|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
7-744 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 274241 [Multi-domain] Cd Length: 730 Bit Score: 1182.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 7 NLEKTLHAALTDAGERRHEYATLEHLLLSLIDDEDAAQVMAACGVDLAELTAVVKQYLEQEYQSLQSDESADPQPTAGFQ 86
Cdd:TIGR02639 4 ELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIEILEECGGDVELLRKRLEDYLEENLPVIPEDIDEEPEQTVGVQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 87 RVIQRAILHVQSSGKDTVTGANVLVALFSERDSYAVYFLQQQDMSRLDAVSFISHGIGKggkpvesrspegaESGEAQGD 166
Cdd:TIGR02639 84 RVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISK-------------DDGKDQLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 167 DKAGDKGKK-ETALDQFTVNLNKKAEDGRIDPLIGRGPEVDRTVQILCRRSKNNPLYVGDPGVGKTAIAEGLARKIVEGD 245
Cdd:TIGR02639 151 EEAGKEEEKgQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 246 VPEVLQEAVIYSLDMGALLAGTRYRGDFEERLKQVVTELEGMPEAILFIDEIHTVIGAGATSGGAMDASNLLKPALSSGA 325
Cdd:TIGR02639 231 VPERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 326 IRCIGSTTYKEFRNHFEKDRALLRRFQKIDVNEPTIEDTVKILKGLKTAFQDHHKVTYTADALKTAVELSARYINDRKLP 405
Cdd:TIGR02639 311 IRCIGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 406 DKAIDVIDEVGAMQMLVPPSRRKKKITAREIEAVIATMARIPPKSVSKDDKKALENLERDLKHVVFGQDAAVKKLATAMK 485
Cdd:TIGR02639 391 DKAIDVIDEAGAAFRLRPKAKKKANVNVKDIENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 486 LSRAGLRDPDKPIGSFLFSGPTGVGKTEVARQLASIMGIELKRFDMSEYMERHSVSRLIGAPPGYVGYDQGGLLTDAVDQ 565
Cdd:TIGR02639 471 RSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEELGVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 566 NPHSVLLLDEIEKAHPDLFNILLQVMDNGRLTDHHGKTVDFRNVVLIMTTNAGAADMASQGIGFGDVSKEDASEEAVKRM 645
Cdd:TIGR02639 551 HPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVILIMTSNAGASEMSKPPIGFGGENRESKSLKAIKKL 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 646 FTPEFRNRLDAIVPFGYLGKDTVARVVDKFILQLELQLAEQNVDIQFDKEARAWLADKGYDRLFGARPMGRLIQDRIKQP 725
Cdd:TIGR02639 631 FSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKP 710
|
730
....*....|....*....
gi 1024463303 726 LAEELLFGKLADGGEVSVT 744
Cdd:TIGR02639 711 LSDEILFGKLKKGGSVKIS 729
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
8-753 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 1019.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 8 LEKTLHAALTDAGERRHEYATLEHLLLSLIDDEDAAQVMAACGVDLAELTAVVKQYLEQEYQSL-QSDESADPQPTAGFQ 86
Cdd:PRK11034 6 LELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLpASEEERDTQPTLSFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 87 RVIQRAILHVQSSGKDTVTGANVLVALFSERDSYAVYFLQQQDMSRLDAVSFISHGIGKggkpvESRSPEGAESGEAQGD 166
Cdd:PRK11034 86 RVLQRAVFHVQSSGRSEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRK-----DEPSQSSDPGSQPNSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 167 DKAGdkgkKETALDQFTVNLNKKAEDGRIDPLIGRGPEVDRTVQILCRRSKNNPLYVGDPGVGKTAIAEGLARKIVEGDV 246
Cdd:PRK11034 161 EQAG----GEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 247 PEVLQEAVIYSLDMGALLAGTRYRGDFEERLKQVVTELEGMPEAILFIDEIHTVIGAGATSGGAMDASNLLKPALSSGAI 326
Cdd:PRK11034 237 PEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 327 RCIGSTTYKEFRNHFEKDRALLRRFQKIDVNEPTIEDTVKILKGLKTAFQDHHKVTYTADALKTAVELSARYINDRKLPD 406
Cdd:PRK11034 317 RVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 407 KAIDVIDEVGAMQMLVPPSRRKKKITAREIEAVIATMARIPPKSVSKDDKKALENLERDLKHVVFGQDAAVKKLATAMKL 486
Cdd:PRK11034 397 KAIDVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKM 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 487 SRAGLRDPDKPIGSFLFSGPTGVGKTEVARQLASIMGIELKRFDMSEYMERHSVSRLIGAPPGYVGYDQGGLLTDAVDQN 566
Cdd:PRK11034 477 SRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKH 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 567 PHSVLLLDEIEKAHPDLFNILLQVMDNGRLTDHHGKTVDFRNVVLIMTTNAGAADMASQGIGFGDVSKEDASEEAVKRMF 646
Cdd:PRK11034 557 PHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIF 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 647 TPEFRNRLDAIVPFGYLGKDTVARVVDKFILQLELQLAEQNVDIQFDKEARAWLADKGYDRLFGARPMGRLIQDRIKQPL 726
Cdd:PRK11034 637 TPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPL 716
|
730 740
....*....|....*....|....*..
gi 1024463303 727 AEELLFGKLADGGEVSVTMKDGKPAFE 753
Cdd:PRK11034 717 ANELLFGSLVDGGQVTVALDKEKNELT 743
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
4-749 |
0e+00 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 870.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 4 FAANLEKTLHAALTDAGERRHEYATLEHLLLSLIDDED--AAQVMAACGVDLAELTAVVKQYLEQeyQSLQSDESADPQP 81
Cdd:COG0542 6 FTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEglAAKLLRKLGVDLDALREELEEALGR--LPKVSGSSGQPYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 82 TAGFQRVIQRAILHVQSSGKDTVTGANVLVALFSERDSYAVYFLQQQDMSR---LDAVSFIShgigkGGKPVESRSPEGa 158
Cdd:COG0542 84 SPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLealREALEELR-----GGSRVTSQNPES- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 159 esgeaqgddkagdkgkKETALDQFTVNLNKKAEDGRIDPLIGRGPEVDRTVQILCRRSKNNPLYVGDPGVGKTAIAEGLA 238
Cdd:COG0542 158 ----------------KTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 239 RKIVEGDVPEVLQEAVIYSLDMGALLAGTRYRGDFEERLKQVVTELEGMP-EAILFIDEIHTVIGAGATSgGAMDASNLL 317
Cdd:COG0542 222 QRIVNGDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEgNIILFIDELHTLVGAGGAE-GAMDAANLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 318 KPALSSGAIRCIGSTTYKEFRNHFEKDRALLRRFQKIDVNEPTIEDTVKILKGLKTAFQDHHKVTYTADALKTAVELSAR 397
Cdd:COG0542 301 KPALARGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 398 YINDRKLPDKAIDVIDEVGA---MQMLVPPS------RR----------------------------------------- 427
Cdd:COG0542 381 YITDRFLPDKAIDLIDEAAArvrMEIDSKPEeldeleRRleqleiekealkkeqdeasferlaelrdelaeleeelealk 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 428 ------------------------------------------------KKKITAREIEAVIATMARIPPKSVSKDDKKAL 459
Cdd:COG0542 461 arweaekelieeiqelkeeleqrygkipelekelaeleeelaelapllREEVTEEDIAEVVSRWTGIPVGKLLEGEREKL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 460 ENLERDLKHVVFGQDAAVKKLATAMKLSRAGLRDPDKPIGSFLFSGPTGVGKTEVARQLASIM-GIE--LKRFDMSEYME 536
Cdd:COG0542 541 LNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLfGDEdaLIRIDMSEYME 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 537 RHSVSRLIGAPPGYVGYDQGGLLTDAVDQNPHSVLLLDEIEKAHPDLFNILLQVMDNGRLTDHHGKTVDFRNVVLIMTTN 616
Cdd:COG0542 621 KHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSN 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 617 AGAADMASQGIGFGDVSK-EDASEEAVKRMFTPEFRNRLDAIVPFGYLGKDTVARVVDKFILQLELQLAEQNVDIQFDKE 695
Cdd:COG0542 701 IGSELILDLAEDEPDYEEmKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDA 780
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1024463303 696 ARAWLADKGYDRLFGARPMGRLIQDRIKQPLAEELLFGKLADGGEVSVTMKDGK 749
Cdd:COG0542 781 AKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGE 834
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
4-749 |
0e+00 |
|
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274529 [Multi-domain] Cd Length: 850 Bit Score: 718.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 4 FAANLEKTLHAALTDAGERRHEYATLEHLLLSLIDDED--AAQVMAACGVDLAELTAVVKQYLEQEYQSlqSDESADPQP 81
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGglARPLLQKAGVNVGALRQALEKELERLPKV--SGPGGQVYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 82 TAGFQRVIQRAILHVQSSGKDTVTGANVLVALFSERDSYAVYFLQ-----QQDMSRLDAVsfishgigKGGKPVESRSPE 156
Cdd:TIGR03346 79 SPDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEagataDALEAAINAV--------RGGQKVTDANAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 157 GaesgeaqgddkagdkgkKETALDQFTVNLNKKAEDGRIDPLIGRGPEVDRTVQILCRRSKNNPLYVGDPGVGKTAIAEG 236
Cdd:TIGR03346 151 D-----------------QYEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 237 LARKIVEGDVPEVLQEAVIYSLDMGALLAGTRYRGDFEERLKQVVTEL---EGmpEAILFIDEIHTVIGAGATsGGAMDA 313
Cdd:TIGR03346 214 LAQRIVNGDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVtksEG--QIILFIDELHTLVGAGKA-EGAMDA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 314 SNLLKPALSSGAIRCIGSTTYKEFRNHFEKDRALLRRFQKIDVNEPTIEDTVKILKGLKTAFQDHHKVTYTADALKTAVE 393
Cdd:TIGR03346 291 GNMLKPALARGELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAAT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 394 LSARYINDRKLPDKAIDVIDEVGA---MQMLVPP------SRR------------------------------------- 427
Cdd:TIGR03346 371 LSHRYITDRFLPDKAIDLIDEAAArirMEIDSKPeeldelDRRiiqleierealkkekdeaskkrledlekeladleeey 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 428 -------------------------------------------------------------------------KKKITAR 434
Cdd:TIGR03346 451 aeleeqwkaekasiqgiqqikeeieqvrleleqaeregdlakaaelqygklpelekqlqaaeqklgeeqnrllREEVTAE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 435 EIEAVIATMARIPpksVSK---DDKKALENLERDLKHVVFGQDAAVKKLATAMKLSRAGLRDPDKPIGSFLFSGPTGVGK 511
Cdd:TIGR03346 531 EIAEVVSRWTGIP---VSKmleGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGK 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 512 TEVARQLASIM---GIELKRFDMSEYMERHSVSRLIGAPPGYVGYDQGGLLTDAVDQNPHSVLLLDEIEKAHPDLFNILL 588
Cdd:TIGR03346 608 TELAKALAEFLfdsEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLL 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 589 QVMDNGRLTDHHGKTVDFRNVVLIMTTNAGAADMASQGIGFGDVSKEDASEEAVKRMFTPEFRNRLDAIVPFGYLGKDTV 668
Cdd:TIGR03346 688 QVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQI 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 669 ARVVDKFILQLELQLAEQNVDIQFDKEARAWLADKGYDRLFGARPMGRLIQDRIKQPLAEELLFGKLADGGEVSVTMKDG 748
Cdd:TIGR03346 768 ARIVEIQLGRLRKRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGG 847
|
.
gi 1024463303 749 K 749
Cdd:TIGR03346 848 R 848
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
22-749 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 670.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 22 RR--HEYATLEHLLLSLIDDED--AAQVMAACGVDLAELTAVVKQYLEQEYQSLQSDESADPQPTagfqRVIQRAILHVQ 97
Cdd:CHL00095 21 RRlgHNFVGTEQILLGLIGEGTgiAARALKSMGVTLKDARIEVEKIIGRGTGFVAVEIPFTPRAK----RVLEMSLEEAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 98 SSGKDTVTGANVLVALFSERDSYAVYFLQQQDMSRLDAVSFISHGIGkggkpvesrspegaESGEAQGDDKAGdKGKKET 177
Cdd:CHL00095 97 DLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLIG--------------EIIEAILGAEQS-RSKTPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 178 aLDQFTVNLNKKAEDGRIDPLIGRGPEVDRTVQILCRRSKNNPLYVGDPGVGKTAIAEGLARKIVEGDVPEVLQEAVIYS 257
Cdd:CHL00095 162 -LEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 258 LDMGALLAGTRYRGDFEERLKQVVTELEGMPEAILFIDEIHTVIGAGATSGgAMDASNLLKPALSSGAIRCIGSTTYKEF 337
Cdd:CHL00095 241 LDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEG-AIDAANILKPALARGELQCIGATTLDEY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 338 RNHFEKDRALLRRFQKIDVNEPTIEDTVKILKGLKTAFQDHHKVTYTADALKTAVELSARYINDRKLPDKAIDVIDEVGA 417
Cdd:CHL00095 320 RKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 418 ----MQMLVPPSRRK------------------------KKITAREIE-------------------------------A 438
Cdd:CHL00095 400 rvrlINSRLPPAAREldkelreilkdkdeaireqdfetaKQLRDREMEvraqiaaiiqskkteeekrlevpvvteediaE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 439 VIATMARIPPKSVSKDDKKALENLERDLKHVVFGQDAAVKKLATAMKLSRAGLRDPDKPIGSFLFSGPTGVGKTEVARQL 518
Cdd:CHL00095 480 IVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKAL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 519 ASIM-GIE--LKRFDMSEYMERHSVSRLIGAPPGYVGYDQGGLLTDAVDQNPHSVLLLDEIEKAHPDLFNILLQVMDNGR 595
Cdd:CHL00095 560 ASYFfGSEdaMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGR 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 596 LTDHHGKTVDFRNVVLIMTTNAGA--ADMASQGIGFgDVSKEDASE-----------EAVKRMFTPEFRNRLDAIVPFGY 662
Cdd:CHL00095 640 LTDSKGRTIDFKNTLIIMTSNLGSkvIETNSGGLGF-ELSENQLSEkqykrlsnlvnEELKQFFRPEFLNRLDEIIVFRQ 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 663 LGKDTVARVVDKFILQLELQLAEQNVDIQFDKEARAWLADKGYDRLFGARPMGRLIQDRIKQPLAEELLFGKLADGGEVS 742
Cdd:CHL00095 719 LTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIII 798
|
....*..
gi 1024463303 743 VTMKDGK 749
Cdd:CHL00095 799 VDVNDEK 805
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
15-748 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 570.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 15 ALTDAGE----RRHEYATLEHLLLSLIDDE--DAAQVMAACGVDLAELTAVVKQYLEQEYQSLQSDesADPQPTAGFQRV 88
Cdd:PRK10865 13 ALADAQSlalgHDNQFIEPLHLMSALLNQEggSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTG--GDVQPSQDLVRV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 89 IQRAILHVQSSGKDTVTGANVLVALFSERDSYAvyflqqqDMsrLDAVSFISHGIgkggkpveSRSPEGAESGEAQGDDK 168
Cdd:PRK10865 91 LNLCDKLAQKRGDNFISSELFVLAALESRGTLA-------DI--LKAAGATTANI--------TQAIEQMRGGESVNDQG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 169 AGDKgkkETALDQFTVNLNKKAEDGRIDPLIGRGPEVDRTVQILCRRSKNNPLYVGDPGVGKTAIAEGLARKIVEGDVPE 248
Cdd:PRK10865 154 AEDQ---RQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 249 VLQEAVIYSLDMGALLAGTRYRGDFEERLKQVVTEL---EGmpEAILFIDEIHTVIGAGaTSGGAMDASNLLKPALSSGA 325
Cdd:PRK10865 231 GLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLakqEG--NVILFIDELHTMVGAG-KADGAMDAGNMLKPALARGE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 326 IRCIGSTTYKEFRNHFEKDRALLRRFQKIDVNEPTIEDTVKILKGLKTAFQDHHKVTYTADALKTAVELSARYINDRKLP 405
Cdd:PRK10865 308 LHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 406 DKAIDVIDEVGA---MQMLVPP---------------------------------------------------------- 424
Cdd:PRK10865 388 DKAIDLIDEAASsirMQIDSKPeeldrldrriiqlkleqqalmkesdeaskkrldmlneelsdkerqyseleeewkaeka 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 425 ---------------------SRR------------------------------------KKKITAREIEAVIATMARIP 447
Cdd:PRK10865 468 slsgtqtikaeleqakiaieqARRvgdlarmselqygkipelekqlaaatqlegktmrllRNKVTDAEIAEVLARWTGIP 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 448 PKSVSKDDKKALENLERDLKHVVFGQDAAVKKLATAMKLSRAGLRDPDKPIGSFLFSGPTGVGKTEVARQLASIM---GI 524
Cdd:PRK10865 548 VSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMfdsDD 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 525 ELKRFDMSEYMERHSVSRLIGAPPGYVGYDQGGLLTDAVDQNPHSVLLLDEIEKAHPDLFNILLQVMDNGRLTDHHGKTV 604
Cdd:PRK10865 628 AMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTV 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 605 DFRNVVLIMTTNAGaADMASQgiGFGDVSKEDASE---EAVKRMFTPEFRNRLDAIVPFGYLGKDTVARVVDKFILQLEL 681
Cdd:PRK10865 708 DFRNTVVIMTSNLG-SDLIQE--RFGELDYAHMKElvlGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYK 784
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024463303 682 QLAEQNVDIQFDKEARAWLADKGYDRLFGARPMGRLIQDRIKQPLAEELLFGKLADGGEVSVTMKDG 748
Cdd:PRK10865 785 RLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDD 851
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
6-738 |
0e+00 |
|
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274528 [Multi-domain] Cd Length: 852 Bit Score: 561.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 6 ANLEKTLHAALTDAGERRHEYATLEHLLLSLID--DEDAAQVMAACGVDLAELtavvKQYLEQEYQSLQSDESADPQPTA 83
Cdd:TIGR03345 3 PTSRRALEQAAALCVARGHPEVELEHWLLALLDqpDSDLAAILRHFGVDLGRL----KADLARALDKLPRGNTRTPVFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 84 GFQRVIQRA-ILHVQSSGKDTVTGANVLVALFSERDSYAVYFLQQQDMSRL--DAVSFISHGIGKGgkpvesrSPEGAES 160
Cdd:TIGR03345 79 HLVELLQEAwLLASLELGDGRIRSGHLLLALLTDPELRRLLGSISPELAKIdrEALREALPALVEG-------SAEASAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 161 GEAQGDDKAGDKGKKETALDQFTVNLNKKAEDGRIDPLIGRGPEVDRTVQILCRRSKNNPLYVGDPGVGKTAIAEGLARK 240
Cdd:TIGR03345 152 AADAAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 241 IVEGDVPEVLQEAVIYSLDMGALLAGTRYRGDFEERLKQVVTELEGMPEA-ILFIDEIHTVIGAGATSGGAmDASNLLKP 319
Cdd:TIGR03345 232 IAAGDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPiILFIDEAHTLIGAGGQAGQG-DAANLLKP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 320 ALSSGAIRCIGSTTYKEFRNHFEKDRALLRRFQKIDVNEPTIEDTVKILKGLKTAFQDHHKVTYTADALKTAVELSARYI 399
Cdd:TIGR03345 311 ALARGELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 400 NDRKLPDKAIDVID----EVGAMQMLVPPS----RRKKKITAREIEA--------------------------------- 438
Cdd:TIGR03345 391 PGRQLPDKAVSLLDtacaRVALSQNATPAAledlRRRIAALELELDAlereaalgadhderlaelraelaaleaelaale 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 439 ------------------------------------------------------------------VIATMARIPPKSVS 452
Cdd:TIGR03345 471 arwqqekelveailalraeleadadapaddddalraqlaeleaalasaqgeeplvfpevdaqavaeVVADWTGIPVGRMV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 453 KDDKKALENLERDLKHVVFGQDAAVKKLATAMKLSRAGLRDPDKPIGSFLFSGPTGVGKTEVARQLASIM-GIE--LKRF 529
Cdd:TIGR03345 551 RDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLyGGEqnLITI 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 530 DMSEYMERHSVSRLIGAPPGYVGYDQGGLLTDAVDQNPHSVLLLDEIEKAHPDLFNILLQVMDNGRLTDHHGKTVDFRNV 609
Cdd:TIGR03345 631 NMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNT 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 610 VLIMTTNAGAADMASQGIGFGDVSKEDASEEAVK----RMFTPEFRNRLdAIVPFGYLGKDTVARVVDKFILQLELQLAE 685
Cdd:TIGR03345 711 VILLTSNAGSDLIMALCADPETAPDPEALLEALRpellKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRLKE 789
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1024463303 686 Q-NVDIQFDKEARAWLADKGYDRLFGARPMGRLIQDRIKQPLAEELLfGKLADG 738
Cdd:TIGR03345 790 NhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL-ERLAAG 842
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
459-660 |
2.72e-87 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 273.28 E-value: 2.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 459 LENLERDLKHVVFGQDAAVKKLATAMKLSRAGLRDPDKPIGSFLFSGPTGVGKTEVARQLASIM---GIELKRFDMSEYM 535
Cdd:cd19499 2 LLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLfgdEDNLIRIDMSEYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 536 ERHSVSRLIGAPPGYVGYDQGGLLTDAVDQNPHSVLLLDEIEKAHPDLFNILLQVMDNGRLTDHHGKTVDFRNVVLIMTT 615
Cdd:cd19499 82 EKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMTS 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1024463303 616 NAgaadmasqgigfgdvskedaseeavkrmFTPEFRNRLDAIVPF 660
Cdd:cd19499 162 NH----------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
496-657 |
5.88e-80 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 253.66 E-value: 5.88e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 496 KPIGSFLFSGPTGVGKTEVARQLASIMGI---ELKRFDMSEYMERHSVSRLIGAPPGYVGYDQGGLLTDAVDQNPHSVLL 572
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 573 LDEIEKAHPDLFNILLQVMDNGRLTDHHGKTVDFRNVVLIMTTNAGAA---DMASQGIGFGDVSKEDASEEAVKRMFTPE 649
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEkisDASRLGDSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 1024463303 650 FRNRLDAI 657
Cdd:pfam07724 161 FLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
360-464 |
6.43e-32 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465544 [Multi-domain] Cd Length: 104 Bit Score: 119.51 E-value: 6.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 360 TIEDTVKILKGLKTAFQDHHKVTYTADALKTAVELSARYINDRKLPDKAIDVIDEVGAMQMLvppSRRKKKITAREIEAV 439
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRL---SQESKPEELEDLERE 77
|
90 100
....*....|....*....|....*
gi 1024463303 440 IATMARIPPKSVSKDDKKALENLER 464
Cdd:pfam17871 78 LAKLEIEKEALEREQDFEKAERLAK 102
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
663-743 |
2.42e-27 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.
Pssm-ID: 463090 [Multi-domain] Cd Length: 81 Bit Score: 105.57 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 663 LGKDTVARVVDKFILQLELQLAEQNVDIQFDKEARAWLADKGYDRLFGARPMGRLIQDRIKQPLAEELLFGKLADGGEVS 742
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 1024463303 743 V 743
Cdd:pfam10431 81 V 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
663-752 |
2.68e-27 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.
Pssm-ID: 198154 [Multi-domain] Cd Length: 90 Bit Score: 105.99 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 663 LGKDTVARVVDKFILQLELQLAEQNVDIQFDKEARAWLADKGYDRLFGARPMGRLIQDRIKQPLAEELLFGKLADGGEVS 742
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 1024463303 743 VTMKDGKPAF 752
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
199-354 |
1.70e-17 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 80.27 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 199 IGRGPEVDRTVQILCRRSKNNPLYVGDPGVGKTAIAEGLARKIVEGDVPevlqeavIYSLDMGALLAGTRYRGDFEERLK 278
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024463303 279 QVVTEL-EGMPEAILFIDEIHTvIGAGATSGGAMDASNLLKPALSSGAIRCIGSTTYKEFRnhfEKDRALLRRFQKI 354
Cdd:cd00009 74 RLLFELaEKAKPGVLFIDEIDS-LSRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLG---DLDRALYDRLDIR 146
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
471-616 |
4.89e-15 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 72.95 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 471 FGQDAAVKKLATAMKlsraglRDPDKPIgsfLFSGPTGVGKTEVARQLA---SIMGIELKRFDMSEYMERHSVSRLIgap 547
Cdd:cd00009 1 VGQEEAIEALREALE------LPPPKNL---LLYGPPGTGKTTLARAIAnelFRPGAPFLYLNASDLLEGLVVAELF--- 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024463303 548 pgyvGYDQGGLLTDAVDQNPHSVLLLDEIEKAHPDLFNILLQVMDNGRLTdhhgkTVDFRNVVLIMTTN 616
Cdd:cd00009 69 ----GHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
221-354 |
1.16e-13 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 68.39 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLARKIvegDVPevlqeavIYSLDMGALLAGtrYRGDFEERLKQVVTELEGMPEAILFIDEIHTV 300
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKEL---GAP-------FIEISGSELVSK--YVGESEKRLRELFEAAKKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024463303 301 IGAGATSGG--AMDASNLLKPAL-----SSGAIRCIGSTtykefrNHFEK-DRALLRRFQKI 354
Cdd:pfam00004 70 AGSRGSGGDseSRRVVNQLLTELdgftsSNSKVIVIAAT------NRPDKlDPALLGRFDRI 125
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
502-616 |
1.70e-12 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 64.92 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 502 LFSGPTGVGKTEVARQLASIMGIELKRFDMSEymerhSVSRLIGAPPGYVgydqGGLLTDAVDQNPhSVLLLDEIEKAHP 581
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-----LVSKYVGESEKRL----RELFEAAKKLAP-CVIFIDEIDALAG 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1024463303 582 -----------DLFNILLQVMDngrltdhhGKTVDFRNVVLIMTTN 616
Cdd:pfam00004 72 srgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
500-616 |
3.00e-11 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 61.54 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 500 SFLFSGPTGVGKTEVARQLAS-IMGIELKRFDMSEYMERhsvSRLIGappGYVGYDQGGLLTDAV----DQNPHsVLLLD 574
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAaLSNRPVFYVQLTRDTTE---EDLFG---RRNIDPGGASWVDGPlvraAREGE-IAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1024463303 575 EIEKAHPDLFNILLQVMDNGRLTDHHGKT---VDFRNVVLIMTTN 616
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
221-369 |
3.74e-11 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 65.70 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLARkivEGDVPevlqeavIYSLDMGALLAGtrYRGDFEERLKQVVTELEGMPEAILFIDEIHTV 300
Cdd:COG0464 195 LLYGPPGTGKTLLARALAG---ELGLP-------LIEVDLSDLVSK--YVGETEKNLREVFDKARGLAPCVLFIDEADAL 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024463303 301 IGA-GATSGGAMDA--SNLLK--PALSSGAIrCIGSTtykefrNHFEK-DRALLRRFQ-KIDVNEPTIEDTVKILK 369
Cdd:COG0464 263 AGKrGEVGDGVGRRvvNTLLTemEELRSDVV-VIAAT------NRPDLlDPALLRRFDeIIFFPLPDAEERLEIFR 331
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
475-616 |
3.84e-11 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 61.92 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 475 AAVKKLATAMKLSRAGLRDPDKPIGSFLFSGPTGVGKTEVARQLASIMGIELKRFDMSEYMERHSvsrligappgYVGYD 554
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYV----------GESEK 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024463303 555 QGGLLTDAVDQNPHSVLLLDEIEKAHPD------------LFNILLQVMDNGRLTDhhgktvdfrNVVLIMTTN 616
Cdd:cd19481 73 NLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
459-698 |
6.55e-10 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 61.85 E-value: 6.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 459 LENLERDLKHVVfgqdAAVKKLATAMKlsRAGLRdpdkPIGSFLFSGPTGVGKTEVARQLASIMGIELKRFDMSEymerh 538
Cdd:COG0464 162 LEEVKEELRELV----ALPLKRPELRE--EYGLP----PPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSD----- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 539 svsrLIGappGYVGYDQGGL--LTDAVDQNPHSVLLLDEIEKAHPD-----------LFNILLQVMDNGRltdhhgktvd 605
Cdd:COG0464 227 ----LVS---KYVGETEKNLreVFDKARGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR---------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 606 fRNVVLIMTTNagaadmasqgigfgdvsKEDASEEAVKRmftpefrnRLDAIVPFGYLGKDTVARvvdkfILQLELQLAE 685
Cdd:COG0464 290 -SDVVVIAATN-----------------RPDLLDPALLR--------RFDEIIFFPLPDAEERLE-----IFRIHLRKRP 338
|
250
....*....|...
gi 1024463303 686 QNVDIQFDKEARA 698
Cdd:COG0464 339 LDEDVDLEELAEA 351
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
502-616 |
1.15e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 502 LFSGPTGVGKTEVARQLASIMGIELKRF---DMSEYMERHSVSRLIGAPPGYVGYDQGG----LLTDAVDQNPHSVLLLD 574
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGViyiDGEDILEEVLDQLLLIIVGGKKASGSGElrlrLALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1024463303 575 EIEKAHPDLFNILLQVMDNGRLTDHHGKtvdFRNVVLIMTTN 616
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTN 124
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
19-65 |
2.19e-08 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 50.98 E-value: 2.19e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1024463303 19 AGERRHEYATLEHLLLSLIDDED--AAQVMAACGVDLAELTAVVKQYLE 65
Cdd:pfam02861 5 ARALGHQYIGTEHLLLALLEEDDglAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
476-616 |
4.68e-08 |
|
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410908 [Multi-domain] Cd Length: 182 Bit Score: 53.72 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 476 AVKKLATAMKlsraglrdpdKPIgsFLFSGPTGVGKTEVARQLASIMGIELKRF------DMSE-------Ymerhsvsr 542
Cdd:cd19500 27 AVRKLKGSMK----------GPI--LCLVGPPGVGKTSLGKSIARALGRKFVRIslggvrDEAEirghrrtY-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 543 lIGAPPGYVgyDQGglLTDAVDQNPhsVLLLDEIEK----AHPDLFNILLQVMD---NGRLTDHH-GKTVDFRNVVLIMT 614
Cdd:cd19500 87 -VGAMPGRI--IQA--LKKAGTNNP--VFLLDEIDKigssFRGDPASALLEVLDpeqNSTFSDHYlDVPFDLSKVLFIAT 159
|
..
gi 1024463303 615 TN 616
Cdd:cd19500 160 AN 161
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
467-578 |
6.25e-08 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 53.15 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 467 KHVVfGQDAAVKKLATA-------MKLSrAGLRDPDKPiGSFLFSGPTGVGKTEVARQLASIMGIELKRFDMSEYMErhs 539
Cdd:cd19498 11 KYII-GQDEAKRAVAIAlrnrwrrMQLP-EELRDEVTP-KNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTE--- 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1024463303 540 vsrligapPGYVGYDQGGLLTDAVDqnphSVLLLDEIEK 578
Cdd:cd19498 85 --------VGYVGRDVESIIRDLVE----GIVFIDEIDK 111
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
223-354 |
6.53e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.38 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 223 VGDPGVGKTAIAEGLARKIVEGDVPEVL-----QEAVIYSLDMGALLAGTRYRGDFEERLKQVVTELEGMPEAILFIDEI 297
Cdd:smart00382 8 VGPPGSGKTTLARALARELGPPGGGVIYidgedILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEI 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1024463303 298 HTVIGAGATSGG-AMDASNLLKPALSSGAIRCIGSTTykefRNHFEKDRALLRRFQKI 354
Cdd:smart00382 88 TSLLDAEQEALLlLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRR 141
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
218-369 |
1.47e-07 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 53.35 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 218 NNPLYVGDPGVGKTAIAEGLARKIvegDVPevlqeavIYSLDMGALLagTRYRGDFEERLKQVVTELEGMPeAILFIDEI 297
Cdd:COG1223 36 RKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSLI--GSYLGETARNLRKLFDFARRAP-CVIFFDEF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 298 HTvIGA--GATSGGA------------MDasnllkpALSSGAIrCIGSTtykefrNHFEK-DRALLRRFQ-KIDVNEPTI 361
Cdd:COG1223 103 DA-IAKdrGDQNDVGevkrvvnallqeLD-------GLPSGSV-VIAAT------NHPELlDSALWRRFDeVIEFPLPDK 167
|
....*...
gi 1024463303 362 EDTVKILK 369
Cdd:COG1223 168 EERKEILE 175
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
460-615 |
3.24e-07 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 52.86 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 460 ENLERDLKHVVFGQDAAVKKLATAMKLsraglrdpDKPIgsfLFSGPTGVGKTEVARQLASIMGIELKRF----DMseyM 535
Cdd:COG0714 4 ARLRAEIGKVYVGQEELIELVLIALLA--------GGHL---LLEGVPGVGKTTLAKALARALGLPFIRIqftpDL---L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 536 ErhsvSRLIGAppgYVgYDQ---------GGLLTdavdqnphSVLLLDEIEKAHPDLFNILLQVMDNGRLT-DhhGKTVD 605
Cdd:COG0714 70 P----SDILGT---YI-YDQqtgefefrpGPLFA--------NVLLADEINRAPPKTQSALLEAMEERQVTiP--GGTYK 131
|
170
....*....|
gi 1024463303 606 FRNVVLIMTT 615
Cdd:COG0714 132 LPEPFLVIAT 141
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
221-445 |
7.34e-07 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 51.93 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLARKIvegdvpevlqEAVIYSLDMGALLagTRYRGDFEERLKQVVTELEGMPEAILFIDEIHTv 300
Cdd:COG1222 116 LLYGPPGTGKTLLAKAVAGEL----------GAPFIRVRGSELV--SKYIGEGARNVREVFELAREKAPSIIFIDEIDA- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 301 IGAGATSGGAMDASNLLKPAL--------SSGAIRCIGSTtykefrNHFEK-DRALLR--RF-QKIDVNEPTIEDTVKIL 368
Cdd:COG1222 183 IAARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAAT------NRPDLlDPALLRpgRFdRVIEVPLPDEEAREEIL 256
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024463303 369 KGLKTAFQDHHKVTYTADALKTAvELSARYIndrklpdKAIdvIDEVGAMQMLvppsRRKKKITAREIEAVIATMAR 445
Cdd:COG1222 257 KIHLRDMPLADDVDLDKLAKLTE-GFSGADL-------KAI--VTEAGMFAIR----EGRDTVTMEDLEKAIEKVKK 319
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
221-354 |
7.77e-07 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 49.59 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLARKIVegdvpevlqeAVIYSLDMGALLagTRYRGDFEERLKQVVTELEGMPEAILFIDEIHTV 300
Cdd:cd19481 30 LLYGPPGTGKTLLAKALAGELG----------LPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024463303 301 IGAGATSGGAMDAS-------NLLKPALSSGAIRCIGSTtykefrNHFEK-DRALLR--RFQKI 354
Cdd:cd19481 98 GRKRDSSGESGELRrvlnqllTELDGVNSRSKVLVIAAT------NRPDLlDPALLRpgRFDEV 155
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
467-523 |
4.99e-06 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 49.69 E-value: 4.99e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024463303 467 KHVVfGQDAAVKKLATA-------MKLSrAGLRD---PdKPIgsfLFSGPTGVGKTEVARQLASIMG 523
Cdd:PRK05201 15 KYII-GQDDAKRAVAIAlrnrwrrMQLP-EELRDevtP-KNI---LMIGPTGVGKTEIARRLAKLAN 75
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
221-309 |
1.16e-05 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410915 [Multi-domain] Cd Length: 161 Bit Score: 46.21 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLArkivegdvpEVLQEAVIySLDMGALLAGtrYRGDFEERLKQVVTELEGMPEAILFIDEIHTV 300
Cdd:cd19507 35 LLVGIQGTGKSLTAKAIA---------GVWQLPLL-RLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEIEKG 102
|
....*....
gi 1024463303 301 IGaGATSGG 309
Cdd:cd19507 103 FS-NADSKG 110
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
467-523 |
1.37e-05 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 48.50 E-value: 1.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024463303 467 KHVVfGQDAAVKKLATA-------MKLSrAGLRD---PdKPIgsfLFSGPTGVGKTEVARQLASIMG 523
Cdd:COG1220 15 KYII-GQDEAKRAVAIAlrnrwrrQQLP-EELRDeitP-KNI---LMIGPTGVGKTEIARRLAKLAN 75
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
224-398 |
2.64e-05 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 47.39 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 224 GDPGVGKTAIAEGLARKIvegdvpevlqEAVIYSLDmgALLAGTryrgdfeERLKQVVTELEGMPEA----ILFIDEIHt 299
Cdd:PRK13342 43 GPPGTGKTTLARIIAGAT----------DAPFEALS--AVTSGV-------KDLREVIEEARQRRSAgrrtILFIDEIHr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 300 vigagatsggamDAsnLLkPALSSGAIRCIGSTTykEfrN-HFEKDRALLRRFQKIDVNEPTIEDtvkILKGLKTAFQDH 378
Cdd:PRK13342 104 fnk------aqqDA--LL-PHVEDGTITLIGATT--E--NpSFEVNPALLSRAQVFELKPLSEED---IEQLLKRALEDK 167
|
170 180
....*....|....*....|....*
gi 1024463303 379 HK--VTYTADALKTAVELS---ARY 398
Cdd:PRK13342 168 ERglVELDDEALDALARLAngdARR 192
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
397-617 |
1.29e-04 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 45.70 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 397 RYINDRKLPDKAIDVID-EVGAMQMLVPPSRRkkkitAREIEAVIATMARIPPKS---VSKDDKKALENLERDLKHVVFG 472
Cdd:PRK10787 256 RKIDAAKMPKEAKEKAEaELQKLKMMSPMSAE-----ATVVRGYIDWMVQVPWNArskVKKDLRQAQEILDTDHYGLERV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 473 QDAAVKKLATAMKLSRAglrdpDKPIgsFLFSGPTGVGKTEVARQLASIMGIELKRFDMSEYMERHSVSrliGAPPGYVG 552
Cdd:PRK10787 331 KDRILEYLAVQSRVNKI-----KGPI--LCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIR---GHRRTYIG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024463303 553 YDQGGLLTDAVD---QNPhsVLLLDEIEKAHPDL----FNILLQVMD---NGRLTDHHGKT-VDFRNVVLIMTTNA 617
Cdd:PRK10787 401 SMPGKLIQKMAKvgvKNP--LFLLDEIDKMSSDMrgdpASALLEVLDpeqNVAFSDHYLEVdYDLSDVMFVATSNS 474
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
470-519 |
1.52e-04 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 44.80 E-value: 1.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1024463303 470 VFGQDAAVKKLATAMKLSRaglrdpdkpIG-SFLFSGPTGVGKTEVARQLA 519
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILA 53
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
221-332 |
2.16e-04 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 42.66 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLARkivEGDVPevlqeavIYSLDMGALLAGtrYRGDFEERLKQVVTELEGMPEAILFIDEIHTV 300
Cdd:cd19503 38 LLHGPPGTGKTLLARAVAN---EAGAN-------FLSISGPSIVSK--YLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
90 100 110
....*....|....*....|....*....|....*...
gi 1024463303 301 IGAGATSGGAMDAS------NLLKPALSSGAIRCIGST 332
Cdd:cd19503 106 APKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAAT 143
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
499-595 |
3.91e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 41.17 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 499 GSFLFSGPTGVGKTEVARQLAS---IMGIELKRFDMSEYME----RHSVSRLIGAPPGYvGYDQGGLLT----DAVDQNP 567
Cdd:pfam13401 6 GILVLTGESGTGKTTLLRRLLEqlpEVRDSVVFVDLPSGTSpkdlLRALLRALGLPLSG-RLSKEELLAalqqLLLALAV 84
|
90 100
....*....|....*....|....*...
gi 1024463303 568 HSVLLLDEIEKAHPDLFNILLQVMDNGR 595
Cdd:pfam13401 85 AVVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
221-520 |
5.29e-04 |
|
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.
Pssm-ID: 273521 [Multi-domain] Cd Length: 733 Bit Score: 43.74 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLARKIvegdvpevlqEAVIYSLDMGALLagTRYRGDFEERLKQVVTELEGMPEAILFIDEIHTV 300
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEA----------GAYFISINGPEIM--SKYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 301 IGAGATSGGAMDAS------NLLKPALSSGAIRCIGSTTYKEfrnhfEKDRALLR--RFQK-IDVNEPTIEDTVKILK-- 369
Cdd:TIGR01243 284 APKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATNRPD-----ALDPALRRpgRFDReIVIRVPDKRARKEILKvh 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 370 ------GLKTAFQDHHKVTY-------TADALKTAVELSARYINDRKLPDKAIDVIDEVgAMQMLVPPSRRKKKITAREI 436
Cdd:TIGR01243 359 trnmplAEDVDLDKLAEVTHgfvgadlAALAKEAAMAALRRFIREGKINFEAEEIPAEV-LKELKVTMKDFMEALKMVEP 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 437 EAVIATMARIPpkSVSKDDKKALENLERDLKhvvfgqDAAVKKLATAMKLSRAGLRDPDkpiGSFLFsGPTGVGKTEVAR 516
Cdd:TIGR01243 438 SAIREVLVEVP--NVRWSDIGGLEEVKQELR------EAVEWPLKHPEIFEKMGIRPPK---GVLLF-GPPGTGKTLLAK 505
|
....
gi 1024463303 517 QLAS 520
Cdd:TIGR01243 506 AVAT 509
|
|
| PRK14953 |
PRK14953 |
DNA polymerase III subunits gamma and tau; Provisional |
470-519 |
6.65e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237867 [Multi-domain] Cd Length: 486 Bit Score: 42.89 E-value: 6.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1024463303 470 VFGQDAAVKKLATAMKLSRAGlrdpdkpiGSFLFSGPTGVGKTEVARQLA 519
Cdd:PRK14953 18 VIGQEIVVRILKNAVKLQRVS--------HAYIFAGPRGTGKTTIARILA 59
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
197-317 |
1.42e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.18 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 197 PLIGRGPEVDRTVQILCRRSKNNPLYV---GDPGVGKTAIAEGLARKIVEGDVPEVLQEAVIYSLDMGALLAGTRyrgdf 273
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPPSVlltGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPLLEALTR----- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1024463303 274 EERLKQVVTELEGMpEAILFIDEIHTVIGAGATSGGAMDASNLL 317
Cdd:pfam13191 76 EGLLRQLLDELESS-LLEAWRAALLEALAPVPELPGDLAERLLD 118
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
221-298 |
2.84e-03 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 38.81 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLARKIVEGDVPEVL------QEAVIYSLDMGALLAgtryrgdfeERLKQVVTElEGMPEAILFI 294
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVFYVQltrdttEEDLFGRRNIDPGGA---------SWVDGPLVR-AAREGEIAVL 72
|
....
gi 1024463303 295 DEIH 298
Cdd:pfam07728 73 DEIN 76
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
221-353 |
4.58e-03 |
|
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410917 [Multi-domain] Cd Length: 163 Bit Score: 38.49 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLARKIvegdvpevlqEAVIYSLDMGALLAgtRYRGDFEERLKQVVTELEGMPEAILFIDEIHTV 300
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024463303 301 IG---AGATSGGAMDASNLLK-----PALSSGAIRCIGSTTYKEfrnhfEKDRALLRRFQK 353
Cdd:cd19509 104 LSergSGEHEASRRVKTEFLVqmdgvLNKPEDRVLVLGATNRPW-----ELDEAFLRRFEK 159
|
|
| ycf46 |
CHL00195 |
Ycf46; Provisional |
221-297 |
5.23e-03 |
|
Ycf46; Provisional
Pssm-ID: 177094 [Multi-domain] Cd Length: 489 Bit Score: 40.00 E-value: 5.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024463303 221 LYVGDPGVGKTAIAEGLARkivEGDVPevlqeavIYSLDMGALLAGTRyrGDFEERLKQVVTELEGMPEAILFIDEI 297
Cdd:CHL00195 263 LLVGIQGTGKSLTAKAIAN---DWQLP-------LLRLDVGKLFGGIV--GESESRMRQMIRIAEALSPCILWIDEI 327
|
|
| PRK06305 |
PRK06305 |
DNA polymerase III subunits gamma and tau; Validated |
470-519 |
5.54e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 180523 [Multi-domain] Cd Length: 451 Bit Score: 40.14 E-value: 5.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1024463303 470 VFGQDAAVKKLATAMKLSRAGlrdpdkpiGSFLFSGPTGVGKTEVARQLA 519
Cdd:PRK06305 19 ILGQDAVVAVLKNALRFNRAA--------HAYLFSGIRGTGKTTLARIFA 60
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
221-300 |
7.59e-03 |
|
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410927 [Multi-domain] Cd Length: 166 Bit Score: 38.19 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024463303 221 LYVGDPGVGKTAIAEGLARK------IVEGdvPEVLqeaviysldmgallagTRYRGDFEERLKQVVTELEGMPEAILFI 294
Cdd:cd19519 38 LLYGPPGTGKTLIARAVANEtgafffLING--PEIM----------------SKLAGESESNLRKAFEEAEKNAPAIIFI 99
|
....*.
gi 1024463303 295 DEIHTV 300
Cdd:cd19519 100 DEIDAI 105
|
|
| |
