEKKIRKQEEKmwR 297
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEA--KKKAEEAKKADEAKKKAEEAKKadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA--K 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 298 QEERLREQEGKmREQEEKMRRQEKR----LREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWR 373
Cdd:PTZ00121 1523 KADEAKKAEEA-KKADEAKKAEEKKkadeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 374 QEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQE-KMWEQVEKMREEKKMQEQEKKTRDQEEKMQEEERI 452
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEkKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 453 REREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEKIWEQEEKIRDQEEmwgqEKK 532
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE----EKK 1757
|
330
....*....|....
gi 749385072 533 MWRQEKMREQEDVE 546
Cdd:PTZ00121 1758 KIAHLKKEEEKKAE 1771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-446 |
9.39e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 199 IEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAkfllpQVQTNTLQEEMWRQE 278
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL-----EAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 279 EELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQK-KLREQEEQMQEQEEKM 357
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 358 WEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEK-MWEQVEKMRE-EKKMQEQ 435
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSeLEELSEELRElESKRSEL 913
|
250
....*....|.
gi 749385072 436 EKKTRDQEEKM 446
Cdd:TIGR02168 914 RRELEELREKL 924
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-628 |
1.07e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 197 RYIEELTKERDALSLELYRNTITNEELKKKNAE----LQEKLRLAESEKSEIQLNVKELKRKLERAKF---LLPQVQTNT 269
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAK 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 270 LQEEMWRQEEELREQEKKIRKQEEKMWRQE----------ERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELRE 339
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEaeaaeekaeaAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 340 QKKLREQEEQMQEQEEKMWEQ----EEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMRE 415
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEkkkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 416 QEKMWEQVEKMREEKKMQEqEKKTRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPE 495
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE 1567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 496 QKEKLWEQEKMQEQEEKIWEQEEKIRDQEEM-WGQEKKMWRQEKMREQEDVETGGEAAGAGEADVGAGGEDAGSGAEDVG 574
Cdd:PTZ00121 1568 EAKKAEEDKNMALRKAEEAKKAEEARIEEVMkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 749385072 575 PGGEDVGAGREAAGEGGENA-GAEEDVAAGGEDAGGEEDAGAGEEDMGPGGEDAR 628
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAkKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
194-544 |
5.75e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 194 KADRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTntlQEE 273
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK---ADE 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 274 MWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQ 353
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 354 EEKMWE----QEEKMREQEEKMWRQEERLWEQEK----QMREQEQKMRDQEERMWEQ----DERLREKEERMREQEKMWE 421
Cdd:PTZ00121 1476 KKKAEEakkaDEAKKKAEEAKKKADEAKKAAEAKkkadEAKKAEEAKKADEAKKAEEakkaDEAKKAEEKKKADELKKAE 1555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 422 QVEKMREEKKMQEQEKKTRDQ------------------EEKMQEEERIREREKKMREEEETMREQEEKMQKQEE---NM 480
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKnmalrkaeeakkaeeariEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkKV 1635
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749385072 481 WEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEKIWEQEEKIRDQEEMWGQEKKMWRQEKMREQED 544
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-436 |
1.52e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 178 AGELQRALSAVSTWHKKADRYIEeLTKERDALSLELYRNTItnEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLER 257
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKE-LKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 258 AKfllpqVQTNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKEL 337
Cdd:TIGR02168 272 LR-----LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 338 RE-QKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLweqeKQMREQEQKMRDQEERMWEQDERLREKEERMREQ 416
Cdd:TIGR02168 347 EElKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV----AQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
|
250 260
....*....|....*....|
gi 749385072 417 EkmwEQVEKMREEKKMQEQE 436
Cdd:TIGR02168 423 I---EELLKKLEEAELKELQ 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
297-790 |
1.58e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 297 RQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREqkkLREQEEQMQEQEEKMWEQEEKMREQ----EEKMW 372
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE---LELELEEAQAEEYELLAELARLEQDiarlEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 373 RQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEEKMQEEERI 452
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 453 REREKKMREEEETMREQEEKMQKQE--ENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEKIWEQEEKIRDQEEMWGQE 530
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLErlEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 531 KKMWRQEKMREQEDVETGGEAAGAGEADVGAGGEDAGSGAEDVGPGGEDV-GAGREAAGEGGENAGAEEDVAAGGEDAGG 609
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLaGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 610 EEDAGAGEEdmgpgGEDARGGEDAGAGEEDAGGGGDDAGAGGEDAGAGREDAGAGGEDVGAGREDAGAGGEDVGAGGEDV 689
Cdd:COG1196 553 VEDDEVAAA-----AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 690 GAGRRRCGssrgcrnRRRSCGNTRRCRSRRSGAEDVGPEGEDVGAGREAAGEGGENAGAEDVAAGGEDAGEEEDAGGEDA 769
Cdd:COG1196 628 VAARLEAA-------LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500
....*....|....*....|.
gi 749385072 770 GAAREDAGAGGDDVGAGREDA 790
Cdd:COG1196 701 AEEEEERELAEAEEERLEEEL 721
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-445 |
3.55e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 193 KKADRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRlaesEKSEIQLNVKELKRKLERAKfllpqvqtntlqe 272
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLR----EINEISSELPELREELEKLE------------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 273 emwrqeeelrEQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQE 352
Cdd:PRK03918 228 ----------KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 353 QEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKmrdqEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKM 432
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
250
....*....|...
gi 749385072 433 QEQEKKTRDQEEK 445
Cdd:PRK03918 374 LERLKKRLTGLTP 386
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
194-525 |
4.12e-09 |
|
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: 60.76 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 194 KADRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLlpQVQTNTLQEE 273
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN--EERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 274 MWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELR-EQEKELREQKKLREQEEQMQE 352
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLkLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 353 QEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKM 432
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 433 QEQEKKTRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEK 512
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330
....*....|...
gi 749385072 513 IWEQEEKIRDQEE 525
Cdd:pfam02463 486 LELLLSRQKLEER 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-628 |
1.42e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 221 EELKKKNAEL----QEKLRLAESEKSEIQLNVKELKRKLERAKFL-LPQVQTNTLQEEMWRQEEELREQEKKIRKQEEKM 295
Cdd:PTZ00121 1325 EEAKKKADAAkkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 296 WRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKmweQEEKMREQEEKMWRQE 375
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEE 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 376 ERLWEQEKQMREQEQKMRDQeermweqderLREKEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEEKMQEEERIRER 455
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADE----------AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 456 EKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRLpeQKEKLWEQEKMQEQEEKIWEQEEKIRDQEEMWGQEKKMWR 535
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 536 QEKMREQEDVETGGEAAGAGEADVGAGGEDAGSGAEDVGPGGEDVGAGREAAGEGGENAGAEEDVAAGGEDAGGEEDAGA 615
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
410
....*....|...
gi 749385072 616 GEEDMGPGGEDAR 628
Cdd:PTZ00121 1710 KEAEEKKKAEELK 1722
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-444 |
1.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 199 IEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQlnvKELKRKLERAKFLLPQVQTNTLQEEMWRQE 278
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE---QDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 279 eelreqekkIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELRE--QKKLREQEEQMQEQEek 356
Cdd:COG1196 332 ---------LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEElaEELLEALRAAAELAA-- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 357 mwEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQE 436
Cdd:COG1196 401 --QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
....*...
gi 749385072 437 KKTRDQEE 444
Cdd:COG1196 479 LAELLEEL 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-443 |
1.79e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 199 IEELTKERDALSLELyrntitnEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQT--NTLQEEMWR 276
Cdd:TIGR02169 683 LEGLKRELSSLQSEL-------RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 277 QEEELREQEKKIRKQEEKMWRQE------------ERLREQEGKMREQEEKMRRQEKRLREQEKEL--REQEKELREQKK 342
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEealndlearlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLnrLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 343 lreqeeqmQEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQ 422
Cdd:TIGR02169 836 --------QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260
....*....|....*....|.
gi 749385072 423 VEKMREEKKMQEQEKKTRDQE 443
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEA 928
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
261-542 |
6.47e-08 |
|
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: 56.67 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 261 LLPQVQTNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQ 340
Cdd:pfam17380 274 LLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 341 KKLREQEEQMQEQEEKMWEQEEKMREQEE-KMWRQEERlwEQEKQMREQEQKMRDQE-ERMWEQDERLREKEERMREQEK 418
Cdd:pfam17380 354 RQEERKRELERIRQEEIAMEISRMRELERlQMERQQKN--ERVRQELEAARKVKILEeERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 419 MWEQVEKMREEKKMQEQEKKTRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQR---LPE 495
Cdd:pfam17380 432 ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqamIEE 511
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 749385072 496 QKEKLWEQEKMQEQEEKIWEQEEKiRDQEEMWGQEKKMWRQEKMREQ 542
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAIYEEERR-REAEEERRKQQEMEERRRIQEQ 557
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-544 |
8.13e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 197 RYIEELTKERDALSLELYRNTitnEELKKKnaelQEKLRLAESEKSEIQLNVKELKRKLERAKFLLP-----QVQTNTLQ 271
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKKA---EEAKKD----AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAikaeeARKADELK 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 272 EEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQE-KRLREQEKELREQEKELREQKKLREQEEQM 350
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAaKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 351 QEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQD---ERLREKEERMR---------EQEK 418
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKkkaDEAKKKAEEKKkadeakkkaEEAK 1444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 419 MWEQVEKMREEKKMQEQ-----EKKTRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRL 493
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEakkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 749385072 494 PEQKEKLWEQEKMQEQEEKIWEQEEKIRDQEEMWGQEKKMWRQEKMREQED 544
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-479 |
8.33e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 197 RYIEELTKERDALSLELYRNTITNEELKKKNAEL------QEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTL 270
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeeEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 271 QEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQM 350
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 351 QEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKmrdqeERMWEQDERLREKEERMREQEKMWEQVEKMREEK 430
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK-----EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 749385072 431 KMQEQEKKTRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEEN 479
Cdd:PTZ00121 1799 KIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEAD 1847
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
195-546 |
2.37e-07 |
|
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: 54.98 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 195 ADRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNtLQEEM 274
Cdd:pfam02463 602 ILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL-LEIQE 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 275 WRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMrrQEKRLREQEKELREQEKELREQKKLREQEEQMQEQE 354
Cdd:pfam02463 681 LQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL--LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 355 EKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKmqe 434
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEEL--- 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 435 QEKKTRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEKIW 514
Cdd:pfam02463 836 EELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEK 915
|
330 340 350
....*....|....*....|....*....|..
gi 749385072 515 EQEEKIRDQEEMWGQEKKMWRQEKMREQEDVE 546
Cdd:pfam02463 916 ENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
199-430 |
3.12e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 199 IEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQEEmwrqe 278
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE----- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 279 eelrEQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLrEQEKELREQEKELREQKKLREQeeqmqeqeekmw 358
Cdd:COG1196 372 ----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELE------------ 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749385072 359 EQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEK 430
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
224-545 |
5.47e-07 |
|
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: 53.59 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 224 KKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEERLR 303
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 304 EQEgKMREQEEKMrrQEKRLREQEKELREqekelREQKKLREQEEQMQEQEEKMWEqEEKMREQEEKMWRQEERLWEQEK 383
Cdd:pfam17380 361 ELE-RIRQEEIAM--EISRMRELERLQME-----RQQKNERVRQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 384 QMREQEQKMRDQEERmweQDERLREKEERMREQEKMWEQVEKMREEKKMqEQEKKTRDQEEKMQEEERIREREKKMREEE 463
Cdd:pfam17380 432 ARQREVRRLEEERAR---EMERVRLEEQERQQQVERLRQQEEERKRKKL-ELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 464 ETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKlweqeKMQeqeekiwEQEEKIRDQEEMWGQEKKMWRQEKMREQE 543
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERR-----KQQ-------EMEERRRIQEQMRKATEERSRLEAMERER 575
|
..
gi 749385072 544 DV 545
Cdd:pfam17380 576 EM 577
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
196-434 |
1.88e-06 |
|
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: 51.90 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 196 DRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQEEMW 275
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 276 RQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQ---EKELREQEKELREQKKLREQEEQMQE 352
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNlleEKENEIEERIKEEAEILLKYEEEPEE 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 353 QEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKM 432
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
..
gi 749385072 433 QE 434
Cdd:pfam02463 1020 KE 1021
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
198-479 |
3.74e-06 |
|
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: 51.13 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 198 YIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQEEmwrq 277
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE---- 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 278 eeeLReqeKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKM 357
Cdd:pfam02463 792 ---KE---EKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 358 WEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQEK 437
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 749385072 438 KTRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEEN 479
Cdd:pfam02463 946 DEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKE 987
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
196-342 |
7.17e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 196 DRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTN----TLQ 271
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyeALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749385072 272 EEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKK 342
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
249-452 |
7.23e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 249 KELKRKLERAkfllpQVQTNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEK 328
Cdd:COG4942 23 AEAEAELEQL-----QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 329 ELREQEKELREQkkLREQEEQMQEQEEKMWEQEEK--------------MREQEEKMWRQEERLWEQEKQMREQEQKMRD 394
Cdd:COG4942 98 ELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749385072 395 QEERMWEQDERLREKEERMREQEKMWEQVEKMREE-----KKMQEQEKKTRDQEEKMQEEERI 452
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAElaaelAELQQEAEELEALIARLEAEAAA 238
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
221-546 |
8.51e-06 |
|
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: 49.97 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 221 EELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEE 300
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 301 RLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLWE 380
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 381 QEKQMREQEQKMRDQEERMWEQDErlREKEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEEKMQEEERIREREKKMR 460
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEE--EEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 461 EEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEKIWEQEEKIRDQEEMWGQEKKMWRQEKMR 540
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
....*.
gi 749385072 541 EQEDVE 546
Cdd:pfam02463 490 LSRQKL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-447 |
1.55e-05 |
|
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: 48.90 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 288 IRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQ------- 360
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQlskelte 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 361 -EEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMRE---------QEKMWEQVEKMREEK 430
Cdd:TIGR02168 759 lEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlrERLESLERRIAATER 838
|
170
....*....|....*..
gi 749385072 431 KMQEQEKKTRDQEEKMQ 447
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIE 855
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
359-443 |
1.70e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 47.57 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 359 EQEEKMREQEEKMWRQEERLWEQEKQMREQ-EQKMRDQEERMWEQDERLREKEERMREQ---EKMWEQVEKMREEKKMQE 434
Cdd:cd16269 194 TEKEKEIEAERAKAEAAEQERKLLEEQQRElEQKLEDQERSYEEHLRQLKEKMEEERENllkEQERALESKLKEQEALLE 273
|
....*....
gi 749385072 435 QEKKTRDQE 443
Cdd:cd16269 274 EGFKEQAEL 282
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
310-422 |
2.16e-05 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 46.62 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 310 REQEEKMRRQEKRLREQEKELREQEKELR-----EQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERL-----W 379
Cdd:pfam13904 68 RQKELQAQKEEREKEEQEAELRKRLAKEKyqewlQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKevlqeW 147
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 749385072 380 EQEKQMREQEQKMRDQEERMWEQderlREKEERMREQEKMWEQ 422
Cdd:pfam13904 148 ERKKLEQQQRKREEEQREQLKKE----EEEQERKQLAEKAWQK 186
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
326-429 |
2.93e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 46.80 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 326 QEKELREQEKELREQKKlreqeeQMQEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDER 405
Cdd:cd16269 189 ADQALTEKEKEIEAERA------KAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEERENLLKEQERALE 262
|
90 100
....*....|....*....|....
gi 749385072 406 LREKEERMREQEKMWEQVEKMREE 429
Cdd:cd16269 263 SKLKEQEALLEEGFKEQAELLQEE 286
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
292-619 |
3.62e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 292 EEKMWRQEERLREQEGKMREQ---EEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQE 368
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEArkaEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 369 EKMWRQEERLWEQEK---QMREQEQKMRDQEERMWEQDERLRE----KEERMREQEKMWEQVEKMREEKKMQEQEKKtrD 441
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRkaeELRKAEDARKAEAARKAEEERKAEEarkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERN--N 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 442 QEEKMQEEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEKIWEQEEKIR 521
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 522 DQEEMWGQEKKMWRQEKMREQEDVETGGEAAGAGEADVGAGGEDAGSGAEDVGPGGEDVGAGREAAGEGGENAGAEEDVA 601
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
330
....*....|....*...
gi 749385072 602 AGGEDAGGEEDAGAGEED 619
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEE 1429
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
222-398 |
3.90e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 222 ELKKKNAE------LQEKLRLAESEKSEIQLNVKE----LKRKLERakfllpqvqtntlqeemwrqeeelreqekKIRKQ 291
Cdd:PRK12704 30 EAKIKEAEeeakriLEEAKKEAEAIKKEALLEAKEeihkLRNEFEK-----------------------------ELRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 292 EEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKlreqeeqmqeqeekmwEQEEKMREQEEKM 371
Cdd:PRK12704 81 RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEE----------------ELEELIEEQLQEL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 749385072 372 WR-----QEE---RLWEQ-EKQMREQEQKM-RDQEER 398
Cdd:PRK12704 145 ERisgltAEEakeILLEKvEEEARHEAAVLiKEIEEE 181
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
221-438 |
6.03e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 221 EELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQT--NTLQEEMWRQEEELREQEKKIRKQEEKMWRQ 298
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 299 EERLRE------------QEGKMREQEEKMRRQEKRLREQEKELREQEK---ELREQ-KKLREQEEQMQEQEEKMWEQEE 362
Cdd:TIGR04523 287 EKQLNQlkseisdlnnqkEQDWNKELKSELKNQEKKLEEIQNQISQNNKiisQLNEQiSQLKKELTNSESENSEKQRELE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 363 KMREQEEKMWRQEERLWEQ----EKQMREQEQKMRDQEERMWEQDERLREKEErmrEQEKMWEQVEKMREEKKMQEQEKK 438
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEiknlESQINDLESKIQNQEKLNQQKDEQIKKLQQ---EKELLEKEIERLKETIIKNNSEIK 443
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-447 |
6.24e-05 |
|
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: 46.98 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 158 SLIPGESKDLAGRLHHSWHFAGELQRALSAVSTWHKKADRYIEELTKERDALSLELyrNTITNEELKKKNAELQEKLRLA 237
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 238 ESEKSEIQLNVKELKRKLERAKFLLPQvqtntLQEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMR 317
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEY-----LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 318 RQEKRLREQEKELREQEKELREQKKlreqeeQMQEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQkmrDQEE 397
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELER------KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE---IPEE 949
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 749385072 398 RMWEQD--ERLREKEERMREQEKMweqveKMREEKKMQEQEKKTRDQEEKMQ 447
Cdd:TIGR02169 950 ELSLEDvqAELQRVEEEIRALEPV-----NMLAIQEYEEVLKRLDELKEKRA 996
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
540-730 |
6.87e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.82 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 540 REQEDVETGGEAAGAGEADVGAGGEDAGSGAEDVGPGGEDVGAGREAAGEGGENAGAEEDVAAGGEDAGGEEDAGAGEED 619
Cdd:PRK12678 95 AEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 620 ----MGPGGEDARGGEDAGAGEEDAGGGGDDAGAGGEDAGAGREDAGAGGEDVGAGREDAGAGGEDVGAGGEDVGAGRRR 695
Cdd:PRK12678 175 rgdrEDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDD 254
|
170 180 190
....*....|....*....|....*....|....*
gi 749385072 696 CGSSRGCRNRRrscGNTRRCRSRRSGAEDVGPEGE 730
Cdd:PRK12678 255 GEGRGGRRGRR---FRDRDRRGRRGGDGGNEREPE 286
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
193-436 |
8.70e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 193 KKADRYIEELTKERDALSLELyrnTITNEELKKKNaELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQE 272
Cdd:PRK03918 521 EKKAEEYEKLKEKLIKLKGEI---KSLKKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 273 EmwrqeeelreqekkirkqeEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKlREQEEQMQE 352
Cdd:PRK03918 597 L-------------------EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK-ELEELEKKY 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 353 QEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKM 432
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
|
....
gi 749385072 433 QEQE 436
Cdd:PRK03918 737 LKER 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
221-431 |
8.84e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 221 EELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLpqvqtNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEE 300
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 301 RLREQEGKM--------------REQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQmqeqeekmwEQEEKMRE 366
Cdd:COG4942 105 ELAELLRALyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---------ELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749385072 367 QEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKK 431
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-444 |
9.80e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 180 ELQRALSAVSTWHKKADRY------IEELTKERDALSLELYRNTItnEELKKKNAELQEKLRLAESEKSEIQLNVKELKR 253
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAkakkeeLERLKKRLTGLTPEKLEKEL--EELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 254 ---KLERAKFLLPqVQTNTLQEEmwrqeeelreqekkirkqeekmwRQEERLREQEGKMREQEEKMRRQEKRLREQEKEL 330
Cdd:PRK03918 427 aieELKKAKGKCP-VCGRELTEE-----------------------HRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 331 REQEKELREQKKLReqeeqmqeQEEKMWEQEEKMREQEEKMWRQE-ERLWEQEKQMREQEQKMRDQEERMWEQDERLREK 409
Cdd:PRK03918 483 RELEKVLKKESELI--------KLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
250 260 270
....*....|....*....|....*....|....*
gi 749385072 410 EERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEE 444
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGFESVEE 589
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
223-497 |
1.00e-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: 46.20 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 223 LKKKNAELQEKLRLAESEKSEIQLNVKELKRKL----------ERAKFL----------LPQVQTNTLQEEMWRQEEELR 282
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLkslerqaekaERYKELkaelrelelaLLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 283 EQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQK-KLREQEEQMQEQEEKMWEQE 361
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILReRLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 362 EKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERM-----------REQEKMWEQVEKMREEK 430
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrskvaqleLQIASLNNEIERLEARL 409
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749385072 431 KMQEQEKKTRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQK 497
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-617 |
1.26e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 197 RYIEELTKERDALSLElyrntitnEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKfllpqvqtntlQEEMWR 276
Cdd:PTZ00121 1128 RKAEEARKAEDARKAE--------EARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR-----------KAEEVR 1188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 277 QEEELrEQEKKIRKQEEKMWRQEERLREQEGKMREQ---EEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQ 353
Cdd:PTZ00121 1189 KAEEL-RKAEDARKAEAARKAEEERKAEEARKAEDAkkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 354 EEKMWEQEEKMREQEekmWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQ 433
Cdd:PTZ00121 1268 RQAAIKAEEARKADE---LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 434 EQEKKtRDQEEKMQEEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEKI 513
Cdd:PTZ00121 1345 AEAAK-AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 514 WEQEEKIRDQEEMWGQEKKMWRQEKMREQEDvETGGEAAGAGEADVGAGGEDAGSGAEDVGPGGEDVGAGREAAGEGGEN 593
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
410 420
....*....|....*....|....
gi 749385072 594 AGAEEDVAAGGEDAGGEEDAGAGE 617
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADE 1526
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
366-445 |
1.36e-04 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 44.91 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 366 EQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERlREKEERM-----REQ-EKMWEQVEKMREEK-KMQEQEKK 438
Cdd:pfam15991 5 KMSEQMWRALKRHIMRERERKKQEQEAKMEEERLRREREE-REKEDRMtleetKEQiLKLEKKLADLKEEKhQLFLQLKK 83
|
....*..
gi 749385072 439 TRDQEEK 445
Cdd:pfam15991 84 VLHEDET 90
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-343 |
1.45e-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: 45.82 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 199 IEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQ---TNTLQEEMW 275
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEE 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749385072 276 RQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKL 343
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
577-796 |
1.53e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 45.76 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 577 GEDVGAGREAAGEGGENAGAEEDVAAGGEDAGGEEDAGAGEEDmgpggedaRGGEDAGAGEEDAGGGGDDAGAGGEDAGA 656
Cdd:TIGR00927 646 GEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIPAE--------RKGEQEGEGEIEAKEADHKGETEAEEVEH 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 657 GREDAGAGGEDVGAGreDAGAGGEDVGAGGEdvgagrrrcGSSRGCRNRRRSCGNTRRCRSRRSGAEDVGPEGEdvgaGR 736
Cdd:TIGR00927 718 EGETEAEGTEDEGEI--ETGEEGEEVEDEGE---------GEAEGKHEVETEGDRKETEHEGETEAEGKEDEDE----GE 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 737 EAAGEGGENAGaEDVAAGGEDAGEEEDAGGEDAGAAREDAGAGGDDVGAGREDAGAGGED 796
Cdd:TIGR00927 783 IQAGEDGEMKG-DEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAEN 841
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
297-445 |
1.67e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 297 RQEERLREQEGKMREQEEKmRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMwrqeE 376
Cdd:COG4717 75 ELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL----E 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749385072 377 RLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQekMWEQVEKMREEKKMQEQEKKTRDQEEK 445
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA--TEEELQDLAEELEELQQRLAELEEELE 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-405 |
1.87e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 180 ELQRALSAVSTWHKKADRYIEELTKERDALSLELyrntitnEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAK 259
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQL-------AALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 260 FLLpQVQTNTLQEEMWRQEEELREQEKKI---RKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKE 336
Cdd:COG4942 97 AEL-EAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749385072 337 LREQKKlrEQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDER 405
Cdd:COG4942 176 LEALLA--ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
301-444 |
2.15e-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: 45.06 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 301 RLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQ-EEKMWRQEERLW 379
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQlEQEEEKLKERLE 740
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749385072 380 EQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEE 444
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEE 805
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
299-444 |
2.17e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 299 EERLREQEGKM-REQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMwEQEEKMREQEEKMWRQEER 377
Cdd:COG4717 48 LERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-EAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749385072 378 LWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEE 444
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
316-434 |
2.33e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 316 MRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMwEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQ 395
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERN-QQRQEARREREELQREEERLVQKEEQLDARAEKLDNL 103
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 749385072 396 EERMWEQDERLREKEERMREQEKMWE----QVEKMREEKKMQE 434
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDnelyRVAGLTPEQARKL 146
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
289-438 |
2.37e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 44.64 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 289 RKQEEKMWRQEERLREQEGKMREQEEKmrrqeKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQE 368
Cdd:pfam15558 26 LQQQAALAWEELRRRDQKRQETLERER-----RLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749385072 369 EKMWRQEERLWEQEKQmrEQEQKMRDQEERMWEQDERLREKEERMREQ-EKMWEQVEKMREEKKMQEQEKK 438
Cdd:pfam15558 101 EDQENQRQEKLERARQ--EAEQRKQCQEQRLKEKEEELQALREQNSLQlQERLEEACHKRQLKEREEQKKV 169
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
73-415 |
4.42e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 73 QQNRAQLKEEKKASHQHQEALRREIEAQDHTIRILTCQKTEL--ETALYYSQDAARKFEDGNLGTPSSFNLALSQAFRGS 150
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELleEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 151 PLGCVSTSLIPGESK-DLAGRLHHSWHFAGE-------LQRALSAVSTWHKKADRYIEELTKERDALSLELYRNTITNEE 222
Cdd:COG1196 507 LEGVKAALLLAGLRGlAGAVAVLIGVEAAYEaaleaalAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 223 LKKKNAELQEKLRLAESEKSEiqlnvkELKRKLERAKFLLPQVQTNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEERL 302
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASD------LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 303 REQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEE-----KMREQEEKMWRQEER 377
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEleeeaLEEQLEAEREELLEE 740
|
330 340 350
....*....|....*....|....*....|....*...
gi 749385072 378 LWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMRE 415
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
564-788 |
5.07e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.74 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 564 EDAGSGAEDVGPGGEDVGAGREAAGEGGENAGAEEDVAAGGEDAGGEEDAGAGEEDMGPGGEDA-RGGEDAGAGEEDAGG 642
Cdd:PRK12678 56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAAsAPEAAQARERRERGE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 643 GGDDAGAGGEDAGAGREDAGAGGEDVGAGREDAGAGGEDVGAGGEDVGAGRRRCGSSRGCRNRRRSCGNTRRCRSRRSGA 722
Cdd:PRK12678 136 AARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRR 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749385072 723 EDVGPEGEDVGAGREAAGEGGENAGAEDVAAGGEDAGEEEDAGGEDAG---AAREDAGAGGDDVGAGRE 788
Cdd:PRK12678 216 EERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGrrfRDRDRRGRRGGDGGNERE 284
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
303-547 |
6.33e-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: 43.51 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 303 REQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLWEQE 382
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 383 KQMREQEQKMR-DQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEEKMQEEERIREREKKMRE 461
Cdd:TIGR02168 746 EERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 462 EEETMREQEEKMQKQEENMWEQEEKEWQQQRLPEQKEKLWEQEKMQEQEEkiwEQEEKIRDQEEMWGQEKKMWRQEKMRE 541
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL---EALLNERASLEEALALLRSELEELSEE 902
|
....*.
gi 749385072 542 QEDVET 547
Cdd:TIGR02168 903 LRELES 908
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-440 |
7.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 199 IEELTKERDALSLELYRNTITN-EELKKKNAELQEkLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQtntlqeemwrq 277
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNlKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELR----------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 278 eeelreqekkirkQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREqeeqmqeqeekm 357
Cdd:COG4717 116 -------------EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA------------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 358 wEQEEKMREQEEKMwrqEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQEK 437
Cdd:COG4717 171 -ELAELQEELEELL---EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
...
gi 749385072 438 KTR 440
Cdd:COG4717 247 EAR 249
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
299-442 |
7.36e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 299 EERLREQEGKMREQEEKMRRQEKRLREQ-EKELREQEKELREQkklreqeeqmqeqeekmweqEEKMREQEEKMWRQEER 377
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNEfEKELRERRNELQKL--------------------EKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749385072 378 LWEQEKQMREQEQKMRDQEERMWEQDERLREKEErmrEQEKMWEQVEKM-REEKK---MQEQEKKTRDQ 442
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIE---EQLQELERISGLtAEEAKeilLEKVEEEARHE 170
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
360-445 |
7.88e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 360 QEEKMREQEEKMWRQEErlwEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKmREEKKMQEQEKKT 439
Cdd:PRK12704 55 KKEALLEAKEEIHKLRN---EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK-ELEQKQQELEKKE 130
|
....*.
gi 749385072 440 RDQEEK 445
Cdd:PRK12704 131 EELEEL 136
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
193-447 |
8.54e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 193 KKADRYIEELTKERDALSlelYRNTItNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQT----- 267
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELE---KLNNK-YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkiqkn 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 268 NTLQEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQE 347
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 348 EQMQEQEEKMWEQE------EKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWE 421
Cdd:TIGR04523 294 KSEISDLNNQKEQDwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
250 260
....*....|....*....|....*...
gi 749385072 422 QVEKMREEKKMQEQ--EKKTRDQEEKMQ 447
Cdd:TIGR04523 374 KLKKENQSYKQEIKnlESQINDLESKIQ 401
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
193-480 |
1.09e-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: 43.04 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 193 KKADRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKEL---KRKLERAKFLLPQVQTNT 269
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEekeEKLKAQEEELRALEEELK 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 270 LQEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQ 349
Cdd:pfam02463 812 EEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESK 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 350 MQEQEEKMwEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREE 429
Cdd:pfam02463 892 EEKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKE 970
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 749385072 430 KKMQEQEKKTRDQEEKmqEEERIREREKKMREEEETMREQEEKMQKQEENM 480
Cdd:pfam02463 971 ELGKVNLMAIEEFEEK--EERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
302-447 |
1.19e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.67 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 302 LREQEGKMREQEEKMRRQEKRLREQ------EKELREQEKELREQkklreqeeqmqeqeekmweQEEKMREQEEKMWRQE 375
Cdd:pfam13779 477 LRIEDGDLSDAERRLRAAQERLSEAlergasDEEIAKLMQELREA-------------------LDDYMQALAEQAQQNP 537
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749385072 376 ERLWEQEKQMReqeQKMRDQE-ERMWEQDERLREkEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEEKMQ 447
Cdd:pfam13779 538 QDLQQPDDPNA---QEMTQQDlQRMLDRIEELAR-SGRRAEAQQMLSQLQQMLENLQAGQPQQQQQQGQSEMQ 606
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
194-440 |
1.19e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 194 KADRYIEELTKERDALSLELyRNTITNEELkkknAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTNTLQEE 273
Cdd:COG3206 193 EAEAALEEFRQKNGLVDLSE-EAKLLLQQL----SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 274 MwrqeeelreqekkiRKQEEKMWRQEERLREQEGkmrEQEEKMRRQEKRLREQEKELREQEKELREQKKlreqeeqmqeq 353
Cdd:COG3206 268 L--------------RAQLAELEAELAELSARYT---PNHPDVIALRAQIAALRAQLQQEAQRILASLE----------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 354 eekmweqeekmreqeekmwRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQ 433
Cdd:COG3206 320 -------------------AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
....*..
gi 749385072 434 EQEKKTR 440
Cdd:COG3206 381 EALTVGN 387
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
193-447 |
1.29e-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: 42.65 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 193 KKADRYIEELTKERDALSLELY--RNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQTntL 270
Cdd:pfam02463 207 KKALEYYQLKEKLELEEEYLLYldYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL--Q 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 271 QEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKEL---------REQEKELREQK 341
Cdd:pfam02463 285 EEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELkeleikreaEEEEEEELEKL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 342 KLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWE 421
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
250 260
....*....|....*....|....*.
gi 749385072 422 QVEKMREEKKMQEQEKKTRDQEEKMQ 447
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKS 470
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
289-370 |
1.33e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 41.78 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 289 RKQEEKMWRQEERLREQEgkmreqEEKMRRQEKRLREQEKELREQEKElrEQKKLreqeeqmqeqeekmweqEEKMREQE 368
Cdd:pfam07946 266 REEEIEKIKKAAEEERAE------EAQEKKEEAKKKEREEKLAKLSPE--EQRKY-----------------EEKERKKE 320
|
..
gi 749385072 369 EK 370
Cdd:pfam07946 321 QR 322
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
181-440 |
1.38e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 181 LQRALSAVSTWHKK---ADRYIEELTKERDALSLELYRNTITNE----ELKKKNAELQEKLRLAES--EKSEIQLNV--K 249
Cdd:pfam05483 305 LQRSMSTQKALEEDlqiATKTICQLTEEKEAQMEELNKAKAAHSfvvtEFEATTCSLEELLRTEQQrlEKNEDQLKIitM 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 250 ELKRKLERAKFLLPQVQTNTLQEEMWRQEEELREQEKKIRKQEEKMwrqeerLREQEGKMREQEEKMRRQEKRLREQEKE 329
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKI------AEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 330 LR----EQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDER 405
Cdd:pfam05483 459 LTaiktSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
250 260 270
....*....|....*....|....*....|....*
gi 749385072 406 LREKEERMReqekmwEQVEKMREEKKMQEQEKKTR 440
Cdd:pfam05483 539 LEEKEMNLR------DELESVREEFIQKGDEVKCK 567
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
289-393 |
1.41e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 289 RKQEEKMWRQEERLREQEgkmREQEEKMRRQEKRLREQEKELREQEKELREQKklreqeeqmqeQEEKMWEQEEKMREQE 368
Cdd:cd16269 204 RAKAEAAEQERKLLEEQQ---RELEQKLEDQERSYEEHLRQLKEKMEEERENL-----------LKEQERALESKLKEQE 269
|
90 100
....*....|....*....|....*
gi 749385072 369 EKMwrqEERLWEQEKQMREQEQKMR 393
Cdd:cd16269 270 ALL---EEGFKEQAELLQEEIRSLK 291
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
299-445 |
1.42e-03 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 42.24 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 299 EERLREQEGKMREQEEKMRRQE-KRLREQEKELREQEKELREQKKlreqEEQMQEQEEKMWEQEEKMREQEEkmwrQEER 377
Cdd:COG4487 32 EKELAERLADAAKREAALELAEaKAKAQLQEQVAEKDAEIAELRA----RLEAEERKKALAVAEEKEKELAA----LQEA 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749385072 378 LWEQEKQMREQEQKMRDQEERMWEQDERLREKEErmreqekmweQVEKMREEKKMQEQEKKTRDQEEK 445
Cdd:COG4487 104 LAEKDAKLAELQAKELELLKKERELEDAKREAEL----------TVEKERDEELDELKEKLKKEEEEK 161
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
191-445 |
2.04e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 191 WHKKADRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKfllpqVQTNTL 270
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK-----KENQSY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 271 QEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEgkmrEQEEKMRRQEKRLREQEKELREQEKELREQKklreqeeqm 350
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ----QEKELLEKEIERLKETIIKNNSEIKDLTNQD--------- 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 351 qEQEEKMWEQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQ-DERLREKEERM----REQEKMWEQVEK 425
Cdd:TIGR04523 450 -SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKlNEEKKELEEKVkdltKKISSLKEKIEK 528
|
250 260
....*....|....*....|
gi 749385072 426 MREEKKmqEQEKKTRDQEEK 445
Cdd:TIGR04523 529 LESEKK--EKESKISDLEDE 546
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
297-478 |
2.11e-03 |
|
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: 41.86 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 297 RQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEE 376
Cdd:pfam15709 342 RAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 377 RLWEQEKQMREQE-QKMRDQEERMWEQDERLREKEERMR---EQEKMWEQVEKMREEKKMQEQEKKTRDQEEkmqeeeri 452
Cdd:pfam15709 422 RQQQEEFRRKLQElQRKKQQEEAERAEAEKQRQKELEMQlaeEQKRLMEMAEEERLEYQRQKQEAEEKARLE-------- 493
|
170 180
....*....|....*....|....*.
gi 749385072 453 rerekkmreeeetmreQEEKMQKQEE 478
Cdd:pfam15709 494 ----------------AEERRQKEEE 503
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
221-447 |
2.16e-03 |
|
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: 41.44 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 221 EELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAKFLLPQVQtNTLQEEMWRQEEELREQEKKIRKQEEKMWRQEE 300
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEID-EFNEEQAEWKELEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 301 RLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLWE 380
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 381 QEKQMREQEQKMRDQEERMWEQDERLREKEERM-------------REQEKMWEQVEKMREEKKMQEQEKKTRDQEEKMQ 447
Cdd:pfam13868 247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEeaekrrmkrlehrRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-381 |
2.38e-03 |
|
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: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 180 ELQRALSAVSTWHKKADRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKRKLERAK 259
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 260 FLLPQVQTNTLQEEMWRQEEELREQ-EKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELR 338
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEeLEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 749385072 339 EQKKLREQEEQMQEQEEKMWEQEEKMREQEEKMWRQEERLWEQ 381
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
577-795 |
2.59e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 41.43 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 577 GEDVGAGREAAGEGGENAGAEEDVAAGGEDAGGEEDAGAGEEDMGPGGEDARGGEDAGAGEEDAGGGGDDAGAGGEDAGA 656
Cdd:PRK12678 49 GELIAAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 657 GREDAGAGGEDVGAGREDAGAGGEDVGAGGEDVGAGRRRCGSSRGCRNRRRscgnTRRCRSRRSGAEDVGPEGEDvgAGR 736
Cdd:PRK12678 129 ERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDRE----DRQAEAERGERGRREERGRD--GDD 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 749385072 737 EAAGEGGENAGAEDVAAGGEDAGEEEDAGGEDAGAAREDAGAGGDDVGAGREDAGAGGE 795
Cdd:PRK12678 203 RDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGR 261
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
297-447 |
3.13e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.26 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 297 RQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREqeeqmqeqeekmwEQEEKMREQEEKMWRQEE 376
Cdd:pfam05557 45 RESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-------------EKESQLADAREVISCLKN 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749385072 377 RLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMWEQVEKMREEKKMQEQEKKTRDQEEKMQ 447
Cdd:pfam05557 112 ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQ 182
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
180-444 |
3.23e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 180 ELQRALSAVSTWHKKADRYIEELTKERDALSLELyrNTITNE---------ELKKKNAELQEKLRLAESEKSEIQLNVKE 250
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL--KKLNEEkkeleekvkDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 251 LKRKLERAKFLLpqvQTNTLQEEmwrqeeelreqekkIRKQEEKMwrqEERLREQEGKMREQEEKmrrqEKRLREQEKEL 330
Cdd:TIGR04523 543 LEDELNKDDFEL---KKENLEKE--------------IDEKNKEI---EELKQTQKSLKKKQEEK----QELIDQKEKEK 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 331 REQEKELREQKKLREQEEQMQEQEEKmweQEEKMREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKE 410
Cdd:TIGR04523 599 KDLIKEIEEKEKKISSLEKELEKAKK---ENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
250 260 270
....*....|....*....|....*....|....
gi 749385072 411 ERMREQEKMWEQVEKMREEKKMqeqEKKTRDQEE 444
Cdd:TIGR04523 676 DDIIELMKDWLKELSLHYKKYI---TRMIRIKDL 706
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
360-443 |
3.43e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.35 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 360 QEEKMREQEEkmwRQEERLWEQEKqmREQEQKMRDQEERMWEQDERLREKEER-----MREQEKMWEQveKMREEKKMQE 434
Cdd:pfam02841 207 EAERAKAEAA---EAEQELLREKQ--KEEEQMMEAQERSYQEHVKQLIEKMEAereqlLAEQERMLEH--KLQEQEELLK 279
|
....*....
gi 749385072 435 QEKKTRDQE 443
Cdd:pfam02841 280 EGFKTEAES 288
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
192-444 |
4.65e-03 |
|
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: 40.29 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 192 HKKADRYIEELTKERDALSLELYRNTITNEELKKKNAELQEKLRLAESekSEIQLNVKELKRKLERAKFLLPQVQTN--- 268
Cdd:pfam13868 30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQE--LEEQIEEREQKRQEEYEEKLQEREQMDeiv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 269 -TLQEEMWRQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQE 347
Cdd:pfam13868 108 eRIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 348 EQMQEQEEKMWEQEEK-------MREQEEKMWRQEERLwEQEKQMREQEQKMRDQEERMWEQDERLREKEERMREQEKMW 420
Cdd:pfam13868 188 RLRAQQEKAQDEKAERdelraklYQEEQERKERQKERE-EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
250 260
....*....|....*....|....
gi 749385072 421 EQVEKMREEKKMQEQEKKTRDQEE 444
Cdd:pfam13868 267 LRKQAEDEEIEQEEAEKRRMKRLE 290
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
572-774 |
4.88e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 40.74 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 572 DVGPGGEDVGAGREAAGEGGENAGAEEDVAAGGEDAGGEEDAGAGEEDMGPGGEDARGGEDAGAGEEDAGGGGDDAGAGG 651
Cdd:PRK07764 585 EAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASD 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 652 EDAGAGREDAGAGGEDVGAGREDAGAGGEDVGAGGEDVGAGRRRCGSSRGCRNRRRSCGNTRRCRSRRSGAEDVGP---E 728
Cdd:PRK07764 665 GGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPlppE 744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749385072 729 GEDVGAGREAAGEGGENAGAEDVAAGG----------EDAGEEEDAGGEDAGAARE 774
Cdd:PRK07764 745 PDDPPDPAGAPAQPPPPPAPAPAAAPAaapppsppseEEEMAEDDAPSMDDEDRRD 800
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
289-523 |
4.99e-03 |
|
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: 40.29 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 289 RKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMWEQEEKMREQE 368
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 369 EKMWRQEERLWEQEKQ-----MREQEQKMRDQEERMWEQDERL--REKEERMREQEKMWEQVEKMREEKKMQEQEKKTRD 441
Cdd:pfam13868 168 EEEREAEREEIEEEKEreiarLRAQQEKAQDEKAERDELRAKLyqEEQERKERQKEREEAEKKARQRQELQQAREEQIEL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 442 QEEKMQEEERIREREKKMREEEETMREQEEKMQKQEENMWEQEEKEW--------QQQRLPEQKEKLWEQEKMQEQEEKI 513
Cdd:pfam13868 248 KERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRElekqieerEEQRAAEREEELEEGERLREEEAER 327
|
250
....*....|
gi 749385072 514 WEQEEKIRDQ 523
Cdd:pfam13868 328 RERIEEERQK 337
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
311-447 |
6.13e-03 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 39.52 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 311 EQEEKMRRQEKR--LREQEKELREQEKELREQKKLReqeeqmqeqeekmweqEEKMREQEEKMWRQEERlwEQEKQMREQ 388
Cdd:pfam15991 5 KMSEQMWRALKRhiMRERERKKQEQEAKMEEERLRR----------------EREEREKEDRMTLEETK--EQILKLEKK 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 749385072 389 EQKMRDQEERMWEQDERLREKEERMREQEKmwEQVEKMreekKMQEQEKKTRDQEEKMQ 447
Cdd:pfam15991 67 LADLKEEKHQLFLQLKKVLHEDETRKRQLK--EQSELF----ALQQAAAQVFLPQLSMQ 119
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
184-397 |
6.66e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.99 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 184 ALSAVSTWHKKADRYIEELTKERDAlSLELYRNTITNEELkkknaELQEKLRLAESEKSEIQLNVKELKRKLERAKFllp 263
Cdd:pfam05262 168 NVSDVDTDSISDKKVVEALREDNEK-GVNFRRDMTDLKER-----ESQEDAKRAQQLKEELDKKQIDADKAQQKADF--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 264 qvqtntlqeemwrqeeelREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQKKL 343
Cdd:pfam05262 239 ------------------AQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKA 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 749385072 344 REQEEQMQEQEEKMWEQEEKMREQEEKMWRQEerlweqekqMREQEQKMRDQEE 397
Cdd:pfam05262 301 KDHKAFDLKQESKASEKEAEDKELEAQKKREP---------VAEDLQKTKPQVE 345
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
290-415 |
6.77e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 40.41 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 290 KQEEKMWRQEERLREQEGKMREQEEkmrRQEKRLREQEKELREQEKELREQKKLREQEEQMQEQEEKMwEQEEKMREQEE 369
Cdd:PRK10811 595 KAEAKPERQQDRRKPRQNNRRDRNE---RRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQA-EVTEKARTQDE 670
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 749385072 370 KmwRQEERlweQEKQMREQEQKMRDQEE----RMWEQDERLREKEERMRE 415
Cdd:PRK10811 671 Q--QQAPR---RERQRRRNDEKRQAQQEakalNVEEQSVQETEQEERVQQ 715
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
297-408 |
7.86e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.06 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 297 RQEERLR-EQEGKMREQEEKMRRQEKRLREQEKELREQEKELREQkklreqeeqmqeqeekmWEQEekmREQEEKMWRQE 375
Cdd:COG0542 418 RRLEQLEiEKEALKKEQDEASFERLAELRDELAELEEELEALKAR-----------------WEAE---KELIEEIQELK 477
|
90 100 110
....*....|....*....|....*....|...
gi 749385072 376 ERLWEQEKQMREQEQKMRDQEERMWEQDERLRE 408
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLRE 510
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
193-341 |
7.92e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.32 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 193 KKADRYIEELTKERDALSLELyrNTITNEELKKKNAELQEKLRLAESEKSEIQLNVKELKrkLERAKFLLPQVQTN--TL 270
Cdd:pfam06008 92 KNLIDNIKEINEKVATLGEND--FALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAE--LKAAQDLLSRIQTWfqSP 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749385072 271 QEEmwrQEEELREQEKKIRKQEEKMWRQEERLREQEGKMREQEEKMRRQEKRLREQEKelreQEKELREQK 341
Cdd:pfam06008 168 QEE---NKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQR----KKEEVSEQK 231
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
536-692 |
8.79e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.57 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 536 QEKMREQEDVETGGEAAGAGEADVGAGGeDAGSGAEDVG-PGGEDVGAGREAAGEGGENAGAEEDVAAGGEDAGGEEDAG 614
Cdd:PHA03169 64 QGHRQTESDTETAEESRHGEKEERGQGG-PSGSGSESVGsPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPS 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749385072 615 AGEEDMGPGGEDARGGEDAGAGEEDAGGGGDDAGAGGEDAGAGREDAGAGGEDVGAGR-EDAGAGGEDVGAGGEDVGAG 692
Cdd:PHA03169 143 HPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSsPPPQSPPDEPGEPQSPTPQQ 221
|
|
| COG5493 |
COG5493 |
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ... |
364-447 |
9.52e-03 |
|
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];
Pssm-ID: 444244 [Multi-domain] Cd Length: 239 Bit Score: 38.81 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749385072 364 MREQEEKMWRQEERLWEQEKQMREQEQKMRDQEERMWEQDERLREKEERMR----EQEKMWEQVEKMREE-KKMQEQEKK 438
Cdd:COG5493 1 MSLLKEELKRELLELLREDPEFRYAVLGLLATKDGLEELLERLEKLEEQMRkweeQLRKLEEEIKKLREQvRKLEEDVKR 80
|
....*....
gi 749385072 439 TRDQEEKMQ 447
Cdd:COG5493 81 LEEQERKLE 89
|
|
| |
