|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
313-954 |
1.04e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.84 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 313 YKSRRNEphigTEKTLDKSRNDgnpLRELRISIAELQQQktgmlhtLQKLREEVDQSKREH-LSVQLSVKDSRAQV---Q 388
Cdd:COG1196 170 YKERKEE----AERKLEATEEN---LERLEDILGELERQ-------LEPLERQAEKAERYReLKEELKELEAELLLlklR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 389 NIMSELHRLQAQRDLCLEEVRVLQGQKcvsrsvsvlereemdRLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQR 468
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAEL---------------AELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 469 EEDSRSLQEKYSELEKQLLHAIREKEQIKLASQKHLDHQIKRFGALERIVAQKELLLQgTQEAKEGLLLELCSLREAHSL 548
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA-ELAEAEEALLEAEAELAEAEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 549 NLREMQNRSKKDMEQEIEKLTLQltkshkEELQNVCKQADDLRSASLSDQAQIhkqsldslhncikmKDEEVKQLKEALK 628
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQL------EELEEAEEALLERLERLEEELEEL--------------EEALAELEEEEEE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 629 QSEEKMRRQQEEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKtedAVRKWRTELDKERRNTLALQSKLTELQ 708
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA---AARLLLLLEAEADYEGFLEGVKAALLL 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 709 KEAEKEAVCLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQSRRWAQDIHAECVHLQELLKHHGLIVETEGSHSSD 788
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGA 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 789 SSTVSSALQMLQ---SLTKSLQQYINDLKTELSTQRRAALQMSREKEQELRV-----------------QKEQLMEEKER 848
Cdd:COG1196 597 IGAAVDLVASDLreaDARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREvtlegeggsaggsltggSRRELLAALLE 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 849 ALAALKEKLIQAHVEEMSSLSRGQLLMKNDEDVDGQCVHLRRQLKAKDEELRQVHNSMAQWKDKTTARIAhkfELELNAE 928
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE---LLEEEAL 753
|
650 660
....*....|....*....|....*.
gi 326667833 929 LERRLPTSKAEQQKRLERLENEMRHL 954
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-950 |
9.59e-13 |
|
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: 72.78 E-value: 9.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 340 ELRISIAELQQQKTGMLHTLQKLREEVDQSKREHLSVQLSVKDSRAQVQNIMSELHRLQAQRDLCLEEVRvlqgqkcvsr 419
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE---------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 420 svsvlerEEMDRLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAirekeQIKLA 499
Cdd:TIGR02168 425 -------ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL-----QARLD 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 500 SQKHLDHQIKRFGALERIVAQKELLLQGTQeakeGLLLELCSLRE----AHSLNLRE-MQNRSKKDmeQEIEKLTLQLTK 574
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKALLKNQSGLSGIL----GVLSELISVDEgyeaAIEAALGGrLQAVVVEN--LNAAKKAIAFLK 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 575 SHKEELQNVC---KQADDLRSASLSDQAQIHKQSLDSLHNCIKMKDEEVKQLK---------EALKQSEEKMRRQQEEFR 642
Cdd:TIGR02168 567 QNELGRVTFLpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvDDLDNALELAKKLRPGYR 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 643 RETEEK-------IVKAASREQRKCEEQREKALQEQRHTLEQKTEDAvrkwrTELDKERRntlALQSKLTELQKEAEKea 715
Cdd:TIGR02168 647 IVTLDGdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKI-----AELEKALA---ELRKELEELEEELEQ-- 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 716 vcLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQSRRWAQDIHAECVHLQELLKHHGLIVETEGSHSSDSSTVSSA 795
Cdd:TIGR02168 717 --LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 796 LQMLQSLTK---SLQQYINDLKTELSTQRRAALQMSREK----------EQELRVQKEQL-------------MEEKERA 849
Cdd:TIGR02168 795 KEELKALREaldELRAELTLLNEEAANLRERLESLERRIaaterrledlEEQIEELSEDIeslaaeieeleelIEELESE 874
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 850 LAALKEKLIQAHVEEMSSLSRGQLLMKNDEDVDGQCVHLRRQLKAKDEELRQVHNSMAQWK---DKTTARIAHKFELELN 926
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEvriDNLQERLSEEYSLTLE 954
|
650 660
....*....|....*....|....*.
gi 326667833 927 --AELERRLPTSKAEQQKRLERLENE 950
Cdd:TIGR02168 955 eaEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
428-744 |
4.41e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.76 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 428 EMDRLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEkqllhaiREKEQIKLASQKHLDHQ 507
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL-------EEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 508 IKRFGALERIVAQKELLLQGTQEAKEGLLlelcslreAHSLNLREMQNRSKKDMEQEIEKLTLQLTKSHKEELQNVckqa 587
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKL--------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE---- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 588 ddLRSASLSDQAQIHKQSLDSLHNCIKMKDEEVKQLKEALKQSEEKmrrqqeefrRETEEKIVKAASREQRKCEEQREKA 667
Cdd:pfam02463 307 --RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK---------REAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326667833 668 LQEQRHTLEQKTEDAVRKWRTELDKErrNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQKQQ 744
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKS--EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
425-855 |
9.07e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 425 EREEMDRLLENAKSElfSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKLASQKHL 504
Cdd:PTZ00121 1464 KKAEEAKKADEAKKK--AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 505 DHQIKRfgaLERIVAQKELllqgtQEAKEGLLLELCSLREAHslnlREMQNRSKKDMEQEIEKLTLQLTKSHKEELQnvc 584
Cdd:PTZ00121 1542 AEEKKK---ADELKKAEEL-----KKAEEKKKAEEAKKAEED----KNMALRKAEEAKKAEEARIEEVMKLYEEEKK--- 1606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 585 KQADDLRSAslsDQAQIHKQSLDslhncikmKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKAAsREQRKCEEQR 664
Cdd:PTZ00121 1607 MKAEEAKKA---EEAKIKAEELK--------KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA-EEAKKAEEDK 1674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 665 EKAlQEQRHTLEQKTEDAVRKWRTEldKERRNTLALQSKLTELQKEAEKeavclkqtlLSSEKELQELRTALREREQKQQ 744
Cdd:PTZ00121 1675 KKA-EEAKKAEEDEKKAAEALKKEA--EEAKKAEELKKKEAEEKKKAEE---------LKKAEEENKIKAEEAKKEAEED 1742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 745 RRTA----RHEQQSRRWAQDIHAECVHLQELLKHHGLIVETEGSHSSDSSTVSSA---------LQMLQSLTKSLQQYIN 811
Cdd:PTZ00121 1743 KKKAeeakKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikdifdnFANIIEGGKEGNLVIN 1822
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 326667833 812 DLK-TELSTQRRAALQMSREKEQELRVQKEQLMEEKERALAALKE 855
Cdd:PTZ00121 1823 DSKeMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKE 1867
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
304-758 |
1.35e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 304 SGRKGKRNLYKSRRNEphigteKTLDKSRNDGNPLRELRISIAELQQQktgmLHTLQKLREEVDQsKREHLSVQLSVKDS 383
Cdd:COG4717 62 QGRKPELNLKELKELE------EELKEAEEKEEEYAELQEELEELEEE----LEELEAELEELRE-ELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 384 RAQVQNIMSELHRLQAQRDLCLEEVRVLQG--QKCVSRSVSVLE-REEMDRLLENAKSELFSEQRRFRNTLDSMQERLDE 460
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELREleEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 461 VNQELEQREEDSRSLQEKYSELEKQLLHAiREKEQIKLASQkhldhQIKRFGALERIVAQKELLLQGTQEAKEGLLLELC 540
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARL-----LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 541 SLreahsLNLREMQNRSKKDMEQEIEKLTLQLTKS--HKEELQNVCKQADDLRSASLsDQAQIHKQSLDSLHNCIKMKDE 618
Cdd:COG4717 285 LL-----ALLFLLLAREKASLGKEAEELQALPALEelEEEELEELLAALGLPPDLSP-EELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 619 EVKQLKeaLKQSEEKMRRQQEEFRRETEEKIVKAASREQRKCEEQREkaLQEQRHTLEQKTEDAVRKWRTELDKERRNTL 698
Cdd:COG4717 359 LEEELQ--LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE--LEELEEQLEELLGELEELLEALDEEELEEEL 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 326667833 699 A-LQSKLTELQKEAEKeavcLKQTLLSSEKELQELRT--ALREREQKQQRRTARHEQQSRRWA 758
Cdd:COG4717 435 EeLEEELEELEEELEE----LREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEWA 493
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
325-742 |
3.16e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 325 EKTLDKSRNDGNPLRELRISIAELQQQKTGMLHTLQKLREEVDQSKREHLSVQLSVKDSRAQVQNIMSELHRLQaqrdlc 404
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK------ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 405 lEEVRVLQGQkcVSRSVSVLEREEMDRLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQE------- 477
Cdd:PRK03918 273 -KEIEELEEK--VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEElkkklke 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 478 ---KYSELEK--QLLHAIREK--------------------------EQIKLASQKHLDHQIKRFGALERIVAQKELLLQ 526
Cdd:PRK03918 350 lekRLEELEErhELYEEAKAKkeelerlkkrltgltpeklekeleelEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 527 GTQEAKEGLLLELCSLREAHSLNLREMQNRSKKDMEQEIEKLTLQLTKSHKE--ELQNVCKQADDLRS-ASLSDQAQIHK 603
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKElrELEKVLKKESELIKlKELAEQLKELE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 604 QSLDSLH-NCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETE-EKIVKAASREQRKCEEQREKALQEQRHtLEQKTED 681
Cdd:PRK03918 510 EKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElKKKLAELEKKLDELEEELAELLKELEE-LGFESVE 588
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326667833 682 AVRKWRTELDKERRNTLALQSKLTELQKEaEKEAVCLKQTLLSSEKELQELRTALREREQK 742
Cdd:PRK03918 589 ELEERLKELEPFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
463-893 |
3.40e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 463 QELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKLASQ--KHLDHQIKRFGALERIVAQKELLLQGTQEAKEglllelc 540
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAAAKKKADEAKKKAEE------- 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 541 sLREAHSLNLREMQNRSKKDMEQEIEKltlqltkshKEELQNVCKQADDLRSASLSDQAQIHKQSLDSLhnciKMKDEEV 620
Cdd:PTZ00121 1430 -KKKADEAKKKAEEAKKADEAKKKAEE---------AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA----KKKAEEA 1495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 621 KQLKEALKQSEEKmRRQQEEFRRETEEKIVKAASR--EQRKCEEQRE----KALQEQRHTLEQKTEDAVRKWRTELDKER 694
Cdd:PTZ00121 1496 KKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKaeEAKKADEAKKaeekKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 695 RNTLALQSklTELQKEAEKEAVCLKQTLLSSEKEL--QELRTALREREQKQQRRTARHEQQSRRWAQDIHAECVHLQELL 772
Cdd:PTZ00121 1575 DKNMALRK--AEEAKKAEEARIEEVMKLYEEEKKMkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 773 K--HHGLIVETEGSHSSDSSTVSSA--------------------------LQMLQSLTKSLQQYINDLKTELSTQRRAA 824
Cdd:PTZ00121 1653 KkaEEENKIKAAEEAKKAEEDKKKAeeakkaeedekkaaealkkeaeeakkAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326667833 825 LQMSREKEQELRVQKEQLMEEKERALAALKEKLIQAHVEEMSSLSRGQLLMKNDEDVDGQCVHLRRQLK 893
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-715 |
3.49e-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: 54.69 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 384 RAQVQNIMSELHRLQAQRDLCLEEVRVLQGQ-KCVSRSVSVLEREEmdRLLENAKSELFSEQRRFRNTLDSMQERLDEVN 462
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRlDELSQELSDASRKI--GEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 463 QELE--------------QREEDSRSLQEKYSELEKQLLHA-IREKEQIKLASQKHLDHQIKRFGALERIVAQKELLLQG 527
Cdd:TIGR02169 751 QEIEnvkselkelearieELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 528 TQEAKEGLL--LELCSLREAHSLNLREMQNRSKKDMEQEIEKLTLQLtKSHKEELQNVCKQADDLRSA---------SLS 596
Cdd:TIGR02169 831 LEKEIQELQeqRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-RDLESRLGDLKKERDELEAQlrelerkieELE 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 597 DQAQIHKQSLDSLHNCIKMKDEEVKQLKEALKQSEEKmrrQQEEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTle 676
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI---PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEV-- 984
|
330 340 350
....*....|....*....|....*....|....*....
gi 326667833 677 QKTEDAVRKWRTELDKERRNTLALQSKLTELQKEAEKEA 715
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
446-759 |
3.86e-07 |
|
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: 54.57 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 446 RFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIK--LAS-QKHLDHQIKRFGALERIVAQKE 522
Cdd:COG3096 344 RQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsqLADyQQALDVQQTRAIQYQQAVQALE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 523 lllqgtqEAKeglllELCSLREAHSLNLREMQNRSKKDMEQEIEKL-----TLQLTKSHKEE----LQNVCKQADDLRSA 593
Cdd:COG3096 424 -------KAR-----ALCGLPDLTPENAEDYLAAFRAKEQQATEEVleleqKLSVADAARRQfekaYELVCKIAGEVERS 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 594 SLSDQAqihkQSLDSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQ------EEFRRETEEKIVKAA--SREQRKCEEQRE 665
Cdd:COG3096 492 QAWQTA----RELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQnaerllEEFCQRIGQQLDAAEelEELLAELEAQLE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 666 KALQEQRHTLEQKTE-----DAVRKWRTELDKERRNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELRTALRERE 740
Cdd:COG3096 568 ELEEQAAEAVEQRSElrqqlEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERD 647
|
330
....*....|....*....
gi 326667833 741 QKQQRRtARHEQQSRRWAQ 759
Cdd:COG3096 648 ELAARK-QALESQIERLSQ 665
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
427-945 |
5.64e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 427 EEMDRLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKLASQKHLDH 506
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 507 QIKRFGALERI--VAQKELLLQGTQEAKEGLLLELCSLREAHSLNLREMQNRSKK-DMEQEIEKLTLQLTKSHKEELQNV 583
Cdd:PTZ00121 1174 DAKKAEAARKAeeVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvKKAEEAKKDAEEAKKAEEERNNEE 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 584 CKQADDLRSASLSDQAQIHKQSLDSLHNCIKmKDEEVKQLKEAlKQSEEKmrRQQEEFRRETEEKivKAASREQRKCEEQ 663
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELK-KAEEKKKADEA-KKAEEK--KKADEAKKKAEEA--KKADEAKKKAEEA 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 664 REKALQEQRHTLEQKTEDAVRKWRTELDKERRNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQKQ 743
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA 1407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 744 QRRTARHEQQSRRWAQDIHAECVHLQELLKHHGliveTEGSHSSDSSTVSSALQMLQSLTKSLQQY--INDLKTELSTQR 821
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEAKKKA----EEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAK 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 822 RAalQMSREKEQELRVQKEQLM---EEKERALAALK--EKLIQAHVEEMSSLSRGQLLMKNDEDVDGQCVHLRRQLKaKD 896
Cdd:PTZ00121 1484 KA--DEAKKKAEEAKKKADEAKkaaEAKKKADEAKKaeEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-KA 1560
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 326667833 897 EELRQVHNSMAQWKDKTTA-------RIAHKFELELNAELERRLPTSKAEQQKRLE 945
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMAlrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
455-775 |
5.72e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 455 QERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKLASQKHLDHQIKRFGALERIVAQKELLLQGTQEAKEG 534
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 535 LLLELCSLREAHSLNLREMQNRSKK---------DMEQEIEKLTLQLtKSHKEELQNVCKQADDLRSASLSDQAQIHKQS 605
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEieelqkelyALANEISRLEQQK-QILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 606 LDSlhNCIKMKDEEVKQLKEALKQSEEKMRRQQEEF--RRETEEKIVKAASREQRKCEEQrEKALQEQRHTLEQKTEDAV 683
Cdd:TIGR02168 337 EEL--AELEEKLEELKEELESLEAELEELEAELEELesRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 684 RkwrtELDKERRNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQSRRWAQDIHA 763
Cdd:TIGR02168 414 D----RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
330
....*....|..
gi 326667833 764 ECVHLQELLKHH 775
Cdd:TIGR02168 490 RLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
451-755 |
6.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 451 LDSMQERLDEVNQELEQREEDSRSLQ------EKYSELEKQLlhaiREKEQIKLAsqKHLDHQIKRFGALERIVAQKELL 524
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAEL----RELELALLV--LRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 525 LQGTQEAKEGLLLELCSLREAHSlNLREMQNRSKKDME---QEIEKLTLQLtKSHKEELQNVCKQADDLRSASLSDQAQI 601
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVS-ELEEEIEELQKELYalaNEISRLEQQK-QILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 602 HKQS---------LDSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRR------ETEEKIVKAASREQR------KC 660
Cdd:TIGR02168 333 DELAeelaeleekLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaQLELQIASLNNEIERlearleRL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 661 EEQREKALQEQRHTLEQKTEDAVRKWRTELDKERRNTLALQSKLTELQKEAEKEAVclkqtllSSEKELQELRTALRERE 740
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE-------ELEEAEQALDAAERELA 485
|
330
....*....|....*
gi 326667833 741 QKQQRRTARHEQQSR 755
Cdd:TIGR02168 486 QLQARLDSLERLQEN 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-629 |
6.78e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 338 LRELRISIAELQQQKTGMLHTLQKLREEVDQSKREHLSVQLSVKDSRAQVQNIMSELHRLQAQRDLCLEEVRVLQGQKCV 417
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 418 SRSVSVL---EREEMDRLLENAKSELFSEQRRfrntLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKE 494
Cdd:TIGR02168 773 AEEELAEaeaEIEELEAQIEQLKEELKALREA----LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 495 QIKlASQKHLDHQIKRFGALERIVAQKELLLQGTQEAKEGLLLELCSLREAHSLNLREMQNRsKKDMEQEIEKLTLQLTK 574
Cdd:TIGR02168 849 ELS-EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK-RSELRRELEELREKLAQ 926
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326667833 575 S--HKEELQNvckQADDLRSAsLSDQAQIHKQSLDSLHNCIKMK----DEEVKQLKEALKQ 629
Cdd:TIGR02168 927 LelRLEGLEV---RIDNLQER-LSEEYSLTLEEAEALENKIEDDeeeaRRRLKRLENKIKE 983
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
438-957 |
7.58e-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: 53.43 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 438 SELFSEQRRFRNTLDSMQERLDEVNQELEQREEdsrSLQEKYSELEKQLLHAIREKEQIKlasQKHLDHQIKRFGALERI 517
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPD---TYHERKQVLEKELKHLREALQQTQ---QSHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 518 VAQKELLLQGTQEAkeglllELCSLREAHSLNLREMQNRSKKDMEQEIEKLTLQLTKSHKEELQNVcKQADDLRSASLSD 597
Cdd:TIGR00618 257 KKQQLLKQLRARIE------ELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL-QSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 598 QAQIHKQSLDSlhncikmkdeevkqlkEALKQSEEKMRRQQEEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQ 677
Cdd:TIGR00618 330 RAAHVKQQSSI----------------EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 678 KtEDAVRKWRTELDKE---------RRNTLALQSKLTELQKEAEKEAVCLK--------QTLLSSEKELQELRTALRERE 740
Cdd:TIGR00618 394 K-LQSLCKELDILQREqatidtrtsAFRDLQGQLAHAKKQQELQQRYAELCaaaitctaQCEKLEKIHLQESAQSLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 741 QKQQRRTARHEQQSRRWAqdihaecVHLQELLKHHGLIVETEGSHSSDSSTVSSA---------LQMLQSLTKSLQQYIN 811
Cdd:TIGR00618 473 QQLQTKEQIHLQETRKKA-------VVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 812 DLKTELSTQRRaALQMSREKEQELRvQKEQLMEEKERALAALKEKLIQAhVEEMSSLSRGQLLMKNDEDVDGQCVHLRRQ 891
Cdd:TIGR00618 546 DVYHQLTSERK-QRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNI-TVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 892 LKAKDEELRQVHNSMAQWKDKTTARIaHKFELELNAELERRLPTSKAEQQKRL----ERLENEMRHLTAQ 957
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTAL-HALQLTLTQERVREHALSIRVLPKELlasrQLALQKMQSEKEQ 691
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
425-957 |
1.74e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 425 EREEM-DRLLENAKSELFSEQRR-----FRNTLDSMQERLDEVNQELEQREEdsRSLQEKYSELEKQLlhairekeqikl 498
Cdd:PRK02224 150 DRQDMiDDLLQLGKLEEYRERASdarlgVERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESEL------------ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 499 asqKHLDHQIkrfgalERIVAQKELLLQGTQEAKEGLllelcslrEAHSLNLREMQnrskkDMEQEIEKLTLQLT----- 573
Cdd:PRK02224 216 ---AELDEEI------ERYEEQREQARETRDEADEVL--------EEHEERREELE-----TLEAEIEDLRETIAetere 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 574 -KSHKEELQNVCKQADDLRSASLSDQAQIHKQSLDslhncikmkDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKA 652
Cdd:PRK02224 274 rEELAEEVRDLRERLEELEEERDDLLAEAGLDDAD---------AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 653 AS-REQRKCEEQREKALQEQRHTLE---QKTEDAVRKWRTELDkerrntlALQSKLTELQKEAEKEAVCLKQTLLSSEkE 728
Cdd:PRK02224 345 ESlREDADDLEERAEELREEAAELEselEEAREAVEDRREEIE-------ELEEEIEELRERFGDAPVDLGNAEDFLE-E 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 729 LQELRTALREREqKQQRRTARHEQQSRRWAQDIHAE--CVHLQELLKHHGlIVETEGSHSSDSSTVSSALQMLQSLTKSL 806
Cdd:PRK02224 417 LREERDELRERE-AELEATLRTARERVEEAEALLEAgkCPECGQPVEGSP-HVETIEEDRERVEELEAELEDLEEEVEEV 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 807 QQYINDLKT-------------------ELSTQRRAALQMSREKEQELRVQKEQLMEEKE--RALAALKEKLIQAHVEEM 865
Cdd:PRK02224 495 EERLERAEDlveaedrierleerredleELIAERRETIEEKRERAEELRERAAELEAEAEekREAAAEAEEEAEEAREEV 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 866 SSLSRGQLLMKNDEDVDGQCVHLRRQLKAKDEELRQVHNSMAQWKDKTTARIAHKFEL-----ELNAEL-ERRLPTSKAE 939
Cdd:PRK02224 575 AELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKrerkrELEAEFdEARIEEARED 654
|
570 580
....*....|....*....|.
gi 326667833 940 QQ---KRLERLENEMRHLTAQ 957
Cdd:PRK02224 655 KEraeEYLEQVEEKLDELREE 675
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
339-745 |
2.67e-06 |
|
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: 51.56 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 339 RELRISIAELQQQKTGMLHTLQKLREEVDQSKREHLSVQLSVKDSRAQVQNIMSELHRLQAQRDLCLEEVRVLQGQ-KCV 417
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQlNQL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 418 SRSVSVLEREEMDRLLENAKSELFSEQRRFRNT---LDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQL------LH 488
Cdd:TIGR04523 294 KSEISDLNNQKEQDWNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELeekqneIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 489 AIREKEQIKLASQKHLDHQIK----RFGALERIVAQKELLLQGTQEAKEGLLLELCSLREAHSLNLREMQNRSKKDMEQE 564
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINdlesKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 565 IE-KLTLQLTKSHKEELQNVCKQADDLRSASLSDQAQI--HKQSLDSLHNCIKMKDEEVKQLKE---ALKQSEEKMRRQQ 638
Cdd:TIGR04523 454 LIiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELksKEKELKKLNEEKKELEEKVKDLTKkisSLKEKIEKLESEK 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 639 EEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQktedavrkwrteLDKERRNTLALQSKLTELQKEAEKEAVCL 718
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE------------LKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
410 420
....*....|....*....|....*..
gi 326667833 719 KQTLLSSEKELQELRTALREREQKQQR 745
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEK 628
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
410-735 |
3.27e-06 |
|
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: 51.28 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 410 VLQGQKCVS--RSVSVLEREEMDRLLENaKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEK-QL 486
Cdd:pfam17380 277 IVQHQKAVSerQQQEKFEKMEQERLRQE-KEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERiRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 487 LHAIREKEQIKlasQKHLDHQIKRFGALERIVAQKelllqgtQEAKEGLLLELCSLREAHSLnlREMQNRSKKDMEQEIE 566
Cdd:pfam17380 356 EERKRELERIR---QEEIAMEISRMRELERLQMER-------QQKNERVRQELEAARKVKIL--EEERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 567 KLTLQLTKSHKEELQNV----CKQADDLRSASLSDQAQIHkqsldslhncIKMKDEEVKQLKEALKQSEEKMRRQQEEFR 642
Cdd:pfam17380 424 QIRAEQEEARQREVRRLeeerAREMERVRLEEQERQQQVE----------RLRQQEEERKRKKLELEKEKRDRKRAEEQR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 643 RETEEKIVKAASR----EQRKC----------------EEQREKALQEQRHTLEQKTEDAVRKWRTELDKERrntlalqS 702
Cdd:pfam17380 494 RKILEKELEERKQamieEERKRkllekemeerqkaiyeEERRREAEEERRKQQEMEERRRIQEQMRKATEER-------S 566
|
330 340 350
....*....|....*....|....*....|...
gi 326667833 703 KLTELQKEAEkeavcLKQTLLSSEKELQELRTA 735
Cdd:pfam17380 567 RLEAMERERE-----MMRQIVESEKARAEYEAT 594
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
371-708 |
4.44e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.23 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 371 REHLSVQLS---VKDSRAQVQNIMSELHRlQAQRDLCLEEVRVLQGQKCVSRSVSVLEREEMDRLLENaKSELFSEQRRF 447
Cdd:COG5022 800 QPLLSLLGSrkeYRSYLACIIKLQKTIKR-EKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKK-ETIYLQSAQRV 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 448 RNTLDSMQErLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKLASQKHLdhqikrfgalerivaqKELLLQG 527
Cdd:COG5022 878 ELAERQLQE-LKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARL----------------KKLLNNI 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 528 tqEAKEGLLLELCSLREAHSLNlreMQNRSKKDMEQEIEKLTLQLTKsHKEELQNVCkqaddlrsaslsDQAQIHKQSLD 607
Cdd:COG5022 941 --DLEEGPSIEYVKLPELNKLH---EVESKLKETSEEYEDLLKKSTI-LVREGNKAN------------SELKNFKKELA 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 608 SLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKAASrEQRKCEEQREKALQEQRHTLEQKTEDAVRKWR 687
Cdd:COG5022 1003 ELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILKPLQ-KLKGLLLLENNQLQARYKALKLRRENSLLDDK 1081
|
330 340
....*....|....*....|.
gi 326667833 688 TELDKERRNTLALQSKLTELQ 708
Cdd:COG5022 1082 QLYQLESTENLLKTINVKDLE 1102
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
368-959 |
4.86e-06 |
|
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: 50.99 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 368 QSKREHLSVQLSVKDSRAQVQNIMSELHRLQAQRDLCLEEVRVLQGQKCVSRSVSVLEREEMDRLLEnAKSELfseQRRF 447
Cdd:pfam12128 217 RLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQE-TSAEL---NQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 448 RNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKLASQKHLDHQIKRFGALERIVAQKELLLQG 527
Cdd:pfam12128 293 RTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQD 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 528 TQEAKEGLLLeLCSLREAHSL--------NLREMQNRSKKDMEQEIEKLTLQLTKSHKEELQNVCKQADDLRSAS----- 594
Cdd:pfam12128 373 VTAKYNRRRS-KIKEQNNRDIagikdklaKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLgelkl 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 595 LSDQAQIHKQSLDSLHNcikmKDEEVKQLKEALKQSEEKMRRQQEEFRREteEKIVKAASREQRKCE---EQREKALQE- 670
Cdd:pfam12128 452 RLNQATATPELLLQLEN----FDERIERAREEQEAANAEVERLQSELRQA--RKRRDQASEALRQASrrlEERQSALDEl 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 671 ------QRHTLEQKTEDAVRKW--------------RTELD------------------------------------KER 694
Cdd:pfam12128 526 elqlfpQAGTLLHFLRKEAPDWeqsigkvispellhRTDLDpevwdgsvggelnlygvkldlkridvpewaaseeelRER 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 695 RNTL--ALQSKlTELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQSRRWAQDIHAEcvhlqell 772
Cdd:pfam12128 606 LDKAeeALQSA-REKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAER-------- 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 773 khhglivetegshssdsstVSSALQMLQSLTKSLQQYINDLKTELSTQRRAALQMSREKEQELRVqkeqLMEEKERALAA 852
Cdd:pfam12128 677 -------------------KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV----VEGALDAQLAL 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 853 LKEKLIQAHVEEMSSLSRGQLLMKND---EDVDGQCVHLRRQlkakdeELRQVHNSMAQW-KDKTTARIAHKFELELNAE 928
Cdd:pfam12128 734 LKAAIAARRSGAKAELKALETWYKRDlasLGVDPDVIAKLKR------EIRTLERKIERIaVRRQEVLRYFDWYQETWLQ 807
|
650 660 670
....*....|....*....|....*....|.
gi 326667833 929 LERRLPTSKAEQQKRLERLENEMRHLTAQCR 959
Cdd:pfam12128 808 RRPRLATQLSNIERAISELQQQLARLIADTK 838
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
385-961 |
1.87e-05 |
|
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: 48.81 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 385 AQVQNIMSELHRLQAQRDLCLEEVRVLQGQKCVSRSVSVLEREEMDRLLENAKSELFSEQRRFRNTLDSMQERLDEVNQE 464
Cdd:TIGR00618 226 KELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 465 LEQREEDSRSLQEKYSELEKQLLH-AIREKEQIKLASQKHLDHQIKRfgalerivaQKELLLQGTQEAKeglllelcSLR 543
Cdd:TIGR00618 306 EQQAQRIHTELQSKMRSRAKLLMKrAAHVKQQSSIEEQRRLLQTLHS---------QEIHIRDAHEVAT--------SIR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 544 EAHSLNLREMQNRSKKDMEQEIEKLTLQLTKSHKEELQNVCKQADDLRSASlsdqaQIHKQSLDSLHNCIKMKDEEVKQL 623
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF-----RDLQGQLAHAKKQQELQQRYAELC 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 624 KEALK---QSEEKMRRQQEEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTEDAVRKWRTELDKERRNTLAL 700
Cdd:TIGR00618 444 AAAITctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 701 QSkLTELQKEAEKEAVCLKQTLLSSEKELQELRT---ALREREQKQQRRTARHEQQSRRWAQDIHAECVHLQELLKHHGL 777
Cdd:TIGR00618 524 GP-LTRRMQRGEQTYAQLETSEEDVYHQLTSERKqraSLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 778 IVETEGSHSSDSSTVSSALQM---LQSLTKSLQQYINDLKTELSTQRRAALQMSREKEQE----LRVQKEQLMEEKERAL 850
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPeqdLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalsIRVLPKELLASRQLAL 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 851 AALkEKLIQAHVEEMSSLSRGQLLMKNDEDVDGQCVHLRRQ-----------LKAKDEELRQVHNSM---AQWKDKTTAR 916
Cdd:TIGR00618 683 QKM-QSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienassslgsdLAAREDALNQSLKELmhqARTVLKARTE 761
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 326667833 917 IAHKFELELNAELERRLPTSKAE-----QQKRLERLENEMRHLTAQCRDH 961
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAELSHLAaeiqfFNRLREEDTHLLKTLEAEIGQE 811
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
433-874 |
1.98e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 433 LENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKlASQKHLDHQIKRFG 512
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR-EELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 513 ALERIvAQKELLLQGTQEAKEGLLLELCSLREAHslNLREMQNRSKKDMEQEIEKLTLQLTKSHKEELQNVCKQADDLRs 592
Cdd:COG4717 130 LYQEL-EALEAELAELPERLEELEERLEELRELE--EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 593 aslsDQAQIHKQSLDSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQ---------------------------------- 638
Cdd:COG4717 206 ----QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaallallglggsllsliltiagvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 639 --------------EEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTEDAVRKWRT--ELDKERRNTLALQS 702
Cdd:COG4717 282 vlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 703 KLTELQKEAEKEAVcLKQTLLSSEKELQELRTALREREQKQQRRTARHEQqsrrwaqdihaecVHLQELLKHHGLIVETE 782
Cdd:COG4717 362 ELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ-------------LEELLGELEELLEALDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 783 GSHSSDSSTVSSALQMLQSLTKSLQQYINDLKTELST-QRRAALQMSREKEQELRVQKEQLmeEKERALAALKEKLIQAH 861
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELREL--AEEWAALKLALELLEEA 505
|
490
....*....|...
gi 326667833 862 VEEMSSLSRGQLL 874
Cdd:COG4717 506 REEYREERLPPVL 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
456-743 |
2.16e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 456 ERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEqiklasqkhldhQIKRFGALERIVAQKELLLqgtqeakegL 535
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE------------KAERYQALLKEKREYEGYE---------L 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 536 LLELCSLREAHSLNLREMQnrskkDMEQEIEKLTLQLTKSHKE------ELQNVCKQADDLRSA-SLSDQAQIH--KQSL 606
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLA-----SLEEELEKLTEEISELEKRleeieqLLEELNKKIKDLGEEeQLRVKEKIGelEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 607 DSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQ---EEFRRETEEKIVKAASREQRKCEEQREKALQEQRhtLEQKTEDAv 683
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLaeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAE--LEEVDKEF- 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 684 RKWRTELDKERRNTLALQSKLTELQKEAEKeavcLKQTLLSSEKELQELRTALREREQKQ 743
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDR----LQEELQRLSEELADLNAAIAGIEAKI 436
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
557-848 |
2.48e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 557 SKKDMEQEIEKLTLQLTKSHKEELQNVCKQADDLRSASLSDQAQIHKQSLDSlhncikmkdeeVKQLKEALKQSEEKMRR 636
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIY-----------AEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 637 QQEEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTE-DAVRKWRTeLDKERRNTLALQSKLTELQKEAEKEA 715
Cdd:pfam17380 354 RQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQElEAARKVKI-LEEERQRKIQQQKVEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 716 VCLKQTLLSSEKELQELRTALREREQKQQ-RRTARHEQQSRRWAQDIHAECVHLQELLKHHGLIVETEgshssdSSTVSS 794
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKE------LEERKQ 506
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 326667833 795 ALQMLQSLTKSLQQYINDLKTELSTQRRaalqmSREKEQELRVQKEqlMEEKER 848
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKAIYEEER-----RREAEEERRKQQE--MEERRR 553
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
528-949 |
3.89e-05 |
|
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: 48.04 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 528 TQEAKEGLLLELCSLREAHSLNLREMQNRSKKDMEQEIEKLTLQLTKSHKEelQNVCKQADDLRSASLSDQAQIHKQSLD 607
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY--LKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 608 SLHNCIKMKDEEVKQLKEAlKQSEEKMRRQQEEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTEDAVRKWR 687
Cdd:pfam02463 259 EIEKEEEKLAQVLKENKEE-EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 688 TELDKErrntLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQKQQRrtaRHEQQSRRWAQDIhAECVH 767
Cdd:pfam02463 338 EELEKE----LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK---LKEEELELKSEEE-KEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 768 LQELLKHHGLIVETEGSHSSDSSTVSSALQMLQSLTKSLQQYINDLKTELSTQRRAALQMSREKEQELRVQKEQLMEEKE 847
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 848 RALAALKEKLIQAHVEEmSSLSRGQLLMKNDEDVDGQCVHLRRQLKAKDEELRQVHNSMA-QWKDKTTARIAHKFELELN 926
Cdd:pfam02463 490 LSRQKLEERSQKESKAR-SGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAvIVEVSATADEVEERQKLVR 568
|
410 420
....*....|....*....|...
gi 326667833 927 AELERRLPTSKAEQQKRLERLEN 949
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPL 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
652-857 |
5.24e-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: 46.68 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 652 AASREQRKCEEQREKALQEQRHTleQKTEDAVRKWRTELDKERRNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQE 731
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAEL--EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 732 LRTALREREQKQQRRTARHEQQSRRWAqdihaecvhLQELLKhhglivetegshSSDSSTVSSALQMLQSLTKSLQQYIN 811
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPP---------LALLLS------------PEDFLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 326667833 812 DLKTELS---------TQRRAALQMSREKEQELRVQKEQLMEEKERALAALKEKL 857
Cdd:COG4942 154 ELRADLAelaalraelEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
396-575 |
5.77e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 396 RLQAQRDLCLEEVRVLQGQKCVSRSVSVLEREEMDRLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSL 475
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 476 QEKYSELEKQLlhAIREKEQIKLASQkhLDHQIKRFGALERIVAQKELLLQGTQEAKEGLLLEL-CSLREAHSLNLREMQ 554
Cdd:PRK12705 104 ENQLEEREKAL--SARELELEELEKQ--LDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVkKIEEEADLEAERKAQ 179
|
170 180
....*....|....*....|.
gi 326667833 555 NRSKKDMEQEIEKLTLQLTKS 575
Cdd:PRK12705 180 NILAQAMQRIASETASDLSVS 200
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
426-860 |
7.64e-05 |
|
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: 46.87 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 426 REEMDRLLE---NAKSELFSEQRrfrnTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQL---LHAIREKEQIKlA 499
Cdd:COG3096 277 ANERRELSEralELRRELFGARR----QLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLnlvQTALRQQEKIE-R 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 500 SQKHLDHQIKRFGALERIVAQKELLLQGTQEAKEGLLLELCSLRE--AHSLNLREMQNRSKKDMEQEIEKLtlqltkshk 577
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSqlADYQQALDVQQTRAIQYQQAVQAL--------- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 578 EELQNVCkQADDLRSASLSDQAQIHKQSLDSLhncikmkDEEVKQLKEALkqSEEKMRRQQEEFRRETEEKIVKAASREQ 657
Cdd:COG3096 423 EKARALC-GLPDLTPENAEDYLAAFRAKEQQA-------TEEVLELEQKL--SVADAARRQFEKAYELVCKIAGEVERSQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 658 --------------RKCEEQREKALQEQRHTLEQKTED--AVRKWRTELDKERRNTLALQSKLTELQKEAEKEavclKQT 721
Cdd:COG3096 493 awqtarellrryrsQQALAQRLQQLRAQLAELEQRLRQqqNAERLLEEFCQRIGQQLDAAEELEELLAELEAQ----LEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 722 LLSSEKELQELRTALREREQKQQRRTARHEQQSRRW--AQDIHAecvHLQELLkhhglivetegshssdsstvSSALQML 799
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWlaAQDALE---RLREQS--------------------GEALADS 625
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 326667833 800 QSLTkslqqyindlktelstqrrAALQMSREKEQELRVQKEQLMEEKERALAALkEKLIQA 860
Cdd:COG3096 626 QEVT-------------------AAMQQLLEREREATVERDELAARKQALESQI-ERLSQP 666
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
487-865 |
9.08e-05 |
|
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: 46.89 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 487 LHAIREKEQIKLASQKHLDHQIKRFGALERIVAQKELLLQGTQEAKEGLLLELCSLREAHSLNLREMQNRSKKDMEQEIE 566
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQ 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 567 KLTLQLTKSHKEE---LQNVCKQADDLRSASLSDQAQIHKQSLDSLhNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRR 643
Cdd:pfam02463 707 REKEELKKLKLEAeelLADRVQEAQDKINEELKLLKQKIDEEEEEE-EKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 644 ETEEKIVKAASREQRKCEEQREKALQ---EQRHTLEQKTEDAVRKWRTELDKERRNTLALQSKLTELQKEAEKEAVCLKQ 720
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKeeaELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 721 TLLSSEKELQELRTALREREQKQQRRTARHEQQSRRW----AQDIHAE----------CVHLQELLKHHGLIVETEGSHS 786
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELeeesQKLNLLEekeneieeriKEEAEILLKYEEEPEELLLEEA 945
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 326667833 787 SDSSTVSSALQMLQSLTKSLQQYInDLKTELSTQRRAALQMSREKEQELRVQKEQLMEEKERALAALKEKLIQAHVEEM 865
Cdd:pfam02463 946 DEKEKEENNKEEEEERNKRLLLAK-EELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
443-759 |
1.28e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 443 EQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKlasqkhldhqiKRFGALERIVAQKE 522
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE-----------QEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 523 LLLQGTQEAKEglllelcslreahslNLREMQnrskKDMEQEIEKLTLQLTKsHKEELQNVckQADDLRSASLSDQAQIH 602
Cdd:TIGR02169 744 EDLSSLEQEIE---------------NVKSEL----KELEARIEELEEDLHK-LEEALNDL--EARLSHSRIPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 603 KQsldslhncikmkDEEVKQLKEALKQSEEKMRRqqEEFRRETEEKIVKAASREQRKCEEQReKALQEQRHTLEQKteda 682
Cdd:TIGR02169 802 KL------------EEEVSRIEARLREIEQKLNR--LTLEKEYLEKEIQELQEQRIDLKEQI-KSIEKEIENLNGK---- 862
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326667833 683 VRKWRTELDKERRNTLALQSKLTELQKEAEKeavcLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQSRRWAQ 759
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
616-744 |
1.88e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 616 KDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKAASREQRK-CEEQREKALQEQRHTLE-QKTEDAVRKWRTELDKE 693
Cdd:PRK09510 75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKqAEEAAKQAALKQKQAEEaAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 326667833 694 RRNTLALQSKlTELQKEAEKEAVclKQTLLSSEKELQELRTALREREQKQQ 744
Cdd:PRK09510 155 RAAAAAKKAA-AEAKKKAEAEAA--KKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
426-760 |
1.92e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 426 REEMDRLLENAkSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQL---LHAIREKEQIKLASqk 502
Cdd:PRK04863 278 ANERRVHLEEA-LELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIERYQ-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 503 hldhqikrfGALERIVAQKELLLQGTQEAKEGLLlelcsLREAHSLNLREMQNRSKKDMEQEIEKLTLQLTKSHK----- 577
Cdd:PRK04863 355 ---------ADLEELEERLEEQNEVVEEADEQQE-----ENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQyqqav 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 578 ---EELQNVCkQADDLRSASLSD-------QAQIHKQSLDSLHNCIKMKDEEVKQLKEALkqseEKMRRQQEEFRRETEE 647
Cdd:PRK04863 421 qalERAKQLC-GLPDLTADNAEDwleefqaKEQEATEELLSLEQKLSVAQAAHSQFEQAY----QLVRKIAGEVSRSEAW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 648 KIVKAASREQR--KCEEQREKALQEQRHTLEQKTED--AVRKWRTELDKERRNTLALQSKLTELQKEAEKEAVCLKQTLl 723
Cdd:PRK04863 496 DVARELLRRLReqRHLAEQLQQLRMRLSELEQRLRQqqRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV- 574
|
330 340 350
....*....|....*....|....*....|....*....
gi 326667833 724 sseKELQELRTALREREQKQQRRTARHEQQSRRW--AQD 760
Cdd:PRK04863 575 ---SEARERRMALRQQLEQLQARIQRLAARAPAWlaAQD 610
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
642-957 |
2.16e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 642 RRETEEKIVKAASREQRkcEEQREKALQEQRHTLEQKTEDAVR--KWRTELdKERRNTLALqSKLTELQKEAEKeavcLK 719
Cdd:COG1196 174 KEEAERKLEATEENLER--LEDILGELERQLEPLERQAEKAERyrELKEEL-KELEAELLL-LKLRELEAELEE----LE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 720 QTLLSSEKELQELRTALREREQKQQRRTARHEQQSRRwaqdihaecvhlqellkhhglivetegshssdsstVSSALQML 799
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELE-----------------------------------LEEAQAEE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 800 QSLTKSLQQYINDLktELSTQRRAALQMSREKEQELRVQKEQLMEEKERALAALKEKLIQAHVEEMSSLSRgqllmknde 879
Cdd:COG1196 291 YELLAELARLEQDI--ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--------- 359
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 326667833 880 dvdgqcvhLRRQLKAKDEELRQVHNSMAQWKDKTTARIAHKFELELNAELERRLPTSKAEQQKRLERLENEMRHLTAQ 957
Cdd:COG1196 360 --------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
559-753 |
2.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 559 KDMEQEIEKL-----TLQLTKSHKEELQNVCKQADDLRSASLSDQAQIHKQSLDSLHNCIKMKDEEVKQLKEALKQSEEK 633
Cdd:COG4913 238 ERAHEALEDAreqieLLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 634 MRRQQEEfRRETEEKIVKAASreqrkceeQREKALQEQRHTLEQKTEDAVRKwRTELDkERRNTLALQSKLTELQ-KEAE 712
Cdd:COG4913 318 LDALREE-LDELEAQIRGNGG--------DRLEQLEREIERLERELEERERR-RARLE-ALLAALGLPLPASAEEfAALR 386
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 326667833 713 KEAVCLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQ 753
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
613-962 |
2.40e-04 |
|
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: 45.34 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 613 IKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTEDAVRKWRTELDK 692
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 693 ERRNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQSRRWAQDIHAECVHLQELL 772
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 773 KHHGLIVETEGSHSSDSSTVSSALQMLQSLTKSLQQYI-NDLKTELSTQRRAALQMSREKEQELRVQKEQL--MEEKERA 849
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIhIRDAHEVATSIREISCQQHTLTQHIHTLQQQKttLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 850 LAALKEKLIQAHVEEMSSLSRgqllmknDEDVDGQCVHLRRQLKAKDEELRQVHNSMAQWKDKTTARIAH---------- 919
Cdd:TIGR00618 398 LCKELDILQREQATIDTRTSA-------FRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHlqesaqslke 470
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 326667833 920 -KFELELNAELERRLPTSKAEQQKRLERLENEMRHLTAQCRDHN 962
Cdd:TIGR00618 471 rEQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
642-954 |
2.55e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 642 RRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTEDAVRKWRTELDKERRNTL---ALQSKLTELQ--------KE 710
Cdd:TIGR02169 155 RRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqALLKEKREYEgyellkekEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 711 AEKEAVCLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQSRRWAQDIHAECVHLQE-LLKHHGLIVETEGSHSSDS 789
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELEAEIASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 790 STVSSA---LQMLQSLTKSLQQYINDLKTELSTQ--RRAALQMSREKEQELRVQKEQLMEEKERALAALKEKLIQAhVEE 864
Cdd:TIGR02169 315 RELEDAeerLAKLEAEIDKLLAEIEELEREIEEErkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY-REK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 865 MSSLSRGQllmkndEDVDGQCVHLRRQLKAKDEELRQVHNSMAQWKDKTTARIAHKFELELN-AELERRLPTSKAE---Q 940
Cdd:TIGR02169 394 LEKLKREI------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADlskY 467
|
330
....*....|....
gi 326667833 941 QKRLERLENEMRHL 954
Cdd:TIGR02169 468 EQELYDLKEEYDRV 481
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
344-681 |
2.84e-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: 45.11 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 344 SIAELQQQKTGMLHTLQKLREEVDQSKRE---HLSVQLSVKDSRAQVQN---IMSELHRLQAQRDLCLEEVRvlqgqkcv 417
Cdd:pfam17380 283 AVSERQQQEKFEKMEQERLRQEKEEKAREverRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIR-------- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 418 srsvsvleREEMDRLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIK 497
Cdd:pfam17380 355 --------QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 498 LASQKHLDHQIKRfgalerivaqkelllqgtqeakegllLELCSLREAHSLNLREM--QNRSKKDMEQEIEKLTLQLTKS 575
Cdd:pfam17380 427 AEQEEARQREVRR--------------------------LEEERAREMERVRLEEQerQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 576 HKEELQnvcKQADDLRSASLSDQAQIHKQSLDSLHNCIKMKDEEVKQLKEALKQsEEKMRRQQEEFRRETEEKIVKAASR 655
Cdd:pfam17380 481 KEKRDR---KRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE-EERRREAEEERRKQQEMEERRRIQE 556
|
330 340
....*....|....*....|....*...
gi 326667833 656 EQRKCEEQREK--ALQEQRHTLEQKTED 681
Cdd:pfam17380 557 QMRKATEERSRleAMEREREMMRQIVES 584
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
556-884 |
2.87e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 556 RSKKDMEQEIEKLTLQLTkSHKEELQNVCKQADDLRsaslsdqaqihkqslDSLHNCIKMKDEEVKQLKealKQSEEKMR 635
Cdd:TIGR02169 230 KEKEALERQKEAIERQLA-SLEEELEKLTEEISELE---------------KRLEEIEQLLEELNKKIK---DLGEEEQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 636 RQQEEFR-----RETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTEdavrkWRTELDKERRNTLALQSKLTELQKE 710
Cdd:TIGR02169 291 RVKEKIGeleaeIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE-----LEREIEEERKRRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 711 AEKeavcLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQSRRWAQDIHAECVHLQELLKHHGLIVETEGSHSSDSS 790
Cdd:TIGR02169 366 LED----LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 791 TVSSALQMLQSLTKSLQQYINDLKTELStqrraalQMSREKEQELRVQKEQlmEEKERALAALKEKLIQAHVEEMSSLSR 870
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYEQ-------ELYDLKEEYDRVEKEL--SKLQRELAEAEAQARASEERVRGGRAV 512
|
330
....*....|....
gi 326667833 871 GQLLMKNDEDVDGQ 884
Cdd:TIGR02169 513 EEVLKASIQGVHGT 526
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
586-749 |
3.40e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.07 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 586 QADDLRSASLSDQAQIHKQSLDSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKAASREQRKCEEQRE 665
Cdd:TIGR02794 33 GGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 666 KALQEQRHTLEQKtedavRKWRTELdKERRNTLALQSKLTELQKEAEKEAvcLKQTLLSSEKELQELRT-------ALRE 738
Cdd:TIGR02794 113 QAEEKQKQAEEAK-----AKQAAEA-KAKAEAEAERKAKEEAAKQAEEEA--KAKAAAEAKKKAEEAKKkaeaeakAKAE 184
|
170
....*....|.
gi 326667833 739 REQKQQRRTAR 749
Cdd:TIGR02794 185 AEAKAKAEEAK 195
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
350-951 |
3.49e-04 |
|
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: 44.71 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 350 QQKTGMLHTLQKLREEVDQSKREHLSVQLSVKDSRAqvqnimselhRLQAQRDLCLEEVRVLQGQKCVSRSVSVLEREEM 429
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKEN----------KLQENRKIIEAQRKAIQELQFENEKVSLKLEEEI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 430 DRllenaKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKL-ASQKHLDHQI 508
Cdd:pfam05483 141 QE-----NKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVqAENARLEMHF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 509 KRFGALERIVAQKELLLQ--GTQEAKEGLLLELCSLREAHSLNLREMQNRSKKDMEQEIEKLTLQltkshKEELQNVCKQ 586
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKeiNDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQ-----DENLKELIEK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 587 ADDLRSaslsdQAQIHKQSLDSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKAASREQRKCeeQREK 666
Cdd:pfam05483 291 KDHLTK-----ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTC--SLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 667 ALQEQRHTLEqKTEDAVRKWRTELDKeRRNTLALQSKLT---ELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQK- 742
Cdd:pfam05483 364 LLRTEQQRLE-KNEDQLKIITMELQK-KSSELEEMTKFKnnkEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQEl 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 743 ----QQRRTARH------------EQQSRRWAQDIHAECVhlQELLKHHGLIVETEGSHSSDSSTVSSALQMLQSLTKSL 806
Cdd:pfam05483 442 ifllQAREKEIHdleiqltaiktsEEHYLKEVEDLKTELE--KEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 807 QQYINDLKTELSTQRRaaLQMSREKEQELRVQKEQLMEEKERALAALKEKLIQAHVEEMSSLSRGQLLMKNDEDVDGQCV 886
Cdd:pfam05483 520 EDIINCKKQEERMLKQ--IENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326667833 887 HLRRQLKAKDEELRQVHNSMAQWKDKTTA--RIAHKFELELNaELERRLPTSKAEQQKRLERLENEM 951
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAenKQLNAYEIKVN-KLELELASAKQKFEEIIDNYQKEI 663
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
338-495 |
4.58e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 338 LRELRISIAELQQQKTGMLHTLQKLREEVDQSKREHLSVQLSVKDSRAQVQNIMSELHRLQAQRDLCLEEV----RVLQG 413
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraRALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 414 QKCVSRSVSVL----------------------EREEMDRL------LENAKSELFSEQRRFRNTLDSMQERLDEVNQEL 465
Cdd:COG3883 98 SGGSVSYLDVLlgsesfsdfldrlsalskiadaDADLLEELkadkaeLEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190
....*....|....*....|....*....|
gi 326667833 466 EQREEDSRSLQEKYSELEKQLLHAIREKEQ 495
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
621-755 |
4.80e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 621 KQLKEALKQSEEKMRRQQEEFRRETE----EKIVKAASREQRKCEE------QREKALQEQRHTLEQKtEDAVRKWRTEL 690
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEaikkEALLEAKEEIHKLRNEfekelrERRNELQKLEKRLLQK-EENLDRKLELL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 691 DKERRNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELrTALREREQKQQ-----RRTARHEQQSR 755
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEAKEIllekvEEEARHEAAVL 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-510 |
6.26e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 256 RLSRENEYCTGQTIQNNGQPFSSDDERTVEETSSEGAKSKLFYRRRHSSGRKGKRNLYKSRRNEphigTEKTLDKSRNDg 335
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAE- 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 336 npLRELRISIAELQQqktgmlhTLQKLREEVDQSKREHLSVQLSVKDSRAQVQNIMSELHRLQAQRDLCLEEVRVLQGQK 415
Cdd:TIGR02168 812 --LTLLNEEAANLRE-------RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 416 CVSRSVSVLEREEMDrLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQ 495
Cdd:TIGR02168 883 ASLEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEN 961
|
250
....*....|....*
gi 326667833 496 IKLASQKHLDHQIKR 510
Cdd:TIGR02168 962 KIEDDEEEARRRLKR 976
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
338-533 |
6.52e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 338 LRELRISIAELQQ-------QKTGMLHTLQKLREEVDQSKREHLSVQLSVKDSRAQVQNIMSELHRLQA----QRDLCLE 406
Cdd:COG4942 29 LEQLQQEIAELEKelaalkkEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleaQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 407 EVRVLQGQKCVSRSVSVLEREEMDRLLENAK--SELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEK 484
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 326667833 485 QLLHAIREKEQIKLASQKHLDHQIKRFGALERIVAQKELLLQGTQEAKE 533
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
615-733 |
7.57e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.56 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 615 MKDEEVkqLKEALKQSEEKMRRQQEEFRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTEDA-------VRKWR 687
Cdd:cd16269 166 VKAEEV--LQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQersyeehLRQLK 243
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 326667833 688 TELDKERRNTLALQSKLTE--LQKEAEKEAVCLKQTLLSSEKELQELR 733
Cdd:cd16269 244 EKMEEERENLLKEQERALEskLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
585-759 |
7.78e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.00 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 585 KQADDLRSASLSDQAQIHKQSLDSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEekivkaasREQRKCEEQR 664
Cdd:pfam13904 17 EESSKHRVPSLSLDSSSQSSSLTYARKLEGLKLERQPLEAYENWLAAKQRQRQKELQAQKEE--------REKEEQEAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 665 EKALQEQRHT--LEQKTEDAvRKWRTELDKERRNTLALQSKLTELQKEAEKEAvclKQTLLSSEKELQELRTALREREQK 742
Cdd:pfam13904 89 RKRLAKEKYQewLQRKARQQ-TKKREESHKQKAAESASKSLAKPERKVSQEEA---KEVLQEWERKKLEQQQRKREEEQR 164
|
170
....*....|....*..
gi 326667833 743 QQRRTARHEQQSRRWAQ 759
Cdd:pfam13904 165 EQLKKEEEEQERKQLAE 181
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
449-672 |
8.46e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 449 NTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQlLHAIREKEQIKLASQKHLDHQIKRFGALERIVAQKELLLQGT 528
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 529 QEAKEGLLLELCSLREAHSLNLREMQNRSKKDMEQEIEKLTL--QLTKSHKEELQNVCKQADDLrsASLSDQAQIHKQSL 606
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELRADLAEL--AALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326667833 607 DSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKAASREQRKCEEQREKALQEQR 672
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
616-962 |
9.00e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 616 KDEEVKQLKEALKQSEEKMRRQQEEfRRETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTEDAVRK---WRTELDK 692
Cdd:COG4717 86 KEEEYAELQEELEELEEELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERleeLRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 693 ERRNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQKQQRRTARHEQQSRR--------WAQDIHAE 764
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleqlenelEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 765 CVHLQELLKHHGLIVETEGSHSSDSSTVSSALQMLQSL--------TKSLQQYINDLKTELSTQRRAALQMSREKEQELR 836
Cdd:COG4717 245 LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 837 VQKEQLMEEKERALAALKEKLIQAHVEEMSSLSRGQLLMKNDEDVDGQCVHLRRQLKAKDEELRQVHNSMAQWKDKTTAR 916
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 326667833 917 --IAHKFELELNAELERRLPTSKAEQQKRLERLENEMRHLTAQCRDHN 962
Cdd:COG4717 405 eeLEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
338-972 |
1.09e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 338 LRELRISIAELQQQKTGMLHTLQKLREEvDQSKREHL------SVQLSVKDSRAQVQNIMSELHRLQAQRDLCLEEVRVL 411
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSE-SQNKIELLlqqhqdRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 412 QGQKCVSRSVSVLEREEMDRLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLlhair 491
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL----- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 492 ekeqiklasQKHLDHQIKRfgalerivaQKELLLQGTQEAKegllleLCSLREAHSLNLREMQnRSKKDMEQEIEKLTlQ 571
Cdd:pfam15921 380 ---------QKLLADLHKR---------EKELSLEKEQNKR------LWDRDTGNSITIDHLR-RELDDRNMEVQRLE-A 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 572 LTKSHKEELQNVCKQ---ADDLRSASLSDQAQIHKQsLDSLHNCIKMKDEEVKQLKEALKQSEEKMR------RQQEEFR 642
Cdd:pfam15921 434 LLKAMKSECQGQMERqmaAIQGKNESLEKVSSLTAQ-LESTKEMLRKVVEELTAKKMTLESSERTVSdltaslQEKERAI 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 643 RETEEKIVKAASREQRKCEEQREKALQEQRHTLEQKTEDAVRKWRTELDKERRNTLALQSKLTELQKEAEKEAVCLKQTL 722
Cdd:pfam15921 513 EATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 723 LSSEKELQELRTALREREQKQQRRTARHEQQSRRwAQDIHAECVHLqellkhhglivetegshssdSSTVSSALQMLQSL 802
Cdd:pfam15921 593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEAR-VSDLELEKVKL--------------------VNAGSERLRAVKDI 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 803 TKSLQQYINDLKTElstqrRAALQMSREKEQELRVQKEQLMEEKERALAALKEKLIQAHveemSSLSRGQLLMKNDEDVD 882
Cdd:pfam15921 652 KQERDQLLNEVKTS-----RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQ----SELEQTRNTLKSMEGSD 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 883 GQCVH----LRRQLKAKDEELRQVHNSMAQWKDK-TTARIAHKFELELNAELERRLPTSKAEQQK---RLERLENEMRHL 954
Cdd:pfam15921 723 GHAMKvamgMQKQITAKRGQIDALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKmagELEVLRSQERRL 802
|
650
....*....|....*...
gi 326667833 955 TAQCRDHNISqLTSAAVQ 972
Cdd:pfam15921 803 KEKVANMEVA-LDKASLQ 819
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
618-739 |
1.99e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 618 EEVKQLKEALKQseekMRRQQEEFRRETEEKIVKAASR---EQRKCEEQREKALQEQRHtlEQKTEDAVRKWRTELDKER 694
Cdd:COG0542 411 EELDELERRLEQ----LEIEKEALKKEQDEASFERLAElrdELAELEEELEALKARWEA--EKELIEEIQELKEELEQRY 484
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326667833 695 RNTLALQSKLTELQKEAEKEAVCLKQT--------------------LLSSEKE-LQELRTALRER 739
Cdd:COG0542 485 GKIPELEKELAELEEELAELAPLLREEvteediaevvsrwtgipvgkLLEGEREkLLNLEEELHER 550
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
316-856 |
2.12e-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: 42.26 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 316 RRNEPHIGTEKTLDKSRNDGNPLRELRISIAELQQQKTGMLHTLQKLREEvdqskrehlsvqlsvkdsraqvqnimselh 395
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE------------------------------ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 396 rlQAQRDLCLEEVRVLQGQKCVSRSVSVLEREEMDrLLENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSL 475
Cdd:TIGR00618 409 --QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAE-LCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 476 QEKYSELEKQLLhaiREKEQIKLASQKHLDHQIKRFGALERIVAQKeLLLQGTQEAKEGLLLELCSLREAHSLNLREMQN 555
Cdd:TIGR00618 486 TRKKAVVLARLL---ELQEEPCPLCGSCIHPNPARQDIDNPGPLTR-RMQRGEQTYAQLETSEEDVYHQLTSERKQRASL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 556 RSKKDMEQEIEKLTLQLTKSHKEELQNVCKQADDLRsaslsdqaqihkqsldslhNCIKMKDEEVKQLKEALKQSEEKMR 635
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ-------------------DLTEKLSEAEDMLACEQHALLRKLQ 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 636 RQQEEFRReteekivkaaSREQRKCEEQREKALQEQRHTLEQKTEDAVR-KWRTELDKERRNTLALQSKLTELQKEAE-- 712
Cdd:TIGR00618 623 PEQDLQDV----------RLHLQQCSQELALKLTALHALQLTLTQERVReHALSIRVLPKELLASRQLALQKMQSEKEql 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 713 ---KEAVCLKQTLLSSEKE-LQELRTALREREQKQQRRTARHEQQSRRWAQDIHAECVHLQELLKHHGLIVETEGSHSSD 788
Cdd:TIGR00618 693 tywKEMLAQCQTLLRELEThIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTA 772
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 326667833 789 SSTVSSALQMLQSLTKSLQQYINDLKTELSTQRRAALQMSREKEQELRVQKEQLMEEKERALAALKEK 856
Cdd:TIGR00618 773 ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEK 840
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
442-685 |
2.22e-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: 41.67 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 442 SEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIklasQKHLDHQIKRFGALERIVAQK 521
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 522 ELLLQGTQEAKEGLLLELCSLREAHSLNLRemqnRSKKDMEQEIEKLTL--QLTKSHKEELQNVCKQADDLrsASLSDQA 599
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALL----LSPEDFLDAVRRLQYlkYLAPARREQAEELRADLAEL--AALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 600 QIHKQSLDSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKivkaasreqrkceEQREKALQEQRHTLEQKT 679
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-------------QQEAEELEALIARLEAEA 236
|
....*.
gi 326667833 680 EDAVRK 685
Cdd:COG4942 237 AAAAER 242
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
433-744 |
2.91e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.67 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 433 LENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAIREKEQIKLASQKHLDHQIKRFG 512
Cdd:pfam09731 130 LEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 513 ALERIVAQKELLLQGTQEAKEGLLLELCSLREAHSLN-LREMQNRSKKDMEQEIEKLTLQLTKSHKEELQnvcKQADDLR 591
Cdd:pfam09731 210 APPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDqYKELVASERIVFQQELVSIFPDIIPVLKEDNL---LSNDDLN 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 592 SASLSDQAQIHKqsldslHNC--IKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKAASRE----QRKCEEQRE 665
Cdd:pfam09731 287 SLIAHAHREIDQ------LSKklAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLrlefEREREEIRE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 666 K-------ALQEQRHTLEQKTEDAVRKWRTELDkeRRNTLALQSKLTElQKEAEKEAVC-LKQTLLSSEKELQELRTALR 737
Cdd:pfam09731 361 SyeeklrtELERQAEAHEEHLKDVLVEQEIELQ--REFLQDIKEKVEE-ERAGRLLKLNeLLANLKGLEKATSSHSEVED 437
|
....*..
gi 326667833 738 EREQKQQ 744
Cdd:pfam09731 438 ENRKAQQ 444
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
451-744 |
4.43e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 451 LDSMQERLDEVNQELEQREEDSRSLQEKYSElekqllhaiREKEQIKLASQKHLDHQIKRFGALERIVAQKELLLQGTQE 530
Cdd:COG5185 270 LGENAESSKRLNENANNLIKQFENTKEKIAE---------YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQN 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 531 AKEGLLLELCSLREAHSlnlREMQNRSKKDMEQEIEKLtlqltkshKEELQNVCKQADDLRSASLSDQAQIHKQS---LD 607
Cdd:COG5185 341 LTAEIEQGQESLTENLE---AIKEEIENIVGEVELSKS--------SEELDSFKDTIESTKESLDEIPQNQRGYAqeiLA 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 608 SLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKivkaasreqrkcEEQREKALQEQRHTLEQKTEDAVRKWR 687
Cdd:COG5185 410 TLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISEL------------NKVMREADEESQSRLEEAYDEINRSVR 477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 326667833 688 TELDKERRNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQKQQ 744
Cdd:COG5185 478 SKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-600 |
4.57e-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: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 358 TLQKLREEVDQSKREHLSVQLSVKDSRAQVQNIMSELHRLQAQRDLCLEEVRVLQGQKcVSRSVSVLEREEMDRLLENAK 437
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR-DKLTEEYAELKEELEDLRAEL 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 438 SELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAireKEQIKLASQKHLDHQIkrfgalERI 517
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL---NAAIAGIEAKINELEE------EKE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 518 VAQKELllqgtqEAKEGLLLELCSLREAHSlnlremqnRSKKDMEQEIEKLTLQLTKShKEELQNVCKQADDLRSASLSD 597
Cdd:TIGR02169 445 DKALEI------KKQEWKLEQLAADLSKYE--------QELYDLKEEYDRVEKELSKL-QRELAEAEAQARASEERVRGG 509
|
...
gi 326667833 598 QAQ 600
Cdd:TIGR02169 510 RAV 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
433-657 |
6.02e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 433 LENAKSELFSEQRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQLLHAirekeqiklasQKHLDHQIKRFG 512
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-----------EAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 513 alERIVAQKElllQGTQEAKEGLLLELCSLREA-HSLNLREMQNRSKKDMEQEIEKLTLQLtKSHKEELQNVCKQADDLR 591
Cdd:COG3883 90 --ERARALYR---SGGSVSYLDVLLGSESFSDFlDRLSALSKIADADADLLEELKADKAEL-EAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 326667833 592 saslsDQAQIHKQSLDSLhncIKMKDEEVKQLKEALKQSEEKMRRQQEEFRRETEEKIVKAASREQ 657
Cdd:COG3883 164 -----AELEAAKAELEAQ---QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
364-747 |
8.93e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.01 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 364 EEVDQSKREHLSVQLSVKdsRAQVQNimselhrLQAQRDLCLEEVRVLQGQKCVSRSVSVLEREEMDRLLENAKSELfSE 443
Cdd:pfam05701 70 EELESTKRLIEELKLNLE--RAQTEE-------AQAKQDSELAKLRVEEMEQGIADEASVAAKAQLEVAKARHAAAV-AE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 444 QRRFRNTLDSMQERLDEVNQELEQREEDSRSLQEKYSELEKQL----LHAIREKEQIKLASQKHLDHQIKRFG---ALER 516
Cdd:pfam05701 140 LKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVeeltIELIATKESLESAHAAHLEAEEHRIGaalAREQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 517 IVAQKELLLQGTQEAKEGLLLELCSLREAHS---------LNLRE-----MQNRSKKDMEQEIE--------KLTLQLTK 574
Cdd:pfam05701 220 DKLNWEKELKQAEEELQRLNQQLLSAKDLKSkletasallLDLKAelaayMESKLKEEADGEGNekktstsiQAALASAK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 575 SHKEELQ-NVCKQADDLR-----SASLSDQAQIHKQSLDSLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEfRRETEEK 648
Cdd:pfam05701 300 KELEEVKaNIEKAKDEVNclrvaAASLRSELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIALVQAK-EKEAREK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 649 IVKAAsreqRKCEEQREKAlqEQRHTLEQKTEDAVRKWRTELDKERRNTLALQSKLTELQKEAEKEAVCLKqTLLSSEKE 728
Cdd:pfam05701 379 MVELP----KQLQQAAQEA--EEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEK-LALAAIKA 451
|
410
....*....|....*....
gi 326667833 729 LQELRTALREREQKQQRRT 747
Cdd:pfam05701 452 LQESESSAESTNQEDSPRG 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
382-578 |
9.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 382 DSRAQVQNIMSELHRLQAQRDLCLEEVRVLQGQKcvsrsvsvLEREEMDRLLENAKSELFSEQRrfrntLDSMQERLDEV 461
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAEL--------DALQERREALQRLAEYSWDEID-----VASAEREIAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 462 NQELEQREEDS---RSLQEKYSELEKQLLHAIREKEQIKLASQKhLDHQIKRfgALERIVAQKELLLQGTQEAKEGLLLE 538
Cdd:COG4913 674 EAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGR-LEKELEQ--AEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 326667833 539 LCSLREAhsLNLREMQNRSKKDMEQEIEKLTLQLTKSHKE 578
Cdd:COG4913 751 LEERFAA--ALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
383-956 |
9.28e-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: 40.21 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 383 SRAQVQNIMSELHRLQAQRDLCLEEVRVLQGQKCVSRSVSVLEReemdrlLENAKSELFSEQRRFRNTLDSMQERLDEVN 462
Cdd:pfam12128 216 SRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELR------LSHLHFGYKSDETLIASRQEERQETSAELN 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 463 QELEQREEDsrsLQEKYSELeKQLLHAIREKEQIKLASQKHLDHQIKRF--GALERIVAQKELLLQGTQEAkEGLLLELC 540
Cdd:pfam12128 290 QLLRTLDDQ---WKEKRDEL-NGELSAADAAVAKDRSELEALEDQHGAFldADIETAAADQEQLPSWQSEL-ENLEERLK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 541 SLREAHSLNLREMQNRSKKDMEQEIEKLTlqltkSHKEELQNVCKQADDLRSASLSDQAQIHKQSLDSLHNCIKMKDEEV 620
Cdd:pfam12128 365 ALTGKHQDVTAKYNRRRSKIKEQNNRDIA-----GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 621 KQLKEALkqSEEKMRRQQEEFRRETEEKI------VKAASREQRKCEEQREkALQEQRHTLEQKTEDAVRKwrteLDKER 694
Cdd:pfam12128 440 YRLKSRL--GELKLRLNQATATPELLLQLenfderIERAREEQEAANAEVE-RLQSELRQARKRRDQASEA----LRQAS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 695 RNTLALQSKLTELQKEAEKEAVCLKQTLLSSEKELQELRTALREREQKQqrRTARH-EQQSRRWAQDIHAECVHLQELLK 773
Cdd:pfam12128 513 RRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLH--RTDLDpEVWDGSVGGELNLYGVKLDLKRI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 774 HHGLIVETEGSHSSDSSTVSSALQMLQSLTKSLQQYINDLKTELSTQRR------AALQMSREKEQELRVQKEQLMEEKE 847
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASReetfarTALKNARLDLRRLFDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 848 RALAA---LKEKLIQAHVEEMSSLSRGQLLMKndEDVDGQCVHLRRQLKAKDEELR-QVHNSMAQWKD-KTTARIAHKFE 922
Cdd:pfam12128 671 KALAErkdSANERLNSLEAQLKQLDKKHQAWL--EEQKEQKREARTEKQAYWQVVEgALDAQLALLKAaIAARRSGAKAE 748
|
570 580 590
....*....|....*....|....*....|....
gi 326667833 923 LELNAELERRLPTSKAEQQKRLERLENEMRHLTA 956
Cdd:pfam12128 749 LKALETWYKRDLASLGVDPDVIAKLKREIRTLER 782
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
598-742 |
9.97e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 326667833 598 QAQIHKQSLDsLHNCIKMKDEEVKQLKEALKQSEEKMRRQQEEFrreteekivkaasreqrkceEQREKALQEQRHTLEQ 677
Cdd:PRK12704 63 KEEIHKLRNE-FEKELRERRNELQKLEKRLLQKEENLDRKLELL--------------------EKREEELEKKEKELEQ 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 326667833 678 KTEDaVRKWRTELDKERRNTLALQSKLTELQKEaekEAvclKQTLLSS-EKELQELRTAL-REREQK 742
Cdd:PRK12704 122 KQQE-LEKKEEELEELIEEQLQELERISGLTAE---EA---KEILLEKvEEEARHEAAVLiKEIEEE 181
|
|
| |
