|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-811 |
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: 1300.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 1 MNFNRFTQRAKKAIDLAFESAKSLGHNIVGSEHILLGLLREEEGIAAKVLSKVGFTEAYLEGKIVDMEGKGEEIS---ED 77
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSgssGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 78 IVLSPRSKQILELSGMFANKLKTNYIGTEHILLAIIQEGEGIANKILNYAGVNDRTLAQLTIDMMGISDKNQYKAENSYt 157
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPESKT- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 158 gnqnqaesKVLDKYGRNLTLYAKQNKIDPVIGREKEIQRVIQILSRRTKNNPVLIGDPGVGKTAIAEGLATNIALGNVPE 237
Cdd:COG0542 160 --------PALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 238 TLKNKTLYSLEMGSLLAGAKYRGEFEERIKEVVDEVVK-NGNIILFIDEMHTIIGAGSTgEGSIDASNILKPALARGEIQ 316
Cdd:COG0542 232 SLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGA-EGAMDAANLLKPALARGELR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 317 VIGATTIDEYRKHVEKDSALERRFQPVMVDEPTKEDSIKILEGLRDKYEAHHKVKITDDAIKAAVELSTRYISDRYLPDK 396
Cdd:COG0542 311 CIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 397 AIDLIDEAASKVRLKENTPPSEIKKLELEIENIDKEKEEAVRCQD---FEKAAKIRDEQGLLKKQLEDVRERWNK----- 468
Cdd:COG0542 391 AIDLIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEALKARWEAekeli 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 469 ----------------------------------SSKHSDLVDGEVIAEVVGLWTGIPVNKILEEEADRLLRLEEILHNR 514
Cdd:COG0542 471 eeiqelkeeleqrygkipelekelaeleeelaelAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHER 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 515 VIGQEQAVKSISKAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELSKALAEVQFGDENQIIRIDMSEYMEKHAVSRMIGS 594
Cdd:COG0542 551 VIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIGA 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 595 PPGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPDVFNILLQILDDGRLTDSKGRTVDFKNTIVIMTSNVGASTIGRQK 674
Cdd:COG0542 631 PPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELILDLA 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 675 tlgfsiakgdeEEKSQYEKMKENIMGELKQRFRPEFLNRIDDIIVFHSLNENHISKIVLLMAAKLQERLKEMDIKLEMSD 754
Cdd:COG0542 711 -----------EDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTD 779
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 489520788 755 EAVKLISKSGFDLEYGARPLKRALQKELEDELSEAILKGNVKKGSNVVAKVKDEKIV 811
Cdd:COG0542 780 AAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-811 |
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: 1056.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 6 FTQRAKKAIDLAFESAKSLGHNIVGSEHILLGLLREEEGIAAKVLSKVGFTEAYLEGKIVD-------MEGKGEEISedi 78
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKelerlpkVSGPGGQVY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 79 vLSPRSKQILELSGMFANKLKTNYIGTEHILLAIIQEGeGIANKILNYAGVNDRTLAQLTIDMMG---ISDKNqykAENS 155
Cdd:TIGR03346 78 -LSPDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDK-GTLGKLLKEAGATADALEAAINAVRGgqkVTDAN---AEDQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 156 YtgnqnqaesKVLDKYGRNLTLYAKQNKIDPVIGREKEIQRVIQILSRRTKNNPVLIGDPGVGKTAIAEGLATNIALGNV 235
Cdd:TIGR03346 153 Y---------EALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 236 PETLKNKTLYSLEMGSLLAGAKYRGEFEERIKEVVDEVVK-NGNIILFIDEMHTIIGAGSTgEGSIDASNILKPALARGE 314
Cdd:TIGR03346 224 PEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKsEGQIILFIDELHTLVGAGKA-EGAMDAGNMLKPALARGE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 315 IQVIGATTIDEYRKHVEKDSALERRFQPVMVDEPTKEDSIKILEGLRDKYEAHHKVKITDDAIKAAVELSTRYISDRYLP 394
Cdd:TIGR03346 303 LHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 395 DKAIDLIDEAASKVRLKENTPPSE-------IKKLELEIENIDKEKEEAV--RCQDFEKA-AKIRDEQGLL--------- 455
Cdd:TIGR03346 383 DKAIDLIDEAAARIRMEIDSKPEEldeldrrIIQLEIEREALKKEKDEASkkRLEDLEKElADLEEEYAELeeqwkaeka 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 456 --------KKQLEDVR------ER---WNKSS--KHSDL-------------------------VDGEVIAEVVGLWTGI 491
Cdd:TIGR03346 463 siqgiqqiKEEIEQVRleleqaERegdLAKAAelQYGKLpelekqlqaaeqklgeeqnrllreeVTAEEIAEVVSRWTGI 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 492 PVNKILEEEADRLLRLEEILHNRVIGQEQAVKSISKAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELSKALAEVQFGDE 571
Cdd:TIGR03346 543 PVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 572 NQIIRIDMSEYMEKHAVSRMIGSPPGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPDVFNILLQILDDGRLTDSKGRT 651
Cdd:TIGR03346 623 DAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRT 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 652 VDFKNTIVIMTSNVGASTIGRQktlgfsiakgdeEEKSQYEKMKENIMGELKQRFRPEFLNRIDDIIVFHSLNENHISKI 731
Cdd:TIGR03346 703 VDFRNTVIIMTSNLGSDFIQEL------------AGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARI 770
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 732 VLLMAAKLQERLKEMDIKLEMSDEAVKLISKSGFDLEYGARPLKRALQKELEDELSEAILKGNVKKGSNVVAKVKDEKIV 811
Cdd:TIGR03346 771 VEIQLGRLRKRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRLV 850
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
3-809 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 995.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 3 FNRFTQRAKKAIDLAFESAKSLGHNIVGSEHILLGLLREEEGIAAKVLSKVGFTEAYLEGKIVDMEGKGEE-ISEDIVLS 81
Cdd:CHL00095 2 FERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGRGTGfVAVEIPFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 82 PRSKQILELSGMFANKLKTNYIGTEHILLAIIQEGEGIANKILNYAGVNDRTLAQLTIDMMGISdknqykAENSYTGNQN 161
Cdd:CHL00095 82 PRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLIGEI------IEAILGAEQS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 162 QAESKVLDKYGRNLTLYAKQNKIDPVIGREKEIQRVIQILSRRTKNNPVLIGDPGVGKTAIAEGLATNIALGNVPETLKN 241
Cdd:CHL00095 156 RSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 242 KTLYSLEMGSLLAGAKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTIIGAGSTgEGSIDASNILKPALARGEIQVIGAT 321
Cdd:CHL00095 236 KLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAA-EGAIDAANILKPALARGELQCIGAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 322 TIDEYRKHVEKDSALERRFQPVMVDEPTKEDSIKILEGLRDKYEAHHKVKITDDAIKAAVELSTRYISDRYLPDKAIDLI 401
Cdd:CHL00095 315 TLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 402 DEAASKVRLKENTPPSEIKKLELEIENIDKEKEEAVRCQDFEKAAKIRDEQGLLKKQLEDV---RERWNKSSKHSDLVDG 478
Cdd:CHL00095 395 DEAGSRVRLINSRLPPAARELDKELREILKDKDEAIREQDFETAKQLRDREMEVRAQIAAIiqsKKTEEEKRLEVPVVTE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 479 EVIAEVVGLWTGIPVNKILEEEADRLLRLEEILHNRVIGQEQAVKSISKAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTE 558
Cdd:CHL00095 475 EDIAEIVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTE 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 559 LSKALAEVQFGDENQIIRIDMSEYMEKHAVSRMIGSPPGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPDVFNILLQI 638
Cdd:CHL00095 555 LTKALASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQI 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 639 LDDGRLTDSKGRTVDFKNTIVIMTSNVGASTIGRQK-TLGFSiAKGDEEEKSQYEKMKENIMGELKQRFRPEFLNRIDDI 717
Cdd:CHL00095 635 LDDGRLTDSKGRTIDFKNTLIIMTSNLGSKVIETNSgGLGFE-LSENQLSEKQYKRLSNLVNEELKQFFRPEFLNRLDEI 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 718 IVFHSLNENHISKIVLLMAAKLQERLKEMDIKLEMSDEAVKLISKSGFDLEYGARPLKRALQKELEDELSEAILKGNVKK 797
Cdd:CHL00095 714 IVFRQLTKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKP 793
|
810
....*....|..
gi 489520788 798 GSNVVAKVKDEK 809
Cdd:CHL00095 794 GDIIIVDVNDEK 805
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-811 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 792.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 1 MNFNRFTQRakkaIDLAFESAKSLG----HNIVGSEHILLGLLREEEGIAAKVLSKVGFTEAYLE-------GKIVDMEG 69
Cdd:PRK10865 1 MRLDRLTNK----FQLALADAQSLAlghdNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRtdinqalSRLPQVEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 70 KGEEI--SEDIVlsprskQILELSGMFANKLKTNYIGTEHILLAIIQEGEGIANkILNYAGVNDRTLAQLTIDMMGISDK 147
Cdd:PRK10865 77 TGGDVqpSQDLV------RVLNLCDKLAQKRGDNFISSELFVLAALESRGTLAD-ILKAAGATTANITQAIEQMRGGESV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 148 NQYKAENsytgnQNQAeskvLDKYGRNLTLYAKQNKIDPVIGREKEIQRVIQILSRRTKNNPVLIGDPGVGKTAIAEGLA 227
Cdd:PRK10865 150 NDQGAED-----QRQA----LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 228 TNIALGNVPETLKNKTLYSLEMGSLLAGAKYRGEFEERIKEVVDEVVKN-GNIILFIDEMHTIIGAGStGEGSIDASNIL 306
Cdd:PRK10865 221 QRIINGEVPEGLKGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQeGNVILFIDELHTMVGAGK-ADGAMDAGNML 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 307 KPALARGEIQVIGATTIDEYRKHVEKDSALERRFQPVMVDEPTKEDSIKILEGLRDKYEAHHKVKITDDAIKAAVELSTR 386
Cdd:PRK10865 300 KPALARGELHCVGATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 387 YISDRYLPDKAIDLIDEAASKVRLKENTPPSEIKKLE---------------------------LEIENIDKEKEEAVRC 439
Cdd:PRK10865 380 YIADRQLPDKAIDLIDEAASSIRMQIDSKPEELDRLDrriiqlkleqqalmkesdeaskkrldmLNEELSDKERQYSELE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 440 QDF--EKA--------------AKIRDEQGL------------------LKKQLEDVRERWNKSSK--HSDLVDGEvIAE 483
Cdd:PRK10865 460 EEWkaEKAslsgtqtikaeleqAKIAIEQARrvgdlarmselqygkipeLEKQLAAATQLEGKTMRllRNKVTDAE-IAE 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 484 VVGLWTGIPVNKILEEEADRLLRLEEILHNRVIGQEQAVKSISKAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELSKAL 563
Cdd:PRK10865 539 VLARWTGIPVSRMLESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKAL 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 564 AEVQFGDENQIIRIDMSEYMEKHAVSRMIGSPPGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPDVFNILLQILDDGR 643
Cdd:PRK10865 619 ANFMFDSDDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGR 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 644 LTDSKGRTVDFKNTIVIMTSNVGASTIgrQKTLGfsiakgdeeeKSQYEKMKENIMGELKQRFRPEFLNRIDDIIVFHSL 723
Cdd:PRK10865 699 LTDGQGRTVDFRNTVVIMTSNLGSDLI--QERFG----------ELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPL 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 724 NENHISKIVLLMAAKLQERLKEMDIKLEMSDEAVKLISKSGFDLEYGARPLKRALQKELEDELSEAILKGNVKKGSNVVA 803
Cdd:PRK10865 767 GEQHIASIAQIQLQRLYKRLEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRL 846
|
....*...
gi 489520788 804 KVKDEKIV 811
Cdd:PRK10865 847 EVNDDRIV 854
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
6-801 |
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: 784.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 6 FTQRAKKAIDLAFESAKSLGHNIVGSEHILLGLLREEEGIAakVLSKVGFTEAYLEGKIVDMEGKG-----EEISEDIVL 80
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIE--ILEECGGDVELLRKRLEDYLEENlpvipEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 81 SPRSKQILELSGMFANKLKTNYIGTEHILLAIIQEGEGIANKILNYAGVNDRTLAQLTIDmmGISDKNQYKAENSYTGNQ 160
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISH--GISKDDGKDQLGEEAGKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 161 NQAESKVLDKYGRNLTLYAKQNKIDPVIGREKEIQRVIQILSRRTKNNPVLIGDPGVGKTAIAEGLATNIALGNVPETLK 240
Cdd:TIGR02639 157 EEKGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 241 NKTLYSLEMGSLLAGAKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTIIGAGSTGEGSIDASNILKPALARGEIQVIGA 320
Cdd:TIGR02639 237 NAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGATSGGSMDASNLLKPALSSGKIRCIGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 321 TTIDEYRKHVEKDSALERRFQPVMVDEPTKEDSIKILEGLRDKYEAHHKVKITDDAIKAAVELSTRYISDRYLPDKAIDL 400
Cdd:TIGR02639 317 TTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 401 IDEAASKVRLKEntppseikkleleieniDKEKEEAVRCQDFEkaakirdeqgllkkqledvrerwnksskhsdlvdgEV 480
Cdd:TIGR02639 397 IDEAGAAFRLRP-----------------KAKKKANVNVKDIE-----------------------------------NV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 481 IAEVvglwTGIPVNKILEEEADRLLRLEEILHNRVIGQEQAVKSISKAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELS 560
Cdd:TIGR02639 425 VAKM----AKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELA 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 561 KALAEvQFGDEnqIIRIDMSEYMEKHAVSRMIGSPPGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPDVFNILLQILD 640
Cdd:TIGR02639 501 KQLAE-ELGVH--LLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMD 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 641 DGRLTDSKGRTVDFKNTIVIMTSNVGASTIGrQKTLGFsiaKGDEEEksqyekmkENIMGELKQRFRPEFLNRIDDIIVF 720
Cdd:TIGR02639 578 YATLTDNNGRKADFRNVILIMTSNAGASEMS-KPPIGF---GGENRE--------SKSLKAIKKLFSPEFRNRLDAIIHF 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 721 HSLNENHISKIVLLMAAKLQERLKEMDIKLEMSDEAVKLISKSGFDLEYGARPLKRALQKELEDELSEAILKGNVKKGSN 800
Cdd:TIGR02639 646 NDLSEEMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGS 725
|
.
gi 489520788 801 V 801
Cdd:TIGR02639 726 V 726
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
10-791 |
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: 728.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 10 AKKAIDLAFESAKSLGHNIVGSEHILLGLLREEEGIAAKVLSKVGFTEAYLEGKI---VDMEGKGEeiSEDIVLSPRSKQ 86
Cdd:TIGR03345 5 SRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLaraLDKLPRGN--TRTPVFSPHLVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 87 ILELSGMFAN-KLKTNYIGTEHILLAIIQEGEgIANKILNYAgvndRTLAQLTIDMM---------GISDKNQYKAENSY 156
Cdd:TIGR03345 83 LLQEAWLLASlELGDGRIRSGHLLLALLTDPE-LRRLLGSIS----PELAKIDREALrealpalveGSAEASAAAADAAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 157 TGNQNQAESK-VLDKYGRNLTLYAKQNKIDPVIGREKEIQRVIQILSRRTKNNPVLIGDPGVGKTAIAEGLATNIALGNV 235
Cdd:TIGR03345 158 AGAAAGAAGTsALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 236 PETLKNKTLYSLEMGSLLAGAKYRGEFEERIKEVVDEVVKNGN-IILFIDEMHTIIGAGSTgEGSIDASNILKPALARGE 314
Cdd:TIGR03345 238 PPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQpIILFIDEAHTLIGAGGQ-AGQGDAANLLKPALARGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 315 IQVIGATTIDEYRKHVEKDSALERRFQPVMVDEPTKEDSIKILEGLRDKYEAHHKVKITDDAIKAAVELSTRYISDRYLP 394
Cdd:TIGR03345 317 LRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 395 DKAIDLIDEAASKVRLKENTPPSEIKKLELEIENIDKE-----KEEAVRCQDFEKAAKIRDEQGLLKKQLEDVRERWNK- 468
Cdd:TIGR03345 397 DKAVSLLDTACARVALSQNATPAALEDLRRRIAALELEldaleREAALGADHDERLAELRAELAALEAELAALEARWQQe 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 469 ----------------------SSKHSDL-----------------------VDGEVIAEVVGLWTGIPVNKILEEEADR 503
Cdd:TIGR03345 477 kelveailalraeleadadapaDDDDALRaqlaeleaalasaqgeeplvfpeVDAQAVAEVVADWTGIPVGRMVRDEIEA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 504 LLRLEEILHNRVIGQEQAVKSISKAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELSKALAEVQFGDENQIIRIDMSEYM 583
Cdd:TIGR03345 557 VLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSEFQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 584 EKHAVSRMIGSPPGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPDVFNILLQILDDGRLTDSKGRTVDFKNTIVIMTS 663
Cdd:TIGR03345 637 EAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILLTS 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 664 NVGASTIgrqktlgfSIAKGDEEEKSQYEKMKENIMGELKQRFRPEFLNRIdDIIVFHSLNENHISKIVLLMAAKLQERL 743
Cdd:TIGR03345 717 NAGSDLI--------MALCADPETAPDPEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIARRL 787
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 489520788 744 KE-MDIKLEMSDEAVKLISKSGFDLEYGARPLKRALQKELEDELSEAIL 791
Cdd:TIGR03345 788 KEnHGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQIL 836
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
152-813 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 577.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 152 AENSYTGNQNQAESKvLDKYGRNLTLYAKQNKIDPVIGREKEIQRVIQILSRRTKNNPVLIGDPGVGKTAIAEGLATNIA 231
Cdd:PRK11034 154 GSQPNSEEQAGGEER-MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 232 LGNVPETLKNKTLYSLEMGSLLAGAKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTIIGAGSTGEGSIDASNILKPALA 311
Cdd:PRK11034 233 QGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLS 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 312 RGEIQVIGATTIDEYRKHVEKDSALERRFQPVMVDEPTKEDSIKILEGLRDKYEAHHKVKITDDAIKAAVELSTRYISDR 391
Cdd:PRK11034 313 SGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDR 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 392 YLPDKAIDLIDEAASKVRLkenTPPSEIKKleleienidkekeeAVRCQDFEkaakirdeqgllkkqledvrerwnkssk 471
Cdd:PRK11034 393 HLPDKAIDVIDEAGARARL---MPVSKRKK--------------TVNVADIE---------------------------- 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 472 hsdlvdgeviaEVVGLWTGIPVNKILEEEADRLLRLEEILHNRVIGQEQAVKSISKAIRRSRAGLKDPNRPIGSFLFLGP 551
Cdd:PRK11034 428 -----------SVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGP 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 552 TGVGKTELSKALAEVqFGDEnqIIRIDMSEYMEKHAVSRMIGSPPGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPDV 631
Cdd:PRK11034 497 TGVGKTEVTVQLSKA-LGIE--LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDV 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 632 FNILLQILDDGRLTDSKGRTVDFKNTIVIMTSNVGASTIGRqKTLGFSiakgdEEEKSQyekmkeNIMGELKQRFRPEFL 711
Cdd:PRK11034 574 FNLLLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETER-KSIGLI-----HQDNST------DAMEEIKKIFTPEFR 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 712 NRIDDIIVFHSLNENHISKIVLLMAAKLQERLKEMDIKLEMSDEAVKLISKSGFDLEYGARPLKRALQKELEDELSEAIL 791
Cdd:PRK11034 642 NRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELL 721
|
650 660
....*....|....*....|..
gi 489520788 792 KGNVKKGSNVVAKVKDEKIVFE 813
Cdd:PRK11034 722 FGSLVDGGQVTVALDKEKNELT 743
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
503-720 |
3.53e-107 |
|
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: 326.06 E-value: 3.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 503 RLLRLEEILHNRVIGQEQAVKSISKAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELSKALAEVQFGDENQIIRIDMSEY 582
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 583 MEKHAVSRMIGSPPGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPDVFNILLQILDDGRLTDSKGRTVDFKNTIVIMT 662
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489520788 663 SNVgastigrqktlgfsiakgdeeeksqyekmkenimgelkqrFRPEFLNRIDDIIVF 720
Cdd:cd19499 161 SNH----------------------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
541-717 |
3.14e-91 |
|
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: 284.09 E-value: 3.14e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 541 RPIGSFLFLGPTGVGKTELSKALAEVQFGDENQIIRIDMSEYMEKHAVSRMIGSPPGYVGHDEGGQLTEKVRRNPYSVIL 620
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 621 FDEIEKAHPDVFNILLQILDDGRLTDSKGRTVDFKNTIVIMTSNVGASTIGRQKTLGFSIAkgdeeeksqYEKMKENIMG 700
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASRLGDSPD---------YELLKEEVMD 151
|
170
....*....|....*..
gi 489520788 701 ELKQRFRPEFLNRIDDI 717
Cdd:pfam07724 152 LLKKGFIPEFLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
349-452 |
6.30e-46 |
|
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: 159.19 E-value: 6.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 349 TKEDSIKILEGLRDKYEAHHKVKITDDAIKAAVELSTRYISDRYLPDKAIDLIDEAASKVRLKENTPPSEIKKLELEIEN 428
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 489520788 429 IDKEKEEAVRCQDFEKAAKIRDEQ 452
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKLE 104
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
723-802 |
1.65e-26 |
|
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: 103.25 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 723 LNENHISKIVLLMAAKLQERLKEMDIKLEMSDEAVKLISKSGFDLEYGARPLKRALQKELEDELSEAILKGNVKKGSNVV 802
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
723-812 |
3.18e-25 |
|
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: 100.21 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 723 LNENHISKIVLLMAAKLQERLKEMDIKLEMSDEAVKLISKSGFDLEYGARPLKRALQKELEDELSEAILKGNVKKGSNVV 802
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 489520788 803 AKVKDEKIVF 812
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
188-341 |
4.89e-18 |
|
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: 81.81 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 188 IGREKEIQRVIQILSRRTKNNPVLIGDPGVGKTAIAEGLATNIALGNVPetlknktLYSLEMGSLLAGAKYRGEFEERIK 267
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489520788 268 EVVDEVVKNG-NIILFIDEMHTIigAGSTGEGSIDASNILKPALA-RGEIQVIGATTIDEYRKhveKDSALERRFQ 341
Cdd:cd00009 74 RLLFELAEKAkPGVLFIDEIDSL--SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGD---LDRALYDRLD 144
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
516-664 |
2.10e-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: 79.88 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 516 IGQEQAVKSISKAIRRsraglkdpnRPIGSFLFLGPTGVGKTELSKALAEVQFGDENQIIRIDMSEYMEKHAVSrmigsp 595
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVA------ 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489520788 596 pGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPDVFNILLQILDDGRLTdskgrTVDFKNTIVIMTSN 664
Cdd:cd00009 66 -ELFGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
211-341 |
3.66e-14 |
|
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: 69.93 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 211 LIGDPGVGKTAIAEGLATNIalgnvpetlkNKTLYSLEMGSLLAgaKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTII 290
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDALA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489520788 291 GAGSTGEG--SIDASNILKPAL-----ARGEIQVIGATT-IDEYrkhvekDSALERRFQ 341
Cdd:pfam00004 71 GSRGSGGDseSRRVVNQLLTELdgftsSNSKVIVIAATNrPDKL------DPALLGRFD 123
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
545-664 |
9.01e-14 |
|
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: 68.86 E-value: 9.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 545 SFLFLGPTGVGKTELSKALAEVQFGDENQIIRidMSEYMEKhavSRMIGS----PPGYVGHDegGQLTEKVRRNpySVIL 620
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnidPGGASWVD--GPLVRAAREG--EIAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489520788 621 FDEIEKAHPDVFNILLQILDDGRLTDSKGRT---VDFKNTIVIMTSN 664
Cdd:pfam07728 72 LDEINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
547-672 |
1.24e-13 |
|
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: 68.94 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 547 LFLGPTGVGKTELSKALAEVQFGDENQIIRIDMSEYMEKHAVSRMIGSPPGYVGHDEGGQ----LTEKVRRNPYSVILFD 622
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489520788 623 EIEKAHPDVFNILLQILDDGRLTDSKGRtvdFKNTIVIMTSNVGASTIGR 672
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGPA 132
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-67 |
2.12e-10 |
|
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: 56.76 E-value: 2.12e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489520788 17 AFESAKSLGHNIVGSEHILLGLLREEEGIAAKVLSKVGFTEAYLEGKIVDM 67
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKL 51
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
210-358 |
3.21e-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: 63.01 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 210 VLIGDPGVGKTAIAEGLATNIalgnvpetlkNKTLYSLEMGSLLAgaKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTI 289
Cdd:COG0464 195 LLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADAL 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489520788 290 IGA-GSTGEGSID-ASNILKPALA--RGEIQVIGATtideYRKHvEKDSALERRFQPVM-VDEPTKEDSIKILE 358
Cdd:COG0464 263 AGKrGEVGDGVGRrVVNTLLTEMEelRSDVVVIAAT----NRPD-LLDPALLRRFDEIIfFPLPDAEERLEIFR 331
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
518-664 |
3.45e-10 |
|
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: 59.22 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 518 QEQAVKSISKAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELSKALAE---VQFgdenqiIRIDMSEYMEKHavsrmigs 594
Cdd:cd19481 1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGelgLPL------IVVKLSSLLSKY-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 595 ppGYVGHDEGGQLTEKVRRNPYSVILFDEIEKAHPD------------VFNILLQILDDGRLTDskgrtvdfkNTIVIMT 662
Cdd:cd19481 67 --VGESEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAA 135
|
..
gi 489520788 663 SN 664
Cdd:cd19481 136 TN 137
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
393-664 |
9.00e-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: 61.47 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 393 LPDKAIDLIDEAASKVRLKENTPPSEIKKLELEIENIDKEKEEAVRCQDFEKAAKIRDEQGLLKKQLEDVRERWNKSSKH 472
Cdd:COG0464 38 LLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 473 SDLVDGEVIAEVVGLWTGIPVNKILEEEADRLLRLEEILhNRVIG---QEQAVKSISKAIRRSRAGLKDPN-RPIGSFLF 548
Cdd:COG0464 118 LLELLRESAEALALAAPLVTYEDIGGLEEELLELREAIL-DDLGGleeVKEELRELVALPLKRPELREEYGlPPPRGLLL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 549 LGPTGVGKTELSKALAEvQFGDenQIIRIDMSEYMEKhavsrmigsppgYVGHDEGG--QLTEKVRRNPYSVILFDEIEK 626
Cdd:COG0464 197 YGPPGTGKTLLARALAG-ELGL--PLIEVDLSDLVSK------------YVGETEKNlrEVFDKARGLAPCVLFIDEADA 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489520788 627 AHPD-----------VFNILLQILDDGRltdskgrtvdfKNTIVIMTSN 664
Cdd:COG0464 262 LAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN 299
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
185-403 |
1.10e-09 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 59.51 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 185 DPVIGRE---KEIQRVIQILSRR---------TKNNPVLIGDPGVGKTAIAEGLATNIalgNVPetlknktLYSLEMGSL 252
Cdd:COG1223 2 DDVVGQEeakKKLKLIIKELRRRenlrkfglwPPRKILFYGPPGTGKTMLAEALAGEL---KLP-------LLTVRLDSL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 253 LAgaKYRGEFEERIKEVVDEVvKNGNIILFIDEMHTIIGAGSTGEGSIDASNILKPALA-----RGEIQVIGATTideyr 327
Cdd:COG1223 72 IG--SYLGETARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQeldglPSGSVVIAATN----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 328 kHVEK-DSALERRFQPVM-VDEPTKEDSIKILE----GLRDKYEAHHK--------------VKITDDAIKAAVELSTRY 387
Cdd:COG1223 144 -HPELlDSALWRRFDEVIeFPLPDKEERKEILElnlkKFPLPFELDLKklakkleglsgadiEKVLKTALKKAILEDREK 222
|
250
....*....|....*.
gi 489520788 388 ISDRYLpDKAIDLIDE 403
Cdd:COG1223 223 VTKEDL-EEALKQRKE 237
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
210-629 |
2.80e-08 |
|
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: 57.61 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 210 VLIGDPGVGKTAIAEGLATNIalgnvpetlkNKTLYSLEMGSLLAgaKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTI 289
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEA----------GAYFISINGPEIMS--KYYGESEERLREIFKEAEENAPSIIFIDEIDAI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 290 IGAGSTGEGSIDAS------NILKPALARGEIQVIGATTideyrKHVEKDSALER--RF-QPVMVDEPTKEDSIKILegl 360
Cdd:TIGR01243 284 APKREEVTGEVEKRvvaqllTLMDGLKGRGRVIVIGATN-----RPDALDPALRRpgRFdREIVIRVPDKRARKEIL--- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 361 rdKYEAHHKVKITDDAIKAAVELSTRYISdrylPDKAIdLIDEAASKVrLKENTPPSeikKLELEIENIDKE--KEEAVR 438
Cdd:TIGR01243 356 --KVHTRNMPLAEDVDLDKLAEVTHGFVG----ADLAA-LAKEAAMAA-LRRFIREG---KINFEAEEIPAEvlKELKVT 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 439 CQDFEKAAKIRDEQGLLKKQLEDVRERWNksskhsdlvdgeviaEVVGLwtgipvnkileEEADRLLRleeilhnrvigq 518
Cdd:TIGR01243 425 MKDFMEALKMVEPSAIREVLVEVPNVRWS---------------DIGGL-----------EEVKQELR------------ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 519 eqavKSISKAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELSKALAEvqfGDENQIIRIDMSEYMEKhavsrmigsppgY 598
Cdd:TIGR01243 467 ----EAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVAT---ESGANFIAVRGPEILSK------------W 527
|
410 420 430
....*....|....*....|....*....|...
gi 489520788 599 VGHDEGG--QLTEKVRRNPYSVILFDEIEKAHP 629
Cdd:TIGR01243 528 VGESEKAirEIFRKARQAAPAIIFFDEIDAIAP 560
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
94-143 |
1.64e-07 |
|
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: 48.29 E-value: 1.64e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489520788 94 FANKLKTNYIGTEHILLAIIQEGEGIANKILNYAGVNDRTLAQLTIDMMG 143
Cdd:pfam02861 4 LARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
547-664 |
2.54e-07 |
|
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: 50.28 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 547 LFLGPTGVGKTELSKALA-EVQFgdenQIIRIDMSEYMEKhavsrmigsppgYVGHDEGG--QLTEKVRRNPYSVILFDE 623
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAkELGA----PFIEISGSELVSK------------YVGESEKRlrELFEAAKKLAPCVIFIDE 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489520788 624 IEKAHP-----------DVFNILLQILDdgrltdskGRTVDFKNTIVIMTSN 664
Cdd:pfam00004 66 IDALAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
211-358 |
4.07e-07 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 52.70 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 211 LIGDPGVGKTAIAEGLATNIalgnvpetlkNKTLYSLEMGSLLAgaKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTiI 290
Cdd:COG1222 117 LYGPPGTGKTLLAKAVAGEL----------GAPFIRVRGSELVS--KYIGEGARNVREVFELAREKAPSIIFIDEIDA-I 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 291 GAGSTGEGSIDASNILKPAL--------ARGEIQVIGAT-TIDEYrkhvekDSALER--RFQPVM-VDEPTKEDSIKILE 358
Cdd:COG1222 184 AARRTDDGTSGEVQRTVNQLlaeldgfeSRGDVLIIAATnRPDLL------DPALLRpgRFDRVIeVPLPDEEAREEILK 257
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
205-345 |
4.15e-07 |
|
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: 50.06 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 205 TKNNPVLIGDPGVGKTAIAEGLATNIALGNVPETLKN-----KTLYSLEMGSLLAGAKYRGEFEERIKEVVDEVVKNGNI 279
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDgedilEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489520788 280 ILFIDEMHTIIGAGSTGEG-SIDASNILKPALARGEIQVIGATTideyRKHVEKDSALERRFQPVMV 345
Cdd:smart00382 81 VLILDEITSLLDAEQEALLlLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRFDRRIV 143
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
211-321 |
9.29e-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: 49.20 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 211 LIGDPGVGKTAIAEGLATNIalgnvpetlkNKTLYSLEMGSLLagAKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTiI 290
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDA-I 97
|
90 100 110
....*....|....*....|....*....|....*....
gi 489520788 291 GAGSTGEGSIDASNILKPAL--------ARGEIQVIGAT 321
Cdd:cd19481 98 GRKRDSSGESGELRRVLNQLlteldgvnSRSKVLVIAAT 136
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
515-625 |
1.57e-06 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 50.78 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 515 VIGQEQAVKSISKAIRRSragLKDPN-------RPIGSFLFLGPTGVGKTELSKALA---EVQFgdenqiIRIDMSEYME 584
Cdd:COG1222 80 IGGLDEQIEEIREAVELP---LKNPElfrkygiEPPKGVLLYGPPGTGKTLLAKAVAgelGAPF------IRVRGSELVS 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489520788 585 KhavsrmigsppgYVGhdEGGQLTEKV----RRNPYSVILFDEIE 625
Cdd:COG1222 151 K------------YIG--EGARNVREVfelaREKAPSIIFIDEID 181
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
210-341 |
1.76e-06 |
|
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. 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: 410929 [Multi-domain] Cd Length: 170 Bit Score: 48.70 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 210 VLIGDPGVGKTAIAEGLATNIalgnvpetlkNKTLYSLEMGSLLAgaKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTI 289
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVATEA----------NSTFFSVSSSDLVS--KWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489520788 290 igAGSTGEGSIDASNILKPALA---------RGEIQVIGATTIDeyrkhVEKDSALERRFQ 341
Cdd:cd19521 112 --CGTRGEGESEASRRIKTELLvqmngvgndSQGVLVLGATNIP-----WQLDSAIRRRFE 165
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
210-341 |
1.94e-06 |
|
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: 48.50 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 210 VLIGDPGVGKTAIAEGLATNIalgnvpetlkNKTLYSLEMGSLLAgaKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTI 289
Cdd:cd19509 36 LLYGPPGTGKTLLARAVASES----------GSTFFSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489520788 290 IgaGSTGEGSIDASNILK----------PALARGEIQVIGATTIDEyrkhvEKDSALERRFQ 341
Cdd:cd19509 104 L--SERGSGEHEASRRVKteflvqmdgvLNKPEDRVLVLGATNRPW-----ELDEAFLRRFE 158
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
210-321 |
2.70e-06 |
|
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 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: 410925 [Multi-domain] Cd Length: 170 Bit Score: 48.27 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 210 VLIGDPGVGKTAIAEGLATNIALGNvpetlkNKTLYSLEMGSLLAgAKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTI 289
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAECSKGG------QKVSFFMRKGADCL-SKWVGEAERQLRLLFEEAYRMQPSIIFFDEIDGL 110
|
90 100 110
....*....|....*....|....*....|....*....
gi 489520788 290 IGAGSTGEGSIDASnILKPALA-------RGEIQVIGAT 321
Cdd:cd19517 111 APVRSSKQEQIHAS-IVSTLLAlmdgldnRGQVVVIGAT 148
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
511-626 |
2.89e-06 |
|
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: 48.53 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 511 LHNRVIGQEQAVKSISKAIR----RSR--AGLKDPNRPiGSFLFLGPTGVGKTELSKALAEVQfgdENQIIRIDMSEYME 584
Cdd:cd19498 9 LDKYIIGQDEAKRAVAIALRnrwrRMQlpEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKFTE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489520788 585 KhavsrmigsppGYVGHDeggqlTEKVRRNPYSVILF-DEIEK 626
Cdd:cd19498 85 V-----------GYVGRD-----VESIIRDLVEGIVFiDEIDK 111
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
210-340 |
3.59e-06 |
|
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-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: 410926 [Multi-domain] Cd Length: 169 Bit Score: 47.78 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 210 VLIGDPGVGKTAIAEGLATNIAlgnVPetlknktLYSLEMGSLLAGAKyrGEFEERIKEVVDEVVKNGNIILFIDEMHTI 289
Cdd:cd19518 38 LLHGPPGCGKTMLANAIAGELK---VP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEIDAI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489520788 290 IG----AGSTGEGSIDAS------NILKPALARGEIQVIGATTIDEyrkhvEKDSALER--RF 340
Cdd:cd19518 106 TPkresAQREMERRIVSQlltcmdELNNEKTAGGPVLVIGATNRPD-----SLDPALRRagRF 163
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
203-341 |
7.22e-06 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. 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: 410930 [Multi-domain] Cd Length: 170 Bit Score: 46.90 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 203 RRTKNNPVLIGDPGVGKTAIAEGLATNIAlgnvpetlknKTLYSLEMGSLlaGAKYRGEFEERIKEVVDEVVKNGNIILF 282
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVATECG----------TTFFNVSSSTL--TSKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 283 IDEMHTIIGA-GSTGEGsiDASNILKPALARGEIQVIGATTIDEYRKHV----------EKDSALERRFQ 341
Cdd:cd19522 98 IDEIDSICSRrGTSEEH--EASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLE 165
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
211-340 |
1.48e-05 |
|
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: 46.13 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 211 LIGDPGVGKTAIAEGLATNIalgnvpetlkNKTLYSLEMGSLLAgaKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTII 290
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSISGPSIVS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDALA 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489520788 291 GAGSTGEGSIDAS------NILKPALARGEIQVIGATT-IDEYrkhvekDSALER--RF 340
Cdd:cd19503 107 PKREEDQREVERRvvaqllTLMDGMSSRGKVVVIAATNrPDAI------DPALRRpgRF 159
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
506-664 |
2.06e-05 |
|
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: 47.08 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 506 RLEEILHNRVIGQEQAVKSISKAIRrsrAGlkdpnRPIgsfLFLGPTGVGKTELSKALAEV---QFgdenqiIRI----D 578
Cdd:COG0714 5 RLRAEIGKVYVGQEELIELVLIALL---AG-----GHL---LLEGVPGVGKTTLAKALARAlglPF------IRIqftpD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 579 MseyMEKHAVSRMIgsppgYVGHDEggqlTEKVRRNPY--SVILFDEIEKAHPDVFNILLQILDDGRLTdSKGRTVDFKN 656
Cdd:COG0714 68 L---LPSDILGTYI-----YDQQTG----EFEFRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVT-IPGGTYKLPE 134
|
....*....
gi 489520788 657 T-IVIMTSN 664
Cdd:COG0714 135 PfLVIATQN 143
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
208-384 |
3.10e-05 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 47.74 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 208 NPVLIGDPGVGKTAIAEGLAtNIALGNVpetlknktlysLEMGSLLAGAKyrgEFEERIKEVVDEVVKNG-NIILFIDEM 286
Cdd:PRK13341 54 SLILYGPPGVGKTTLARIIA-NHTRAHF-----------SSLNAVLAGVK---DLRAEVDRAKERLERHGkRTILFIDEV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 287 HTIIGAGStgegsiDAsniLKPALARGEIQVIGATTIDEYrkhVEKDSALERR-----FQPVmvdepTKEDSIKILE-GL 360
Cdd:PRK13341 119 HRFNKAQQ------DA---LLPWVENGTITLIGATTENPY---FEVNKALVSRsrlfrLKSL-----SDEDLHQLLKrAL 181
|
170 180
....*....|....*....|....*.
gi 489520788 361 RDKYEAHHK--VKITDDAIKAAVELS 384
Cdd:PRK13341 182 QDKERGYGDrkVDLEPEAEKHLVDVA 207
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
515-641 |
4.70e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 45.65 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 515 VIGQEQAVKSISKAIR-------RSRAGLKDPNRpigsFLFLGPTGVGKTELSKALAE---VQFGdenqIIRID--MSEY 582
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAGelkLPLL----TVRLDslIGSY 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489520788 583 MEKHAvsRMIgsppgyvghdegGQLTEKVRRNPySVILFDEIE---------KAHPD---VFNILLQILDD 641
Cdd:COG1223 76 LGETA--RNL------------RKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDG 131
|
|
| UVR |
pfam02151 |
UvrB/uvrC motif; |
423-458 |
6.36e-05 |
|
UvrB/uvrC motif;
Pssm-ID: 308001 [Multi-domain] Cd Length: 36 Bit Score: 40.46 E-value: 6.36e-05
10 20 30
....*....|....*....|....*....|....*.
gi 489520788 423 ELEIENIDKEKEEAVRCQDFEKAAKIRDEQGLLKKQ 458
Cdd:pfam02151 1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALKKQ 36
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
509-566 |
6.71e-05 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX 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: 410905 [Multi-domain] Cd Length: 251 Bit Score: 45.28 E-value: 6.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489520788 509 EILHNRVIGQEQAVKSISKAI----RRSRAGLKDPNRPI----GSFLFLGPTGVGKTELSKALAEV 566
Cdd:cd19497 8 EHLDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKI 73
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
515-564 |
9.04e-05 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 45.57 E-value: 9.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489520788 515 VIGQEQAVKSISKAIRRSRaglkdpnrpIG-SFLFLGPTGVGKTELSKALA 564
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILA 53
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
396-459 |
9.13e-05 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 46.19 E-value: 9.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489520788 396 KAI-DLIDEAASKVRLKENTPPSEIKKLEleienidKEKEEAVRCQDFEKAAKIRDEQGLLKKQL 459
Cdd:PRK05298 591 KKIrDILDSVYKKDKLSKKELEKLIKELE-------KQMKEAAKNLEFEEAARLRDEIKELKEEL 648
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
545-643 |
1.15e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 42.71 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 545 SFLFL-GPTGVGKTELSKALAEVQFGDENQIIRIDMSEYMEKHAVSRMIGS---PPGYVGHDEG---GQLTEKV-RRNPY 616
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRalgLPLSGRLSKEellAALQQLLlALAVA 85
|
90 100
....*....|....*....|....*..
gi 489520788 617 SVILFDEIEKAHPDVFNILLQILDDGR 643
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| RecA-like_CDC48_r1-like |
cd19519 |
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ... |
210-321 |
1.45e-04 |
|
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: 43.19 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 210 VLIGDPGVGKTAIAEGLATNIA----LGNVPETLknktlyslemgsllagAKYRGEFEERIKEVVDEVVKNGNIILFIDE 285
Cdd:cd19519 38 LLYGPPGTGKTLIARAVANETGafffLINGPEIM----------------SKLAGESESNLRKAFEEAEKNAPAIIFIDE 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489520788 286 MHTIIGAGSTGEGSIDAS------NILKPALARGEIQVIGAT 321
Cdd:cd19519 102 IDAIAPKREKTHGEVERRivsqllTLMDGLKQRAHVIVMAAT 143
|
|
| UvrB |
COG0556 |
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair]; |
365-458 |
2.47e-04 |
|
Excinuclease UvrABC helicase subunit UvrB [Replication, recombination and repair];
Pssm-ID: 440322 [Multi-domain] Cd Length: 657 Bit Score: 44.62 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 365 EAHHkvkITDDAIKAAVE--LSTRYISDRYLPDKAIDLIDEAASKVRLKEntppsEIKKLEleienidKEKEEAVRCQDF 442
Cdd:COG0556 577 EEHG---ITPQTIKKSIRdiLEGTYEADEETEELVAEADAAKLSKEELEK-----LIKELE-------KEMKEAAKNLEF 641
|
90
....*....|....*.
gi 489520788 443 EKAAKIRDEQGLLKKQ 458
Cdd:COG0556 642 EEAARLRDEIKELKKE 657
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
186-231 |
2.64e-04 |
|
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: 42.49 E-value: 2.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489520788 186 PVIGREKEIQRVIQILSRRTKNNP---VLIGDPGVGKTAIAEGLATNIA 231
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALE 49
|
|
| McsA |
COG3880 |
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein ... |
420-461 |
3.95e-04 |
|
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443088 [Multi-domain] Cd Length: 173 Bit Score: 41.80 E-value: 3.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489520788 420 KKLELEIENIDKEKEEAVRCQDFEKAAKIRDEQGLLKKQLED 461
Cdd:COG3880 129 LRIKREIEELKEELQEAVEKEEYEEAAELRDEIRELEKELGE 170
|
|
| RecA-like_Figl-1 |
cd19525 |
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ... |
210-341 |
5.42e-04 |
|
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. 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: 410933 [Multi-domain] Cd Length: 186 Bit Score: 41.90 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 210 VLIGDPGVGKTAIAEGLATNialgnvpetlKNKTLYSLEMGSLLagAKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTI 289
Cdd:cd19525 59 LLFGPPGTGKTLIGKCIASQ----------SGATFFSISASSLT--SKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSL 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 290 IgaGSTGEGSIDASNILKPALArgeIQVIGATTIDEYRKHV--------EKDSALERRFQ 341
Cdd:cd19525 127 L--SQRGEGEHESSRRIKTEFL---VQLDGATTSSEDRILVvgatnrpqEIDEAARRRLV 181
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
443-557 |
6.12e-04 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 42.93 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 443 EKAAKIRDEQGLLKKQLEDVRERWNKSSKHSDLVDGEVIAEVVGLwtGIPvnkilEEEADRLLrlEEILHNrvIGQEQAV 522
Cdd:COG1419 74 EELEELRRELAELKELLEEQLSGLAGESARLPPELAELLERLLEA--GVS-----PELARELL--EKLPED--LSAEEAW 142
|
90 100 110
....*....|....*....|....*....|....*....
gi 489520788 523 KSISKAIRRSragLKDPNRPIGS----FLFLGPTGVGKT 557
Cdd:COG1419 143 RALLEALARR---LPVAEDPLLDeggvIALVGPTGVGKT 178
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
547-652 |
1.09e-03 |
|
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 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: 410925 [Multi-domain] Cd Length: 170 Bit Score: 40.57 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 547 LFLGPTGVGKTELSKALAEVQFGDENQIiridmSEYMEKHA--VSRMIGSppgyvGHDEGGQLTEKVRRNPYSVILFDEI 624
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAECSKGGQKV-----SFFMRKGAdcLSKWVGE-----AERQLRLLFEEAYRMQPSIIFFDEI 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 489520788 625 -----------EKAHPDVFNILLQILDDgrlTDSKGRTV 652
Cdd:cd19517 108 dglapvrsskqEQIHASIVSTLLALMDG---LDNRGQVV 143
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
532-625 |
1.17e-03 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). 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: 410919 [Multi-domain] Cd Length: 159 Bit Score: 40.34 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 532 SRAGLkdpnRPIGSFLFLGPTGVGKTELSKALA---EVQFgdenqiIRIDMSEYMEKhavsrmigsppgYVGHDEGG--Q 606
Cdd:cd19511 20 KRLGI----RPPKGVLLYGPPGCGKTLLAKALAseaGLNF------ISVKGPELFSK------------YVGESERAvrE 77
|
90
....*....|....*....
gi 489520788 607 LTEKVRRNPYSVILFDEIE 625
Cdd:cd19511 78 IFQKARQAAPCIIFFDEID 96
|
|
| RecA-like_spastin |
cd19524 |
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ... |
203-340 |
2.11e-03 |
|
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. 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: 410932 [Multi-domain] Cd Length: 164 Bit Score: 39.83 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 203 RRTKNNPVLIGDPGVGKTAIAEGLATNialgnvpetlKNKTLYSLEMGSLLAgaKYRGEFEERIKEVVDEVVKNGNIILF 282
Cdd:cd19524 30 RAPARGLLLFGPPGNGKTMLAKAVAAE----------SNATFFNISAASLTS--KYVGEGEKLVRALFAVARELQPSIIF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489520788 283 IDEMHTIIGAGSTGEGsiDASNILK----------PALARGEIQVIGATTideyrKHVEKDSALERRF 340
Cdd:cd19524 98 IDEVDSLLSERSEGEH--EASRRLKtefliefdgvQSNGDDRVLVMGATN-----RPQELDDAVLRRF 158
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
187-232 |
2.82e-03 |
|
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: 40.54 E-value: 2.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 489520788 187 VIGREKEIQRV-IQILSRRtknnPVLI-GDPGVGKTAIAEGLATNIAL 232
Cdd:COG0714 14 YVGQEELIELVlIALLAGG----HLLLeGVPGVGKTTLAKALARALGL 57
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
494-564 |
3.16e-03 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 40.80 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 494 NKILEEEA---------DRLLRLEEI---LHNRVIGQEQAVKSISKAI----RRSRAGLKDPNRP------IgsfLFLGP 551
Cdd:COG1219 41 NEIIEEELkeeeaeeelKKLPKPKEIkafLDEYVIGQERAKKVLSVAVynhyKRLNSGSKDDDDVeleksnI---LLIGP 117
|
90
....*....|...
gi 489520788 552 TGVGKTELSKALA 564
Cdd:COG1219 118 TGSGKTLLAQTLA 130
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
210-465 |
3.17e-03 |
|
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: 41.05 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 210 VLIGDPGVGKTAIAEGLAT----NIALGNVPETLknktlyslemgsllagAKYRGEFEERIKEVVDEVVKNGNIILFIDE 285
Cdd:TIGR01243 491 LLFGPPGTGKTLLAKAVATesgaNFIAVRGPEIL----------------SKWVGESEKAIREIFRKARQAAPAIIFFDE 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 286 MHTIIGAGSTGEGSIDASNILKPALAR-------GEIQVIGATTideyRKHVeKDSALER--RF-QPVMVDEPTKEDSIK 355
Cdd:TIGR01243 555 IDAIAPARGARFDTSVTDRIVNQLLTEmdgiqelSNVVVIAATN----RPDI-LDPALLRpgRFdRLILVPPPDEEARKE 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 356 IleglrdkYEAH-HKVKITDDAikAAVELSTRyiSDRYLPDKAIDLIDEAA-SKVRLKENTPPSEikklELEIENIDKEK 433
Cdd:TIGR01243 630 I-------FKIHtRSMPLAEDV--DLEELAEM--TEGYTGADIEAVCREAAmAALRESIGSPAKE----KLEVGEEEFLK 694
|
250 260 270
....*....|....*....|....*....|....*..
gi 489520788 434 EEAVRCQDFEKAAK-----IRDEQGLLKKQLEDVRER 465
Cdd:TIGR01243 695 DLKVEMRHFLEALKkvkpsVSKEDMLRYERLAKELKR 731
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
416-466 |
3.75e-03 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 36.68 E-value: 3.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489520788 416 PSEIKKLELEIENIDKEKEEAVRCQDFEKAAKIRDEQGLLKKQLEDVRERW 466
Cdd:pfam16326 14 EAEIEKLEEEIAELEAQLADPELYSDYEKLQELSAELEELEAELEELYERW 64
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
515-641 |
4.48e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 40.31 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 515 VIGQEQAVKSISKAIRRSRAGlkdpnrpiGSFLFLGPTGVGKTELSKALAE---VQFGDEN----------QIIRIDMSE 581
Cdd:PRK14956 20 VIHQDLAIGALQNALKSGKIG--------HAYIFFGPRGVGKTTIARILAKrlnCENPIGNepcnectsclEITKGISSD 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489520788 582 YMEKHAVSRMigsppgyvGHDEGGQLTEKVRRNP----YSVILFDEIEKAHPDVFNILLQILDD 641
Cdd:PRK14956 92 VLEIDAASNR--------GIENIRELRDNVKFAPmggkYKVYIIDEVHMLTDQSFNALLKTLEE 147
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
494-566 |
4.86e-03 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 40.14 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 494 NKILEEE-------ADRLLRLEEI---LHNRVIGQEQAVKSISKAI----RRSRAGLKDPNRP------IgsfLFLGPTG 553
Cdd:PRK05342 42 NEIIREElkeeaveLKELPTPKEIkahLDQYVIGQERAKKVLSVAVynhyKRLRHGDKKDDDVelqksnI---LLIGPTG 118
|
90
....*....|...
gi 489520788 554 VGKTELSKALAEV 566
Cdd:PRK05342 119 SGKTLLAQTLARI 131
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
211-322 |
6.63e-03 |
|
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). 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: 410919 [Multi-domain] Cd Length: 159 Bit Score: 38.03 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489520788 211 LIGDPGVGKTAIAEGLATNIALGNVpeTLKNKTLYSlemgsllagaKYRGEFEERIKEVVDEVVKNGNIILFIDEMHTII 290
Cdd:cd19511 32 LYGPPGCGKTLLAKALASEAGLNFI--SVKGPELFS----------KYVGESERAVREIFQKARQAAPCIIFFDEIDSLA 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 489520788 291 GAGSTGEGSIDASNILKPAL-------ARGEIQVIGATT 322
Cdd:cd19511 100 PRRGQSDSSGVTDRVVSQLLteldgieSLKGVVVIAATN 138
|
|
| |
