|
Name |
Accession |
Description |
Interval |
E-value |
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
152-678 |
0e+00 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 645.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 152 PVLIDTAAPFESVKEAVSKFGGITDWKAHKIQTIERRKTVDQELEKIQEDMPDYKKQAVVAEEAKHQVVMELERTRNVVE 231
Cdd:pfam05701 1 RGLIDTAAPFESVKEAVSKFGGIVDWKAHRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 232 ELKLELEKAEKEEQQAKQDSDLAKLRVEEMEQGIAGEVSVAAKSQLEVAKARHLSAVSELGTIREEIEMVSNEYESLLTE 311
Cdd:pfam05701 81 ELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 312 KDLAAKKAEDSVLKAKDVEKQMEGLTMEVIATKQLLELAHATHLEAQEKKLDAAMARDQDVYNQEKELKMVEDEIKRFRQ 391
Cdd:pfam05701 161 RDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 392 DIDAADDVKTKLKTASALQQDLRAEIAAYKDSNMG---------KRNNSDIQAAVDSARKELEEVISNIEKANSEVKTLK 462
Cdd:pfam05701 241 QLLSAKDLKSKLETASALLLDLKAELAAYMESKLKeeadgegneKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 463 IIVGSLQSELAREKHDLSETRQRN--------------------------REDTREEKCTEIAKKLQEASREAEEAKSLA 516
Cdd:pfam05701 321 VAAASLRSELEKEKAELASLRQREgmasiavssleaelnrtkseialvqaKEKEAREKMVELPKQLQQAAQEAEEAKSLA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 517 IAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQETEYANKIEDISSSPKSIIISVEEYYE 596
Cdd:pfam05701 401 QAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKALQESESSAESTNQEDSPRGVTLSLEEYYE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 597 LSKQAHEVEEAANRKLAEIVSKIEVAKEEESRILENLEEVSRETAIRKVELKEAMTKVEKARDGKVGMDHELRKWRSDNG 676
Cdd:pfam05701 481 LSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQELRKWRAEHE 560
|
..
gi 332193998 677 NR 678
Cdd:pfam05701 561 QR 562
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
245-658 |
1.79e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 245 QQAKQDSDLAKLRVEEMEQGIAGEVSVAAKSQLEVAKARHLSAVSELGTIREEIEMVSNEYESLLTEKDLAAKKAEDSVL 324
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 325 KAKDVEKQMEGLTMEVIATKQLLELAHATHlEAQEKKLDAAMARDQDVYNQEKELKMVEDEIKRFRQDIDAADDVKTKLK 404
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEA-EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 405 TASALQQDLRAEIAAYKDSNMGKRNNSDIQAA------------VDSARKELEEVISNIEKANSEVKTLKIIVGSLQSEL 472
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKAdeakkkaeeakkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 473 AREKHDLSETRQRNREDTREEKCTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVE-------RQLM 545
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkkaeelKKAE 1561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 546 ESKKEMEASRASEKLALAAIKAlqetEYANKIEDISSSPKSIIIsvEEYYELSKQAHEVEEAANRKLAEIVSKIEVAKEE 625
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKA----EEAKKAEEARIEEVMKLY--EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
410 420 430
....*....|....*....|....*....|...
gi 332193998 626 ESRILENLEEVSRETAIRKVELKEAMTKVEKAR 658
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
257-693 |
5.42e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 257 RVEEMEQGIAGEVSVAAKSQLEVAKARHLSAVSELGTIR-----EEIEMVSNEYESLLTEKDLAAKKAEDSVLKAKDVEK 331
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 332 QMEGLTMEVIATKQLLELAHATHLEAQEKkldAAMARDQDVYNQEKELKMVEDEIKRfrQDIDAADDVKTKLKTASALQQ 411
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIK---AEEARKADELKKAEEKKKADEAKKA--EEKKKADEAKKKAEEAKKADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 412 DLRAEIAAYKDSNMGKRNNSDIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSEL------AREKHDLSETRQR 485
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaakkkAEEKKKADEAKKK 1399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 486 NREDTR----------EEKCTEIAKKLQEASREAEEAKSLAIAAR--EELRKAKEESDEAKTGLSAVE--RQLMESKKEM 551
Cdd:PTZ00121 1400 AEEDKKkadelkkaaaAKKKADEAKKKAEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKA 1479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 552 EASRASEKLALAAIKALQETEYANKIEDISSSPKSIIISVEeyyelSKQAHEVEEAANRKLAEivskiEVAKEEESRILE 631
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE-----AKKADEAKKAEEAKKAD-----EAKKAEEKKKAD 1549
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332193998 632 NL---EEVSRETAIRKVELKE--------AMTKVEKARDGKVGMDHELRKWRSDNGNRSPEGGNKENLSKSKS 693
Cdd:PTZ00121 1550 ELkkaEELKKAEEKKKAEEAKkaeedknmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
254-690 |
2.18e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 254 AKLRVEEMEQGIAGEVSVAAKSQLEVAKARHLSAVSELGTIrEEIEMVSNEYESLLTEKDLAAKKAEDSvLKAKDVEKQM 333
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKA-EDARKAEEARKAEDAKRVEIARKAEDA-RKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 334 EGLTMEviATKQLLELAHATHLEAQEKKLDAAMARDQDVYNQEKELKMVEDEikRFRQDIDAADDVKTKLKTAS-ALQQD 412
Cdd:PTZ00121 1174 DAKKAE--AARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKkAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 413 LRAEIAAYKDSNMGKRNNSDIQAAVDSARKElEEVISNIEKANSEvktlkiivgslQSELAREKHDLSETRQRNRE---- 488
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKA-DELKKAEEKKKAD-----------EAKKAEEKKKADEAKKKAEEakka 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 489 DTREEKCTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKAL 568
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 569 QETEYANKIEDISSSPKSIIISVEeyyELSKQAHEVEEAAN-RKLAEIVSKIEVAKE--EESRILENLEEVSRETaiRKV 645
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKAD---EAKKKAEEKKKADEaKKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEA--KKA 1472
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 332193998 646 ElkEAMTKVEKARDGKvgmdhELRKWRSDNGNRSPEGGNKENLSK 690
Cdd:PTZ00121 1473 D--EAKKKAEEAKKAD-----EAKKKAEEAKKKADEAKKAAEAKK 1510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
162-690 |
2.73e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 162 ESVKEAVSKFGGITDWKAHKIQTIERRKTVDQELEKIQE---DMPDYKKQAVVAEEAKHQVVMELERTRNVVEELKLELE 238
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 239 KAEKEEQQAKQDSDLAKLRVEEMEQgiagevsvaaksqlevaKARHLSAVSELGTIREEIEMVSNEyeslLTEKDLAAKK 318
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKK-----------------KAEEKKKADEAKKKAEEDKKKADE----LKKAAAAKKK 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 319 AEDSVLKAKDVEKQMEgltmeviaTKQLLELAHathlEAQEKKLDAAMARDQDVYNQEKELKMVEDEIKRFRQDIDAADD 398
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADE--------AKKKAEEAK----KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE 1487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 399 VKTKLKTASALQQDLRAEIAAYKDSNMGKRNNSDIQAavDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHD 478
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 479 LSETRQRNREDTREEKCTEIAKKLQEASREA--EEAKSLAIAAREELRKAKEE---------SDEAKTGLSAVERQLMES 547
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmKLYEEEKKMKAEEAKKAEEAkikaeelkkAEEEKKKVEQLKKKEAEE 1645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 548 KKEMEASRASEKLAL--AAIKALQETEYANKIEDISSSPKSIIISVEEYYELSKQAHEVEEAANRKLAEIVSKIEVAKEE 625
Cdd:PTZ00121 1646 KKKAEELKKAEEENKikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332193998 626 ESRILEnLEEVSRETAIRKVELKEAmtKVEKARDGKVGMDHELRKWRSDNGNRSPEGGNKENLSK 690
Cdd:PTZ00121 1726 EENKIK-AEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
178-631 |
8.66e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 8.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 178 KAHKIQTIERRKTVDQELEKIQEdmpdyKKQAvvaEEAKHQVVMELERTRNVVEELKLELEKAEKEEQ-QAKQDSDLAKL 256
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEE-----KKKA---DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKaEEKKKADEAKK 1438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 257 RVEEmeqgiAGEVSVAAKSQLEVAKARHLSAVSELGTIREEIEMVSNEYEslltEKDLAAKKAEDSVLKAKDVEKQMEGl 336
Cdd:PTZ00121 1439 KAEE-----AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK----KADEAKKKAEEAKKKADEAKKAAEA- 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 337 TMEVIATKQLLELAHATHLEAQEKKLDAAMARDQDVYNQEKELKMVED-----EIKRFRQDIDAADDVKTKLKTASALQQ 411
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 412 DLRAEIaaykdSNMGKRNNSDIQAAVDSARKELEEVI--SNIEKANSEVKTlkiiVGSLQSELAREKHDLSETRQRnrED 489
Cdd:PTZ00121 1589 AEEARI-----EEVMKLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKA--EE 1657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 490 TREEKCTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQ 569
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332193998 570 ETEYANKIEDISSSPKSIIISVEEYyelsKQAHEVEEAANRKLAEIVSKIEVAKEEESRILE 631
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHL----KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
187-655 |
3.84e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 187 RRKTVDQELEKIQEDmpdyKKQAVVAEEAKHQVVMELERTRNVVEELKLELEKAEKEEQQAKQDSDLAKLRVEEMEQ--- 263
Cdd:PRK02224 214 ELAELDEEIERYEEQ----REQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRErle 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 264 GIAGEVS-VAAKSQLEVAKARHLSAV-----SELGTIREEIEMVSNEYESLLTEKDLAAKKAEDSVLKAKDVEKQMEGLT 337
Cdd:PRK02224 290 ELEEERDdLLAEAGLDDADAEAVEARreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 338 MEVIATKQLLELAhATHLEAQEKKLDAAMAR----DQDVYNQEKELKMVEDEIKRFRQDIDaadDVKTKLKTASALQQDL 413
Cdd:PRK02224 370 SELEEAREAVEDR-REEIEELEEEIEELRERfgdaPVDLGNAEDFLEELREERDELREREA---ELEATLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 414 RAEIAAYKDSNMGKR-NNSDIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQS--ELAREKHDLSETRQRNRE-- 488
Cdd:PRK02224 446 EALLEAGKCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEEli 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 489 DTREEKCTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEasraseklALAAIKAL 568
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE--------SLERIRTL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 569 QEteyanKIEDISSSPKSIIISVEEYYELSKQAHEVEEAANRKLAEIVSKIEVAKEEESR--------ILENLEEVSRET 640
Cdd:PRK02224 598 LA-----AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARedkeraeeYLEQVEEKLDEL 672
|
490
....*....|....*
gi 332193998 641 AIRKVELKEAMTKVE 655
Cdd:PRK02224 673 REERDDLQAEIGAVE 687
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-569 |
2.08e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 276 QLEVAKARHLSAVSELGTIREEIEMVSNEYESLLTEKDLAAKKAEDSVLKAKDVEKQMEGLTMEVIATKQLLElahatHL 355
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-----RL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 356 EAQEKKLDAAMARDqdvynqEKELKMVEDEIKRFRQDID----AADDVKTKLKTASALQQDLRAEIA-AYKDSNMGKRNN 430
Cdd:TIGR02168 301 EQQKQILRERLANL------ERQLEELEAQLEELESKLDelaeELAELEEKLEELKEELESLEAELEeLEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 431 SDIQAAVDSARKELEEVISNIEKANSEVKTLKIivgslqselarEKHDLsetrQRNREDTREEKcTEIAKKLQEASREAE 510
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEA-----------RLERL----EDRRERLQQEI-EELLKKLEEAELKEL 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 332193998 511 EAKSLAIaaREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQ 569
Cdd:TIGR02168 439 QAELEEL--EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-534 |
3.36e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 206 KKQAVVAEEAKhqvvmELErtrnvveelkLELEKAEKEEQQAKQDSDLAKLRVEEMEQGIAGEVSVAAKSQLEVAKARHL 285
Cdd:COG1196 206 ERQAEKAERYR-----ELK----------EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 286 SAVSELGTIREEIEMVSNEYESLLTEKDLAAKKAEDSVLKAKDVEKQMEGLTMEVIATKQLLELAHATHLEAQEKKLDAA 365
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 366 MARDQDVYNQEKELKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRAEIAAYkdsnmgKRNNSDIQAAVDSARKELE 445
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL------EEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 446 EVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRNREDTREEKctEIAKKLQEASREAEEAKSLAIAAREELRK 525
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEAD 502
|
....*....
gi 332193998 526 AKEESDEAK 534
Cdd:COG1196 503 YEGFLEGVK 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
375-565 |
1.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 375 QEKELKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRAEIAAYKDsnmgKRNNSDIQAAVDSARKELEEVISNIEKA 454
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK----LLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 455 NSEVKTLKiivgSLQSELAREKHDLSETRQRnREDTREEKCTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAK 534
Cdd:COG4717 152 EERLEELR----ELEEELEELEAELAELQEE-LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190
....*....|....*....|....*....|.
gi 332193998 535 TGLSAVERQLMESKKEMEASRASEKLALAAI 565
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAA 257
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
426-676 |
3.90e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 426 GKRNNSDI--QAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRNRE-----DTREEKCTEI 498
Cdd:TIGR02168 666 AKTNSSILerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkdlARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 499 AKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRaSEKLALAAIKALQETEYANKIE 578
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-EALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 579 DISSSPKSIIISVEEYYELSKQAHEVEEaanrKLAEIVSKIEVAKEEESRILENLEEVSRETAIRKVELKEAmtkvekaR 658
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSE----DIESLAAEIEELEELIEELESELEALLNERASLEEALALL-------R 893
|
250
....*....|....*...
gi 332193998 659 DGKVGMDHELRKWRSDNG 676
Cdd:TIGR02168 894 SELEELSEELRELESKRS 911
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
290-639 |
1.19e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 290 ELGTIREEIEMVSNEYESLLTEKDLAAKKAEDSVLKAKDVEKQMEGLTMEVIATKQLlelahathlEAQEKKLDAAMARD 369
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE---------EEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 370 QDVYNQEKElkMVEDEIKRFRQDIDAADDVKTKLKTA-SALQQDLRAEIAAYKDSNMGKrnnsdiqaaVDSARKELEEVI 448
Cdd:TIGR02169 746 LSSLEQEIE--NVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIPEIQAELSK---------LEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 449 SNIEKANSEVKTLKIIVGSLQSELAREKHDLSEtrqrnREDTREEKCTEIAKKLQEASREAEEAKSLAIAAREELRKAKE 528
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 529 ESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQETEyaNKIEDISSSPKSIIISVEEYYELSKQAHEVEEA- 607
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL--SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEi 967
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 332193998 608 ----------------ANRKLAEIVSKIEVAKEEESRILENLEEVSRE 639
Cdd:TIGR02169 968 ralepvnmlaiqeyeeVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
186-570 |
1.36e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 186 ERRKTVDqELEKIQEDmpDYKKQAVVAEEAkhQVVMELERTRNVVEELKLELEKAEKEEQQAKQDSDLaKLRVEEMEQGI 265
Cdd:TIGR02169 154 ERRKIID-EIAGVAEF--DRKKEKALEELE--EVEENIERLDLIIDEKRQQLERLRREREKAERYQAL-LKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 266 AGEVSVAAKSQLEVAKARHLSAVSELGTIREEIEMVSNEYESLLTEKDLAAKKAED-SVLKAKDVEKQMEGLTMEVIATK 344
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 345 QLLELAhathlEAQEKKLDAAMARDQ-DVYNQEKELKMVEDEIKRFRQDIDAaddVKTKLKTASALQQDLRAEIAAYKDS 423
Cdd:TIGR02169 308 RSIAEK-----ERELEDAEERLAKLEaEIDKLLAEIEELEREIEEERKRRDK---LTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 424 NMGKRnnsdiqAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRNREdtREEKCTEIAKKLQ 503
Cdd:TIGR02169 380 FAETR------DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE--LEEEKEDKALEIK 451
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332193998 504 EASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQE 570
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
340-553 |
2.57e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 340 VIATKQ--LLELAHATHLEAQEKKLDAAMARDQ----DVYNQEKELKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDL 413
Cdd:COG4913 245 EDAREQieLLEPIRELAERYAAARERLAELEYLraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 414 RAEIAAYKDSNMGKRNNsDIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELARekhdlsetrQRNREDTREE 493
Cdd:COG4913 325 LDELEAQIRGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA---------LRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 494 KCTEIAKKLQEASREAEEAKSlaiAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEA 553
Cdd:COG4913 395 ALEEELEALEEALAEAEAALR---DLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
433-570 |
2.71e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 50.91 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 433 IQAA---VDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLsetrQRNREDTREEKCTEIAKKLQEASREA 509
Cdd:COG1193 502 IERArelLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREEL----EEKLEELEEEKEEILEKAREEAEEIL 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332193998 510 EEAKSLAIAAREELRKAKEESDEAKtglsAVERQLMESKKEMEASRASEKLALAAIKALQE 570
Cdd:COG1193 578 REARKEAEELIRELREAQAEEEELK----EARKKLEELKQELEEKLEKPKKKAKPAKPPEE 634
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
369-576 |
3.13e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 369 DQDVYNQEKELKMVEDEIKRFRQDIDAA----DDVKTKLKTASALQQDLRAEIAAykdsnmgkrnnsdIQAAVDSARKEL 444
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELneeyNELQAELEALQAEIDKLQAEIAE-------------AEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 445 EEVISNIEKANSEVKTLKIIVGSLQ-SELAREKHDLSETRQRNRE-----DTREEKCTEIAKKLQEASREAEEAKSLAIA 518
Cdd:COG3883 89 GERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADlleelKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 332193998 519 AREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQETEYANK 576
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
374-658 |
4.34e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 374 NQEKELKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRAEIaaykdsNMGKRNNSDIQAAVDSARKELEEVisniEK 453
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI------NEISSELPELREELEKLEKEVKEL----EE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 454 ANSEVKTLKIIVGSLQSELAREKHDLSETRQRNRE-DTREEKCTEIAKKLQEASREAEEAKSLaiaaREELRKAKEESDE 532
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEElKKEIEELEEKVKELKELKEKAEEYIKL----SEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 533 AKTGLSAVERQLMESKKEM-EASRASEKLalaaikalqeteyaNKIEDISSSPKSIIISVEEYYELSKQAHEVEEAANR- 610
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIkELEEKEERL--------------EELKKKLKELEKRLEELEERHELYEEAKAKKEELERl 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 332193998 611 ----------KLAEIVSKIEVAKEEESRILENLEEVSRETAIRKVELKEAMTKVEKAR 658
Cdd:PRK03918 378 kkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK 435
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
440-687 |
7.40e-06 |
|
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: 49.68 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 440 ARKELEEVISNIEKANSEVKTLKIIVGSLQSElaREKhdlSETRQRNREDTREEKCTEIAKKLQEASREAEEAKSLAIAA 519
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERLRRE--REK---AERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 520 REELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLA----LAAIKALQETEYANKIEDISSSPKSIIISVEEYY 595
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekIGELEAEIASLERSIAEKERELEDAEERLAKLEA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 596 ELSKQAHEVE------EAANRKLAEIVSKIEVAKEEESRILENLEEVSRETAIRKVELKEAMTKVEKARDGKVGMDHELR 669
Cdd:TIGR02169 330 EIDKLLAEIEelereiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
250
....*....|....*...
gi 332193998 670 KWRSDNGNRSPEGGNKEN 687
Cdd:TIGR02169 410 RLQEELQRLSEELADLNA 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
272-659 |
8.62e-06 |
|
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: 49.30 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 272 AAKSQLEVAKARHLSAVSELGTIREEIEMVSNEYESLLTEKDLAAKKAE----DSVLKAKDVEKQMEGLTMEVIATKQll 347
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKEAIERQLASLEE-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 348 elahatHLEAQEKKLDAamaRDQDVYNQEKELKMVEDEIKRFRQDIDAAddVKTKLKTASALQQDLRAEIAAYKdsnmgk 427
Cdd:TIGR02169 252 ------ELEKLTEEISE---LEKRLEEIEQLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKE------ 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 428 RNNSDIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRnredtreekcteiakkLQEASR 507
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE----------------LEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 508 EAEEAKSLAIAAREELRKAKEESDEAKTGLsaveRQLMESKKEMEASRASEKLALAAIKAlQETEYANKIEDISsspksi 587
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKREL----DRLQEELQRLSEELADLNAAIAGIEA-KINELEEEKEDKA------ 447
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332193998 588 iisveeyYELSKQAHEVEEAAnRKLAEIVSKIEVAKEEESRILENLEEVSRETAIRKVELKEAMTKVEKARD 659
Cdd:TIGR02169 448 -------LEIKKQEWKLEQLA-ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRA 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
364-572 |
1.02e-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: 48.61 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 364 AAMARDQDVYNQEKELKMVEDEIKRFRQDIDAA-----------DDVKTKLKTASALQQDLRAEIAAYKDS-NMGKRNNS 431
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALkkeekallkqlAALERRIAALARRIRALEQELAALEAElAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 432 DIQAAVDSARKELEEVISNIEKaNSEVKTLKIIVGSLQ-SELAREKHDLSETRQRNREDTRE--EKCTEIAKKLQEASRE 508
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYR-LGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332193998 509 AEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQETE 572
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
392-694 |
1.11e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 392 DIDAADDVKTKLKTASALQQDLRAEiAAYKDSNMGKRNNSDIQAAVDSARKELEEV----ISNIEKANSEVKTLKIIVGS 467
Cdd:PTZ00121 1049 DEDIDGNHEGKAEAKAHVGQDEGLK-PSYKDFDFDAKEDNRADEATEEAFGKAEEAkkteTGKAEEARKAEEAKKKAEDA 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 468 LQSELAREKHDLSETRQRNREDtrEEKCTEIAKKLQEAsREAEEAKSLAIAAR-------EELRKAKEESDEAKTGLSAV 540
Cdd:PTZ00121 1128 RKAEEARKAEDARKAEEARKAE--DAKRVEIARKAEDA-RKAEEARKAEDAKKaeaarkaEEVRKAEELRKAEDARKAEA 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 541 ERQLMESKKEMEASRASEKLALAAIKALQETEyaNKIEDISSSPKSIIISVEEYYELSKQAHEVEEAANRKLAEIVSKIE 620
Cdd:PTZ00121 1205 ARKAEEERKAEEARKAEDAKKAEAVKKAEEAK--KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE 1282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332193998 621 VAKEEESRileNLEEVSRETAIRKVElkEAMTKVEKARDG-KVGMDHELRKWRSDNGNRSPEGGNKENLSKSKSA 694
Cdd:PTZ00121 1283 LKKAEEKK---KADEAKKAEEKKKAD--EAKKKAEEAKKAdEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
186-639 |
2.08e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 186 ERRKTVDQELEKIQEDMPDYKKQAVVAEEAKHQVVMELERTRNVVEELKLELEKAEKEEQQAKQDSDLAKLRVEEMEQGI 265
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 266 AGEVSVAAKSQLEVAKARHLSAVSELGTIREEIEM---VSNEYESLLtEKDLAAKKAEDSVLKAKDVEKQMEGLTMEVIA 342
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVligVEAAYEAAL-EAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 343 TKQLLELAHATHLEAQEKKLDAAM---ARDQDVYNQEKELKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRAEIAA 419
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAigaAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 420 YKDSNMGKRNNSDIQAAVDSARKELEEVISNIEKANSEVKtlkiivgsLQSELAREKHDLSETRQRNREDTREEKCTEIA 499
Cdd:COG1196 653 GEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--------LELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 500 KKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEasrASEKLALAAIKALQETEyankied 579
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE---ALGPVNLLAIEEYEELE------- 794
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 580 issspksiiisvEEYYELSKQAHEVEEAANrKLAEIVSKIEvaKEEESRILENLEEVSRE 639
Cdd:COG1196 795 ------------ERYDFLSEQREDLEEARE-TLEEAIEEID--RETRERFLETFDAVNEN 839
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
433-570 |
2.99e-05 |
|
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: 46.07 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 433 IQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRNREDtrEEKCTEI--AKKLQEASREAE 510
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--EEQLGNVrnNKEYEALQKEIE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 511 EAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQE 570
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-532 |
3.57e-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: 47.36 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 192 DQELEKIQEDMpdyKKQAVVAEEAKhqvvMELERTRNVVEELKLELEKAEKEEQQAKQDSDLAKLRVEEMEQGIagevsv 271
Cdd:TIGR02168 676 RREIEELEEKI---EELEEKIAELE----KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV------ 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 272 aaksqlevakARHLSAVSELGTIREEIEMVSNEYESLLTEKDLAAKKAEDsvlKAKDVEKQMEGLTMEVIATKQLLELAH 351
Cdd:TIGR02168 743 ----------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA---EIEELEAQIEQLKEELKALREALDELR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 352 A----THLEAQEKKLDAAMARDQDVYnQEKELKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRAEIAAYKDSnmgk 427
Cdd:TIGR02168 810 AeltlLNEEAANLRERLESLERRIAA-TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS---- 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 428 rnnsdIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQrnREDTREEKCTEIAK-KLQEAS 506
Cdd:TIGR02168 885 -----LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV--RIDNLQERLSEEYSlTLEEAE 957
|
330 340
....*....|....*....|....*.
gi 332193998 507 REAEEAKSLAIAAREELRKAKEESDE 532
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
348-658 |
4.07e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 348 ELAHATHLEAQEKKLDAAMARDQDVYNQEKELKMV-EDEIKRFRQDidaaddvKTKLKTASALQQDLRAEIAAYKDSnmg 426
Cdd:pfam17380 311 EVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMErERELERIRQE-------ERKRELERIRQEEIAMEISRMREL--- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 427 KRNNSDIQAAVDSARKELEEviSNIEKANSEVKTLKIIVGSLQSELAREKHDlsETRQRNREDTREEKCTEIAKKLQEAS 506
Cdd:pfam17380 381 ERLQMERQQKNERVRQELEA--ARKVKILEEERQRKIQQQKVEMEQIRAEQE--EARQREVRRLEEERAREMERVRLEEQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 507 REAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRaseklalaaiKALQETEYANKIEDIssspks 586
Cdd:pfam17380 457 ERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK----------QAMIEEERKRKLLEK------ 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332193998 587 iiisveeyyELSKQAHEVEEAANRKLAEIVSKIEVAKEEESRILENL----EEVSRETAI-RKVELKEAMTKVEKAR 658
Cdd:pfam17380 521 ---------EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMrkatEERSRLEAMeREREMMRQIVESEKAR 588
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
472-670 |
4.31e-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: 46.97 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 472 LAREKHDLSETRQRNREDTRE--EKCTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKK 549
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEaeEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 550 EMEASRA-------------SEKLALAAIKALQETEYANKIEDISSSPKSIIISVEEYYELSKQAHEVE---EAANRKLA 613
Cdd:TIGR02168 310 RLANLERqleeleaqleeleSKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqlETLRSKVA 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 332193998 614 EIVSKIEVAKEEESRILENLEEVSRETAIRKVELKEAMTKVEKARDGKVGMDHELRK 670
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
376-572 |
5.33e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 376 EKELKMVEDEIKRFRQD---IDAADDVKTKLKTASALQQDLRAEIAAYkdsnmgkrnnSDIQAAVDSARKELEEVISNIE 452
Cdd:COG3206 188 RKELEEAEAALEEFRQKnglVDLSEEAKLLLQQLSELESQLAEARAEL----------AEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 453 --KANSEVKTLKIIVGSLQSELAR------EKH-DLSETRQRnREDTREEKCTEIAKKLQEASREAEEAKSLAIAAREEL 523
Cdd:COG3206 258 elLQSPVIQQLRAQLAELEAELAElsarytPNHpDVIALRAQ-IAALRAQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 332193998 524 RKAKEESDEaktgLSAVERQLMESKKEMEASRASEKLALAAIKALQETE 572
Cdd:COG3206 337 AQLEARLAE----LPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
380-603 |
7.65e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 380 KMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRAEIAAYKDSNMGKRNN---------SDIQAAVDSARKELEEVISN 450
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNkydelveeaKTIKAEIEELTDELLNLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 451 IEKANSEVKTLKIIVGSLQSELAR--------EKHDLSETRQRNREDTrEEKCTEIAKKLQEASREAEEAKSlaiaAREE 522
Cdd:PHA02562 250 IEDPSAALNKLNTAAAKIKSKIEQfqkvikmyEKGGVCPTCTQQISEG-PDRITKIKDKLKELQHSLEKLDT----AIDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 523 LRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQEtEYANKIEDISSSPKSIIISVEEYYELSKQAH 602
Cdd:PHA02562 325 LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA-EFVDNAEELAKLQDELDKIVKTKSELVKEKY 403
|
.
gi 332193998 603 E 603
Cdd:PHA02562 404 H 404
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
220-639 |
1.93e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 220 VMELERTRNVVEELKLELEKAEKEEQQAKQDSDLAKLRVEEMEQgiagevsvAAKSQLEvakaRHLSAVSELGtiREEIE 299
Cdd:pfam01576 680 VHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQ--------ALKAQFE----RDLQARDEQG--EEKRR 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 300 MVSNEYESLLTEKDLAAKKAEDSVLKAKDVEKQMEGLTMEVIATKQLLELA--HATHLEAQEKKL-----DAAMARDqDV 372
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAvkQLKKLQAQMKDLqreleEARASRD-EI 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 373 YNQ----EKELKMVEDEIKRFRQDIDAADDVKtklKTASALQQDLRAEIAaykDSNMGKRNNSD----IQAAVDSARKEL 444
Cdd:pfam01576 825 LAQskesEKKLKNLEAELLQLQEDLAASERAR---RQAQQERDELADEIA---SGASGKSALQDekrrLEARIAQLEEEL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 445 EEVISNIEKANSEVKTLKIIVGSLQSELAREKHdlSETRQRNREDTREEKCTEIAKKLQEASREAEEAKSLAIAAREelr 524
Cdd:pfam01576 899 EEEQSNTELLNDRLRKSTLQVEQLTTELAAERS--TSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALE--- 973
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 525 kAKEESDEAKTGLSAVERQlmeskkemeasrASEKLALAAIKALQETeyankiedissspksiIISVEEYYELSKQAHEV 604
Cdd:pfam01576 974 -AKIAQLEEQLEQESRERQ------------AANKLVRRTEKKLKEV----------------LLQVEDERRHADQYKDQ 1024
|
410 420 430
....*....|....*....|....*....|....*
gi 332193998 605 EEAANRKLAEIVSKIEVAKEEESRILENLEEVSRE 639
Cdd:pfam01576 1025 AEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRE 1059
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
432-554 |
3.65e-04 |
|
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: 42.60 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 432 DIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETR--------------QRNREDTREEKCTE 497
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqkeiesLKRRISDLEDEILE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 332193998 498 IAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEAS 554
Cdd:COG1579 115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
325-536 |
4.06e-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: 43.21 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 325 KAKDVEKQMEGLTMEVIATKQLLElahatHLEAQEKKLDAAMAR-DQDVYNQEKELKMVEDEIKRFRQDIDAADDVKTKL 403
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELA-----ALKKEEKALLKQLAAlERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 404 KTASALQQDLRAE--IAAYKDSNMGKR----NNSDIQAAVDSA--------------------RKELEEVISNIEKANSE 457
Cdd:COG4942 96 RAELEAQKEELAEllRALYRLGRQPPLalllSPEDFLDAVRRLqylkylaparreqaeelradLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332193998 458 VKTLKIIVGSLQSELAREKHDLSETRQRNREDTREEKcTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTG 536
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
438-692 |
4.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 438 DSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSetRQRNREDTREEKCTEIAKKLQEASREAEEAKSLAi 517
Cdd:PRK03918 144 DESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIK--RTENIEELIKEKEKELEEVLREINEISSELPELR- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 518 AAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQETEyaNKIEDISSSPKSIIISVEEYYEL 597
Cdd:PRK03918 221 EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI--EELEEKVKELKELKEKAEEYIKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 598 SKQAHEVEEAANR----------KLAEIVSKIEVAKEEESRiLENLEEVSRETAIRKVELKEAMTKVEKARDGKVgmdhE 667
Cdd:PRK03918 299 SEFYEEYLDELREiekrlsrleeEINGIEERIKELEEKEER-LEELKKKLKELEKRLEELEERHELYEEAKAKKE----E 373
|
250 260
....*....|....*....|....*..
gi 332193998 668 LRKWRSDNGNRSPEGGNK--ENLSKSK 692
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKelEELEKAK 400
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
179-655 |
4.48e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 179 AHKIQTIERRKTVDQELEKIQEDmpdYKKQAVVAEEAKHQ-VVMELERTRNVVEELKLELEKAEKEEQQAKQDSDLAKLR 257
Cdd:pfam15921 84 SHQVKDLQRRLNESNELHEKQKF---YLRQSVIDLQTKLQeMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 258 VEEMEQGIAGEVSvaaksQLEVAKARHLSAVSELGTIREEIEMVSN----EYESLLT----------EKDLAAKKAEDSV 323
Cdd:pfam15921 161 KEDMLEDSNTQIE-----QLRKMMLSHEGVLQEIRSILVDFEEASGkkiyEHDSMSTmhfrslgsaiSKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 324 LKAK--DVEKQMEGLTMEVIATKQLLELAHATHLEaqekkldaamardQDVYNQEKELKMVEDEIKRFRQDidaADDVKT 401
Cdd:pfam15921 236 LKGRifPVEDQLEALKSESQNKIELLLQQHQDRIE-------------QLISEHEVEITGLTEKASSARSQ---ANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 402 KLKTasaLQQDLRAEIAAYKdsnmgkRNNSDIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSElAREKHDLSE 481
Cdd:pfam15921 300 QLEI---IQEQARNQNSMYM------RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTE-ARTERDQFS 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 482 TRQRNREDTREEKCTEIAKKLQEASREAEEAKSLAiaareelrkakeesdEAKTGLSAVERQLmesKKEMEaSRASEKLA 561
Cdd:pfam15921 370 QESGNLDDQLQKLLADLHKREKELSLEKEQNKRLW---------------DRDTGNSITIDHL---RRELD-DRNMEVQR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 562 LAAIKALQETEYANKIEDISSSPKSIIISVEEYYELSKQAHEVEEAANRKLAEIVSK---IEVAKEEESRILENLEEVSR 638
Cdd:pfam15921 431 LEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKkmtLESSERTVSDLTASLQEKER 510
|
490
....*....|....*..
gi 332193998 639 ETAIRKVELKEAMTKVE 655
Cdd:pfam15921 511 AIEATNAEITKLRSRVD 527
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
321-546 |
6.44e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 321 DSVLKAK--DVEKQMEGLTMEVIATKQLLELaHATHLEAQEKKLDAAMARDQDVYNQ----EKELKM----VEDEIKRFR 390
Cdd:PHA02562 169 DKLNKDKirELNQQIQTLDMKIDHIQQQIKT-YNKNIEEQRKKNGENIARKQNKYDElveeAKTIKAeieeLTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 391 QDIDAADDVKTKLKTASAlqqDLRAEIAAY-KDSNMGKRNN---------SDIQAAVDSARKELEEVISNIEKANSEVKT 460
Cdd:PHA02562 248 MDIEDPSAALNKLNTAAA---KIKSKIEQFqKVIKMYEKGGvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 461 LKIIVGSLQsELAREKHDL-SETRQRNREDTREEKCteiAKKLQeasREAEEAKSLAIAAREELRKAKEESDEAKTGLSA 539
Cdd:PHA02562 325 LEEIMDEFN-EQSKKLLELkNKISTNKQSLITLVDK---AKKVK---AAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
....*..
gi 332193998 540 VERQLME 546
Cdd:PHA02562 398 LVKEKYH 404
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
434-639 |
7.07e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 43.09 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 434 QAAVDSARKELEEVISNIEKANSEVKTLKIIVgslqselareKHDLSETRQRNREDTREEKCTEIAKK----LQEASREA 509
Cdd:pfam05667 334 EEELEELQEQLEDLESSIQELEKEIKKLESSI----------KQVEEELEELKEQNEELEKQYKVKKKtldlLPDAEENI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 510 EEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLME--SKKEMEASRASEKlalaaIKALQEtEYANKIEDISSSPKSI 587
Cdd:pfam05667 404 AKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEakSNKEDESQRKLEE-----IKELRE-KIKEVAEEAKQKEELY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 332193998 588 IISVEEYYELSKQAHEveEAANRKLAEIVSKIEVAKEEESRILENLEEVSRE 639
Cdd:pfam05667 478 KQLVAEYERLPKDVSR--SAYTRRILEIVKNIKKQKEEITKILSDTKSLQKE 527
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
346-542 |
1.17e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 346 LLELAHATHLEAQEKKLDAAMARDQDVYNQEKELKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRAEIAA------ 419
Cdd:COG3096 886 LADETLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAlsevvq 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 420 ------YKDSNMGKRNNSDI-----------QAAVDSARKELEEVISNIEKANSEVKTLKiivGSLQS------ELAREK 476
Cdd:COG3096 966 rrphfsYEDAVGLLGENSDLneklrarleqaEEARREAREQLRQAQAQYSQYNQVLASLK---SSRDAkqqtlqELEQEL 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 477 HDL-------SETRQRNREDTREE-------KCTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVER 542
Cdd:COG3096 1043 EELgvqadaeAEERARIRRDELHEelsqnrsRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLR 1122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
245-454 |
1.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 245 QQAKQDSDLAKLRVEEMEQGIA--GEVSVAAKSQLEVAKARHLSAVSELGTIREEIEMVSNEY--------ESLLTEKDL 314
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLEllEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 315 AAKKAEDSVLKAKDVEKQMEGLTMEVIATKQLLELAHATHLEAQEKkldaamardqdvynqekelkmVEDEIKRFRQDID 394
Cdd:COG4913 350 LERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA---------------------LEEELEALEEALA 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 395 AADDVKTKLKTAsalQQDLRAEIAAYKdsnmgkRNNSDIQAAVDSARKELEEVISNIEKA 454
Cdd:COG4913 409 EAEAALRDLRRE---LRELEAEIASLE------RRKSNIPARLLALRDALAEALGLDEAE 459
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
193-646 |
1.43e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 193 QELEKIQEDMPDYKKQAVVAEEAKHQVVMELERTRnvvEELKLELEKAEKEEQQAKQDSDLAKLRvEEMEQGIAGEVSVA 272
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLEQNKNHINNELESKE---EQLSSYEDKLFDVCGSQDEESDLERLK-EEIEKSSKQRAMLA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 273 AKSQLEVAKARHLSAVSE--------LGTIREEIEMVSNEYESLLTekdLAAKKAEDSVLKAKDVEKQMEGLTMEVIATK 344
Cdd:TIGR00606 660 GATAVYSQFITQLTDENQsccpvcqrVFQTEAELQEFISDLQSKLR---LAPDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 345 QLLELAHATHLEAQEK--KLDAAMARDQ-DVYNQEKELKMVEDEIKrfrqdidAADDVKTKLKTASALQQDLR------A 415
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKlqKVNRDIQRLKnDIEEQETLLGTIMPEEE-------SAKVCLTDVTIMERFQMELKdverkiA 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 416 EIAAYKDSNMGKRNNSDIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQS---ELAREKHDLSETRQRNR--EDT 490
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQqfEEQ 889
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 491 REEKCTEIAKKLQEASREAEEAKSLAIAAREELRkakeesdeaktglsavERQLMESKKEMEASRASEKLALAAIKALQE 570
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQ----------------EKEELISSKETSNKKAQDKVNDIKEKVKNI 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 571 TEYANKIEDISSSPKSIIISVEEyYELSKQAHEVEEAANRK------LAEIVSKIEVAKEEESRILENLEEVSRETAIRK 644
Cdd:TIGR00606 954 HGYMKDIENKIQDGKDDYLKQKE-TELNTVNAQLEECEKHQekinedMRLMRQDIDTQKIQERWLQDNLTLRKRENELKE 1032
|
..
gi 332193998 645 VE 646
Cdd:TIGR00606 1033 VE 1034
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
441-658 |
1.59e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 441 RKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRNREDTREEKctEIAKKLQEASREAEEAKSLAIAAR 520
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEA--ELAKKKAEERREAETARAEAEAAY 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 521 EELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKlalAAIKALQETEYANKIEDISSSPksiiisveeyyELSKQ 600
Cdd:COG2268 269 EIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELE---ADVRKPAEAEKQAAEAEAEAEA-----------EAIRA 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 332193998 601 AHEVEEAANRKLAEIVSKIEVAKEEESRIlENLEEVSRETAirkvelkEAMTKVEKAR 658
Cdd:COG2268 335 KGLAEAEGKRALAEAWNKLGDAAILLMLI-EKLPEIAEAAA-------KPLEKIDKIT 384
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
297-648 |
1.62e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 297 EIEMVSNEYESLLTEKDLAAKKAEDSVLKAKD-----VEKQMEGLTMEVI-ATKQLLELAHATHLEAQEKKLDAAMARDQ 370
Cdd:PTZ00440 992 EWEHFKSEIDKLNVNYNILNKKIDDLIKKQHDdiielIDKLIKEKGKEIEeKVDQYISLLEKMKTKLSSFHFNIDIKKYK 1071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 371 DVYNQE--KELK-MVEDEIKRFRQDIDAADDVKTKL---KTASALQQDLRAEIAAYKDSNMGK---------------RN 429
Cdd:PTZ00440 1072 NPKIKEeiKLLEeKVEALLKKIDENKNKLIEIKNKShehVVNADKEKNKQTEHYNKKKKSLEKiykqmektlkelenmNL 1151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 430 NSDIQAAVDSARKELEEVISN--IEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRNREDTREEKCTEIAKKLQEASR 507
Cdd:PTZ00440 1152 EDITLNEVNEIEIEYERILIDhiVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAYYDKATASYE 1231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 508 EAEEAKSLAIAAREELRKAKEeSDEAKTGLSAVERQLMESKKEMEASraseKLALAAIKALQETEYANKIEDISSSPKSI 587
Cdd:PTZ00440 1232 NIEELTTEAKGLKGEANRSTN-VDELKEIKLQVFSYLQQVIKENNKM----ENALHEIKNMYEFLISIDSEKILKEILNS 1306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332193998 588 IISVEEYyelSKQAHEVEEAANRKLAEIVSKIEVAKEEESRILENLEEVSRETAIRKVELK 648
Cdd:PTZ00440 1307 TKKAEEF---SNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEDKQIDDEIKKIEQI 1364
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
344-550 |
2.07e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 344 KQLLELAHATHLEAQEKKLDAAMARDQDVYNQEKE-LKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRA-----EI 417
Cdd:COG5185 316 EQLAAAEAEQELEESKRETETGIQNLTAEIEQGQEsLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIEStkeslDE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 418 AAYKDSNMGKRNNSDIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRNREDTREEKCTE 497
Cdd:COG5185 396 IPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 332193998 498 IAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKE 550
Cdd:COG5185 476 VRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKD 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
177-462 |
2.51e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 177 WKAHKIQTIERRKTVDQELEKIQEDMPDYKKQAVVAEEAkhqvVMELERTRNVVEELKLELEKAEKEEQQAKQDSDLAKL 256
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 257 R-VEEMEQGIAGEVSVAAksQLEVAKARHLSAVSELGTIREEIEMVSNEYESLLTEKDLAAKKAEDSVLKAKDVEKQMEG 335
Cdd:TIGR02168 306 IlRERLANLERQLEELEA--QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 336 LTMEVIATKQLLELAHATHLEAQEKKLDAAMARDQDVYNQEKEL-KMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLR 414
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 332193998 415 AEIAAYKDSNMGKRNNSDIQAAVDSARKE-LEEVISNIEKANSEVKTLK 462
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDsLERLQENLEGFSEGVKALL 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-639 |
2.80e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 355 LEAQEKKLDAAMARDQDVYNQEKELKMVEDEIKRFRQDIDAAD-------DVKTKLKTASALQQDLRAEIAAykdsnmgk 427
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeiDVASAEREIAELEAELERLDAS-------- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 428 rnNSDIQAA---VDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRNREDTREekctEIAKKLQE 504
Cdd:COG4913 684 --SDDLAALeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----LLEERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 505 ASREAEEAKsLAIAAREELRKAKEESDEAKTglsAVERQLMESKKEMEASRASEKLALAAIkalqeTEYA---NKIEDis 581
Cdd:COG4913 758 ALGDAVERE-LRENLEERIDALRARLNRAEE---ELERAMRAFNREWPAETADLDADLESL-----PEYLallDRLEE-- 826
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 332193998 582 sspksiiISVEEYYELSKQAheVEEAANRKLAEIVSKIEvakEEESRILENLEEVSRE 639
Cdd:COG4913 827 -------DGLPEYEERFKEL--LNENSIEFVADLLSKLR---RAIREIKERIDPLNDS 872
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
434-658 |
3.06e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 434 QAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSETRQRNREdtREEKCTEIAKKLQEASREAEEAK 513
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA--LEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 514 SLAIAAREELRK------------------AKEESDEAKTGLSAVERQLMESKKEMEASRAsEKLALAAIKALQETEYAN 575
Cdd:COG4942 97 AELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 576 KIEDISSSPKSIiisvEEYYELSKQAHEVEEAANRKLAEIVSKIEVAKEEESRILENLEEVSRETAIRKVELKEAMTKVE 655
Cdd:COG4942 176 LEALLAELEEER----AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
...
gi 332193998 656 KAR 658
Cdd:COG4942 252 KGK 254
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
272-659 |
3.12e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 272 AAKSQLEVAKARHLSAVSelgTIREEIEMVSNEYESLLTEKDLAAKKAEDSVLKA---KDVEKQMEGLTMEVIATKQLLE 348
Cdd:pfam15921 437 AMKSECQGQMERQMAAIQ---GKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKmtlESSERTVSDLTASLQEKERAIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 349 LAHAtHLEAQEKKLDAAMARDQDVYNQEKELKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRAEIAayKDSNMGKR 428
Cdd:pfam15921 514 ATNA-EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG--RTAGAMQV 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 429 NNSDIQAAVDSARKELEEVISNIEKANSEVKTLKIIVGSLQSELAREKHDLSEtRQRNREDTREEKcteiAKKLQEASRE 508
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSE-RLRAVKDIKQER----DQLLNEVKTS 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 509 AEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASR-------ASEKLALAAIKALQETEYANKIEDIS 581
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmeGSDGHAMKVAMGMQKQITAKRGQIDA 745
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332193998 582 SSPKSIIISvEEYYELSKQAHEVEEAANrKLAEIVSKIEVAKEEESRILENLEEVSRetairkvELKEAMTKVEKARD 659
Cdd:pfam15921 746 LQSKIQFLE-EAMTNANKEKHFLKEEKN-KLSQELSTVATEKNKMAGELEVLRSQER-------RLKEKVANMEVALD 814
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
374-658 |
3.99e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 374 NQEKELKMVEDEIKRFRQDIDAADDVKTKLKTASALQQDLRAEIAAYKDSNMGKRNNSDIQAAVDSARK-----ELEEVI 448
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKaaplaAHIKAV 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 449 SNIEKANSEVKT-LKIIVGSLQSELARE----KHDLSETRQRNREDTREEKCTEIAkklqeasREAEEAKSLaiaaREEL 523
Cdd:TIGR00618 303 TQIEQQAQRIHTeLQSKMRSRAKLLMKRaahvKQQSSIEEQRRLLQTLHSQEIHIR-------DAHEVATSI----REIS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 524 RKAKEESDEAKTglsavERQLMESKKEMEASRASEKLALAAIKALQETEYAN-KIEDISSSPKSIIISVEEYYELSKQAH 602
Cdd:TIGR00618 372 CQQHTLTQHIHT-----LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 332193998 603 EVEEAANRKLAEI-VSKIEVAKEEESRILENLEEVS-RETAIRKVELKEAMTKVEKAR 658
Cdd:TIGR00618 447 ITCTAQCEKLEKIhLQESAQSLKEREQQLQTKEQIHlQETRKKAVVLARLLELQEEPC 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-668 |
4.35e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 359 EKKLDAAMARDQDVYNQEKELKMVEDEIkrfRQDIDAADDVKTKLKTASALQQDLRaEIAAY---KDSNMGKRNNSDIQA 435
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEK---RQQLERLRREREKAERYQALLKEKR-EYEGYellKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 436 AVDSARKELEEVISNIEKANSEVKTLKIivgsLQSELAREKHDLSETRQRnredtreekctEIAKKLQEASREAEEAKSL 515
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQ----LLEELNKKIKDLGEEEQL-----------RVKEKIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 516 AIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQEteyankiedissspksiiisveEYY 595
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE----------------------ELE 367
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332193998 596 ELSKQAHEVEEAAN---RKLAEIVSKIEVAKEEESRILENLEEVSRETAIRKVELKEAMTKVEKARDGKVGMDHEL 668
Cdd:TIGR02169 368 DLRAELEEVDKEFAetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
469-559 |
5.60e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 39.39 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 469 QSELAREKHDLSETRQ-RNRED-------TREEKC----TEIAKKLQEASREAEEAKSLAI-AAREELRKAKEESDEAKT 535
Cdd:PRK06991 151 QADAARARHDARQARLrREREAaearaaaRAAASAaaaaAEASAAAAPAADDAEAKKRAIIaAALERARKKKEELAAQGA 230
|
90 100
....*....|....*....|....
gi 332193998 536 GLSAVERQLMESKKEMEASRASEK 559
Cdd:PRK06991 231 GPKNTEGVSAAVQAQIDAAEARRK 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
434-635 |
6.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 434 QAAVDSARKELEEVISNIEKANSEVKTLKiivgSLQSELAREKHDLSETRQRNREDTReekcteiAKKLQEASREAEEAK 513
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALE----AELDALQERREALQRLAEYSWDEID-------VASAEREIAELEAEL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 514 SLAIAAREELRKAKEESDEAKTGLSAVERQLmeskKEMEASRASEKLALAAIKALQETEYANKIEDISSSPKSIIISVEE 593
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEEL----DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 332193998 594 YYelskQAHEVEEAANRKLAEIVSKIEVAKEEESRILENLEE 635
Cdd:COG4913 754 RF----AAALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
484-670 |
8.59e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 484 QRNREDTREEKCTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALA 563
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 564 AIKALQEtEYANKIEDISSSPKSIIISV----EEYYELSKQAhEVEEAANRKLAEIVSKIEVAKEEESRILENLEEVSRE 639
Cdd:COG4942 98 ELEAQKE-ELAELLRALYRLGRQPPLALllspEDFLDAVRRL-QYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|.
gi 332193998 640 TAIRKVELKEAMTKVEKARDGKVGMDHELRK 670
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
501-655 |
8.89e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 501 KLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGLSAVERQLMESKKEMEASRASEKLALAAIKALQE--TEYANKIE 578
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 579 DISSSPKSIIISVEEYYElskQAHEVEEAAN--------RKLAEIVSKIEVAKEEESRILENLEEVSRETAIRKVELKEA 650
Cdd:TIGR02169 755 NVKSELKELEARIEELEE---DLHKLEEALNdlearlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
....*
gi 332193998 651 MTKVE 655
Cdd:TIGR02169 832 EKEIQ 836
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
391-568 |
9.12e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 9.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 391 QDIDAADDVKTKLKTAS----------ALQQDLRAEIAAYKDSNMGKRNNSDIQAAVDSARKELEEvisniekANSEVKT 460
Cdd:PRK11281 33 GDLPTEADVQAQLDALNkqklleaedkLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQ-------AQAELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 461 LKiivgslqselareKHDLSETRQRNRE---DTREEKCTEIAKKLQEASREAEEAKSLAIAAREELRKAKEESDEAKTGL 537
Cdd:PRK11281 106 LK-------------DDNDEETRETLSTlslRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRL 172
|
170 180 190
....*....|....*....|....*....|.
gi 332193998 538 SAVERQLMESKKEMEASRASEKLALAAIKAL 568
Cdd:PRK11281 173 QQIRNLLKGGKVGGKALRPSQRVLLQAEQAL 203
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
186-453 |
9.13e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 186 ERRKTVDQELEKIQEDMPDYKKQAVVAEEAKHQVVMELERTRNVVEELKLELEKAEKEEQQAKQDSDLAKLRVEEMEQGI 265
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 266 AgevsvAAKSQLEVAKARHLSAVSELGTIREEIEMVSNEYESLLTEKDLAAKKAEDSVLKAKDVEKQMEGLTMEVIATKQ 345
Cdd:TIGR02168 792 E-----QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 346 LLELAHA--THLEAQEKKLDAAMARDQDVY-NQEKELKMVEDEIKRFRQDIDAA-------------------------- 396
Cdd:TIGR02168 867 LIEELESelEALLNERASLEEALALLRSELeELSEELRELESKRSELRRELEELreklaqlelrleglevridnlqerls 946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332193998 397 -------DDVKTKLKTASALQQDLRAEIAAYKDS--NMGKRNNSDIQAA----------------VDSARKELEEVISNI 451
Cdd:TIGR02168 947 eeysltlEEAEALENKIEDDEEEARRRLKRLENKikELGPVNLAAIEEYeelkerydfltaqkedLTEAKETLEEAIEEI 1026
|
..
gi 332193998 452 EK 453
Cdd:TIGR02168 1027 DR 1028
|
|
| |
