|
Name |
Accession |
Description |
Interval |
E-value |
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
74-255 |
9.79e-71 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 234.03 E-value: 9.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 74 ELSKEDLIQLLSIMEGELQAREDVIHMLKTEKTKPEVLEAHYGSAEPEKVLRVLHRDAILAQEKSIGEDVYE----KPIS 149
Cdd:pfam09727 1 DLSKDDLLKLLSILEGELQARDIVIAVLKAEKVKQLLLEARYGFKYPSDPLLALQRDSELLRDQSQDEDVYEamyeKPLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 150 ELDRLEEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKEN 229
Cdd:pfam09727 81 ELEKLVEKQRETQRRMLEQLAAAEKRHRRVIRELEEEKRKHARDTAQGDDFTYLLEKERERLKQELEQEKAQQKRLEKEL 160
|
170 180
....*....|....*....|....*.
gi 530383134 230 AKRLNKLRDELVKLKSFALMLVDERQ 255
Cdd:pfam09727 161 KKLLEKLEEELSKQKQIALLLVKERK 186
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
205-738 |
1.73e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 97.83 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 205 EQERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKLKSfALMLVDERQMHIEQLGLQSQKVQdltQKLREEEEKLKA 284
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEK-EVKELEELKEEIEELEKELESLE---GSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 285 ITSKSKEDRQKLLKLEV---------DFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKA 355
Cdd:PRK03918 264 LEERIEELKKEIEELEEkvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 356 EEELQELRDKIAKGECGNS------SLMAEVENLRKRVlemegKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQ 429
Cdd:PRK03918 344 KKKLKELEKRLEELEERHElyeeakAKKEELERLKKRL-----TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 430 KRMSELEKLEEAFSKSKSEC--TQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVM 507
Cdd:PRK03918 419 KEIKELKKAIEELKKAKGKCpvCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 508 --LVDERKNM--------MEKIKQEERKVDGLNKNFKVEQGKVMDVtEKLIEESKKLLKLKSEMEEKVYNLTRERDELIG 577
Cdd:PRK03918 499 keLAEQLKELeeklkkynLEELEKKAEEYEKLKEKLIKLKGEIKSL-KKELEKLEELKKKLAELEKKLDELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 578 KLKSEEEKsselscSVDLLKKRLDGIEEVEREITRGRSRKgSELtcpeDNKIKELTLEIERLKKRLQQLEVVEGDLMKTE 657
Cdd:PRK03918 578 ELEELGFE------SVEELEERLKELEPFYNEYLELKDAE-KEL----EREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 658 DEYDQLEQKFRTEQ---------DKANFLSQQLEEIKHQIAKNKAIEKG-EVVSQEAELRHRFRLEEAKSRDLKAEVQAL 727
Cdd:PRK03918 647 KELEELEKKYSEEEyeelreeylELSRELAGLRAELEELEKRREEIKKTlEKLKEELEEREKAKKELEKLEKALERVEEL 726
|
570
....*....|.
gi 530383134 728 KEKIHELMNKE 738
Cdd:PRK03918 727 REKVKKYKALL 737
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-779 |
2.99e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.81 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 145 EKPISELDRLEEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQAR 224
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKK 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 225 KEKENAKRLNKLRDELVKLKSFALMLVDERQMHIEQlglQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFE 304
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE---AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 305 HKASRFSQEHEEMNA--KLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVEN 382
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 383 LRKRVLEMEGKDEEITKTESQCR--ELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAfsKSKSEctqlHLNLEKEK 460
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA--KKKAD----EAKKAEEA 1521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 461 NLTKDLLNELEvvKSRVKELECSESRLEKAELSLKDDLTKlksftvmlVDERKNMMEKIKQEERKVDGLNKN---FKVEQ 537
Cdd:PTZ00121 1522 KKADEAKKAEE--AKKADEAKKAEEKKKADELKKAEELKK--------AEEKKKAEEAKKAEEDKNMALRKAeeaKKAEE 1591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 538 GKVMDVTEKLIEESK-KLLKLKSEMEEKVynltrERDELIGKLKSEEEKSSELSCSVDLLKKrldgIEEVEREITRGRSR 616
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKmKAEEAKKAEEAKI-----KAEELKKAEEEKKKVEQLKKKEAEEKKK----AEELKKAEEENKIK 1662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 617 KGSELTCPEDNKIK--ELTLEIERLKKRLQQLEVVEGDLMKTEdeydQLEQKFRTEQDKANFLSQQLEE--IKHQIAKNK 692
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKaeEAKKAEEDEKKAAEALKKEAEEAKKAE----ELKKKEAEEKKKAEELKKAEEEnkIKAEEAKKE 1738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 693 AIE---KGEVVSQEAE----LRHRFRLEEAKSRDLKAEVQALkekIHELMNKEDQLSQLQVDYSVlQQRFMEEEN--KNK 763
Cdd:PTZ00121 1739 AEEdkkKAEEAKKDEEekkkIAHLKKEEEKKAEEIRKEKEAV---IEEELDEEDEKRRMEVDKKI-KDIFDNFANiiEGG 1814
|
650
....*....|....*.
gi 530383134 764 NMGQEVLNLTKELELS 779
Cdd:PTZ00121 1815 KEGNLVINDSKEMEDS 1830
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-525 |
1.10e-15 |
|
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: 82.41 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 194 MNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKEN-------AKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQ 266
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKAERYKELKAELRelelallVLRLEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 267 KVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQ---EHEEMNAKLANQESHNRQLRLKLVGLTQRIE 343
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANlerQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 344 ELEEtnkNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEMEgkdEEITKTESQCRELRKKLQEEEHHSKELRL 423
Cdd:TIGR02168 348 ELKE---ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE---LQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 424 EVEKLQKRMSELEKLEeafsksksectqLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKS 503
Cdd:TIGR02168 422 EIEELLKKLEEAELKE------------LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
330 340
....*....|....*....|..
gi 530383134 504 ftvmlvdeRKNMMEKIKQEERK 525
Cdd:TIGR02168 490 --------RLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-759 |
2.99e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 204 LEQERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLK 283
Cdd:COG1196 205 LERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 284 AITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELR 363
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 364 DKiakgecgnssLMAEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQkrmSELEKLEEAFS 443
Cdd:COG1196 365 EA----------LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE---EELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 444 KSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIkQEE 523
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL-EGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 524 RKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLDGI 603
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 604 EEVEREITRGRSRKGSELTC------PEDNKIKELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFL 677
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREadaryyVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 678 SQQLEEIKHQIAKnkaiEKGEVVSQEAELRHRFRLEEAKSRDLKAEVQALKEKIHELMNKEDQLSQLQVDYSVLQQRFME 757
Cdd:COG1196 671 LAALLEAEAELEE----LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
..
gi 530383134 758 EE 759
Cdd:COG1196 747 LL 748
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-834 |
4.16e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.49 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 197 SDDFTNLLEQERERLKKLLEQEKAYQARKEKENAKRLNKLRD-ELVKLKSFALMLVDERQMHIEQLGLQSQKVQDL--TQ 273
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaEDARKAEEARKAEDAKRVEIARKAEDARKAEEArkAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 274 KLREEEEKLKAITSKSKEDRQKllKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRlklvgltqRIEELEETNKNLQ 353
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAEELRK--AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK--------KAEEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 354 KAEEE--LQELRDKIAKGECGNSSLMAEVENLRKRVLEMEGKDEEITKTES--------QCRELRKKlQEEEHHSKELRL 423
Cdd:PTZ00121 1244 KAEEErnNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkaeekkKADEAKKK-AEEAKKADEAKK 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 424 EVEKLQKRMSELEKLEEAFSK----SKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKA-ELSLKDDL 498
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKaaeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdEAKKKAEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 499 TKLKSFTVMLVDERKNMMEKIK---QEERKVDGLNKnfKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKvynltRERDEL 575
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKkkaEEKKKADEAKK--KAEEAKKADEAKKKAEEAKKAEEAKKKAEEA-----KKADEA 1475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 576 IGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRKGSELTCPEDNKIKELTLEIERLKK---RLQQLEVVEGD 652
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKaeeKKKADELKKAE 1555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 653 LMKTEDEYDQLEQKFRTEQDKANFL-----SQQLEEIKHQIAKNKAIEKGEVVSQEA--ELRHRFRLEEA-KSRDLKAEV 724
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELkKAEEEKKKV 1635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 725 QALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEENKNKNMGQEvlnLTKELELSKRYSRALRPSVNGRRMVdvpvtstg 804
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE---AKKAEEDEKKAAEALKKEAEEAKKA-------- 1704
|
650 660 670
....*....|....*....|....*....|
gi 530383134 805 vqtDAVSGEAAEEETPAVFIRKSfQEENHI 834
Cdd:PTZ00121 1705 ---EELKKKEAEEKKKAEELKKA-EEENKI 1730
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
250-785 |
6.77e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 250 LVDERQMHIEQLGLQSQKVQDLTQKLREE-EEKLKAITSKSKEDRQ---KLLKLEVDFEHKASRFSqEHEEMNAKLANQE 325
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKElEEVLREINEISSELPElreELEKLEKEVKELEELKE-EIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 326 SHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGEcgnsSLMAEVENLRKRVLEMEgkdEEITKTESQCR 405
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI----KLSEFYEEYLDELREIE---KRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 406 ELRKKLQEEEHHS---KELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKdllnelEVVKSRVKELEC 482
Cdd:PRK03918 325 GIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP------EKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 483 SESRLEKAELSLKDDLTKLKSftvmLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKvmDVTEKLIEESKKLLKLKSEME 562
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKK----EIKELKKAIEELKKAKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 563 EKVYNLTRERDELIGKLKSEEEKSSelscsvdlLKKRLDGIEEVEreitrgrsrkgSELTCPEDNKIKELTLEIERLKKR 642
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIK--------LKELAEQLKELE-----------EKLKKYNLEELEKKAEEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 643 LQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKN--KAIEKGEVVSQEAELRHRFRLE------- 713
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfESVEELEERLKELEPFYNEYLElkdaeke 613
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383134 714 -EAKSRDLKAEVQALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEENKNKNmgqevlnlTKELELSKRYSRA 785
Cdd:PRK03918 614 lEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR--------EEYLELSRELAGL 678
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
141-696 |
1.59e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 141 EDVYEKPISELDRLEEKQK--ETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQE 218
Cdd:PRK03918 213 SSELPELREELEKLEKEVKelEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 219 KAYQARKE--KENAKRLNKLRDELVKLKSfalmLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKL 296
Cdd:PRK03918 293 EEYIKLSEfyEEYLDELREIEKRLSRLEE----EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 297 LKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQElrdkiAKGECGN--- 373
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-----AKGKCPVcgr 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 374 -----------SSLMAEVENLRKRVLEMEGKDEEITKTEsqcRELRKKLQEEEHHSKELRL--EVEKLQKRMSE--LEKL 438
Cdd:PRK03918 444 elteehrkellEEYTAELKRIEKELKEIEEKERKLRKEL---RELEKVLKKESELIKLKELaeQLKELEEKLKKynLEEL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 439 EEAfSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEK 518
Cdd:PRK03918 521 EKK-AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 519 IKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEkvynltrerdeligklkseeeksselscsvdlLKK 598
Cdd:PRK03918 600 FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE--------------------------------LRK 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 599 RLdgiEEVEREITRGRSRKGSELTCPEDNKIKELTLEIERLKKRLQQlevVEGDLMKTEDEYDQLEQKfRTEQDKANFLS 678
Cdd:PRK03918 648 EL---EELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE---IKKTLEKLKEELEEREKA-KKELEKLEKAL 720
|
570
....*....|....*...
gi 530383134 679 QQLEEIKHQIAKNKAIEK 696
Cdd:PRK03918 721 ERVEELREKVKKYKALLK 738
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
151-734 |
3.81e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 151 LDRLEE--KQKETYRRMLEQL--------LLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLE---- 216
Cdd:COG1196 202 LEPLERqaEKAERYRELKEELkeleaellLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEelel 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 217 -----QEKAYQARKEKE--------NAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLK 283
Cdd:COG1196 282 eleeaQAEEYELLAELArleqdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 284 AITSKSKEDRQKLLKLevdfEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELR 363
Cdd:COG1196 362 EAEEALLEAEAELAEA----EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 364 DkiakgecgnsslmAEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFS 443
Cdd:COG1196 438 E-------------EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 444 kSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKD-DLTKLKSFTVMLVDERKNMMEKIKQE 522
Cdd:COG1196 505 -GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDeVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 523 ERKVDGLNKNFKVEQGKVMDVTEKLIEESKKllklksemeekvynLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLDG 602
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADAR--------------YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 603 IEEVEREITRGRSRKGSELTcpEDNKIKELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLE 682
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRE--LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 530383134 683 EIKHQIAKNKAIEKGEVVSQEAELRHRFRLEEAKSRDLKAEVQALKEKIHEL 734
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-576 |
4.77e-13 |
|
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: 73.95 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 204 LEQERERLKKLLEQEKAYQARKEkenakRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQdltQKLREEEEKLK 283
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELR-----RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLK---ERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 284 AITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNA--------KLANQESHNRQLRLKLVGLTQRIEELE-ETNKNLQK 354
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlshsRIPEIQAELSKLEEEVSRIEARLREIEqKLNRLTLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 355 ---AEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEMEgkdEEITKTESQCRELRKKLqeeehhsKELRLEVEKLQKR 431
Cdd:TIGR02169 828 keyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE---EELEELEAALRDLESRL-------GDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 432 MSELEKLEEafsksksectQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLE---KAELSLkddltklksftvml 508
Cdd:TIGR02169 898 LRELERKIE----------ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipEEELSL-------------- 953
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530383134 509 vderknmmEKIKQEERKVDglnknfkVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELI 576
Cdd:TIGR02169 954 --------EDVQAELQRVE-------EEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
328-787 |
1.68e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 328 NRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKgecgnssLMAEVENLRKRVLEMEgkdEEITKTESQCREL 407
Cdd:PRK03918 143 SDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEK-------FIKRTENIEELIKEKE---KELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 408 RKKLqeeehhsKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRL 487
Cdd:PRK03918 213 SSEL-------PELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 488 EKAElSLKDDLTKLKSFtvmlvderknmMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEkvyn 567
Cdd:PRK03918 286 KELK-EKAEEYIKLSEF-----------YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE---- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 568 lTRERDELIGKLKSEEEKSSELSCSVDLLKKRLDG--IEEVEREITRGRSRKgseltcpednkiKELTLEIERLKKRLQQ 645
Cdd:PRK03918 350 -LEKRLEELEERHELYEEAKAKKEELERLKKRLTGltPEKLEKELEELEKAK------------EEIEEEISKITARIGE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 646 LEVVEGDLMKTEDEYDQLEQKFR------TEQDKANFLSQQLEEIkhqiaKNKAIEKGEVVSQEAELRHRFRlEEAKSRD 719
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGKCPvcgrelTEEHRKELLEEYTAEL-----KRIEKELKEIEEKERKLRKELR-ELEKVLK 490
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383134 720 LKAEVQALKEKIHELMNKEDQLSQLQV-DYSVLQQRFMEEENKNKNMGQEVLNLTKELELSKRYSRALR 787
Cdd:PRK03918 491 KESELIKLKELAEQLKELEEKLKKYNLeELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA 559
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-564 |
2.25e-12 |
|
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: 71.64 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 251 VDERQMHIEQLGLQSQKVQdltqKLREEEEKLKAITSKSKEDRQKLLKLEVDfEHKASRfsqehEEMNAKLANQESHNRQ 330
Cdd:TIGR02169 186 IERLDLIIDEKRQQLERLR----REREKAERYQALLKEKREYEGYELLKEKE-ALERQK-----EAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 331 LRLKLVGLTQRIEELEETNKNLQK-----AEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEMEGK----DEEITKTE 401
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKkikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERlaklEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 402 SQCRELRKKLQEEEHHSKELRLEVEKLQKRM----SELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRV 477
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELedlrAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 478 KELECSESRLEKAELSLKDDLTKLKSftvmlvdERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKL 557
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKINELEE-------EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
....*..
gi 530383134 558 KSEMEEK 564
Cdd:TIGR02169 489 QRELAEA 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-785 |
2.68e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 149 SELDRLEEKQKETYRRMLE-QLLLAEkcHRRTVYELENEKHKHT----DYMNKSDDFTNLLEQERERLKKLLEQEKAYQA 223
Cdd:TIGR02168 246 EELKEAEEELEELTAELQElEEKLEE--LRLEVSELEEEIEELQkelyALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 224 RKEkENAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDF 303
Cdd:TIGR02168 324 QLE-ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 304 ----------EHKASRFSQEHEEMNAKLANQESHNRQLRLKLV--GLTQRIEELEETNKNLQKAEEELQELRDKIAKGEC 371
Cdd:TIGR02168 403 erlearlerlEDRRERLQQEIEELLKKLEEAELKELQAELEELeeELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 372 GNSSLMAEVENLRKRVLEMEGKDE---EITKTESQCRELRKKLQEEEHHSKELRLEVEK-LQKRMSEL--EKLEEAFS-- 443
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEgvkALLKNQSGLSGILGVLSELISVDEGYEAAIEAaLGGRLQAVvvENLNAAKKai 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 444 -----KSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELecseSRLEKAELSLKDDLTKLKSfTVMLVDERKNMMEK 518
Cdd:TIGR02168 563 aflkqNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVA----KDLVKFDPKLRKALSYLLG-GVLVVDDLDNALEL 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 519 IKQE----------------------------------ERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEK 564
Cdd:TIGR02168 638 AKKLrpgyrivtldgdlvrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 565 VYNLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRKGSELTCPE--DNKIKELTLEIERLKKR 642
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeaEAEIEELEAQIEQLKEE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 643 LQQLE----VVEGDLMKTEDEYDQLEQKFRTEQDK-------ANFLSQQLEEIKHQIAKNKA------------------ 693
Cdd:TIGR02168 798 LKALRealdELRAELTLLNEEAANLRERLESLERRiaaterrLEDLEEQIEELSEDIESLAAeieeleelieeleselea 877
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 694 --IEKGEVVSQEAELRHRFRLEEAKSRDLKAEVQALKEKIHELMNK----EDQLSQLQVDYSVLQQRFMEEENKNknmGQ 767
Cdd:TIGR02168 878 llNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKlaqlELRLEGLEVRIDNLQERLSEEYSLT---LE 954
|
730
....*....|....*...
gi 530383134 768 EVLNLTKELELSKRYSRA 785
Cdd:TIGR02168 955 EAEALENKIEDDEEEARR 972
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
338-793 |
4.53e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 338 LTQRIEELEETNKNLQKAEEELQELRDKIAKgecgnssLMAEVENLRKRVLEMEgKDEEITKTESQCRELRKKLQEEEHH 417
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEE-------LEAELEELREELEKLE-KLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 418 SKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQL--HLNLEKEKNLtKDLLNELEVVKSRVKELecsESRLEKAELSLK 495
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELleQLSLATEEEL-QDLAEELEELQQRLAEL---EEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 496 DDLTKLKSFTVMLVDERKNmmEKIKQEERK------------VDGLNKNFKVEQGKVMDVTEKLI-----EESKKLLKLK 558
Cdd:COG4717 224 ELEEELEQLENELEAAALE--ERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLLallflLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 559 SEMEEKVYNLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRkgseltcpednkikELTLEIER 638
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL--------------EEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 639 LKKRLQQLevVEGDLMKTEDEYDQLEQKFRTEQDkanfLSQQLEEIKHQI-AKNKAIEKGEVVSQEAELRHRFRLEEAKS 717
Cdd:COG4717 368 LEQEIAAL--LAEAGVEDEEELRAALEQAEEYQE----LKEELEELEEQLeELLGELEELLEALDEEELEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 718 RDLKAEVQALKEKIHELmnkEDQLSQLQVD--YSVLQQRFMEEENKNKNMGQE--VLNLTKEL--ELSKRYSRALRPSVN 791
Cdd:COG4717 442 EELEEELEELREELAEL---EAELEQLEEDgeLAELLQELEELKAELRELAEEwaALKLALELleEAREEYREERLPPVL 518
|
..
gi 530383134 792 GR 793
Cdd:COG4717 519 ER 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-690 |
1.17e-11 |
|
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: 69.33 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 343 EELEETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELR 422
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 423 LEVE-KLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKnlTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKL 501
Cdd:TIGR02169 754 ENVKsELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 502 KSFTVMLVDERKNMMEKIKQEERKVDGLNKNFkveqgkvmdvtEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLKS 581
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKK-----------EELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 582 EEEKSSELSCSVDLLKKRLD----GIEEVEREITR-GRSRKGSELTCPEDNKIKELTLEIERLKKRLQQLEVVEgdlMKT 656
Cdd:TIGR02169 901 LERKIEELEAQIEKKRKRLSelkaKLEALEEELSEiEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVN---MLA 977
|
330 340 350
....*....|....*....|....*....|....
gi 530383134 657 EDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAK 690
Cdd:TIGR02169 978 IQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
213-777 |
7.69e-11 |
|
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: 66.58 E-value: 7.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 213 KLLEQEKAYQARKEKENAKRLNKLRDELVKLKSfaLMLVDERQMH-----IEQLGLQSQKVQDLTQKLREEEEKLKAITS 287
Cdd:TIGR04523 78 KILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--EIKNDKEQKNkleveLNKLEKQKKENKKNIDKFLTEIKKKEKELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 288 KSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVgltqrieeleetnkNLQKAEEELQELRDKIA 367
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS--------------NLKKKIQKNKSLESQIS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 368 KGECGNSSLMAEVENLRKrvlEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLeeaFSKSKS 447
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ---LNQLKS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 448 ECtqLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVD 527
Cdd:TIGR04523 296 EI--SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 528 GLNKNfkveqgkvmdvTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEEKSSELSCSVDLLKKRldgIEEVE 607
Cdd:TIGR04523 374 KLKKE-----------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET---IIKNN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 608 REItrgrsrkgSELTcpedNKIKELTLEIERLKKRL----QQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEE 683
Cdd:TIGR04523 440 SEI--------KDLT----NQDSVKELIIKNLDNTResleTQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 684 IKHQIaKNKAIEKGEVVSQEAELRHRFRLEEAKSRDLKAEVQALKEKIH------ELMNKEDQLSQLQVDYSVLQQRFME 757
Cdd:TIGR04523 508 LEEKV-KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkenlekEIDEKNKEIEELKQTQKSLKKKQEE 586
|
570 580
....*....|....*....|
gi 530383134 758 EENKNKNMGQEVLNLTKELE 777
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIE 606
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-501 |
8.03e-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: 66.62 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 149 SELDRLEEKQKEtyrrMLEQLLLAEKchrrtvyELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKE 228
Cdd:TIGR02168 677 REIEELEEKIEE----LEEKIAELEK-------ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 229 nAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKAS 308
Cdd:TIGR02168 746 -EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 309 RFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVL 388
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 389 EMEgkdEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAF-----SKSKSECTQLHLNLEKEKNLT 463
Cdd:TIGR02168 905 ELE---SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEaealeNKIEDDEEEARRRLKRLENKI 981
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530383134 464 KDL-------LNELEVVKSRVKELECSESRLEKAELSLKDDLTKL 501
Cdd:TIGR02168 982 KELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-481 |
1.03e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 194 MNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKENAKRLNKLRDEL---------------------VKLKSFALMLVD 252
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrkeleelsrqiSALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 253 ERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQ----------EHEEMNAKLA 322
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealdelraELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 323 NQESHNRQLRLKLVGLTQRIEELEETNKNLQKAE-------EELQELRDKIAKGECGNSSLMAEVE-NLRKRVLEMEGKD 394
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIeslaaeiEELEELIEELESELEALLNERASLEeALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 395 EEITKTESQCRELRKKLQEEEHHSKELRLEVEKL-QKRMSELEKLEEAFSksksectqlhLNLEKEKNLTKDLLNELEVV 473
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERLSEEYS----------LTLEEAEALENKIEDDEEEA 970
|
....*...
gi 530383134 474 KSRVKELE 481
Cdd:TIGR02168 971 RRRLKRLE 978
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
27-552 |
1.61e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 27 AGEKSLSEDAKKKKKSNRKEDDvmasgtvkrhLKTSGECERKTKKSLELSKEDLIQLLSIMEGELQAREDvihmlKTEKT 106
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADE----------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-----EAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 107 KPEVLEAHYGSAEPEKVLRVLHRDAilaQEKSIGEDVYEKPISELDRLEE-KQKETYRRMLEQLLLAEKCHRRTvyeleN 185
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKA---EEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEKKKA-----D 1434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 186 EKHKHTDYMNKSDDFTNLLEQER---ERLKKLLEQEKAYQARKEKENAKRLNKLRD--ELVKLKSFALMLVDERQMHIEQ 260
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKkaeEAKKKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEAKKAAEAKKKADE 1514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 261 LGLQSQKVQdlTQKLREEEEKLKAITSKSKEDRQKLLKLEvdfehKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQ 340
Cdd:PTZ00121 1515 AKKAEEAKK--ADEAKKAEEAKKADEAKKAEEKKKADELK-----KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 341 RIEE--LEETNKNLQ-----KAEEELQELRDKIAKGECGNSS-LMAEVENLRKRVLEMEGKDEEITKTESQCR----ELR 408
Cdd:PTZ00121 1588 KAEEarIEEVMKLYEeekkmKAEEAKKAEEAKIKAEELKKAEeEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaEEA 1667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 409 KKLQEEEHHSKELRLEVEKLQKRMSELEKLEEafskSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELEC-SESRL 487
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE----EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKeAEEDK 1743
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530383134 488 EKAELSLKDDLTKLKsfTVMLVDERKNMMEKIKQEERKVdgLNKNFKVEQGKVMDVTEKLIEESK 552
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKK--IAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKKIKDIF 1804
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
152-803 |
9.17e-10 |
|
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: 63.21 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 152 DRLEEKQKETYRRMleQLLLAEKCHR--RTVYELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKEN 229
Cdd:pfam15921 245 DQLEALKSESQNKI--ELLLQQHQDRieQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 230 AKRLNKLRDELVKLKSfalMLVDErqmhIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLkleVDFEHKASR 309
Cdd:pfam15921 323 ESTVSQLRSELREAKR---MYEDK----IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL---ADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 310 FSQEHEEmNAKLANQESHNR----QLRLKLVGLTQRIEELEETNKNLQ-----KAEEELQELRDKIAKGEcGNSSLMAEV 380
Cdd:pfam15921 393 LSLEKEQ-NKRLWDRDTGNSitidHLRRELDDRNMEVQRLEALLKAMKsecqgQMERQMAAIQGKNESLE-KVSSLTAQL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 381 EN----LRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKR----MSELEKL---EEAFSKSKSEC 449
Cdd:pfam15921 471 EStkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRvdlkLQELQHLkneGDHLRNVQTEC 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 450 TQLHLNLEKEKNLTKDLLNELEVVKSRVKE--LECSESRLEKAEL--SLKDDLTKLKSFTVMlvDERKNmmEKIKQEERK 525
Cdd:pfam15921 551 EALKLQMAEKDKVIEILRQQIENMTQLVGQhgRTAGAMQVEKAQLekEINDRRLELQEFKIL--KDKKD--AKIRELEAR 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 526 VDGLNKnfkveqgkvmdvteklieESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLdgiee 605
Cdd:pfam15921 627 VSDLEL------------------EKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF----- 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 606 vereitRGRSRKGSELTCPEDNKIKELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIK 685
Cdd:pfam15921 684 ------RNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 686 HQIAKNKAIEKGE--VVSQEAELRHRFRLEEAKSRD-LKAEVQALKEKIhelMNKEDQLSQLQVDYSVLQQRFMEEENKN 762
Cdd:pfam15921 758 TNANKEKHFLKEEknKLSQELSTVATEKNKMAGELEvLRSQERRLKEKV---ANMEVALDKASLQFAECQDIIQRQEQES 834
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 530383134 763 KNMGQEVLNLTKELE------LSKRYSRALRPSVNGRRMVDVPVTST 803
Cdd:pfam15921 835 VRLKLQHTLDVKELQgpgytsNSSMKPRLLQPASFTRTHSNVPSSQS 881
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-711 |
1.06e-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: 63.15 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 314 HEEMNAKLANQESHNRQLRLKLVGLTQRIEELE-----------ETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVEN 382
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEkalaelrkeleELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 383 LRKRV----LEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRM----SELEKLEEAFSKSKSECTQLHL 454
Cdd:TIGR02168 745 LEERIaqlsKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalrEALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 455 NLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFK 534
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 535 VEQGKVMDVTEKLIEESKKLLKLKSEMEEkvynLTRERDELIGKLKSEEEKSselscsvdllkkrLDGIEEVEREItrgr 614
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEG----LEVRIDNLQERLSEEYSLT-------------LEEAEALENKI---- 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 615 srkgseltcpeDNKIKELTLEIERLKKRLQQLEVVEgdlMKTEDEYDQLEQKFRteqdkanFLSQQLEEIkhqiakNKAI 694
Cdd:TIGR02168 964 -----------EDDEEEARRRLKRLENKIKELGPVN---LAAIEEYEELKERYD-------FLTAQKEDL------TEAK 1016
|
410
....*....|....*....
gi 530383134 695 EKGEVVSQE--AELRHRFR 711
Cdd:TIGR02168 1017 ETLEEAIEEidREARERFK 1035
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-734 |
1.74e-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: 62.38 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 378 AEVENLRKRVLEMEGKDEEITKtesQCRELRKKLQeeehhskELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLE 457
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEK---ALAELRKELE-------ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 458 KEKNLTKDLLNELEVvksrvkELECSESRLEKAELSLKDDLTKLKSftvmLVDERKNMMEKIKQEERKVDGLNKNFKVEQ 537
Cdd:TIGR02168 747 ERIAQLSKELTELEA------EIEELEERLEEAEEELAEAEAEIEE----LEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 538 GKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGklkseeeksselscsvdlLKKRLDGIEEVEREITRGRsrk 617
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES------------------LAAEIEELEELIEELESEL--- 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 618 gseltcpeDNKIKELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAI--E 695
Cdd:TIGR02168 876 --------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlsE 947
|
330 340 350
....*....|....*....|....*....|....*....
gi 530383134 696 KGEVVSQEAELRHRFRleEAKSRDLKAEVQALKEKIHEL 734
Cdd:TIGR02168 948 EYSLTLEEAEALENKI--EDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
181-780 |
5.69e-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: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 181 YELENEKHKHTDYMNKSDDFTNLLEQERERLKKlleqekayQARKEKENAKRLNKLRDELVKLKsfalmLVDERQMHIEQ 260
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKE--------QAKKALEYYQLKEKLELEEEYLL-----YLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 261 LglqsQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQ 340
Cdd:pfam02463 239 I----DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 341 RIEELEETNKNLQKAEEELQElrdkiakgecgnsslmaEVENLRKRVLEMEGKDEEITKTESQCRELRKKL-QEEEHHSK 419
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKE-----------------EIEELEKELKELEIKREAEEEEEEELEKLQEKLeQLEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 420 ELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLN-ELEVVKSRVKELECSESRLEKAELSLKDDL 498
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKeELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 499 TKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLiEESKKLLKLKSEMEEKVYNLTRERDELIGK 578
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR-SGLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 579 LKSEEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRKGSELTCPEDNKIKEltleierLKKRLQQLEVVEGDLMKTED 658
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKL-------PLKSIAVLEIDPILNLAQLD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 659 EYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAIEKGEVVSQEAEL---RHRFRLEEAKSRDLKAEVQALKEKIHELM 735
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGlaeKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 530383134 736 NKEDQLSQLQvDYSVLQQRFMEEENKNKNMGQEVLNLTKELELSK 780
Cdd:pfam02463 690 AKEEILRRQL-EIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
182-576 |
8.74e-09 |
|
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: 59.65 E-value: 8.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 182 ELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQaRKEKENAKRLNKLRDELVKLKSFALMLVDERQMHIEQL 261
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKI-QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 262 GLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDF---EHKASRFSQEHE-----EMNAKLANQESHNRQLRL 333
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQN 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 334 KLVGLTQRIEELEETNKNLQK----AEEELQELRDKIAKGEcgnsslmAEVENLRKrvlEMEGKDEEITKTESQCRELRK 409
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKeltnSESENSEKQRELEEKQ-------NEIEKLKK---ENQSYKQEIKNLESQINDLES 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 410 KLQEEEHHSKELRLEVEKLQKRMSELEK-----------LEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVK 478
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKeierlketiikNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 479 ELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLI---------- 548
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNkddfelkken 558
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 530383134 549 ----------------EESKKLLKLKSEMEEKVYNLTRERDELI 576
Cdd:TIGR04523 559 lekeideknkeieelkQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
345-685 |
9.39e-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: 60.07 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 345 LEETNKNLQKAEEELQELRDKI----AKGECGNS--SLMAEVENLRKRVL---------EMEGKDEEITKTESQCRELRK 409
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLksleRQAEKAERykELKAELRELELALLvlrleelreELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 410 KLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSEctqlhlnLEKEKNLTKDllnELEVVKSRVKELECSESRLEK 489
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRE---RLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 490 AELSLKDDLTKLKsftvmlvderknmmEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLT 569
Cdd:TIGR02168 331 KLDELAEELAELE--------------EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 570 RERDELIgklkseeeksselscsvdLLKKRLdgiEEVEREITRGRSRKGSELTCPEDNKIKELTLEIERLKKRL----QQ 645
Cdd:TIGR02168 397 SLNNEIE------------------RLEARL---ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeelqEE 455
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 530383134 646 LEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIK 685
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
149-776 |
1.24e-08 |
|
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: 59.26 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 149 SELDRLEEKQKETyrrmleqlllaEKCHRRTVYELENeKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKE 228
Cdd:TIGR04523 124 VELNKLEKQKKEN-----------KKNIDKFLTEIKK-KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 229 NAKRLNKLRDELVKLKSFaLMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKAS 308
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 309 RFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEE--LEETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKr 386
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 387 vlemegkdeEITKTESQCRELRKKLQEEEhhsKELRLEVEKLQKRMSELEKLEeafskskSECTQLHLNLEKEKNLTKDL 466
Cdd:TIGR04523 350 ---------ELTNSESENSEKQRELEEKQ---NEIEKLKKENQSYKQEIKNLE-------SQINDLESKIQNQEKLNQQK 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 467 LNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEK 546
Cdd:TIGR04523 411 DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 547 LIEESKKLLKL---KSEMEEKVYNLTRERDELIgklkseeeksselscsvdllkkrldgieevereitrgrsrkgseltc 623
Cdd:TIGR04523 491 LKSKEKELKKLneeKKELEEKVKDLTKKISSLK----------------------------------------------- 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 624 pedNKIKELTLEIERLKKRLQQLEVvEGDLMKTEDEYDQLEQKFRTEQdkanflsQQLEEIKHQiakNKAIEKgevvSQE 703
Cdd:TIGR04523 524 ---EKIEKLESEKKEKESKISDLED-ELNKDDFELKKENLEKEIDEKN-------KEIEELKQT---QKSLKK----KQE 585
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383134 704 aELRHRFRLEEAKSRDLKAEVQALKEKIHELmnkEDQLSQLQVDYSVLQQRFMEEENKNKNMGQEVLNLTKEL 776
Cdd:TIGR04523 586 -EKQELIDQKEKEKKDLIKEIEEKEKKISSL---EKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
121-748 |
2.06e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 121 EKVLRVLHRDAILAQEKSIGEDVY----EKP--ISELDRLEEkQKETYRRMLEQLLLAEKCHRRtvyeLENEKHKHTDYM 194
Cdd:COG4913 191 EKALRLLHKTQSFKPIGDLDDFVReymlEEPdtFEAADALVE-HFDDLERAHEALEDAREQIEL----LEPIRELAERYA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 195 NKSDDFtNLLEQERERLKKLLEQEKAYQARKEKENAKR-LNKLRDELVKLKS-FALMLVDERQMHIEQLGLQSQKVQDLT 272
Cdd:COG4913 266 AARERL-AELEYLRAALRLWFAQRRLELLEAELEELRAeLARLEAELERLEArLDALREELDELEAQIRGNGGDRLEQLE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 273 QKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRlklvgltqriEELEETNKNL 352
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALE----------EALAEAEAAL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 353 QKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLemegkdEEITKTESQCR---ELRKKLQEEEH---------HSKE 420
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSNIPARLLALRDALA------EALGLDEAELPfvgELIEVRPEEERwrgaiervlGGFA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 421 LRLEVEklqkrmselEKLEEAFSKS-KSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLE---KAELSlkd 496
Cdd:COG4913 489 LTLLVP---------PEHYAAALRWvNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRawlEAELG--- 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 497 dltklKSFTVMLVDERknmmEKIKQEERKV--DGL----------NKNFKVEQGKVM--DVTEKLIEESKKLLKLKSEME 562
Cdd:COG4913 557 -----RRFDYVCVDSP----EELRRHPRAItrAGQvkgngtrhekDDRRRIRSRYVLgfDNRAKLAALEAELAELEEELA 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 563 EkvynLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLDgIEEVEREITRGRSRKGSELTcpEDNKIKELTLEIERLKKR 642
Cdd:COG4913 628 E----AEERLEALEAELDALQERREALQRLAEYSWDEID-VASAEREIAELEAELERLDA--SSDDLAALEEQLEELEAE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 643 LQQLevvegdlmktEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAknkAIEKGEVVSQEAELRHRF------RLEEAK 716
Cdd:COG4913 701 LEEL----------EEELDELKGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFaaalgdAVEREL 767
|
650 660 670
....*....|....*....|....*....|..
gi 530383134 717 SRDLKAEVQALKEKIHelmNKEDQLSQLQVDY 748
Cdd:COG4913 768 RENLEERIDALRARLN---RAEEELERAMRAF 796
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
222-446 |
2.22e-08 |
|
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: 57.47 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 222 QARKEKENAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEV 301
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 302 DFEHKASRFSQ---------EHEEMNAKLANQESHNRQLRLKLVG-----LTQRIEELEETNKNLQKAEEELQELRDKIA 367
Cdd:COG4942 98 ELEAQKEELAEllralyrlgRQPPLALLLSPEDFLDAVRRLQYLKylapaRREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 368 KgecgnssLMAEVENLRKRV-LEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEA--FSK 444
Cdd:COG4942 178 A-------LLAELEEERAALeALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAagFAA 250
|
..
gi 530383134 445 SK 446
Cdd:COG4942 251 LK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
128-787 |
2.55e-08 |
|
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: 58.19 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 128 HRDAILAQEKSIGEDVYEKPISELdRLEEKQKETYRRMLEQL-------LLAEKCHRR----TVYELENEKHKHTdYMNK 196
Cdd:pfam05483 111 NRKIIEAQRKAIQELQFENEKVSL-KLEEEIQENKDLIKENNatrhlcnLLKETCARSaektKKYEYEREETRQV-YMDL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 197 SDDFTNLLeQERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKLksfalmlVDERQMHIEQLGLQS----QKVQDLT 272
Cdd:pfam05483 189 NNNIEKMI-LAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKE-------INDKEKQVSLLLIQItekeNKMKDLT 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 273 QKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNL 352
Cdd:pfam05483 261 FLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEEL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 353 QKAEEELQELRDKIAKGECGNSSLM-AEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRL---EVEKL 428
Cdd:pfam05483 341 NKAKAAHSFVVTEFEATTCSLEELLrTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKilaEDEKL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 429 QKRMSELEKLEEAFSKSKSECTQLHLNLEKEknlTKDLLNELEVVKSR----VKELECSESRLEKAEL---SLKDDLTKL 501
Cdd:pfam05483 421 LDEKKQFEKIAEELKGKEQELIFLLQAREKE---IHDLEIQLTAIKTSeehyLKEVEDLKTELEKEKLkniELTAHCDKL 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 502 KSFTVMLVDERKNMMEKIKQEERKVDglnkNFKVEQGKVMDVTEKLIEeskKLLKLKSEMEEKVYNLTRERDELIGKLKS 581
Cdd:pfam05483 498 LLENKELTQEASDMTLELKKHQEDII----NCKKQEERMLKQIENLEE---KEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 582 EEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRKgseltcpeDNKIKELTLEIERLKKR----LQQLEVVEGDLMKTE 657
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK--------NKNIEELHQENKALKKKgsaeNKQLNAYEIKVNKLE 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 658 DEYDQLEQKF----RTEQDKANFLSQQLEEIKHQIAKNKAIEKGEV-VSQEAELRHRFRLeeaksrdlkAEVQALKEKIH 732
Cdd:pfam05483 643 LELASAKQKFeeiiDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVkLQKEIDKRCQHKI---------AEMVALMEKHK 713
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 733 ELMNK--EDQLSQLQVDYSVLQQRFMEE---ENKNKNMGQEVLNLTKELELSKRYSRALR 787
Cdd:pfam05483 714 HQYDKiiEERDSELGLYKNKEQEQSSAKaalEIELSNIKAELLSLKKQLEIEKEEKEKLK 773
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
153-775 |
2.60e-08 |
|
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: 58.52 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 153 RLEEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNLLEQERERL-----KKLLEQEKAYQARKEK 227
Cdd:TIGR00606 287 ELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELlveqgRLQLQADRHQEHIRAR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 228 ENAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKA 307
Cdd:TIGR00606 367 DSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 308 SRFSQEHEEMNAK---LANQESHNRQLRLKLVGLTQRIEELEETNKN-----LQKAEEELQELRDKIAKGECGNSSLMAE 379
Cdd:TIGR00606 447 EILEKKQEELKFVikeLQQLEGSSDRILELDQELRKAERELSKAEKNsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQ 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 380 VENLRKRVLEMEG-------KDEEITKTESQ--------------CRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKL 438
Cdd:TIGR00606 527 LNHHTTTRTQMEMltkdkmdKDEQIRKIKSRhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQN 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 439 EEAFSKSKSECTQLHLNLEK---EKNLTKDLLNELEVVKSRVKelecsESRLEKAELSLKDDLtkLKSFTVMLVDERKNM 515
Cdd:TIGR00606 607 KNHINNELESKEEQLSSYEDklfDVCGSQDEESDLERLKEEIE-----KSSKQRAMLAGATAV--YSQFITQLTDENQSC 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 516 MEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLiEESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEEKSSELSCSVDL 595
Cdd:TIGR00606 680 CPVCQRVFQTEAELQEFISDLQSKLRLAPDKL-KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 596 LKKRL-DGIEEVEREITRGRSRKGSELTCPEDNKIKE-LTLEIERLKKRLQQLeVVEGDLMKTEDEYDQLEQKFRTEQDK 673
Cdd:TIGR00606 759 DIQRLkNDIEEQETLLGTIMPEEESAKVCLTDVTIMErFQMELKDVERKIAQQ-AAKLQGSDLDRTVQQVNQEKQEKQHE 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 674 ANFLSQQLEEIKHQIA-KNKAIE---------KGEVVSQEAELRHRFRLEEaKSRDLKAEVQALKEKIHELMNKEDQLSQ 743
Cdd:TIGR00606 838 LDTVVSKIELNRKLIQdQQEQIQhlksktnelKSEKLQIGTNLQRRQQFEE-QLVELSTEVQSLIREIKDAKEQDSPLET 916
|
650 660 670
....*....|....*....|....*....|..
gi 530383134 744 LQVDYSVLQQRFMEEENKNKNMGQEVLNLTKE 775
Cdd:TIGR00606 917 FLEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-734 |
5.28e-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: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 346 EETNKNLQKAEEELQELRDkiakgecgnssLMAEVEN------------LRKRVLEMEGKDEEITKTESQCRELRKKLQE 413
Cdd:COG1196 175 EEAERKLEATEENLERLED-----------ILGELERqleplerqaekaERYRELKEELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 414 EEHHSKELRLEVEKLQKRMSELEKLEEafsksksectQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELS 493
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELE----------ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 494 LKDDLTKLKsftvmlvDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERD 573
Cdd:COG1196 314 LEERLEELE-------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 574 ELIGKLKSEEEksselscsvdlLKKRLDGIEEVEREITRGRSRKGSELtcpEDNKIKELTLEIERLKKRLQQLEVVEgDL 653
Cdd:COG1196 387 ELLEALRAAAE-----------LAAQLEELEEAEEALLERLERLEEEL---EELEEALAELEEEEEEEEEALEEAAE-EE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 654 MKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAIEKgevVSQEAELRHRFRLEEAKSRDLKAEVQALKEKIHE 733
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
.
gi 530383134 734 L 734
Cdd:COG1196 529 L 529
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
203-741 |
5.33e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 203 LLEQERERLKKLLEQekaYQARKEKENAKRLNKLRDELvklksfalmlvDERQMHIEQlgLQSQKVQdltqkLREEEEKL 282
Cdd:PRK02224 181 VLSDQRGSLDQLKAQ---IEEKEEKDLHERLNGLESEL-----------AELDEEIER--YEEQREQ-----ARETRDEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 283 KAITSKSKEDRQKLLKLEvdfehkasrfsQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELeetnknlqkaEEELQEL 362
Cdd:PRK02224 240 DEVLEEHEERREELETLE-----------AEIEDLRETIAETEREREELAEEVRDLRERLEEL----------EEERDDL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 363 RDKIAKGECGNSSLMAEVENLRKRVLEMEGKDEE----ITKTESQCRELRKKLQEEEHHSKELRLEV-----------EK 427
Cdd:PRK02224 299 LAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLREDADDLEERAEELREEAaeleseleearEA 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 428 LQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECS----ESRLEKAEL----------- 492
Cdd:PRK02224 379 VEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATlrtaRERVEEAEAlleagkcpecg 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 493 -SLKDdltklkSFTVMLVDERKNMMEKIKQEERKVdglnknfKVEQGKVmdvtEKLIEESKKLLKLKSEMEEKvynltRE 571
Cdd:PRK02224 459 qPVEG------SPHVETIEEDRERVEELEAELEDL-------EEEVEEV----EERLERAEDLVEAEDRIERL-----EE 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 572 RDELIgklkseeeksselscsVDLLKKRLDGIEEVEREITRGRSRKGsELTCPEDNKIKELTLEIERLKKRLQQLEVVEG 651
Cdd:PRK02224 517 RREDL----------------EELIAERRETIEEKRERAEELRERAA-ELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 652 DLMKTEDEYDQLEqKFRTEQDKANFLSQQLEEIKHQIA---------KNKAIEKGEVVSQEAELRHRFRLEEAKSRDLKA 722
Cdd:PRK02224 580 KLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREalaelnderRERLAEKRERKRELEAEFDEARIEEAREDKERA 658
|
570 580
....*....|....*....|.
gi 530383134 723 E--VQALKEKIHELMNKEDQL 741
Cdd:PRK02224 659 EeyLEQVEEKLDELREERDDL 679
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
328-780 |
1.11e-07 |
|
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: 56.18 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 328 NRQLRLK--LVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGecgNSSLMAEVENLRKRVLEMEGKDEEITKTESQCR 405
Cdd:TIGR04523 51 NKEKELKnlDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKN---KDKINKLNSDLSKINSEIKNDKEQKNKLEVELN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 406 ELRKKLQEEEHHSKELRLEVEKLQ--------------KRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELE 471
Cdd:TIGR04523 128 KLEKQKKENKKNIDKFLTEIKKKEkeleklnnkyndlkKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 472 VVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEES 551
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 552 KKLLKLKSEME----EKVYNLTRE-RDELIGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRKGS---ELTc 623
Cdd:TIGR04523 288 KQLNQLKSEISdlnnQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEkqrELE- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 624 PEDNKIKELTLEIERLKKRLQQLEV----VEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAiEKGEV 699
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESqindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS-EIKDL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 700 VSQEAELRHRFRLEEAKSRDLKAEVQALKEKIHELMNKEDQLSQlqvDYSVLQQRFMEEENKNKNMGQEVLNLTKELELS 779
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
.
gi 530383134 780 K 780
Cdd:TIGR04523 523 K 523
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
263-728 |
1.15e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 263 LQSQKVQDLTQKLREEEEKLKAITSKsKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNR--QLRLKLVGLTQ 340
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 341 RIEELEEtnknlqkAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEMegKDEEITKTESQCRELRKKLQEEEHHSKE 420
Cdd:COG4717 147 RLEELEE-------RLEELRELEEELEELEAELAELQEELEELLEQLSLA--TEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 421 LRLEVEKLQKRMSELEKLEEAFSKSKSectqlhlnLEKEKNLTkdllneleVVKSRVKELECSESRLEKAELSLKDDLTK 500
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEER--------LKEARLLL--------LIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 501 LKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLK 580
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 581 SEEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRkgseltcpednkiKELTLEIERLKKRLQQLEVVEGDLMKTEDEy 660
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY-------------QELKEELEELEEQLEELLGELEELLEALDE- 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383134 661 DQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKA-IEKGEVVSQEAELRHRFRLEEAKSRDLKAEVQALK 728
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAeLEQLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
149-492 |
1.60e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 149 SELDRLEEkQKETYRRMLEQLLLAEKCHRRTVYELENekhkhtdymnksddftnlLEQERERLkklleQEKAYQARKEKE 228
Cdd:PRK02224 220 EEIERYEE-QREQARETRDEADEVLEEHEERREELET------------------LEAEIEDL-----RETIAETERERE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 229 NAK-RLNKLRDELVKLKSFALMLVDERQM---HIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFE 304
Cdd:PRK02224 276 ELAeEVRDLRERLEELEEERDDLLAEAGLddaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 305 HKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKN----LQKAEEELQELRDKIAKGECGNSSLMAEV 380
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREREAELEATL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 381 ENLRKRVLEME-----GK---------DEEITKTESQCRELRKKLQEEehhSKELRLEVEKLQKRMSELEKLEEAFSKsk 446
Cdd:PRK02224 436 RTARERVEEAEalleaGKcpecgqpveGSPHVETIEEDRERVEELEAE---LEDLEEEVEEVEERLERAEDLVEAEDR-- 510
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 530383134 447 sectqlhlnLEKEKNLTKDLLNELEVVKSRV--KELECSESRLEKAEL 492
Cdd:PRK02224 511 ---------IERLEERREDLEELIAERRETIeeKRERAEELRERAAEL 549
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
799-1154 |
1.66e-07 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 55.69 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 799 PVTSTGVQTDAVSGEAAEEETPAVfirksfQEENHIMSNLRQVGLKKPVERSSVLDRyPPAANELTMRKSWIPWMRKREN 878
Cdd:pfam05109 425 PESTTTSPTLNTTGFAAPNTTTGL------PSSTHVPTNLTAPASTGPTVSTADVTS-PTPAGTTSGASPVTPSPSPRDN 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 879 GpsiTQEKGPRTNSspghPGEVVLSPKQG--QPLHIRVTPDHENSTATLEITSPTSeeffSSTTVIPTLGNQKPRITiIP 956
Cdd:pfam05109 498 G---TESKAPDMTS----PTSAVTTPTPNatSPTPAVTTPTPNATSPTLGKTSPTS----AVTTPTPNATSPTPAVT-TP 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 957 SPN-VMPQKQKSGDT---TLGPERAMSPVTITTFSREKTPESGRGAFADRP--TSPIQIMTVS--------TSAAPAEIA 1022
Cdd:pfam05109 566 TPNaTIPTLGKTSPTsavTTPTPNATSPTVGETSPQANTTNHTLGGTSSTPvvTSPPKNATSAvttgqhniTSSSTSSMS 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 1023 VSPESqempMGRTILKVTPEKQTVPTPVRKY-----NSNANIITTEDNKIHIHLGSQFKRSPGTSGEGVSP---VITVRP 1094
Cdd:pfam05109 646 LRPSS----ISETLSPSTSDNSTSHMPLLTSahptgGENITQVTPASTSTHHVSTSSPAPRPGTTSQASGPgnsSTSTKP 721
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383134 1095 vnvtAEKEVSTGTvlrSPRNHLSSRPGASKVTSTITITPV---TTSSARGTQSVKASSFTSYE 1154
Cdd:pfam05109 722 ----GEVNVTKGT---PPKNATSPQAPSGQKTAVPTVTSTggkANSTTGGKHTTGHGARTSTE 777
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
219-666 |
2.36e-07 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 55.44 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 219 KAYQARKEKenakRLNKLRDELVKLKS---FALMLVDErqmhieQLGLQSQKVQDLTQKLReeeeKLKAITSKSKEDRQK 295
Cdd:PTZ00108 991 DLYKKRKEY----LLGKLERELARLSNkvrFIKHVING------ELVITNAKKKDLVKELK----KLGYVRFKDIIKKKS 1056
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 296 LLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQriEELEETNKNLQKAEEELQELRDKiakgecgnss 375
Cdd:PTZ00108 1057 EKITAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSLTK--EKVEKLNAELEKKEKELEKLKNT---------- 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 376 lmaEVENLRKRVLEmegkdeeitktesqcrELRKKLQEEEHHSKELRLEVEKLQKRmselekleEAFSKSKSECTQLHLN 455
Cdd:PTZ00108 1125 ---TPKDMWLEDLD----------------KFEEALEEQEEVEEKEIAKEQRLKSK--------TKGKASKLRKPKLKKK 1177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 456 LEKEKNLTKDLLNELEVVKSRvKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKV 535
Cdd:PTZ00108 1178 EKKKKKSSADKSKKASVVGNS-KRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSED 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 536 EQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEEKSSelscSVDLLKKRLDGIEEVEREITRGRS 615
Cdd:PTZ00108 1257 NDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKK----KVKKRLEGSLAALKKKKKSEKKTA 1332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 530383134 616 RKGSELTCPEDNKIKELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQK 666
Cdd:PTZ00108 1333 RKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDEDDED 1383
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
312-441 |
2.45e-07 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 54.86 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 312 QEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLqkaEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEME 391
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERL---EAEVEELEAELEEKDERIERLERELSEARSEERREI 461
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 530383134 392 GKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLqKRMSELEKLEEA 441
Cdd:COG2433 462 RKDREISRLDREIERLERELEEERERIEELKRKLERL-KELWKLEHSGEL 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
405-781 |
2.92e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 405 RELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLtkdLLNELEVVKSRVKELECSE 484
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ---LEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 485 SRLEKAELSLKDDLTKLKSftvmlvdERKNMMEKIKQEERKVDGLnknfkvEQGKVMDVTEKLIEESKKLLKLKSEMEEK 564
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEA-------RIEELEEDLHKLEEALNDL------EARLSHSRIPEIQAELSKLEEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 565 VYNLTRERDELIGKLKSEEEKSSELSCSVDLLKKRldgIEEVEREITRGRSRKGseltcpednkikELTLEIERLKKRLQ 644
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ---IKSIEKEIENLNGKKE------------ELEEELEELEAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 645 QLEVVEGDLMKtedEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAiEKGEVVSQEAELRHRFRL------EEAKSR 718
Cdd:TIGR02169 879 DLESRLGDLKK---ERDELEAQLRELERKIEELEAQIEKKRKRLSELKA-KLEALEEELSEIEDPKGEdeeipeEELSLE 954
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383134 719 DLKAEVQALKEKIHEL----MNKEDQLSQLQVDYSVLQQRFM--EEENKnknmgqEVLNLTKELELSKR 781
Cdd:TIGR02169 955 DVQAELQRVEEEIRALepvnMLAIQEYEEVLKRLDELKEKRAklEEERK------AILERIEEYEKKKR 1017
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
122-576 |
4.28e-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: 54.59 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 122 KVLRVLHRDAILAQEKSIGEDVYEKPISELDRLEEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFT 201
Cdd:pfam02463 596 VLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 202 NLLEQERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKLKsfalMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEK 281
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE----AEELLADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 282 LKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNaklanqeshNRQLRLKLvgltQRIEELEETNKNLQKAEEELQE 361
Cdd:pfam02463 752 EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKV---------EEEKEEKL----KAQEEELRALEEELKEEAELLE 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 362 LRDKIAKGEcgnsslmaevENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEa 441
Cdd:pfam02463 819 EEQLLIEQE----------EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE- 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 442 fsKSKSECTQLHLNLEKEKNLTKDllnelevVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKnMMEKIKQ 521
Cdd:pfam02463 888 --LESKEEKEKEEKKELEEESQKL-------NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK-EENNKEE 957
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 530383134 522 EERKVDGLNKNFKVEqgkvMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELI 576
Cdd:pfam02463 958 EEERNKRLLLAKEEL----GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
63-769 |
4.70e-07 |
|
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: 54.20 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 63 GECERKTKKSLELSKEDLIQLLSIME-GELQAREDVIHmlKTEKTKPEVLEAHYGSAE---PEKVLRVLHRDAILAQE-K 137
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLDQyTQLALMEFAKK--KSLHGKAELLTLRSQLLTlctPCMPDTYHERKQVLEKElK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 138 SIGEDVYEKPISE--LDRLEEKQKETYR--RMLEQLLLAEKCHRRTVYELEN---------------EKHKHTDYMNK-- 196
Cdd:TIGR00618 230 HLREALQQTQQSHayLTQKREAQEEQLKkqQLLKQLRARIEELRAQEAVLEEtqerinrarkaaplaAHIKAVTQIEQqa 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 197 SDDFTNLLEQERERLKKLLEQEKAYQARKEKENAKRL--------NKLRDELVKLKSFALMLVDER---------QMHIE 259
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLlqtlhsqeIHIRDAHEVATSIREISCQQHtltqhihtlQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 260 QLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRlKLVGLT 339
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 340 QRIEELEETNKNLQKAEEELQELRDKIAKGECGNSSLmaevenLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSK 419
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP------LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLET 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 420 -------ELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECsESRLEKAEL 492
Cdd:TIGR00618 543 seedvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC-EQHALLRKL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 493 SLKDDLTKL--------KSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEK 564
Cdd:TIGR00618 622 QPEQDLQDVrlhlqqcsQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 565 VYNLTRERDELIGKLKSEEEKSSELSCS-VDLLKKRLDGIEEVEREITRGRSRKGSELTCPEDNKIKELTLEIERLkkrl 643
Cdd:TIGR00618 702 CQTLLRELETHIEEYDREFNEIENASSSlGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTG---- 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 644 qqlevvegdlmkteDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIaknkaiekgevvsqEAELRHRFRLEEAKSRDLKAE 723
Cdd:TIGR00618 778 --------------AELSHLAAEIQFFNRLREEDTHLLKTLEAEI--------------GQEIPSDEDILNLQCETLVQE 829
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 530383134 724 VQALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEENKNKNMGQEV 769
Cdd:TIGR00618 830 EEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-491 |
7.09e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 272 TQKLREEEEKLKAITSKSKEDRQKLLKLEVdfehKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEetnKN 351
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKK----EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE---KE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 352 LQKAEEELQELRDKIAK--------GECGNSSLMAEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRL 423
Cdd:COG4942 92 IAELRAELEAQKEELAEllralyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530383134 424 EVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELevvKSRVKELECSESRLEKAE 491
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL---QQEAEELEALIARLEAEA 236
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
178-761 |
7.80e-07 |
|
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: 53.51 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 178 RTVYELENEKHKHTDYMNKSDDFTNLLEQE----RERLKKLLEQ-----EKAYQARKEKENAKRLNKLRDELVKLKSFAL 248
Cdd:TIGR00606 577 DWLHSKSKEINQTRDRLAKLNKELASLEQNknhiNNELESKEEQlssyeDKLFDVCGSQDEESDLERLKEEIEKSSKQRA 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 249 MLVDERQMH---IEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQE 325
Cdd:TIGR00606 657 MLAGATAVYsqfITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 326 SHnrqlrlklvgLTQRIEELEETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRK--------RVLEMEGKDEE- 396
Cdd:TIGR00606 737 SI----------IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltdvtimERFQMELKDVEr 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 397 -----ITKTES-----QCRELRKKLQEEEHHSKELRLEVEKLQK----RMSELEKLEEAFSKSKSECTQLHLNLEKEKNL 462
Cdd:TIGR00606 807 kiaqqAAKLQGsdldrTVQQVNQEKQEKQHELDTVVSKIELNRKliqdQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQF 886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 463 TKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMD 542
Cdd:TIGR00606 887 EEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 543 VTEK-LIEESKKLLKLKSEMEEKVYNLTRERDELigklkseeeksselscsvDLLKKRLDGIEEVEREITRGRSRKGSEl 621
Cdd:TIGR00606 967 GKDDyLKQKETELNTVNAQLEECEKHQEKINEDM------------------RLMRQDIDTQKIQERWLQDNLTLRKRE- 1027
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 622 tcpedNKIKELTLEIERLKKRLQQLEVVEgdlmkTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIaknkaiekgevVS 701
Cdd:TIGR00606 1028 -----NELKEVEEELKQHLKEMGQMQVLQ-----MKQEHQKLEENIDLIKRNHVLALGRQKGYEKEI-----------KH 1086
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530383134 702 QEAELRH-RFRLEEAKSRDLKAEVQALKEKIHELMNKEDQLSQLQVDYSVLQqrfMEEENK 761
Cdd:TIGR00606 1087 FKKELREpQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMK---MEEINK 1144
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
181-784 |
7.86e-07 |
|
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: 53.58 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 181 YELENEKHKHTDYMNKSDDFTNLLEQERERLKKLleQEKAYQARKEKENAKRLnkLRDELVKLKSFALMLVDERQMHIEQ 260
Cdd:pfam15921 57 YEVELDSPRKIIAYPGKEHIERVLEEYSHQVKDL--QRRLNESNELHEKQKFY--LRQSVIDLQTKLQEMQMERDAMADI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 261 LGLQSQKVQDLTQKLREEEEKLKAITSkSKEDR----------------------QKLLKLEVDFEHKASRFSQEHEEMN 318
Cdd:pfam15921 133 RRRESQSQEDLRNQLQNTVHELEAAKC-LKEDMledsntqieqlrkmmlshegvlQEIRSILVDFEEASGKKIYEHDSMS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 319 A----KLANQESHN-RQLRLKLVGLTQRIEELEETNKNLQ-----KAEEELQELRDK----IAKGECGNSSLMAEVENLR 384
Cdd:pfam15921 212 TmhfrSLGSAISKIlRELDTEISYLKGRIFPVEDQLEALKsesqnKIELLLQQHQDRieqlISEHEVEITGLTEKASSAR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 385 KRVLEMEGKDEEIT-KTESQCRELRKKLQEEEHHSKELRLEVEKlQKRMSE--LEKLEEAFSKSKSECTQLHLNLEKEKN 461
Cdd:pfam15921 292 SQANSIQSQLEIIQeQARNQNSMYMRQLSDLESTVSQLRSELRE-AKRMYEdkIEELEKQLVLANSELTEARTERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 462 LTKDLLNELEVVKSRVKELEcSESRLEKAELSLKDDLTKLKSFTvmlVDERKNMMEKIKQEERKVDGLNKNFKVE-QGKV 540
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKRE-KELSLEKEQNKRLWDRDTGNSIT---IDHLRRELDDRNMEVQRLEALLKAMKSEcQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 541 ---MDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRK 617
Cdd:pfam15921 447 erqMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 618 gseltcpeDNKIKEltleierlkkrLQQLEVVEGDLMKTEDEYDQLEQKFrTEQDKA-NFLSQQLEEIKhQIAKNKAIEK 696
Cdd:pfam15921 527 --------DLKLQE-----------LQHLKNEGDHLRNVQTECEALKLQM-AEKDKViEILRQQIENMT-QLVGQHGRTA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 697 GEVVSQEAELR-----HRFRLEE---------AKSRDLKAEVQALKEKIHELMNKEDQlsQLQVDYSVLQQRfMEEENKN 762
Cdd:pfam15921 586 GAMQVEKAQLEkeindRRLELQEfkilkdkkdAKIRELEARVSDLELEKVKLVNAGSE--RLRAVKDIKQER-DQLLNEV 662
|
650 660
....*....|....*....|..
gi 530383134 763 KNMGQEVLNLTKELELSKRYSR 784
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLKRNFR 684
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
190-777 |
8.35e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.52 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 190 HTDYMNKSDDFTNLLEQERERLKKLLeqekayqARKEKENAKRLNKLRDELvKLKSFALMLVDERQMHIEQLGLQSQKVQ 269
Cdd:TIGR01612 1050 HTSIYNIIDEIEKEIGKNIELLNKEI-------LEEAEINITNFNEIKEKL-KHYNFDDFGKEENIKYADEINKIKDDIK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 270 DLTQKLREEEEKLKAITSKSK----EDRQKLLKLEvDFEHKASrFSQEHEEMNAKLANqeshnrqlrlklvgLTQRIEEL 345
Cdd:TIGR01612 1122 NLDQKIDHHIKALEEIKKKSEnyidEIKAQINDLE-DVADKAI-SNDDPEEIEKKIEN--------------IVTKIDKK 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 346 EETNKNLQKAEEELQEL-RDKIAKGECGNSSlMAEVENLRKrvLEMEGKDEEITKTESQCRELR---KKLQEEEHHSKEL 421
Cdd:TIGR01612 1186 KNIYDEIKKLLNEIAEIeKDKTSLEEVKGIN-LSYGKNLGK--LFLEKIDEEKKKSEHMIKAMEayiEDLDEIKEKSPEI 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 422 RLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLN-------LEKEKNLTKDLLNELEVVKSRvKELECSESRLEKAELSL 494
Cdd:TIGR01612 1263 ENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHdenisdiREKSLKIIEDFSEESDINDIK-KELQKNLLDAQKHNSDI 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 495 KDDLTKLKS-FTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEqgkvMDVTEKLIEESKKLLKL---KSEMEEKVYNltR 570
Cdd:TIGR01612 1342 NLYLNEIANiYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDE----LDKSEKLIKKIKDDINLeecKSKIESTLDD--K 1415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 571 ERDELIGKLKSEEEKSSELSCSVDLLKKRLDGIEE----VEREITRGRSRKGSELTCPEDNKIKELTLEIERLKKRLQQL 646
Cdd:TIGR01612 1416 DIDECIKKIKELKNHILSEESNIDTYFKNADENNEnvllLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKS 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 647 EVVEGDLMKTEDEYDQLEQKFRT-EQDKANFLSQQLE-EIKHQIAKNKAiEKGEVVSQEAELRHRFRLEEAKSRDLKAEV 724
Cdd:TIGR01612 1496 KGCKDEADKNAKAIEKNKELFEQyKKDVTELLNKYSAlAIKNKFAKTKK-DSEIIIKEIKDAHKKFILEAEKSEQKIKEI 1574
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 530383134 725 QALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEENKNKNMGQEVLNLTKELE 777
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETE 1627
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
189-513 |
8.44e-07 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.54 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 189 KHTDYMNKSDDFTNL-----LEQERERLKKLLE-----QEKAYQARKEKENAKRLNKLRDELVKLKsFALMLVDERQMHI 258
Cdd:COG5022 785 RLVDYELKWRLFIKLqpllsLLGSRKEYRSYLAciiklQKTIKREKKLRETEEVEFSLKAEVLIQK-FGRSLKAKKRFSL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 259 EQ---LGLQSQ-KVQDLTQKLREEEEKLKAITS---KSKEDRQKLLKLEVDFEhkaSRFSQEHEEMNAKLANQESHNRQL 331
Cdd:COG5022 864 LKketIYLQSAqRVELAERQLQELKIDVKSISSlklVNLELESEIIELKKSLS---SDLIENLEFKTELIARLKKLLNNI 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 332 RLKLvgltQRIEELEEtNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEMEGKDEEITKTESQcrelRKKL 411
Cdd:COG5022 941 DLEE----GPSIEYVK-LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ----YGAL 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 412 QEEEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNeLEVVKSRVKELECSESRLEKAE 491
Cdd:COG5022 1012 QESTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKA-LKLRRENSLLDDKQLYQLESTE 1090
|
330 340
....*....|....*....|...
gi 530383134 492 -LSLKDDLTKLKSFTVMLVDERK 513
Cdd:COG5022 1091 nLLKTINVKDLEVTNRNLVKPAN 1113
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
182-777 |
5.20e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 182 ELENEKHKHTDYMNKSDDFTNLLEQERerlKKLLEQEKAYQARKEKENAKRlNKLRDELV----KLKSFA---LMLVDER 254
Cdd:pfam01576 72 ELEEILHELESRLEEEEERSQQLQNEK---KKMQQHIQDLEEQLDEEEAAR-QKLQLEKVtteaKIKKLEediLLLEDQN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 255 QMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEhKASRFSQEHEEMNAKLanqESHNRQLRLK 334
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLK-KEEKGRQELEKAKRKL---EGESTDLQEQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 335 LVGLTQRIEELEetnKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLE----MEGKDEEITKTESQCRELRKK 410
Cdd:pfam01576 224 IAELQAQIAELR---AQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISElqedLESERAARNKAEKQRRDLGEE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 411 LQ----EEEHHSKELRLEVEKLQKRMSELEKLEEAF-SKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSES 485
Cdd:pfam01576 301 LEalktELEDTLDTTAAQQELRSKREQEVTELKKALeEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 486 RLEKAELSLKDDLTKLKSftvmlvderknmmekikqeeRKVDGLNKNFKVEqGKVMDVTEKLIEESKKllklKSEMEEKV 565
Cdd:pfam01576 381 ALESENAELQAELRTLQQ--------------------AKQDSEHKRKKLE-GQLQELQARLSESERQ----RAELAEKL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 566 YNLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRKGSELTCPED--NKIKELTLEIERLKKRL 643
Cdd:pfam01576 436 SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDerNSLQEQLEEEEEAKRNV 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 644 Q-QLEVVEGDLM----KTEDE---YDQLEQKFRTEQDKANFLSQQLEEikhqiaKNKAIEKGEvvsqeaelRHRFRLEEa 715
Cdd:pfam01576 516 ErQLSTLQAQLSdmkkKLEEDagtLEALEEGKKRLQRELEALTQQLEE------KAAAYDKLE--------KTKNRLQQ- 580
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383134 716 KSRDLKAEVQALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEENKNKNMGQE----VLNLTKELE 777
Cdd:pfam01576 581 ELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREketrALSLARALE 646
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
338-796 |
9.08e-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: 50.07 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 338 LTQRIEELEETNKNLQKAEEELQELRDKIAKgecgNSSLMAEVENLRKRVLEMEGKDEEItktesqcRELRKKLQEEE-- 415
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEENIER----LDLIIDEKRQQLERLRREREKAERY-------QALLKEKREYEgy 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 416 ---HHSKELRLEVEKLQKRMS----ELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLL-NELEVVKSRVKELECSESRL 487
Cdd:TIGR02169 227 ellKEKEALERQKEAIERQLAsleeELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeEEQLRVKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 488 EKAELSLKDDLTKLKsftvmlvDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYN 567
Cdd:TIGR02169 307 ERSIAEKERELEDAE-------ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 568 LTRERDELigklkseeeksselscsvDLLKKRLDGIEEVEREITRGRSRKGSELtcpednkiKELTLEIERLKkrlQQLE 647
Cdd:TIGR02169 380 FAETRDEL------------------KDYREKLEKLKREINELKRELDRLQEEL--------QRLSEELADLN---AAIA 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 648 VVEGDLMKTEDEYDQLEQKFRTEQdkanflsQQLEEIKHQIAKnkaiekgevvsqeaelrhrfrlEEAKSRDLKAEVQAL 727
Cdd:TIGR02169 431 GIEAKINELEEEKEDKALEIKKQE-------WKLEQLAADLSK----------------------YEQELYDLKEEYDRV 481
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383134 728 kekihelmnkEDQLSQLQVDYSVLQQRfmeeenknknmgqevlnltkelelskrySRALRPSVNGRRMV 796
Cdd:TIGR02169 482 ----------EKELSKLQRELAEAEAQ----------------------------ARASEERVRGGRAV 512
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
182-772 |
9.45e-06 |
|
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: 50.05 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 182 ELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKEnaKRLNKLRDELVKLKSFALMLVDERQMHIEQL 261
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK--KQMEKDNSELELKMEKVFQGTDEQLNDLYHN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 262 glQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKlaNQESHNRQLRLKLVGLtQR 341
Cdd:TIGR00606 310 --HQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRAR--DSLIQSLATRLELDGF-ER 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 342 IEELEETNKNLQKAEEELQELRDKIAKGECGN--SSLMAEVENLRKRVLEMEG-------KDEEITKTESQCRELRKKLQ 412
Cdd:TIGR00606 385 GPFSERQIKNFHTLVIERQEDEAKTAAQLCADlqSKERLKQEQADEIRDEKKGlgrtielKKEILEKKQEELKFVIKELQ 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 413 EEEHHSKELRLEVEKLQKRMSELEKLEEafsKSKSECtqLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAEL 492
Cdd:TIGR00606 465 QLEGSSDRILELDQELRKAERELSKAEK---NSLTET--LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 493 SLKDDLT------KLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVY 566
Cdd:TIGR00606 540 LTKDKMDkdeqirKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 567 NLTRERDELIgklkseeeksseLSCSVDLLKKRLDGIEEvEREITRGRSRKGSELTCPEDNKIKELTLEIERLKKRLQQL 646
Cdd:TIGR00606 620 QLSSYEDKLF------------DVCGSQDEESDLERLKE-EIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 647 EVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQI---AKNKAIEKGEVVSQEAELRHRFRLEEAKSRDLKAE 723
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 530383134 724 VQALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEENKNKNMGQEVLNL 772
Cdd:TIGR00606 767 IEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
291-445 |
1.18e-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: 48.00 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 291 EDRQKLLKLEvDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEetnKNLQKAEEELQELRDKIAK-- 368
Cdd:COG1579 4 EDLRALLDLQ-ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---KEIKRLELEIEEVEARIKKye 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 369 ---GECGNS----SLMAEVENLRKRV-------LEMEGKDEEITKTESQCRELRKKLQEE-EHHSKELRLEVEKLQKRMS 433
Cdd:COG1579 80 eqlGNVRNNkeyeALQKEIESLKRRIsdledeiLELMERIEELEEELAELEAELAELEAElEEKKAELDEELAELEAELE 159
|
170
....*....|..
gi 530383134 434 ELEKLEEAFSKS 445
Cdd:COG1579 160 ELEAEREELAAK 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
149-347 |
1.39e-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: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 149 SELDRLEEKQKETyRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKE 228
Cdd:COG4942 27 AELEQLQQEIAEL-EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 229 NAKRLNKL---------------RDELVKLKSFALM--LVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKE 291
Cdd:COG4942 106 LAELLRALyrlgrqpplalllspEDFLDAVRRLQYLkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530383134 292 DRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEE 347
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
57-438 |
1.52e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 57 RHLKTSGECER---KTKKSLELSKEDLIQL----------LSIMEGELQA--------REDVIHMLKTEKTKPEVLEAHY 115
Cdd:PRK04863 283 VHLEEALELRRelyTSRRQLAAEQYRLVEMarelaelneaESDLEQDYQAasdhlnlvQTALRQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 116 GSAEPEKVLRVLHRDAILAQEK-SIGEDVYEKPISEL----DRLEEKQKET--YRRMLEQLLLAEKCHRRTVYELENEKH 188
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARaEAAEEEVDELKSQLadyqQALDVQQTRAiqYQQAVQALERAKQLCGLPDLTADNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 189 KHTDYMNKSDDFTNLLEQERERL---KKLLEQ-EKAYQA-RK-----EKENAKrlNKLRDELVKLKSFalmlvderQMHI 258
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEQKLsvaQAAHSQfEQAYQLvRKiagevSRSEAW--DVARELLRRLREQ--------RHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 259 EQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKlEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGL 338
Cdd:PRK04863 513 EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 339 TQRIEELEETNKNLQKAEEELQELRDKIakGECGNSSlmAEVENLRKRVLEMEgkdeeitktesqcRELRKKLQEEEHHS 418
Cdd:PRK04863 592 QARIQRLAARAPAWLAAQDALARLREQS--GEEFEDS--QDVTEYMQQLLERE-------------RELTVERDELAARK 654
|
410 420
....*....|....*....|.
gi 530383134 419 KELRLEVEKLQKR-MSELEKL 438
Cdd:PRK04863 655 QALDEEIERLSQPgGSEDPRL 675
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
152-527 |
1.79e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 152 DRLEEKQKETYRRMLEQLLLAEKCHRRTVYELENE----KHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKAYQArkek 227
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESRVAELKEElrqsREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEA---- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 228 enakRLNKLRDELVKLKSFALmlvdERQMHIEQLglqSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFehka 307
Cdd:pfam07888 130 ----RIRELEEDIKTLTQRVL----ERETELERM---KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF---- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 308 srfsqehEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENL---R 384
Cdd:pfam07888 195 -------QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMaaqR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 385 KRVL-EMEGKDEEITKTESQCRELRKKLQEEEHHSKELR--------LEVEKLQKRMSELEKLEEAFSKSKSECTQLHLN 455
Cdd:pfam07888 268 DRTQaELHQARLQAAQLTLQLADASLALREGRARWAQERetlqqsaeADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530383134 456 LEKEKNLtkdllnelevvkSRVkelECSESRLEKAElsLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVD 527
Cdd:pfam07888 348 LGREKDC------------NRV---QLSESRRELQE--LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
182-545 |
3.81e-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: 48.09 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 182 ELENEKHKHTDYMNKSDDFTNLLEQERERLKKLLEQEKayqaRKEKENAKRLNKLRDELVKLKSfalmLVDERQMHIEQL 261
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT----NSESENSEKQRELEEKQNEIEK----LKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 262 GLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEhkasRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQR 341
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE----RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 342 IEELEE-----------TNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEMEGKDE----EITKTESQCRE 406
Cdd:TIGR04523 463 RESLETqlkvlsrsinkIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEklesEKKEKESKISD 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 407 LRKKLQEEEHHSKELRLEVEKLQKRmSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESR 486
Cdd:TIGR04523 543 LEDELNKDDFELKKENLEKEIDEKN-KEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 530383134 487 LEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTE 545
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIE 680
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
148-696 |
4.46e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 148 ISELDRLEEKQKETYRRMLE---QLLLAEKCHRRTVYELENEKhkhTDYMNKSDDFtNLLEQERERLKKLLEQEKAYQAr 224
Cdd:PRK01156 182 ISNIDYLEEKLKSSNLELENikkQIADDEKSHSITLKEIERLS---IEYNNAMDDY-NNLKSALNELSSLEDMKNRYES- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 225 KEKENAKRLNKLRDELVKLKSfalmlVDERQMHIEQLGLQSQ--------KVQDLTQKLREEEEKLKAITSKSKEDRQKL 296
Cdd:PRK01156 257 EIKTAESDLSMELEKNNYYKE-----LEERHMKIINDPVYKNrnyindyfKYKNDIENKKQILSNIDAEINKYHAIIKKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 297 LKLEVDFehkaSRFSQEHEEMNaKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGECGNSS- 375
Cdd:PRK01156 332 SVLQKDY----NDYIKKKSRYD-DLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDa 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 376 LMAEVENLRKRVLEMEGKdeeITKTESQCRELRKKLQEEEHHSKELR-----------LEVEKLQKRM----SELEKLEE 440
Cdd:PRK01156 407 IKKELNEINVKLQDISSK---VSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttLGEEKSNHIInhynEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 441 AFSKSKSECTQLHlnlEKEKNLtKDLLNELEvvKSRVKELECSESRLEKAELSLKDDLTKL-----KSFTVMLVDERKNM 515
Cdd:PRK01156 484 KIREIEIEVKDID---EKIVDL-KKRKEYLE--SEEINKSINEYNKIESARADLEDIKIKInelkdKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 516 MEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEEKSSELSCSVDL 595
Cdd:PRK01156 558 LKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 596 LKKRLDGIEEVEREITRGRSRKgSELTCPEDNKiKELTLEIERLKKRLQQlevVEGDLMKTEDEYDQLEQKFRTEQDKAN 675
Cdd:PRK01156 638 IQENKILIEKLRGKIDNYKKQI-AEIDSIIPDL-KEITSRINDIEDNLKK---SRKALDDAKANRARLESTIEILRTRIN 712
|
570 580
....*....|....*....|.
gi 530383134 676 FLSQQLEEIKHQIAKNKAIEK 696
Cdd:PRK01156 713 ELSDRINDINETLESMKKIKK 733
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
204-784 |
7.31e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 204 LEQERERLKKLLEQEKAYQARKEKEnaKRlnKLRDELVKLKSfalMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLK 283
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQ--RR--DLGEELEALKT---ELEDTLDTTAAQQELRSKREQEVTELKKALEEETR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 284 AITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKnlqKAEEELQELR 363
Cdd:pfam01576 342 SHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRK---KLEGQLQELQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 364 DKIAKGECGN-------SSLMAEVENLRKRVLEMEGKD----EEITKTESQCRELRKKLQEEEHH-----SKELRLEVEK 427
Cdd:pfam01576 419 ARLSESERQRaelaeklSKLQSELESVSSLLNEAEGKNiklsKDVSSLESQLQDTQELLQEETRQklnlsTRLRQLEDER 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 428 --LQKRMSELEKLEEAFSK-----------SKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSL 494
Cdd:pfam01576 499 nsLQEQLEEEEEAKRNVERqlstlqaqlsdMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 495 KDDLTKLksftVMLVDERKNMMEKIKQEERKVDGLNKNFKVeqgkvmdVTEKLIEESKKLLKLKSEMEEKVYNLTRERDE 574
Cdd:pfam01576 579 QQELDDL----LVDLDHQRQLVSNLEKKQKKFDQMLAEEKA-------ISARYAEERDRAEAEAREKETRALSLARALEE 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 575 LIGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREITRgrSRKGSEltcpedNKIKELTLEIERLKKRLQQLE------V 648
Cdd:pfam01576 648 ALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER--SKRALE------QQVEEMKTQLEELEDELQATEdaklrlE 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 649 VEGDLMKTEDEYD------QLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAIEK---GEVVSQEAELRHRFRLEEAKSRD 719
Cdd:pfam01576 720 VNMQALKAQFERDlqardeQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKkleLDLKELEAQIDAANKGREEAVKQ 799
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530383134 720 LKAEVQALKEKIHELmnKEDQLSQlqvDYSVLQQRfmEEENKNKNMGQEVLNLTKELELSKRYSR 784
Cdd:pfam01576 800 LKKLQAQMKDLQREL--EEARASR---DEILAQSK--ESEKKLKNLEAELLQLQEDLAASERARR 857
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
73-768 |
7.38e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 73 LELSKEDLIQLLSIMEGELQAREDVIHMLKTEKTKPEV----LEAHYGSAE--------------------PEKVLRVLH 128
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQhiqdLEEQLDEEEaarqklqlekvtteakikklEEDILLLED 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 129 RDAILAQEKSIGEDVYEKPISELDRLEEKQKE------TYRRMLEQLLLAEKCHRRTVYELENEKHkhtdymnKSDDFTN 202
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSlsklknKHEAMISDLEERLKKEEKGRQELEKAKR-------KLEGEST 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 203 LLEQERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKlKSFALMLVDERQMHIEQLG-------LQSQKVQDLTQKL 275
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQ-KNNALKKIRELEAQISELQedleserAARNKAEKQRRDL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 276 REEEEKLKA-------ITSKSKEDR----QKLLKLEVDFEHKASRFSQEHEEMNAKlanqesHNRQlrlkLVGLTQRIEE 344
Cdd:pfam01576 298 GEELEALKTeledtldTTAAQQELRskreQEVTELKKALEEETRSHEAQLQEMRQK------HTQA----LEELTEQLEQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 345 LEETNKNLQKAEEELqelrdkiakgECGNSSLMAEVENLRKRVLEMEGKDEeitKTESQCRELRKKLQEEEHHSKELrle 424
Cdd:pfam01576 368 AKRNKANLEKAKQAL----------ESENAELQAELRTLQQAKQDSEHKRK---KLEGQLQELQARLSESERQRAEL--- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 425 VEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDllnelevvksrVKELECSESRlEKAELSlkddlTKLKSf 504
Cdd:pfam01576 432 AEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD-----------TQELLQEETR-QKLNLS-----TRLRQ- 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 505 tvmLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLlklkSEMEEKVYNLTRErdeligklkseee 584
Cdd:pfam01576 494 ---LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL----EALEEGKKRLQRE------------- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 585 ksselscsVDLLKKRLDGIEEVEREITRGRSRKGSEL---TCPEDNKiKELTLEIERLKKRLQQLEVVEGDL-MKTEDEY 660
Cdd:pfam01576 554 --------LEALTQQLEEKAAAYDKLEKTKNRLQQELddlLVDLDHQ-RQLVSNLEKKQKKFDQMLAEEKAIsARYAEER 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 661 DQLEQKFRTEQDKANFLSQQLEE---IKHQIAKNKAIEKGE----VVSQEAELRHRFRLEEAKsRDLKAEVQALKEKIHE 733
Cdd:pfam01576 625 DRAEAEAREKETRALSLARALEEaleAKEELERTNKQLRAEmedlVSSKDDVGKNVHELERSK-RALEQQVEEMKTQLEE 703
|
730 740 750
....*....|....*....|....*....|....*....
gi 530383134 734 LMNK----EDQLSQLQVDYSVLQQRFMEEENKNKNMGQE 768
Cdd:pfam01576 704 LEDElqatEDAKLRLEVNMQALKAQFERDLQARDEQGEE 742
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
259-781 |
8.66e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 259 EQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSqEHEEMNAKLANQEshnRQLRLKLVGL 338
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCA-EAEEMRARLAARK---QELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 339 TQRIEELEETNKNLQ----KAEEELQELRDKIAKGECGNSSLM-------AEVENLRKRVLEMEGKDEEITKT----ESQ 403
Cdd:pfam01576 81 ESRLEEEEERSQQLQnekkKMQQHIQDLEEQLDEEEAARQKLQlekvtteAKIKKLEEDILLLEDQNSKLSKErkllEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 404 CRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELevvKSRVKELECS 483
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL---QAQIAELRAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 484 esrLEKAELSLKDDLTKLKSFTVmlvdERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEE 563
Cdd:pfam01576 238 ---LAKKEEELQAALARLEEETA----QKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 564 KVyNLTRERDELigklkseeekSSELSCSVDLLKKRLDgieeverEITRGRSRKGSELTCPEDNKIKELTLEIERLKKRL 643
Cdd:pfam01576 311 TL-DTTAAQQEL----------RSKREQEVTELKKALE-------EETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 644 QQLE----VVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEI--KHQIAKNKAIEKGEVVSQ-EAELR---HRFRLE 713
Cdd:pfam01576 373 ANLEkakqALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELqaRLSESERQRAELAEKLSKlQSELEsvsSLLNEA 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383134 714 EAKSRDLKAEVQALKEKIH---ELMNKEDQ--------LSQLQVDYSVLQQRFMEEENKNKNMGQEVLNLTKELELSKR 781
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQdtqELLQEETRqklnlstrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
266-572 |
1.02e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 266 QKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEvdfeHKASRFSQEHEEMNAKLanqeshnRQLRLKLVGLtqrIEEL 345
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELN----EELKELAEKRDELNAQV-------KELREEAQEL---REKR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 346 EETNKNLQKAEEELQELRDKIakgecgnSSLMAEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEV 425
Cdd:COG1340 67 DELNEKVKELKEERDELNEKL-------NELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 426 EKLQKRMSELEKLEEAfsksksectqlhlnlEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFT 505
Cdd:COG1340 140 EKIKELEKELEKAKKA---------------LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEA 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530383134 506 VMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRER 572
Cdd:COG1340 205 DELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
150-421 |
1.17e-04 |
|
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: 46.27 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 150 ELDRL-EEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKsddftnllEQERERLKKLLEQEKAyqaRKEKE 228
Cdd:pfam17380 349 ELERIrQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ--------ELEAARKVKILEEERQ---RKIQQ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 229 NAKRLNKLRDELVKLKSFAL-MLVDERQMHIEQLGLQSQKVQDLTQKLREEEEklkaitskskEDRQKLLKLEvdfehKA 307
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVrRLEEERAREMERVRLEEQERQQQVERLRQQEE----------ERKRKKLELE-----KE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 308 SRFSQEHEEMNAKLANQESHNRQlrlklvgltQRIEELEETNKNLQKAEEELQ-----ELRDKIAKGECGNSSLMAEVEN 382
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERK---------QAMIEEERKRKLLEKEMEERQkaiyeEERRREAEEERRKQQEMEERRR 553
|
250 260 270
....*....|....*....|....*....|....*....
gi 530383134 383 LRKRVLEMEGKDEEITKTESQcRELRKKLQEEEHHSKEL 421
Cdd:pfam17380 554 IQEQMRKATEERSRLEAMERE-REMMRQIVESEKARAEY 591
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
204-363 |
1.27e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 204 LEQERERLKKLLEQ-EKAYQARKEKEN-----------AKRLNKLRDELVKLKSFALMLVDERQMHIEQLG--------- 262
Cdd:COG3206 180 LEEQLPELRKELEEaEAALEEFRQKNGlvdlseeakllLQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalpel 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 263 LQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEvdfEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRI 342
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALR---AQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
170 180
....*....|....*....|.
gi 530383134 343 EELEETNKNLQKAEEELQELR 363
Cdd:COG3206 337 AQLEARLAELPELEAELRRLE 357
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
378-492 |
1.28e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 378 AEVENLRKRVLeMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLE 457
Cdd:PRK12704 49 KEAEAIKKEAL-LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 530383134 458 KEK----NLTKDLLNELEVV--------KSRV-KELEcSESRLEKAEL 492
Cdd:PRK12704 128 KKEeeleELIEEQLQELERIsgltaeeaKEILlEKVE-EEARHEAAVL 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
259-503 |
1.32e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 259 EQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNaklanqeshnrqlrlklvgl 338
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELT-------------------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 339 tqriEELEETNKNLQKAEEELQELRDKIAKgecgnssLMAEVENLRKrVLEMEGKDEEITKTESQCRELRKKLQEEEHHS 418
Cdd:PHA02562 241 ----DELLNLVMDIEDPSAALNKLNTAAAK-------IKSKIEQFQK-VIKMYEKGGVCPTCTQQISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 419 KELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELEcSESRLEKAELS-LKDD 497
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQ-AEFVDNAEELAkLQDE 387
|
....*.
gi 530383134 498 LTKLKS 503
Cdd:PHA02562 388 LDKIVK 393
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
337-481 |
1.37e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.39 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 337 GLTQRIEELEETNKNLQKAEEELQELRDKIAKGecgNSSLMAEVENLRKRVLEMEGKDEEITKtesqcrELRKKLQEEEH 416
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRDR---KDALEEELRQLKQLEDELEDCDPTELD------RAKEKLKKLLQ 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530383134 417 HSKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDL-LNELEVVKSRVKELE 481
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFtFKEIEKLKEQLKLLQ 284
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
635-757 |
1.50e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 635 EIERLKKRLQQLEVvegdlmktedEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKnkaiekgEVVSQEAELRHRFRLEE 714
Cdd:COG3206 264 VIQQLRAQLAELEA----------ELAELSARYTPNHPDVIALRAQIAALRAQLQQ-------EAQRILASLEAELEALQ 326
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 530383134 715 AKSRDLKAEVQALKEKIHELMNKEDQLSQLQVDYSVLQQRFME 757
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
852-1094 |
2.64e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 45.45 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 852 VLDRYPpAANELTMRKSWIPWMR----------------KRENGPSITQEKGPRTNSSPGHPGEVVLSPKqgQPLHIRVT 915
Cdd:PTZ00449 454 IKDRIP-ANNDIYMLKFDEYWTRiskiqftqeikklikkSKKKLAPIEEEDSDKHDEPPEGPEASGLPPK--APGDKEGE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 916 PDH----ENSTATLEITSPTSEEFFSSTTVIPTLGNQKP-RITIIPSPNVMPQKQKSGDTTLGPERAMSPVTITTFSREK 990
Cdd:PTZ00449 531 EGEhedsKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPsKIPTLSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPK 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 991 TPEsgRGAFADRPTSPIQIMTVSTSAAPAEiAVSPESQEMPMGRTILKvTPEKQTVPTP--------------VRKYNSN 1056
Cdd:PTZ00449 611 SPK--LPELLDIPKSPKRPESPKSPKRPPP-PQRPSSPERPEGPKIIK-SPKPPKSPKPpfdpkfkekfyddyLDAAAKS 686
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 530383134 1057 ANIITTE--DNKIHIHLGSQFKRSPGTSGEGVSPVITVRP 1094
Cdd:PTZ00449 687 KETKTTVvlDESFESILKETLPETPGTPFTTPRPLPPKLP 726
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
202-417 |
3.02e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 202 NLLEQERERLKKLLEQEKAyqarKEKENAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEK 281
Cdd:PHA02562 191 DHIQQQIKTYNKNIEEQRK----KNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 282 LKAitskskeDRQKLLKLEVDFE--HKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEEL 359
Cdd:PHA02562 267 IKS-------KIEQFQKVIKMYEkgGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530383134 360 QELRDKIAKGECGNSSLMAEVENLRKRVLEMEG----KDEEITKTESQCRELRKKLQE---EEHH 417
Cdd:PHA02562 340 LELKNKISTNKQSLITLVDKAKKVKAAIEELQAefvdNAEELAKLQDELDKIVKTKSElvkEKYH 404
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
237-777 |
3.59e-04 |
|
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: 44.73 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 237 RDELVKLKSFALMLVDErqmhIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEE 316
Cdd:pfam05557 1 RAELIESKARLSQLQNE----KKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 317 MN-AKLANQESHNRQLRLKlvglTQRIEELEETNKNLQKaeeELQELRDKIAKGECGNSSLMAEVENLRKRVLEMEGKDE 395
Cdd:pfam05557 77 LNrLKKKYLEALNKKLNEK----ESQLADAREVISCLKN---ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 396 EITKTESQCRELRKKLQEEEHHSKEL----------RLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLN------LEKE 459
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELefeiqsqeqdSEIVKNSKSELARIPELEKELERLREHNKHLNENienkllLKEE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 460 KNLTKDLLNELEVVKSRVKELECSESRLE-------KAELSLKDDLTK---LKSFTVMLVDERKNMMEKIKQEERKVDGL 529
Cdd:pfam05557 230 VEDLKRKLEREEKYREEAATLELEKEKLEqelqswvKLAQDTGLNLRSpedLSRRIEQLQQREIVLKEENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 530 NKNFKVEQGKVMDVTEKLIEESKKLLKLKS---EMEEKVYNLTRERDELIGKLKSEEEKSSELSCSVDLLkKRLDGIEEV 606
Cdd:pfam05557 310 EKARRELEQELAQYLKKIEDLNKKLKRHKAlvrRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLL-ERIEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 607 EREITRGRSRKGSELTCPEDN----KIKELTLEIERLKKRLQQLevvEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLE 682
Cdd:pfam05557 389 TQKMQAHNEEMEAQLSVAEEElggyKQQAQTLERELQALRQQES---LADPSYSKEEVDSLRRKLETLELERQRLREQKN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 683 EIKHQIAKNKAIEKGEVVSQEAeLRHR-------FRLEEAKSRDLKAEVQALKEKIHELMNKEDQLSQLQVDYSVLQQRf 755
Cdd:pfam05557 466 ELEMELERRCLQGDYDPKKTKV-LHLSmnpaaeaYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFK- 543
|
570 580
....*....|....*....|..
gi 530383134 756 meeenknknmgqEVLNLTKELE 777
Cdd:pfam05557 544 ------------EVLDLRKELE 553
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
298-675 |
3.71e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 298 KLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKgecgnsslm 377
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY--------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 378 aeVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLE 457
Cdd:pfam02463 226 --LLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 458 KEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKvdglnknfkveQ 537
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL-----------E 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 538 GKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEEKSSELSCSvdllKKRLDGIEEVEREITRGRSRK 617
Cdd:pfam02463 373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKE----ELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 530383134 618 GSELTCPEDNKIKELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKAN 675
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKAR 506
|
|
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
395-513 |
3.90e-04 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 42.59 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 395 EEITKTESQCRELRKKLQEeehhskeLRLEVEKLQKRMS---ELEKLEEAFSKSKSECTQLHLNLEKEKnltkdLLNELE 471
Cdd:pfam09727 80 AELEKLVEKQRETQRRMLE-------QLAAAEKRHRRVIrelEEEKRKHARDTAQGDDFTYLLEKERER-----LKQELE 147
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530383134 472 VVKSRVKELEcseSRLEKAELSLKDDLTKLKSFTVMLVDERK 513
Cdd:pfam09727 148 QEKAQQKRLE---KELKKLLEKLEEELSKQKQIALLLVKERK 186
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
429-764 |
4.17e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 429 QKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSL-KDDLTKLKSFTVM 507
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLnEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 508 LVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDEL------IGKLKS 581
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLkesekeKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 582 EEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRKGSELTCPEDNKIKELTLEIERLKKRLQQLEVVEGDLMKTEDEYD 661
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 662 QLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAIEKGEVVSQEAELRHRFRLEEAKSRDLK-AEVQALKEKIHELMNKEDQ 740
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKkSEDLLKETQLVKLQEQLEL 488
|
330 340
....*....|....*....|....
gi 530383134 741 LSQLQVDYSVLQQRFMEEENKNKN 764
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVL 512
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
198-478 |
4.29e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 198 DDFTNLLEQERERLKKLLEQEKAYQARKEKENAKR-------------LNKLRDELVKLKSF--------ALMLVDERQM 256
Cdd:pfam06160 107 EELDELLESEEKNREEVEELKDKYRELRKTLLANRfsygpaidelekqLAEIEEEFSQFEELtesgdyleAREVLEKLEE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 257 HIEQLGLQSQKVQDLTQKLREE-EEKLKAItsksKEDRQKLLKLEVDFEHKAsrFSQEHEEMNAKLANQESHNRQLRLK- 334
Cdd:pfam06160 187 ETDALEELMEDIPPLYEELKTElPDQLEEL----KEGYREMEEEGYALEHLN--VDKEIQQLEEQLEENLALLENLELDe 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 335 ----LVGLTQRIEELEETnknLQK-------AEEELQELRDKIAKGECGNSSLMAEVENLRKR-------VLEMEGKDEE 396
Cdd:pfam06160 261 aeeaLEEIEERIDQLYDL---LEKevdakkyVEKNLPEIEDYLEHAEEQNKELKEELERVQQSytlneneLERVRGLEKQ 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 397 ITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSectqlhlNLEKEKNLTKDLLNELEVVKSR 476
Cdd:pfam06160 338 LEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQ-------SLRKDELEAREKLDEFKLELRE 410
|
..
gi 530383134 477 VK 478
Cdd:pfam06160 411 IK 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
212-437 |
6.29e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 212 KKLLEQEKAYQARKEKENAKRLNKLRDELVKLKSFALMLVDErqmHIEQLGLQSQKVQDLTQKLREEEEKLKaiTSKSKE 291
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE---ELLELLDRIEELQELLREAEELEEELQ--LEELEQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 292 DRQKLLKL-----EVDFEHKASRFSQEHE------EMNAKLANQESHNRQLrLKLVGLTQRIEELEETNKNLQKAEEELQ 360
Cdd:COG4717 371 EIAALLAEagvedEEELRAALEQAEEYQElkeeleELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELE 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530383134 361 ELRDKIAKgecgnsslmaevenLRKRVLEMEgKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEK 437
Cdd:COG4717 450 ELREELAE--------------LEAELEQLE-EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
253-414 |
6.89e-04 |
|
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: 44.17 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 253 ERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEvDFEHKASRFSQEHEEMNAKLANQESHNRQLR 332
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-ELEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 333 LKLVGLTQRIEELEETNKNLQKAEEELQELRDKIakGECGNSSlmAEVENLRKRVLEMEgkdEEITKTESQCRELRKKLQ 412
Cdd:COG3096 585 QQLEQLRARIKELAARAPAWLAAQDALERLREQS--GEALADS--QEVTAAMQQLLERE---REATVERDELAARKQALE 657
|
..
gi 530383134 413 EE 414
Cdd:COG3096 658 SQ 659
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
312-728 |
7.50e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.13 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 312 QEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEME 391
Cdd:pfam19220 3 QRNELLRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 392 GkdeEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKleeafsksksectQLHLNLEKEKNLT---KDLLN 468
Cdd:pfam19220 83 G---ELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALER-------------QLAAETEQNRALEeenKALRE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 469 ELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSftvmLVDErknMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLI 548
Cdd:pfam19220 147 EAQAAEKALQRAEGELATARERLALLEQENRRLQA----LSEE---QAAELAELTRRLAELETQLDATRARLRALEGQLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 549 EESKKLLKLKSEMEEKVYNLTRERDELigklkseeeksselSCSVDLLKKRLDGIEEVEREiTRGRSRKGSELTCPEDNK 628
Cdd:pfam19220 220 AEQAERERAEAQLEEAVEAHRAERASL--------------RMKLEALTARAAATEQLLAE-ARNQLRDRDEAIRAAERR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 629 IKELTLEIERLKKRlqqLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEeikhqiAKNKAIEKGE-----VVSQE 703
Cdd:pfam19220 285 LKEASIERDTLERR---LAGLEADLERRTQQFQEMQRARAELEERAEMLTKALA------AKDAALERAEeriasLSDRI 355
|
410 420
....*....|....*....|....*....
gi 530383134 704 AELRHRFRLE----EAKSRDLKAEVQALK 728
Cdd:pfam19220 356 AELTKRFEVEraalEQANRRLKEELQRER 384
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
265-470 |
8.43e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 265 SQKVQDLTQKLREEEEKLKAITSKSKEdrqkllkleVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEE 344
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGL---------VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 345 LEETNKNLQkAEEELQELRDKIAKgecgnssLMAEVENLRKRVLE----MEGKDEEITKTESQCR-ELRKKLQEEEHHSK 419
Cdd:COG3206 252 GPDALPELL-QSPVIQQLRAQLAE-------LEAELAELSARYTPnhpdVIALRAQIAALRAQLQqEAQRILASLEAELE 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530383134 420 ELRLEVEKLQKRMSELEKLEEAFSKSKSEctqlHLNLEKEKNLTKDLLNEL 470
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAE----LRRLEREVEVARELYESL 370
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
206-465 |
1.00e-03 |
|
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: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 206 QERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKLksfaLMLVDERQMHIEQLGLQSQ--KVQDLT-QKLREEEEKL 282
Cdd:pfam05667 243 RKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAEL----LSSFSGSSTTDTGLTKGSRftHTEKLQfTNEAPAATSS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 283 KAITSKSKEDRQKLLKLEVD-FEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQE 361
Cdd:pfam05667 319 PPTKVETEEELQQQREEELEeLQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPD 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 362 LRDKIAKgecgnssLMAEVENLRKRVLEMEGKDEEITKTE-SQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEklEE 440
Cdd:pfam05667 399 AEENIAK-------LQALVDASAQRLVELAGQWEKHRVPLiEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVA--EE 469
|
250 260
....*....|....*....|....*.
gi 530383134 441 AFSKSksectQLHLNLEKE-KNLTKD 465
Cdd:pfam05667 470 AKQKE-----ELYKQLVAEyERLPKD 490
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
199-575 |
1.23e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 43.22 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 199 DFTNLLEQERERLKKLleqekayqarKEKENAKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKV------QDLT 272
Cdd:pfam18971 403 DFMEFLAQNNTKLDNL----------SEKEKEKFQNEIEDFQKDSKAYLDALGNDRIAFVSKKDTKHSALitefnnGDLS 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 273 QKLREEEEKlkaitSKSKEDRQKLLKLEVDFEHKASRFSqehEEMNAKLANQESHNRqlrlKLVGLTQRIEELEE----- 347
Cdd:pfam18971 473 YTLKDYGKK-----ADKALDREKNVTLQGSLKHDGVMFV---DYSNFKYTNASKNPN----KGVGATNGVSHLEAgfnkv 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 348 ----------------TNKNLQKAEE----ELQELRDKIAKGECGNSSLMAEVENLRKRVLEME--GKDEEITKTEsqcR 405
Cdd:pfam18971 541 avfnlpdlnnlaitsfVRRNLENKLTakglSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKstGNYDEVKKAQ---K 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 406 ELRKKLQEEEHHSKELRlevEKLQKRMSELEKLeEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELecsES 485
Cdd:pfam18971 618 DLEKSLRKREHLEKEVE---KKLESKSGNKNKM-EAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKREL---SD 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 486 RLEKAELSLKDdltKLKSFtvmlvDERKNmmekikqeerkvdGLNKNF-KVEQgkvmdvTEKLIEESKKLLKLKSEMEEK 564
Cdd:pfam18971 691 KLEKISKDLKD---FSKSF-----DEFKN-------------GKNKDFsKAEE------TLKALKGSVKDLGINPEWISK 743
|
410
....*....|.
gi 530383134 565 VYNLTRERDEL 575
Cdd:pfam18971 744 VENLNAALNEF 754
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
192-448 |
1.40e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 192 DYMNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKENAKrLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDL 271
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ-VKELREEAQELREKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 272 TQKLREEEEKLKAITSKS---KEDRQKLLKLEVDFEHKASRFSQEheemnaklanqeshnRQLRLKLVGLTQRIEELE-- 346
Cdd:COG1340 91 REELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEEE---------------KELVEKIKELEKELEKAKka 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 347 -ETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEMEGKDEEITK----TESQCRELRKKLQEEEHHSKEL 421
Cdd:COG1340 156 lEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKeadeLHKEIVEAQEKADELHEEIIEL 235
|
250 260
....*....|....*....|....*..
gi 530383134 422 RLEVEKLQKRMSELEKLEEAFSKSKSE 448
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALKREKEK 262
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
262-553 |
1.44e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 262 GLQSQKVQDLTQKLREEEEK---LKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNA--KLANQE-SHNRQLRLKL 335
Cdd:PLN02939 124 QLSDFQLEDLVGMIQNAEKNillLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDAriKLAAQEkIHVEILEEQL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 336 VGLTQRIEELEETNKNLQKA-EEELQELRDKiakgecgNSSLMAEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEE 414
Cdd:PLN02939 204 EKLRNELLIRGATEGLCVHSlSKELDVLKEE-------NMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLREL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 415 EHHSKELRLEVEKLQKR-----MSELEKLEEAFSKSKSECTQLHLNLEKEKnltkDLLNELEVVKSRVKELECSESRLEK 489
Cdd:PLN02939 277 ESKFIVAQEDVSKLSPLqydcwWEKVENLQDLLDRATNQVEKAALVLDQNQ----DLRDKVDKLEASLKEANVSKFSSYK 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530383134 490 AELSLKddltKLKsftvmLVDERknmMEKIKQEERKVDGLNKNFKVEqgkVMDVTEKLIEESKK 553
Cdd:PLN02939 353 VELLQQ----KLK-----LLEER---LQASDHEIHSYIQLYQESIKE---FQDTLSKLKEESKK 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
628-785 |
1.61e-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: 42.06 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 628 KIKELTLEIERLKKRLQQLE----VVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAK--------NKAIE 695
Cdd:COG4942 42 ELAALKKEEKALLKQLAALErriaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlGRQPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 696 KGEVVSQE--AELRHRFRLEEAKSRDLKAEVQALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEENKNKNMGQEVLNLT 773
Cdd:COG4942 122 LALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170
....*....|..
gi 530383134 774 KELELSKRYSRA 785
Cdd:COG4942 202 ARLEKELAELAA 213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
596-777 |
1.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 596 LKKRLDGIEEVEREITRGRSRKGSELtcpEDNKIKELTLEIERLKKRLQQLEVVEGDLmktEDEYDQLEQKFRTEQdkan 675
Cdd:COG4913 267 ARERLAELEYLRAALRLWFAQRRLEL---LEAELEELRAELARLEAELERLEARLDAL---REELDELEAQIRGNG---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 676 flSQQLEEIKHQIAKNKAiEKGEVVSQEAELRHRFR---LEEAKSRD----LKAEVQALKEKIHELMNK--------EDQ 740
Cdd:COG4913 337 --GDRLEQLEREIERLER-ELEERERRRARLEALLAalgLPLPASAEefaaLRAEAAALLEALEEELEAleealaeaEAA 413
|
170 180 190
....*....|....*....|....*....|....*..
gi 530383134 741 LSQLQVDYSVLQQRFMEEENKNKNMGQEVLNLTKELE 777
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
425-529 |
1.73e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 39.99 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 425 VEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRLEKAELSLKDDLTKLKSf 504
Cdd:pfam11559 44 LQQRDRDLEFRESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKN- 122
|
90 100
....*....|....*....|....*
gi 530383134 505 tvMLVDERKNMMEKIKQEERKVDGL 529
Cdd:pfam11559 123 --ALQQIKTQFAHEVKKRDREIEKL 145
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
44-450 |
1.79e-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: 42.65 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 44 RKEDDVMASGTVKRHLKTSGECERKTKKSLELSKEDLIQLLSIMEGELQAREDVIHMLktekTKPEVLEAHYGSAEPEKV 123
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL----QNITVRLQDLTEKLSEAE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 124 LRVLHRDAILAQEKSIGEDVYEKpiseldRLEEKQKETYrrmlEQLLLAEKchrrTVYELENEKHKHTDYMNKSDDFTNL 203
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLQDV------RLHLQQCSQE----LALKLTAL----HALQLTLTQERVREHALSIRVLPKE 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 204 LEQERERLKKLLEQEKAYQARKEKENAKRLNKLRDELVKLKSFalmlvdERQMHIEQLGLQSQKvqdltQKLREEEEKLK 283
Cdd:TIGR00618 674 LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY------DREFNEIENASSSLG-----SDLAAREDALN 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 284 AITSKSKEDRQKLLKLEVDFEHKASrfsqEHEEMNAKLANQESHNRQlrlklvGLTQRIEELEETNKNLQKAEEEL-QEL 362
Cdd:TIGR00618 743 QSLKELMHQARTVLKARTEAHFNNN----EEVTAALQTGAELSHLAA------EIQFFNRLREEDTHLLKTLEAEIgQEI 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 363 RDKIAKGECGNSSLMAEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQ-KRMSELEKLEEA 441
Cdd:TIGR00618 813 PSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNgINQIKIQFDGDA 892
|
....*....
gi 530383134 442 FSKSKSECT 450
Cdd:TIGR00618 893 LIKFLHEIT 901
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
251-524 |
1.98e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 251 VDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQ 330
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 331 LRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGE--CGNSSL-----------MAEVENLRKRVLEMEGKDEEI 397
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrQQTEVLspeeekelvekIKELEKELEKAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 398 TKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSEctqLHLNLEKEKNLTKDLLNELEVVKSRV 477
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE---LHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 530383134 478 KELECSESRLEKAELSLKDDLTKLKSFtvmlvDERKNMMEKIKQEER 524
Cdd:COG1340 240 RELRKELKKLRKKQRALKREKEKEELE-----EKAEEIFEKLKKGEK 281
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
155-481 |
2.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 155 EEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYmNKSDDFTNLLEQERERLKKLLEQEKAYQARKEKENA--KR 232
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY-QELEALEAELAELPERLEELEERLEELRELEEELEEleAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 233 LNKLRDELV-KLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSK---------SKEDRQKLLKLEVD 302
Cdd:COG4717 172 LAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleqleneleAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 303 F-----------------------------------------EHKASRFSQEHEEMNAKLANQESHNRQLR--LKLVGLT 339
Cdd:COG4717 252 LliaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKEAEELQALPALEELEEEELEelLAALGLP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 340 ------------QRIEELEETNKNLQKAEEELQ--ELRDKIAK--GECGNSSLmAEVENLRKRVLEMEGKDEEITKTESQ 403
Cdd:COG4717 332 pdlspeellellDRIEELQELLREAEELEEELQleELEQEIAAllAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 404 CRELRKKLQE--EEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTkDLLNELEVVKSRVKELE 481
Cdd:COG4717 411 LEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA-ELLQELEELKAELRELA 489
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
129-755 |
2.60e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 129 RDAIlAQEKSIGEDVYEKPISELDRLEEKQKETYRRmlEQLLLAEKchrrtvyeLENEKHKHTDYMNKSDDFTNLlEQER 208
Cdd:pfam12128 403 REAR-DRQLAVAEDDLQALESELREQLEAGKLEFNE--EEYRLKSR--------LGELKLRLNQATATPELLLQL-ENFD 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 209 ERLKKLleQEKAYQARKEKENAKR----LNKLRDELVKLKSFALMLVDERQMHIEQLGLQ-SQKVQDLTQKLREEEEKLK 283
Cdd:pfam12128 471 ERIERA--REEQEAANAEVERLQSelrqARKRRDQASEALRQASRRLEERQSALDELELQlFPQAGTLLHFLRKEAPDWE 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 284 AITSKSKeDRQKLLKLEVDFEHKASRFSQEHEEMNAKLanqeshnrqlRLKLVGLTQRIEELEETNKNLQKAEEELQELR 363
Cdd:pfam12128 549 QSIGKVI-SPELLHRTDLDPEVWDGSVGGELNLYGVKL----------DLKRIDVPEWAASEEELRERLDKAEEALQSAR 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 364 DKIAKGECGNSSLMAEVENLRKRvlemegkdEEITKTESQCRELRKKlqeeehhskelRLEVEKlqkrMSELEKLEEAFS 443
Cdd:pfam12128 618 EKQAAAEEQLVQANGELEKASRE--------ETFARTALKNARLDLR-----------RLFDEK----QSEKDKKNKALA 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 444 KSKSECTQLHLNLEKEKNLtkdLLNELEVVKSRVKElECSESRLEKAELSLkddltklksftvMLVDERKNMMEKIKQEe 523
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQ---LDKKHQAWLEEQKE-QKREARTEKQAYWQ------------VVEGALDAQLALLKAA- 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 524 rkVDGLNKNFKVEQgkvmdvtEKLIEESKKLLKLKSEMEEKVYNLTRERDELIgklkseeeksselscsvdllkKRLDGI 603
Cdd:pfam12128 738 --IAARRSGAKAEL-------KALETWYKRDLASLGVDPDVIAKLKREIRTLE---------------------RKIERI 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 604 EEVEREITRGR---------SRKGSELTCPEDN-KIKELTLEIERL----KKRLQQLEVVEGDLMKTEDEYDQLEQKFRT 669
Cdd:pfam12128 788 AVRRQEVLRYFdwyqetwlqRRPRLATQLSNIErAISELQQQLARLiadtKLRRAKLEMERKASEKQQVRLSENLRGLRC 867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 670 EQDKANFLS--QQLEEIKHQIAKN-------KAIEKGEVVSQEAELRHRFRLEEAKSRDLKAEV-QALKEKIHELMNKED 739
Cdd:pfam12128 868 EMSKLATLKedANSEQAQGSIGERlaqledlKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETwESLREEDHYQNDKGI 947
|
650
....*....|....*.
gi 530383134 740 QLSQLQVDYSVLQQRF 755
Cdd:pfam12128 948 RLLDYRKLVPYLEQWF 963
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
355-560 |
2.79e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 355 AEEELQELRDKIakgecgnSSLMAEVENLRKRVLEMegkDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSE 434
Cdd:COG3883 14 ADPQIQAKQKEL-------SELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 435 L-EKLEE-AFSKSKSECTQLHLNLEKEKNLTKDLLNELEVV-------KSRVKELECSESRLEKAELSLKDDLTKLKSFT 505
Cdd:COG3883 84 RrEELGErARALYRSGGSVSYLDVLLGSESFSDFLDRLSALskiadadADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530383134 506 VMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSE 560
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
535-777 |
2.89e-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: 41.97 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 535 VEQGKVMDVTE-------KLIEESKKLLKLKSEMEEKVYNLTRERDELigklkseeeksselscsvdllkKRLDGI-EEV 606
Cdd:TIGR02168 141 IEQGKISEIIEakpeerrAIFEEAAGISKYKERRKETERKLERTRENL----------------------DRLEDIlNEL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 607 EREItrGRSRKGSELTcpedNKIKELTLEIERLKKRLQQLEVVE--GDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEI 684
Cdd:TIGR02168 199 ERQL--KSLERQAEKA----ERYKELKAELRELELALLVLRLEElrEELEELQEELKEAEEELEELTAELQELEEKLEEL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 685 KHQIAK-------------NKAIEKGEVVSQEAELRHRFRLEEAKSRDLKAEVQALKEKIHELMNK----EDQLSQLQVD 747
Cdd:TIGR02168 273 RLEVSEleeeieelqkelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEElaelEEKLEELKEE 352
|
250 260 270
....*....|....*....|....*....|
gi 530383134 748 YSVLQQRFMEEENKNKNMGQEVLNLTKELE 777
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLE 382
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-575 |
3.25e-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: 41.29 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 374 SSLMAEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEK----LEEAFSKSKSEC 449
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaaLEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 450 TQLHLNLEKEKNLTKDLLNELEVVkSRVKELecsesrleKAELSLKDDLTKLKSFTVM--LVDERKNMMEKIKQEERKVD 527
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRL-GRQPPL--------ALLLSPEDFLDAVRRLQYLkyLAPARREQAEELRADLAELA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 530383134 528 GLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDEL 575
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
631-740 |
3.30e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 631 ELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAIEKGEVVSQ--EAELRH 708
Cdd:PRK12705 78 ELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKllDAELEE 157
|
90 100 110
....*....|....*....|....*....|..
gi 530383134 709 rfrleeaksrDLKAEVQALKEKIHELMNKEDQ 740
Cdd:PRK12705 158 ----------EKAQRVKKIEEEADLEAERKAQ 179
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
204-575 |
3.37e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 204 LEQERERLKKLLEQEKAYQARKEkENAKRLNKLRDELVKLKSF--ALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEK 281
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 282 LKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKaEEELQE 361
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 362 LRDKIAKGE---------CGNSSLMAEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRm 432
Cdd:COG4717 241 LEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 433 sELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNELEvvkSRVKELECSESRLEKAELSLKDDLTKLKSFT--VMLVD 510
Cdd:COG4717 320 -ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAE---ELEEELQLEELEQEIAALLAEAGVEDEEELRaaLEQAE 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530383134 511 ERKNMMEKIKQEERKVDGLNKNFKVEQGKVmdVTEKLIEESKKLLKLKSEMEEKVYNLTRERDEL 575
Cdd:COG4717 396 EYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAEL 458
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
508-747 |
3.48e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 508 LVDERKNMMEKIKQEERKVDGLN---KNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEE 584
Cdd:COG1340 13 LEEKIEELREEIEELKEKRDELNeelKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 585 KSSELSCSVDLLKKRLDGIEEVEREITRGRSRKGSELTCPED-----NKIKELTLEIERLKKRLQQLEvvegDLMKTEDE 659
Cdd:COG1340 93 ELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEekelvEKIKELEKELEKAKKALEKNE----KLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 660 YDQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKaiEKGEVVSQEA-ELRHRFRLEEAKSRDLKAEVQALKEKIHELMNKE 738
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAQELHEEMIELY--KEADELRKEAdELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246
|
....*....
gi 530383134 739 DQLSQLQVD 747
Cdd:COG1340 247 KKLRKKQRA 255
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
204-368 |
3.74e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 204 LEQERERLKKLLEQekayqARKEKENAKRLNKL--RDELVKLKSFALMLVDERQmhieqlglqsQKVQDLTQKLREEEEK 281
Cdd:PRK12704 33 IKEAEEEAKRILEE-----AKKEAEAIKKEALLeaKEEIHKLRNEFEKELRERR----------NELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 282 LKAITSKSKEDRQKLLKLEVDFEHKASRFSQEHEEMNAKLANQeshnRQLRLKLVGLTQR------IEELE-----ETNK 350
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQ----LQELERISGLTAEeakeilLEKVEeearhEAAV 173
|
170
....*....|....*...
gi 530383134 351 NLQKAEEELQELRDKIAK 368
Cdd:PRK12704 174 LIKEIEEEAKEEADKKAK 191
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
72-742 |
4.34e-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: 41.21 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 72 SLELSKEDLIQLLSIMEGELQAREDVIHMLKTE----------KTKPEVLEAHYGSAEPEKVLRVLHRDAILAQEKSIGE 141
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKikdlgeeeqlRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 142 DV----YEKPISELDRleekQKETYRRMLEQlLLAEKCHRRTVYElenekhkhtdymnksdDFTNLLEQERERLKKLLEQ 217
Cdd:TIGR02169 328 EAeidkLLAEIEELER----EIEEERKRRDK-LTEEYAELKEELE----------------DLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 218 EKAYQarkekenaKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLL 297
Cdd:TIGR02169 387 LKDYR--------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 298 KLEVDFEhkasRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRdkiaKGECGNSSLM 377
Cdd:TIGR02169 459 QLAADLS----KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASI----QGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 378 AEVENLRKRVLEMEG---------KDEEITKtesQCRELRK-------------KLQEEEHHSKELRLE----------- 424
Cdd:TIGR02169 531 GSVGERYATAIEVAAgnrlnnvvvEDDAVAK---EAIELLKrrkagratflplnKMRDERRDLSILSEDgvigfavdlve 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 425 ------------------VEKL--------QKRMSELEKleEAFSKSKSeCTQLHLNLEKEKNLTKDLLNELEVVKSRVK 478
Cdd:TIGR02169 608 fdpkyepafkyvfgdtlvVEDIeaarrlmgKYRMVTLEG--ELFEKSGA-MTGGSRAPRGGILFSRSEPAELQRLRERLE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 479 ELECSESRL--EKAEL-SLKDDLTKLKSFTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLL 555
Cdd:TIGR02169 685 GLKRELSSLqsELRRIeNRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 556 KLKSEMEEKVYNLTRErdeligklkseeeksselscsvdllkkrldgIEEVEREITRGRSRKgseltcpEDNKIKELTLE 635
Cdd:TIGR02169 765 ARIEELEEDLHKLEEA-------------------------------LNDLEARLSHSRIPE-------IQAELSKLEEE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 636 IERLKKRLQQLevvEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAiEKGEVVSQEAELRHRFRLEEA 715
Cdd:TIGR02169 807 VSRIEARLREI---EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG-KKEELEEELEELEAALRDLES 882
|
730 740
....*....|....*....|....*..
gi 530383134 716 KSRDLKAEVQALKEKIHELMNKEDQLS 742
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELE 909
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
148-362 |
4.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 148 ISELDRLEEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTN--LLEQERERLKKLLEQ-------- 217
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEagvedeee 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 218 --EKAYQARKEKENAKRLNKLRDELVKLKSFALMLVDErqmhiEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQK 295
Cdd:COG4717 387 lrAALEQAEEYQELKEELEELEEQLEELLGELEELLEA-----LDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383134 296 LLKLEVDfeHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKN--LQKAEEELQEL 362
Cdd:COG4717 462 LEQLEED--GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPpvLERASEYFSRL 528
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
235-365 |
5.41e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 40.39 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 235 KLRDELVKLKSFALMLVDERQMHI----EQLGLQSQKVQDLTQKL-REEEEklkaiTSKSKEDRQKLLKLEVDFEHKASR 309
Cdd:pfam04849 182 KLRSEASHLKTETDTYEEKEQQLMsdcvEQLSEANQQMAELSEELaRKMEE-----NLRQQEEITSLLAQIVDLQHKCKE 256
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 530383134 310 FSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETnknLQKAEEELQELRDK 365
Cdd:pfam04849 257 LGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGM---LHEAQEELKELRKK 309
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
517-752 |
5.52e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 517 EKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERDELIGKLKSEEEKSSELSCSVDLL 596
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 597 KKRLDGIEEvereitrgrsrKGSELTC-----PEDNKIKELTLEIERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQ 671
Cdd:PHA02562 275 QKVIKMYEK-----------GGVCPTCtqqisEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 672 DKanfLSQQLEEIKHQIAKNKAIEKgevVSQEAELRHRFRLEEaksrdLKAEVQALKEKIHELMNKEDQLSQLQVDYSVL 751
Cdd:PHA02562 344 NK---ISTNKQSLITLVDKAKKVKA---AIEELQAEFVDNAEE-----LAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
.
gi 530383134 752 Q 752
Cdd:PHA02562 413 K 413
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
272-565 |
5.55e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 272 TQKLREEEEKLKAITSKSKEDRQKLLKLEVDfehkasrfsqeheEMNAKLANQESHNRQLRLKLVGLTQRIEELEEtnkN 351
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAKESSSKPSELALN-------------EMIEKLKKEIDLEYTEAVIAMGLQERLENLRE---E 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 352 LQKAEEELQ----ELRDKIAK---------GECGN-SSLMAEVENLR---KRVLEMEGKDeeitKTESQCRELRKKLQE- 413
Cdd:PLN03229 495 FSKANSQDQlmhpVLMEKIEKlkdefnkrlSRAPNyLSLKYKLDMLNefsRAKALSEKKS----KAEKLKAEINKKFKEv 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 414 -EEHHSKElRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKE-KNLTKDLLNELEVVKSRVKELECS---ESRLE 488
Cdd:PLN03229 571 mDRPEIKE-KMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIELElAGVLKSMGLEVIGVTKKNKDTAEQtppPNLQE 649
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530383134 489 KAElSLKDDLTKlKSFTVMLVDERKNMMEKIKQEERKVdglnknfkveqGKVMDVTEKlieesKKLLKLKSEMEEKV 565
Cdd:PLN03229 650 KIE-SLNEEINK-KIERVIRSSDLKSKIELLKLEVAKA-----------SKTPDVTEK-----EKIEALEQQIKQKI 708
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
459-794 |
6.05e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 459 EKNLT--KDLLNELEvvkSRVKELEcSESrlEKAE--LSLKDDLTKLKSFtvMLVDERKNMMEKIKQEERKVDGLNKNFK 534
Cdd:COG1196 185 EENLErlEDILGELE---RQLEPLE-RQA--EKAEryRELKEELKELEAE--LLLLKLRELEAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 535 VEQGKVMDVTEKLIEESKKLLKLKSEMEEKvynltRERDELIGKLkseeeksselscsvdllkkrldgIEEVEREITRGR 614
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEA-----QAEEYELLAE-----------------------LARLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 615 SRkgseltcpednkIKELTLEIERLKKRL-----------QQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEE 683
Cdd:COG1196 309 ER------------RRELEERLEELEEELaeleeeleeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 684 IKHQIAK------NKAIEKGEVVSQEAELRHRFRLEEAKSRDLKAEVQALKEKIHELMNKEDQLSQLQVDysvLQQRFME 757
Cdd:COG1196 377 AEEELEElaeellEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAE 453
|
330 340 350
....*....|....*....|....*....|....*..
gi 530383134 758 EENKNKNMGQEVLNLTKELELSKRYSRALRPSVNGRR 794
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
338-481 |
6.28e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 338 LTQRIEELEETNKnlqkaeeELQELRDKIAKGECGNSSLMAEVENLRKRVLEME-----------GKDEEITKTESQCRE 406
Cdd:PRK09039 48 ISGKDSALDRLNS-------QIAELADLLSLERQGNQDLQDSVANLRASLSAAEaersrlqallaELAGAGAAAEGRAGE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 407 LRKKLQEEEHHSKELRLEVEKLQKRMSELEK----LEEAFSKSKSEctqlhlnlEKEKNLT-KDLLNELEV-VKSRVKEL 480
Cdd:PRK09039 121 LAQELDSEKQVSARALAQVELLNQQIAALRRqlaaLEAALDASEKR--------DRESQAKiADLGRRLNVaLAQRVQEL 192
|
.
gi 530383134 481 E 481
Cdd:PRK09039 193 N 193
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
230-735 |
6.31e-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: 40.71 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 230 AKRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQSQKVQDLTQKLREEEEKLKAITSKSKEDRQKLLKLEVDFEHKASR 309
Cdd:COG5185 106 LIKLPNYEWSADILISLLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 310 FSQEHEEMNAKLANQEshnrqlrlKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLE 389
Cdd:COG5185 186 LGLLKGISELKKAEPS--------GTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 390 MEGKDEEITktESQCRELRKKLQEEEHHSKELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHlNLEKEKNLTKDLLNE 469
Cdd:COG5185 258 LVEQNTDLR--LEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLA-AAEAEQELEESKRET 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 470 LEVVKSRVKELECSESRLEKAELSLKDDLTKLksFTVMLVDERKNMMEKIKQEerkvdgLNKNFKVEQGKVMDVTEKLIE 549
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLTENLEAIKEEIENI--VGEVELSKSSEELDSFKDT------IESTKESLDEIPQNQRGYAQE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 550 ESKKLLKLKSEMEEKVYNLTRE-RDELIGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREITRGRSRKGSELTCPEDNK 628
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQiEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEE 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 629 IKELTLEIERLKKRLQQLEV-VEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAKNKAIEKGEVVSQEAELR 707
Cdd:COG5185 487 LTQIESRVSTLKATLEKLRAkLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLR 566
|
490 500
....*....|....*....|....*...
gi 530383134 708 HRFRLEEAKSRDLKAEVQALKEKIHELM 735
Cdd:COG5185 567 TAVIDELTQYLSTIESQQAREDPIPDQA 594
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
340-690 |
6.35e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 340 QRIEELEETNK--NLQKAEEELQELRDKIAKGEcgnsslmAEVENLRKRVLEMEGKDE----EITKTESQCRELRKKLQE 413
Cdd:pfam06160 67 ELLFEAEELNDkyRFKKAKKALDEIEELLDDIE-------EDIKQILEELDELLESEEknreEVEELKDKYRELRKTLLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 414 EEHHSKELrleVEKLQKRMSELEKLEEAFSKSKSECtqlhlNLEKEKNLTKDLLNELEVVKSRVKELEcseSRLEKAELS 493
Cdd:pfam06160 140 NRFSYGPA---IDELEKQLAEIEEEFSQFEELTESG-----DYLEAREVLEKLEEETDALEELMEDIP---PLYEELKTE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 494 LKDDLTKLKS-FTVMLVD----ERKNMMEKIKQEERKVDGLNKNfkVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVY-- 566
Cdd:pfam06160 209 LPDQLEELKEgYREMEEEgyalEHLNVDKEIQQLEEQLEENLAL--LENLELDEAEEALEEIEERIDQLYDLLEKEVDak 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 567 -NLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLdGIEEVEREITRGRSRKGSELtcpeDNKIKELTLEI--------- 636
Cdd:pfam06160 287 kYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSY-TLNENELERVRGLEKQLEEL----EKRYDEIVERLeekevayse 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530383134 637 --ERLKKRLQQLEVVEGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQIAK 690
Cdd:pfam06160 362 lqEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEK 417
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
593-780 |
6.61e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 593 VDLLKKRLDGIEEVEREITRGRSRKgSELtcpeDNKIKELTLEIERLKKRLQQLEVVEgDLMKTEDEYDQLEQKFRTEQD 672
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEEL-EEL----EEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 673 KANFLSQQLEEIKHQIAKNKAIEkgevvsQEAElRHRFRLEEAKSRDLKAEVQALKEKIHELMNKEDQLSQLQVDYSVLQ 752
Cdd:COG4717 147 RLEELEERLEELRELEEELEELE------AELA-ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180
....*....|....*....|....*...
gi 530383134 753 QRFMEEENKNKNMGQEVLNLTKELELSK 780
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKE 247
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
294-573 |
7.57e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 294 QKLLKLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQELRDKIAKGECGN 373
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 374 SSLMAEVEN----LRKRVLEMEGKDEEITKTESQCRELRKklqEEEHHSKELRLeveKLQKRMSELEKLEEAFSKSKSEC 449
Cdd:pfam07888 128 EARIRELEEdiktLTQRVLERETELERMKERAKKAGAQRK---EEEAERKQLQA---KLQQTEEELRSLSKEFQELRNSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 450 TQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRL----EKAELS------LKDDLTKLKS---------------- 503
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELrslqERLNASerkvegLGEELSSMAAqrdrtqaelhqarlqa 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530383134 504 --FTVMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEKVYNLTRERD 573
Cdd:pfam07888 282 aqLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKD 353
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
347-564 |
7.70e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 347 ETNKNLQKAEEELQELRDKIAKGECGNSSLMAEVENLRKRVLEMEGK-------DEEITKTESQCRELRKKLQEEEHHSK 419
Cdd:pfam17380 313 ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKrelerirQEEIAMEISRMRELERLQMERQQKNE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 420 ELRLEVEKLQKRMSELEKLEEAFSKSKSECTQLHLNLEKEKNLTKDLLNElevvkSRVKELEcsesRLEKAELSLKDDLT 499
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE-----ERAREME----RVRLEEQERQQQVE 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530383134 500 KLKSftvMLVDERKNMMEKIKQEERKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKLKSEMEEK 564
Cdd:pfam17380 464 RLRQ---QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER 525
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
353-527 |
7.70e-03 |
|
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: 39.52 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 353 QKAEEELQELRDKIAKgecgnssLMAEVENLRKRVLEMEgkdEEITKTESQCRELRKKLQEEEHHSKELRLEVEKLQKRM 432
Cdd:COG1579 6 LRALLDLQELDSELDR-------LEHRLKELPAELAELE---DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 433 SELEKLEEAFSKSK------SECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELecsESRLEKAELSLKDDLTKLKSFTV 506
Cdd:COG1579 76 KKYEEQLGNVRNNKeyealqKEIESLKRRISDLEDEILELMERIEELEEELAEL---EAELAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|.
gi 530383134 507 MLVDERKNMMEKIKQEERKVD 527
Cdd:COG1579 153 ELEAELEELEAEREELAAKIP 173
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
413-682 |
7.81e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 413 EEEHHSKELRLEVEKLQKRMSELEKLEEAFSK-SKSECTQLHLNLEKEKNLTKDLLNELEVVKSRVKELECSESRL--EK 489
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEALDKLRSYLPKlNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELenEI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 490 AEL-SLKDDLTKLKSFTVMLVDERKNmmEKIKqeeRKVDGLNKNFKVEQGKVMDVTEKLIEESKKLLKL-----KSEMEE 563
Cdd:PRK05771 117 KELeQEIERLEPWGNFDLDLSLLLGF--KYVS---VFVGTVPEDKLEELKLESDVENVEYISTDKGYVYvvvvvLKELSD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 564 KVYNLTRErdeligklkseeeksselscsVDLLKKRLDGIEEVEREITRGRSRKGSEltcpeDNKIKELTLEIERLKKRL 643
Cdd:PRK05771 192 EVEEELKK---------------------LGFERLELEEEGTPSELIREIKEELEEI-----EKERESLLEELKELAKKY 245
|
250 260 270
....*....|....*....|....*....|....*....
gi 530383134 644 QQLEVVegdlmktedEYDQLEQkfrtEQDKANFLSQQLE 682
Cdd:PRK05771 246 LEELLA---------LYEYLEI----ELERAEALSKFLK 271
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
534-748 |
8.01e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 534 KVEQGKVMDVTEKLIEESKKLLKLKSEMEEkvynltrerdeliGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREItrg 613
Cdd:PRK05771 39 ELSNERLRKLRSLLTKLSEALDKLRSYLPK-------------LNPLREEKKKVSVKSLEELIKDVEEELEKIEKEI--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 614 rsrkgSELTcpedNKIKELTLEIERLKKRLQQLEVVEG-DL-MKTEDEYDQLEQKF-RTEQDKANFLSQQLEEIKHQIAK 690
Cdd:PRK05771 103 -----KELE----EEISELENEIKELEQEIERLEPWGNfDLdLSLLLGFKYVSVFVgTVPEDKLEELKLESDVENVEYIS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 691 NK--------AIEKGEVVSQEAELR-HRFR-------------LEEAKSR--DLKAEVQALKEKIHELMNKEDQLSQLQV 746
Cdd:PRK05771 174 TDkgyvyvvvVVLKELSDEVEEELKkLGFErleleeegtpselIREIKEEleEIEKERESLLEELKELAKKYLEELLALY 253
|
..
gi 530383134 747 DY 748
Cdd:PRK05771 254 EY 255
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
141-361 |
8.36e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.52 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 141 EDVYEKPISELDRLEEKQKETYRRMLEQLLLAEKCHRRTVYELENEKHKHTDYMNKSDDFTNL---LEQERERLKKLLEQ 217
Cdd:pfam00038 35 SELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLrtsAENDLVGLRKDLDE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 218 ekAYQARKEKENakRLNKLRDELVKLKSFALMLVDERQMHIEQLGLQ----SQKVQDLTQKLREEEEKLKAITSKSKEDr 293
Cdd:pfam00038 115 --ATLARVDLEA--KIESLKEELAFLKKNHEEEVRELQAQVSDTQVNvemdAARKLDLTSALAEIRAQYEEIAAKNREE- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530383134 294 qkllkLEVDFEHKASRFSQEHEEMNAKLANQESHNRQLRLKLVGLTQRIEELEETNKNLQKAEEELQE 361
Cdd:pfam00038 190 -----AEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEE 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
464-781 |
8.44e-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: 40.39 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 464 KDLLNELEVVKsrvKELECSESRLEKAELSLKDDLTKLKSFTV---MLVDERKNMMEKIKQEERKVDGLNKN---FKVEQ 537
Cdd:TIGR04523 36 KQLEKKLKTIK---NELKNKEKELKNLDKNLNKDEEKINNSNNkikILEQQIKDLNDKLKKNKDKINKLNSDlskINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 538 GKVMDVTEKLIEESKKLLKLKSEMEEKVY-------NLTRERDELIGKLKSEEEKSSELSCSVDLLKKRLDGIEEVEREI 610
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDkflteikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 611 TRGRSRKGSELTCPE--DNKIKELTLEIERLKKRLQQLEvveGDLMKTEDEYDQLEQKFRTEQDKANFLSQQLEEIKHQI 688
Cdd:TIGR04523 193 KNKLLKLELLLSNLKkkIQKNKSLESQISELKKQNNQLK---DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 689 ---------AKNKAIEKGEVVSQ-EAELRH-RFRLEEAKSRDLKAEVQALKEKIHELMNK----EDQLSQLQVDYSVLQQ 753
Cdd:TIGR04523 270 sekqkeleqNNKKIKELEKQLNQlKSEISDlNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnNKIISQLNEQISQLKK 349
|
330 340
....*....|....*....|....*...
gi 530383134 754 RFMEEENKNKNMGQEVLNLTKELELSKR 781
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKK 377
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
378-870 |
9.67e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 378 AEVENLRKRVLEMEGKDEEITKTESQCRELRKKLQEEEHHSKELR---LEVEKLQKRMSELEKLEEAFSKSKSECTQLHL 454
Cdd:PRK01156 149 AQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKssnLELENIKKQIADDEKSHSITLKEIERLSIEYN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 455 NLEKEKNLTKDLLNEL----EVVKSRVKELECSESRLEKAEL------SLKDDLTKLKSFTVMLVDERKNMMEKIKQEER 524
Cdd:PRK01156 229 NAMDDYNNLKSALNELssleDMKNRYESEIKTAESDLSMELEknnyykELEERHMKIINDPVYKNRNYINDYFKYKNDIE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 525 KVDGLNKNFKVEQGKVMDVTEKLIEESK---KLLKLKSEMEEkvynLTRERDELIGKLKSEEEKSSelscSVDLLKKRld 601
Cdd:PRK01156 309 NKKQILSNIDAEINKYHAIIKKLSVLQKdynDYIKKKSRYDD----LNNQILELEGYEMDYNSYLK----SIESLKKK-- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 602 gIEEVEREITR-----GRSRKGSELTCPEDNKI-KELTLEIERLKKRLQQLEVVEGDLMKTEDEY--------------- 660
Cdd:PRK01156 379 -IEEYSKNIERmsafiSEILKIQEIDPDAIKKElNEINVKLQDISSKVSSLNQRIRALRENLDELsrnmemlngqsvcpv 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 661 -------DQLEQKFRTEQDKANFLSQQL-----------EEIKHQIAKNKAIEKGEVVSQEAELRhrfrleeaKSRDLKA 722
Cdd:PRK01156 458 cgttlgeEKSNHIINHYNEKKSRLEEKIreieievkdidEKIVDLKKRKEYLESEEINKSINEYN--------KIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383134 723 EVQALKEKIHELMNKEDQLSQLQVDYSVLQQRFMEEENKNKNMGQEVLNLTKELELSKRY---SRALRPSVNGRRMVDVP 799
Cdd:PRK01156 530 DLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSneiKKQLNDLESRLQEIEIG 609
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530383134 800 VTSTGVQTDAVSGEaAEEETPAVFIRKSFQEENHIMSNLRQVGLKKPVERSSVLDRYPPAANELTMRKSWI 870
Cdd:PRK01156 610 FPDDKSYIDKSIRE-IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDI 679
|
|
| |
