|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-802 |
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: 1374.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 1 MLFGRLTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVIEEVEKLIGHG---QDHVGT 77
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLpkvSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 78 LHYTPRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGNPEMSNKNAQAsks 157
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGEGVAARILKKLGITLEALREALEELRGGSRVTSQNPES--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 158 nNTPTLDSLARDLTVIAKDGTLDPVIGRDKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVPETLKDK 237
Cdd:COG0542 158 -KTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 238 RVMSLDMGTVVAGTKYRGEFEERLKKVMEEIQQ-AGNVILFIDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATT 316
Cdd:COG0542 237 RVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKsEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 317 LDEYRKNIEKDAALERRFQPVQVDEPSVVDTVAILKGLRDRYEAHHRINISDEAIEAAVKLSNRYVSDRFLPDKAIDLID 396
Cdd:COG0542 317 LDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLID 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 397 EASSKVRLKSHTTPNNLKEIEQEIEKVKNEKDAAVHAQE---FENAANLRDKQTKLEKQYEEAKNEWKNAQNG------- 466
Cdd:COG0542 397 EAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEALKARWEAEKELieeiqel 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 467 -------------------------------MSTSLSEEDIAEVIAGWTGIPLTKINETESEKLLSLEDTLHERVIGQKD 515
Cdd:COG0542 477 keeleqrygkipelekelaeleeelaelaplLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKLLNLEEELHERVIGQDE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 516 AVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESMFGDDDAMIRVDMSEFMEKHAVSRLVGAPPGYVG 595
Cdd:COG0542 557 AVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYMEKHSVSRLIGAPPGYVG 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 596 HDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRTVDFRNTIIIMTSNVGAQELQDQrfagfgg 675
Cdd:COG0542 637 YEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSNIGSELILDL------- 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 676 SSDGQDYETIRKTMLKELKNSFRPEFLNRVDDIIVFHKLTKEELKEIVTMMVNKLTNRLSEQNINIIVTDKAKDKIAEEG 755
Cdd:COG0542 710 AEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDAAKDFLAEKG 789
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 613363399 756 YDPEYGARPLIRAIQKTIEDNLSELILDGNQIEGKKVTVDHDGKEFK 802
Cdd:COG0542 790 YDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
3-808 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 1105.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 3 FGRLTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVIEEVEKLIGHGQDHVGT-LHYT 81
Cdd:CHL00095 2 FERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVEKIIGRGTGFVAVeIPFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 82 PRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGN-PEMSNKNAQASKSnnT 160
Cdd:CHL00095 82 PRAKRVLEMSLEEARDLGHNYIGTEHLLLALLEEGEGVAARVLENLGVDLSKIRSLILNLIGEiIEAILGAEQSRSK--T 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 161 PTLDSLARDLTVIAKDGTLDPVIGRDKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVPETLKDKRVM 240
Cdd:CHL00095 160 PTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDILEDKLVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 241 SLDMGTVVAGTKYRGEFEERLKKVMEEIQQAGNVILFIDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATTLDEY 320
Cdd:CHL00095 240 TLDIGLLLAGTKYRGEFEERLKRIFDEIQENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIGATTLDEY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 321 RKNIEKDAALERRFQPVQVDEPSVVDTVAILKGLRDRYEAHHRINISDEAIEAAVKLSNRYVSDRFLPDKAIDLIDEASS 400
Cdd:CHL00095 320 RKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAIDLLDEAGS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 401 KVRLKSHTTPNNLKEIEQEIEKVKNEKDAAVHAQEFENAANLRDKQTKLEKQYEEAKNEWKNAQNGMST--SLSEEDIAE 478
Cdd:CHL00095 400 RVRLINSRLPPAARELDKELREILKDKDEAIREQDFETAKQLRDREMEVRAQIAAIIQSKKTEEEKRLEvpVVTEEDIAE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 479 VIAGWTGIPLTKINETESEKLLSLEDTLHERVIGQKDAVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARAL 558
Cdd:CHL00095 480 IVSAWTGIPVNKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKAL 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 559 AESMFGDDDAMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGH 638
Cdd:CHL00095 560 ASYFFGSEDAMIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGR 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 639 LTDTKGRTVDFRNTIIIMTSNVGAQELQDQRF-AGFGGSSDGQD---YETIRKTMLKELKNSFRPEFLNRVDDIIVFHKL 714
Cdd:CHL00095 640 LTDSKGRTIDFKNTLIIMTSNLGSKVIETNSGgLGFELSENQLSekqYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQL 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 715 TKEELKEIVTMMVNKLTNRLSEQNINIIVTDKAKDKIAEEGYDPEYGARPLIRAIQKTIEDNLSELILDGNQIEGKKVTV 794
Cdd:CHL00095 720 TKNDVWEIAEIMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIV 799
|
810
....*....|....*
gi 613363399 795 D-HDGKEFKYDIAEQ 808
Cdd:CHL00095 800 DvNDEKEVKILLINK 814
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-801 |
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: 1065.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 6 LTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVIEEVEKLI-------GHGQDhvgtL 78
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELerlpkvsGPGGQ----V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 79 HYTPRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENeGVAARVFAnlDLNITKARA-QVVKAL-GNPEMSNKNAQASK 156
Cdd:TIGR03346 77 YLSPDLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDK-GTLGKLLK--EAGATADALeAAINAVrGGQKVTDANAEDQY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 157 SnntpTLDSLARDLTVIAKDGTLDPVIGRDKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVPETLKD 236
Cdd:TIGR03346 154 E----ALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 237 KRVMSLDMGTVVAGTKYRGEFEERLKKVMEEIQQA-GNVILFIDELHTLVGAGGAEGAIDASNILKPALARGELQCIGAT 315
Cdd:TIGR03346 230 KRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSeGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGAT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 316 TLDEYRKNIEKDAALERRFQPVQVDEPSVVDTVAILKGLRDRYEAHHRINISDEAIEAAVKLSNRYVSDRFLPDKAIDLI 395
Cdd:TIGR03346 310 TLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 396 DEASSKVRLKSHTTPNNLKEIE---------------------------------------------------------- 417
Cdd:TIGR03346 390 DEAAARIRMEIDSKPEELDELDrriiqleierealkkekdeaskkrledlekeladleeeyaeleeqwkaekasiqgiqq 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 418 --QEIEKVKNEKDAAVHAQEFENAANLR-DKQTKLEKQYEEAKNEWKNAQNGM-STSLSEEDIAEVIAGWTGIPLTKINE 493
Cdd:TIGR03346 470 ikEEIEQVRLELEQAEREGDLAKAAELQyGKLPELEKQLQAAEQKLGEEQNRLlREEVTAEEIAEVVSRWTGIPVSKMLE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 494 TESEKLLSLEDTLHERVIGQKDAVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESMFGDDDAMIRVD 573
Cdd:TIGR03346 550 GEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRID 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 574 MSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRTVDFRNTI 653
Cdd:TIGR03346 630 MSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTV 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 654 IIMTSNVGAQELQDQrfagfggsSDGQDYETIRKTMLKELKNSFRPEFLNRVDDIIVFHKLTKEELKEIVTMMVNKLTNR 733
Cdd:TIGR03346 710 IIMTSNLGSDFIQEL--------AGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKR 781
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613363399 734 LSEQNINIIVTDKAKDKIAEEGYDPEYGARPLIRAIQKTIEDNLSELILDGNQIEGKKVTVDHDGKEF 801
Cdd:TIGR03346 782 LAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRL 849
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-798 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 815.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 1 MLFGRLTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVIEEVEKLIGHGQDHVGT--- 77
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTggd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 78 LHYTPRAKKVIELSMDEARKLHHNFVGTEHILLGLIrENEGVAARVFANLDLNITKARAQVVKALGNPEMSNKNAQASKS 157
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAAL-ESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 158 nntpTLDSLARDLTVIAKDGTLDPVIGRDKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVPETLKDK 237
Cdd:PRK10865 160 ----ALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 238 RVMSLDMGTVVAGTKYRGEFEERLKKVMEEI-QQAGNVILFIDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATT 316
Cdd:PRK10865 236 RVLALDMGALVAGAKYRGEFEERLKGVLNDLaKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 317 LDEYRKNIEKDAALERRFQPVQVDEPSVVDTVAILKGLRDRYEAHHRINISDEAIEAAVKLSNRYVSDRFLPDKAIDLID 396
Cdd:PRK10865 316 LDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLID 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 397 EASSKVRLKSHTTPNNLKEIEQEIEKVKNEKDAAvhAQEFENAAN-----LRDKQTKLEKQYEEAKNEWK---------- 461
Cdd:PRK10865 396 EAASSIRMQIDSKPEELDRLDRRIIQLKLEQQAL--MKESDEASKkrldmLNEELSDKERQYSELEEEWKaekaslsgtq 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 462 -------------------------------------------NAQNGMSTSL-----SEEDIAEVIAGWTGIPLTKINE 493
Cdd:PRK10865 474 tikaeleqakiaieqarrvgdlarmselqygkipelekqlaaaTQLEGKTMRLlrnkvTDAEIAEVLARWTGIPVSRMLE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 494 TESEKLLSLEDTLHERVIGQKDAVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESMFGDDDAMIRVD 573
Cdd:PRK10865 554 SEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRID 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 574 MSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRTVDFRNTI 653
Cdd:PRK10865 634 MSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTV 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 654 IIMTSNVGAQELQDqRFAGFggssdgqDYETIRKTMLKELKNSFRPEFLNRVDDIIVFHKLTKEELKEIVTMMVNKLTNR 733
Cdd:PRK10865 714 VIMTSNLGSDLIQE-RFGEL-------DYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKR 785
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613363399 734 LSEQNINIIVTDKAKDKIAEEGYDPEYGARPLIRAIQKTIEDNLSELILDGNQIEGKKVTVDHDG 798
Cdd:PRK10865 786 LEERGYEIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVND 850
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
6-795 |
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: 771.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 6 LTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAakVLESFNITEDKVIEEVEKLIGHG-----QDHVGTLHY 80
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEAIE--ILEECGGDVELLRKRLEDYLEENlpvipEDIDEEPEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 81 TPRAKKVIELSMDEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGNPEMSNKNAQASKSNNT 160
Cdd:TIGR02639 79 TVGVQRVIQRALLHVKSAGKKEIDIGDLLVALFDEEDSHASYFLKSQGITRLDILNYISHGISKDDGKDQLGEEAGKEEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 161 PTLDSLAR---DLTVIAKDGTLDPVIGRDKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVPETLKDK 237
Cdd:TIGR02639 159 KGQDALEKytvDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 238 RVMSLDMGTVVAGTKYRGEFEERLKKVMEEIQQAGNVILFIDELHTLVGAG-GAEGAIDASNILKPALARGELQCIGATT 316
Cdd:TIGR02639 239 KIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNAILFIDEIHTIVGAGaTSGGSMDASNLLKPALSSGKIRCIGSTT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 317 LDEYRKNIEKDAALERRFQPVQVDEPSVVDTVAILKGLRDRYEAHHRINISDEAIEAAVKLSNRYVSDRFLPDKAIDLID 396
Cdd:TIGR02639 319 YEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDVID 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 397 EASSKVRLKShttpnnlkeieqeiekvKNEKDAAVhaqefenaanlrdkqtklekqyeeaknewknaqngmstslSEEDI 476
Cdd:TIGR02639 399 EAGAAFRLRP-----------------KAKKKANV----------------------------------------NVKDI 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 477 AEVIAGWTGIPLTKINETESEKLLSLEDTLHERVIGQKDAVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELAR 556
Cdd:TIGR02639 422 ENVVAKMAKIPVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAK 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 557 ALAESMfgdDDAMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDD 636
Cdd:TIGR02639 502 QLAEEL---GVHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDY 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 637 GHLTDTKGRTVDFRNTIIIMTSNVGAQELqDQRFAGFGGssdgqdyETIRKTMLKELKNSFRPEFLNRVDDIIVFHKLTK 716
Cdd:TIGR02639 579 ATLTDNNGRKADFRNVILIMTSNAGASEM-SKPPIGFGG-------ENRESKSLKAIKKLFSPEFRNRLDAIIHFNDLSE 650
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613363399 717 EELKEIVTMMVNKLTNRLSEQNINIIVTDKAKDKIAEEGYDPEYGARPLIRAIQKTIEDNLSELILDGNQIEGKKVTVD 795
Cdd:TIGR02639 651 EMAEKIVKKFLDELQDQLNEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKIS 729
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
6-795 |
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: 707.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 6 LTERAQRVLAHAQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVIEEVEKLIGhgQDHVGTLHYTPRAK 85
Cdd:TIGR03345 1 LNPTSRRALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALD--KLPRGNTRTPVFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 86 KVIEL--------SMDearkLHHNFVGTEHILLGLIRENE--GVAARVFANLD-LNITKARAQVVKAL-GNPEMS----- 148
Cdd:TIGR03345 79 HLVELlqeawllaSLE----LGDGRIRSGHLLLALLTDPElrRLLGSISPELAkIDREALREALPALVeGSAEASaaaad 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 149 -NKNAQASKSNNTPTLDSLARDLTVIAKDGTLDPVIGRDKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVN 227
Cdd:TIGR03345 155 aAPAGAAAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 228 NEVPETLKDKRVMSLDMGTVVAGTKYRGEFEERLKKVMEEIQQAGN-VILFIDELHTLVGAGGAEGAIDASNILKPALAR 306
Cdd:TIGR03345 235 GDVPPALRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQpIILFIDEAHTLIGAGGQAGQGDAANLLKPALAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 307 GELQCIGATTLDEYRKNIEKDAALERRFQPVQVDEPSVVDTVAILKGLRDRYEAHHRINISDEAIEAAVKLSNRYVSDRF 386
Cdd:TIGR03345 315 GELRTIAATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 387 LPDKAIDLIDEASSKVRLKSHTTPNNLKEIEQEIEKVKNEKDAAVHAQEF-----ENAANLRDKQTKLEKQYEEAKNEW- 460
Cdd:TIGR03345 395 LPDKAVSLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREAALgadhdERLAELRAELAALEAELAALEARWq 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 461 -----------------------------------------KNAQNG---MSTSLSEEDIAEVIAGWTGIPLTKINETES 496
Cdd:TIGR03345 475 qekelveailalraeleadadapaddddalraqlaeleaalASAQGEeplVFPEVDAQAVAEVVADWTGIPVGRMVRDEI 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 497 EKLLSLEDTLHERVIGQKDAVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESMFGDDDAMIRVDMSE 576
Cdd:TIGR03345 555 EAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLITINMSE 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 577 FMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRTVDFRNTIIIM 656
Cdd:TIGR03345 635 FQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKNTVILL 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 657 TSNVGAQEL----QDQRFAgfggssdgQDYETIRKTMLKELKNSFRPEFLNRVdDIIVFHKLTKEELKEIVTMMVNKLTN 732
Cdd:TIGR03345 715 TSNAGSDLImalcADPETA--------PDPEALLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIAR 785
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613363399 733 RLSEQ-NINIIVTDKAKDKIAEEGYDPEYGARPLIRAIQKTIEDNLSELILD--GNQIEGKKVTVD 795
Cdd:TIGR03345 786 RLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILErlAAGEPIERIHLD 851
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
26-818 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 570.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 26 HSNIGTEHLLLGLMKEPEgiAAKVLESFNITEDKVIEEVEKLIGH------GQDHVGTLHYTPRAKKVIELSMDEARKLH 99
Cdd:PRK11034 22 HEFMTVEHLLLALLSNPS--AREALEACSVDLVALRQELEAFIEQttpvlpASEEERDTQPTLSFQRVLQRAVFHVQSSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 100 HNFVGTEHILLGLIRENEGVAARVFANLDLnitkARAQVVKALGNPEMSNKNAQASKSNNTPT----------LDSLARD 169
Cdd:PRK11034 100 RSEVTGANVLVAIFSEQESQAAYLLRKHEV----SRLDVVNFISHGTRKDEPSQSSDPGSQPNseeqaggeerMENFTTN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 170 LTVIAKDGTLDPVIGRDKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVPETLKDKRVMSLDMGTVVA 249
Cdd:PRK11034 176 LNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 250 GTKYRGEFEERLKKVMEEIQQAGNVILFIDELHTLVGAGGAEGA-IDASNILKPALARGELQCIGATTLDEYRKNIEKDA 328
Cdd:PRK11034 256 GTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEKDR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 329 ALERRFQPVQVDEPSVVDTVAILKGLRDRYEAHHRINISDEAIEAAVKLSNRYVSDRFLPDKAIDLIDEASSKVRLksht 408
Cdd:PRK11034 336 ALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARL---- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 409 TPNNlkeieqeiekvknekdaavhaqefenaanlRDKQTklekqyeeaknewknaqngmstsLSEEDIAEVIAGWTGIPL 488
Cdd:PRK11034 412 MPVS------------------------------KRKKT-----------------------VNVADIESVVARIARIPE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 489 TKINETESEKLLSLEDTLHERVIGQKDAVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESMfgdDDA 568
Cdd:PRK11034 439 KSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIE 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 569 MIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRTVD 648
Cdd:PRK11034 516 LLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKAD 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 649 FRNTIIIMTSNVGAQELQDQRFaGFggssDGQDYETirkTMLKELKNSFRPEFLNRVDDIIVFHKLTKEELKEIVTMMVN 728
Cdd:PRK11034 596 FRNVVLVMTTNAGVRETERKSI-GL----IHQDNST---DAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIV 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 729 KLTNRLSEQNINIIVTDKAKDKIAEEGYDPEYGARPLIRAIQKTIEDNLSELILDGNQIEGK--KVTVDHDGKEFKYDIa 806
Cdd:PRK11034 668 ELQAQLDQKGVSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGqvTVALDKEKNELTYGF- 746
|
810
....*....|..
gi 613363399 807 eqTSETKTPSQA 818
Cdd:PRK11034 747 --QSAQKHKAEA 756
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
498-711 |
8.14e-108 |
|
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: 327.60 E-value: 8.14e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 498 KLLSLEDTLHERVIGQKDAVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESMFGDDDAMIRVDMSEF 577
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 578 MEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTDTKGRTVDFRNTIIIMT 657
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613363399 658 SNVgaqelqdqrfagfggssdgqdyetirktmlkelknsFRPEFLNRVDDIIVF 711
Cdd:cd19499 161 SNH------------------------------------FRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
536-708 |
2.09e-92 |
|
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: 287.17 E-value: 2.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 536 RPIGSFIFLGPTGVGKTELARALAESMFGDDDAMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQLTEKVRRKPYSVIL 615
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 616 FDEIEKAHPDVFNILLQVLDDGHLTDTKGRTVDFRNTIIIMTSNVGAQELQDQRfagfgGSSDGQDYETIRKTMLKELKN 695
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDAS-----RLGDSPDYELLKEEVMDLLKK 155
|
170
....*....|...
gi 613363399 696 SFRPEFLNRVDDI 708
Cdd:pfam07724 156 GFIPEFLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
343-446 |
2.28e-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: 160.73 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 343 SVVDTVAILKGLRDRYEAHHRINISDEAIEAAVKLSNRYVSDRFLPDKAIDLIDEASSKVRLKSHTTPNNLKEIEQEIEK 422
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 613363399 423 VKNEKDAAVHAQEFENAANLRDKQ 446
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, ... |
714-794 |
8.12e-31 |
|
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: 115.58 E-value: 8.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 714 LTKEELKEIVTMMVNKLTNRLSEQNINIIVTDKAKDKIAEEGYDPEYGARPLIRAIQKTIEDNLSELILDGNQIEGKKVT 793
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 613363399 794 V 794
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, ... |
714-802 |
1.66e-28 |
|
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: 109.46 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 714 LTKEELKEIVTMMVNKLTNRLSEQNINIIVTDKAKDKIAEEGYDPEYGARPLIRAIQKTIEDNLSELILDGNQIEGKKVT 793
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*....
gi 613363399 794 VDHDGKEFK 802
Cdd:smart01086 81 VDVDDGELV 89
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
183-335 |
6.72e-21 |
|
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: 89.90 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 183 IGRDKEITRVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVPetlkdkrVMSLDMGTVVAGTKYRGEFEERLK 262
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAP-------FLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613363399 263 KVMEEI-QQAGNVILFIDELHTLvGAGGAEGAIDASNILKPALA-RGELQCIGATTLDEYRKnieKDAALERRFQ 335
Cdd:cd00009 74 RLLFELaEKAKPGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGD---LDRALYDRLD 144
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
511-659 |
4.60e-20 |
|
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: 87.59 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 511 IGQKDAVNSISKAVRRAraglkdPKRPIgsfIFLGPTGVGKTELARALAESMFGDDDAMIRVDMSEFMEKHAVSRLvgap 590
Cdd:cd00009 1 VGQEEAIEALREALELP------PPKNL---LLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAEL---- 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613363399 591 pgyVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLTdtkgrTVDFRNTIIIMTSN 659
Cdd:cd00009 68 ---FGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATN 128
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-69 |
3.30e-15 |
|
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: 70.24 E-value: 3.30e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 613363399 17 AQEEAIRLNHSNIGTEHLLLGLMKEPEGIAAKVLESFNITEDKVIEEVEKLIG 69
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
540-671 |
6.69e-15 |
|
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: 72.33 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 540 SFIFLGPTGVGKTELARALAESMFGDDDAMirVDMSEFMEKhavSRLVG----APPGYVGHDdgGQLTEKVRRKpySVIL 615
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFY--VQLTRDTTE---EDLFGrrniDPGGASWVD--GPLVRAAREG--EIAV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 613363399 616 FDEIEKAHPDVFNILLQVLDDGHLTDTKGRT---VDFRNTIIIMTSNVGAQELQDQRFA 671
Cdd:pfam07728 72 LDEINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMNPLDRGLNELSPA 130
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
542-659 |
2.71e-14 |
|
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: 70.87 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 542 IFLGPTGVGKTELARALAESMFGDDDAMIRVDMSEFMEKHAVSRLVGAPPGYVGHDDGGQ----LTEKVRRKPYSVILFD 617
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 613363399 618 EIEKAHPDVFNILLQVLDDGHLTDTKGRtvdFRNTIIIMTSN 659
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTN 124
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
206-335 |
3.36e-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: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 206 LIGEPGVGKTAIAEGLAQAIvnnevpetlkDKRVMSLDMGTVVAgtKYRGEFEERLKKVMEEIQQAGNVILFIDELHTLV 285
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAKKLAPCVIFIDEIDALA 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 613363399 286 GAGGAEG---AIDASNILKPAL-----ARGELQCIGATTldeyrkNIEK-DAALERRFQ 335
Cdd:pfam00004 71 GSRGSGGdseSRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFD 123
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
513-659 |
6.01e-12 |
|
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: 64.23 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 513 QKDAVNSISKAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESMFGDddaMIRVDMSEFMEKHavsrlvgappG 592
Cdd:cd19481 1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLP---LIVVKLSSLLSKY----------V 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613363399 593 YVGHDDGGQLTEKVRRKPYSVILFDEIEKAHPD------------VFNILLQVLDDGHLTDtkgrtvdfrNTIIIMTSN 659
Cdd:cd19481 68 GESEKNLRKIFERARRLAPCILFIDEIDAIGRKrdssgesgelrrVLNQLLTELDGVNSRS---------KVLVIAATN 137
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
93-143 |
1.21e-11 |
|
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: 60.23 E-value: 1.21e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 613363399 93 DEARKLHHNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALG 143
Cdd:pfam02861 3 ELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
205-352 |
5.32e-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: 65.32 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 205 VLIGEPGVGKTAIAEGLAQAIvnnevpetlkDKRVMSLDMGTVVAgtKYRGEFEERLKKVMEEIQQAGNVILFIDELHTL 284
Cdd:COG0464 195 LLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLVS--KYVGETEKNLREVFDKARGLAPCVLFIDEADAL 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613363399 285 VGAGGAEGAIDAS---NILKPALA--RGELQCIGATtldeYRK-NIekDAALERRFQ-PVQVDEPSVVDTVAILK 352
Cdd:COG0464 263 AGKRGEVGDGVGRrvvNTLLTEMEelRSDVVVIAAT----NRPdLL--DPALLRRFDeIIFFPLPDAEERLEIFR 331
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
471-726 |
9.70e-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: 64.55 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 471 LSEEDIAEVIAGWTGIPLTKINETESEKLLSLEDTLhERVIG---QKDAVNSISKAVR-----RARAGLKDPKRpigsFI 542
Cdd:COG0464 121 LLRESAEALALAAPLVTYEDIGGLEEELLELREAIL-DDLGGleeVKEELRELVALPLkrpelREEYGLPPPRG----LL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 543 FLGPTGVGKTELARALAESMFGDddaMIRVDMSEFMEKhavsrlvgappgYVGHddggqlTEK--------VRRKPYSVI 614
Cdd:COG0464 196 LYGPPGTGKTLLARALAGELGLP---LIEVDLSDLVSK------------YVGE------TEKnlrevfdkARGLAPCVL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 615 LFDEIEKAHPD-----------VFNILLQVLDDGHltdtkgrtvdfRNTIIIMTSNvgaqelqdqRFagfgGSSDgqdye 683
Cdd:COG0464 255 FIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------SDVVVIAATN---------RP----DLLD----- 305
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 613363399 684 tirktmlkelknsfrPEFLNRVDDIIVFHKLTKEELKEIVTMM 726
Cdd:COG0464 306 ---------------PALLRRFDEIIFFPLPDAEERLEIFRIH 333
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
542-659 |
9.73e-10 |
|
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: 57.22 E-value: 9.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 542 IFLGPTGVGKTELARALAESMFGDddaMIRVDMSEFMEKHavsrlVGAPPGYVghddgGQLTEKVRRKPYSVILFDEIEK 621
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSKY-----VGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 613363399 622 AHP-----------DVFNILLQVLDdghltdtkGRTVDFRNTIIIMTSN 659
Cdd:pfam00004 69 LAGsrgsggdsesrRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
200-334 |
1.06e-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: 54.69 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 200 TKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVPETLKD-----KRVMSLDMGTVVAGTKYRGEFEERLKKVMEEIQQAGNV 274
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDgedilEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613363399 275 ILFIDELHTLVGAG--GAEGAIDASNILKPALARGELQCIGATTldeyRKNIEKDAALERRF 334
Cdd:smart00382 81 VLILDEITSLLDAEqeALLLLLEELRLLLLLKSEKNLTVILTTN----DEKDLGPALLRRRF 138
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
178-419 |
4.83e-08 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 56.25 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 178 TLDPVIG------RDKEITRVIEvlsrrTKNNPVLI--GEPGVGKTAIAEGLAQAIvnnevpetlkDKRVMSLDmgTVVA 249
Cdd:PRK13342 10 TLDEVVGqehllgPGKPLRRMIE-----AGRLSSMIlwGPPGTGKTTLARIIAGAT----------DAPFEALS--AVTS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 250 GTKyrgefeeRLKKVMEEIQQA----GNVILFIDELHTLvgaggaegaidasN-----ILKPALARGELQCIGATTldEy 320
Cdd:PRK13342 73 GVK-------DLREVIEEARQRrsagRRTILFIDEIHRF-------------NkaqqdALLPHVEDGTITLIGATT--E- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 321 rkN--IEKDAALERR-----FQPVQVDEpsvvdtvaiLKGLRDRYEAHHR---INISDEAIEAAVKLSN---Ryvsdrfl 387
Cdd:PRK13342 130 --NpsFEVNPALLSRaqvfeLKPLSEED---------IEQLLKRALEDKErglVELDDEALDALARLANgdaR------- 191
|
250 260 270
....*....|....*....|....*....|..
gi 613363399 388 pdKAIDLIDEAsskVRLKSHTTPNNLKEIEQE 419
Cdd:PRK13342 192 --RALNLLELA---ALGVDSITLELLEEALQK 218
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
436-620 |
5.92e-08 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 55.40 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 436 FENAANLRDKQTKLEKQYEEAKNEWKNAQNGMSTSLSEEDIAEVIAGWTGIPLTKINETESEKLlSLEDtlherVIGQKD 515
Cdd:COG1222 12 KALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDV-TFDD-----IGGLDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 516 AVNSISKAVRRaraGLKDP-------KRPIGSFIFLGPTGVGKTELARALAESMfgdDDAMIRVDMSEFMEKhavsrlvg 588
Cdd:COG1222 86 QIEEIREAVEL---PLKNPelfrkygIEPPKGVLLYGPPGTGKTLLAKAVAGEL---GAPFIRVRGSELVSK-------- 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 613363399 589 appgYVGhdDGGQLTEKV----RRKPYSVILFDEIE 620
Cdd:COG1222 152 ----YIG--EGARNVREVfelaREKAPSIIFIDEID 181
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
506-621 |
9.17e-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: 52.77 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 506 LHERVIGQKDAVNSISKAVR------RARAGLKDPKRPiGSFIFLGPTGVGKTELARALAESMfgdDDAMIRVDMSEFME 579
Cdd:cd19498 9 LDKYIIGQDEAKRAVAIALRnrwrrmQLPEELRDEVTP-KNILMIGPTGVGKTEIARRLAKLA---GAPFIKVEATKFTE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 613363399 580 KhavsrlvgappGYVGHDdggqlTEKVRRKPYSVILF-DEIEK 621
Cdd:cd19498 85 V-----------GYVGRD-----VESIIRDLVEGIVFiDEIDK 111
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
206-312 |
2.14e-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: 51.13 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 206 LIGEPGVGKTAIAEGLAQAIVNNevpetlkdkrVMSLDMGTVVagTKYRGEFEERLKKVMEEIQQAGNVILFIDELHTLV 285
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGELGLP----------LIVVKLSSLL--SKYVGESEKNLRKIFERARRLAPCILFIDEIDAIG 98
|
90 100
....*....|....*....|....*..
gi 613363399 286 GAGGAEGAIDASNILKPALargeLQCI 312
Cdd:cd19481 99 RKRDSSGESGELRRVLNQL----LTEL 121
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
206-284 |
1.44e-06 |
|
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: 48.83 E-value: 1.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613363399 206 LIGEPGVGKTAIAEGLAqaivnNEVpetlkDKRVMSLDMGTVVAgtKYRGEFEERLKKVMEEIQQAGNVILFIDELHTL 284
Cdd:cd19503 39 LHGPPGTGKTLLARAVA-----NEA-----GANFLSISGPSIVS--KYLGESEKNLREIFEEARSHAPSIIFIDEIDAL 105
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
540-638 |
9.42e-06 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 45.80 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 540 SFIFL-GPTGVGKTELARALAESMFGDDDAMIRVDMSEFMEK----HAVSRLVGAPPGYVG--HDDGGQLTEKV-RRKPY 611
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLskEELLAALQQLLlALAVA 85
|
90 100
....*....|....*....|....*..
gi 613363399 612 SVILFDEIEKAHPDVFNILLQVLDDGH 638
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
545-664 |
9.71e-06 |
|
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: 48.24 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 545 GPTGVGKTELARALAESMFGDddaMIRV----DMsefMEkhavSRLVGAppgYVGHDDGGQltEKVRRKPY--SVILFDE 618
Cdd:COG0714 38 GVPGVGKTTLAKALARALGLP---FIRIqftpDL---LP----SDILGT---YIYDQQTGE--FEFRPGPLfaNVLLADE 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 613363399 619 IEKAHPDVFNILLQVLDDGHLTdTKGRTVDFRNT-IIIMTSNVGAQE 664
Cdd:COG0714 103 INRAPPKTQSALLEAMEERQVT-IPGGTYKLPEPfLVIATQNPIEQE 148
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
198-335 |
1.73e-05 |
|
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: 46.13 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 198 RRTKNNPVLIGEPGVGKTAIAEGLAqaivnNEVPETLkdkrvmsLDMGTVVAGTKYRGEFEERLKKVMEEIQQAGNVILF 277
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVA-----TECGTTF-------FNVSSSTLTSKYRGESEKLVRLLFEMARFYAPTTIF 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613363399 278 IDELHTLVGAGGAEGAIDASNILKPALARGELQCIGATTLDEYRKNI----------EKDAALERRFQ 335
Cdd:cd19522 98 IDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLE 165
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
178-379 |
1.97e-05 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 47.74 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 178 TLDPVIG------RDKEITRVIEvlsrrTKNNPVLI--GEPGVGKTAIAEGLAQAIvnnevpetlkDKRVMSLDmgTVVA 249
Cdd:COG2256 23 TLDEVVGqehllgPGKPLRRAIE-----AGRLSSMIlwGPPGTGKTTLARLIANAT----------DAEFVALS--AVTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 250 GTKyrgefeeRLKKVMEEIQQA----GNVILFIDELHTLvgaggaegaidasN-----ILKPALARGELQCIGATTldEy 320
Cdd:COG2256 86 GVK-------DIREVIEEARERraygRRTILFVDEIHRF-------------NkaqqdALLPHVEDGTITLIGATT--E- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613363399 321 rkN--IEKDAALERR-----FQPVQVDepsvvDTVAILK-GLRD--RYEAHHRINISDEAIEAAVKLSN 379
Cdd:COG2256 143 --NpsFEVNSALLSRcrvfvLKPLSEE-----DLEQLLErALADdeRGLGGYKLELDDEALEALARLAD 204
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
508-631 |
2.45e-05 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 47.11 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 508 ERVIGQKDAVNSISKAVRRARaglkdpkrpIG-SFIFLGPTGVGKTELARALAESMF---GDD-------------DAMI 570
Cdd:COG2812 10 DDVVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILAKALNcenGPTgepcgecescraiAAGS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613363399 571 RVDMSEfMEKHAVSRLVgappgyvghDDGGQLTEKVRRKPYS----VILFDEIEKAHPDVFNILL 631
Cdd:COG2812 81 HPDVIE-IDAEASNIGV---------DDIRELIEKVSYAPVEgrykVYIIDEAHMLTTEAFNALL 135
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
179-284 |
4.12e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 46.03 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 179 LDPVIGRD---KEITRVIEVLSRR---------TKNNPVLIGEPGVGKTAIAEGLAQAIvnnevpetlkDKRVMSLDMGT 246
Cdd:COG1223 1 LDDVVGQEeakKKLKLIIKELRRRenlrkfglwPPRKILFYGPPGTGKTMLAEALAGEL----------KLPLLTVRLDS 70
|
90 100 110
....*....|....*....|....*....|....*...
gi 613363399 247 VVagTKYRGEFEERLKKVMEEIQQAGnVILFIDELHTL 284
Cdd:COG1223 71 LI--GSYLGETARNLRKLFDFARRAP-CVIFFDEFDAI 105
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
520-670 |
4.20e-05 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 47.20 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 520 ISKAVRRARAGLKDPkRPIgsFIfLGPTGVGKTELARALAESMFGDDDAMIRVDMSEFMEKHAVSRLVGAPPG-YVGHDD 598
Cdd:COG3284 330 MRRALRRARRLADRD-IPV--LI-LGETGTGKELFARAIHAASPRADGPFVAVNCAAIPEELIESELFGYEPGaFTGARR 405
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613363399 599 GGQlTEKVRRKPYSVILFDEIEKAHPDVFNILLQVLDDGHLT---DTKGRTVDFRntIIIMTSNVGAQELQDQRF 670
Cdd:COG3284 406 KGR-PGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREVTplgGTKPIPVDVR--LIAATHRDLRELVAAGRF 477
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
205-334 |
4.70e-05 |
|
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: 43.82 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 205 VLIGEPGVGKTAIAEGLAQAIVNNEVpetlkdkRVMSLDMGTVVAGTKYRGEFEERLKK-----VMEEIQQAGnvILFID 279
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPV-------FYVQLTRDTTEEDLFGRRNIDPGGASwvdgpLVRAAREGE--IAVLD 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 280 ELHtlvgaggaEGAIDASNILKPAL---------ARGELQC------IGATTLDEYRKNIEKDAALERRF 334
Cdd:pfam07728 74 EIN--------RANPDVLNSLLSLLderrlllpdGGELVKAapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| HolB |
COG0470 |
DNA polymerase III, delta prime subunit [Replication, recombination and repair]; |
513-659 |
1.08e-04 |
|
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
Pssm-ID: 440238 [Multi-domain] Cd Length: 289 Bit Score: 44.97 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 513 QKDAVNSISKAVRRARAGlkdpkrpiGSFIFLGPTGVGKTELARALAESMFGDDDAmirvDMSEFMEKHAVSRLVGAPPG 592
Cdd:COG0470 1 QEEAWEQLLAAAESGRLP--------HALLLHGPPGIGKTTLALALARDLLCENPE----GGKACGQCHSRLMAAGNHPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 593 Y--VGHDDGG---------QLTEKVRRKPYS----VILFDEIEKAHPDVFNILLQVLDDGHltdtkgrtvdfRNTIIIMT 657
Cdd:COG0470 69 LleLNPEEKSdqigidqirELGEFLSLTPLEggrkVVIIDEADAMNEAAANALLKTLEEPP-----------KNTPFILI 137
|
..
gi 613363399 658 SN 659
Cdd:COG0470 138 AN 139
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
205-281 |
1.37e-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: 45.67 E-value: 1.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613363399 205 VLIGEPGVGKTAIAEGLAQAIVNNEVpeTLKDKRVMSldmgtvvagtKYRGEFEERLKKVMEEIQQAGNVILFIDEL 281
Cdd:TIGR01243 216 LLYGPPGTGKTLLAKAVANEAGAYFI--SINGPEIMS----------KYYGESEERLREIFKEAEENAPSIIFIDEI 280
|
|
| McsA |
COG3880 |
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein ... |
414-458 |
1.38e-04 |
|
Protein-arginine kinase activator protein McsA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443088 [Multi-domain] Cd Length: 173 Bit Score: 43.35 E-value: 1.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 613363399 414 KEIEQEIEKVKNEKDAAVHAQEFENAANLRDKQTKLEKQYEEAKN 458
Cdd:COG3880 129 LRIKREIEELKEELQEAVEKEEYEEAAELRDEIRELEKELGEEGE 173
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
182-225 |
1.90e-04 |
|
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: 44.39 E-value: 1.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 613363399 182 VIGRDKEITRV-IEVLSRRtknnPVLI-GEPGVGKTAIAEGLAQAI 225
Cdd:COG0714 14 YVGQEELIELVlIALLAGG----HLLLeGVPGVGKTTLAKALARAL 55
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
181-230 |
2.15e-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: 2.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 613363399 181 PVIGRDKEITRVIEVLSRRTKNNP---VLIGEPGVGKTAIAEGLAQAIVNNEV 230
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALERDGG 53
|
|
| UVR |
pfam02151 |
UvrB/uvrC motif; |
417-452 |
2.27e-04 |
|
UvrB/uvrC motif;
Pssm-ID: 308001 [Multi-domain] Cd Length: 36 Bit Score: 38.92 E-value: 2.27e-04
10 20 30
....*....|....*....|....*....|....*.
gi 613363399 417 EQEIEKVKNEKDAAVHAQEFENAANLRDKQTKLEKQ 452
Cdd:pfam02151 1 KKLIKELEEEMEEAAENEDFEKAAKLRDQINALKKQ 36
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
532-634 |
2.64e-04 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 42.73 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 532 KDPKRPIgsFIFL-GPTGVGKTELARALAESMFGDDDAmIRVDMSEFMEKH----AVSRLVGAPPGYVGHDDGGQLTEKV 606
Cdd:pfam06414 6 TSQERPK--AILLgGQPGAGKTELARALLDELGRQGNV-VRIDPDDFRELHphyrELQAADPKTASEYTQPDASRWVEKL 82
|
90 100 110
....*....|....*....|....*....|..
gi 613363399 607 RRKP----YSVILfdEIEKAHPDVFNILLQVL 634
Cdd:pfam06414 83 LQHAiengYNIIL--EGTLRSPDVAKKIARAL 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 ... |
205-281 |
3.06e-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: 42.04 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 205 VLIGEPGVGKTAIAEGLAqaivnNEVPE---TLKDKRVMSldmgtvvagtKYRGEFEERLKKVMEEIQQAGNVILFIDEL 281
Cdd:cd19519 38 LLYGPPGTGKTLIARAVA-----NETGAfffLINGPEIMS----------KLAGESESNLRKAFEEAEKNAPAIIFIDEI 102
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
510-597 |
3.48e-04 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 43.91 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 510 VIGQKDAVNSISKAVR-RAR-----AGLKD---PKrpigSFIFLGPTGVGKTELARALAESMfgddDA-MIRVDMSEFME 579
Cdd:PRK05201 17 IIGQDDAKRAVAIALRnRWRrmqlpEELRDevtPK----NILMIGPTGVGKTEIARRLAKLA----NApFIKVEATKFTE 88
|
90
....*....|....*...
gi 613363399 580 khaVsrlvgappGYVGHD 597
Cdd:PRK05201 89 ---V--------GYVGRD 95
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
206-281 |
4.19e-04 |
|
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: 41.59 E-value: 4.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613363399 206 LIGEPGVGKTAIAEGLAqaivnNEVPETLkdkrvMSLDMGTVVAGtkYRGEFEERLKKVMEEIQQAGNVILFIDEL 281
Cdd:cd19507 36 LVGIQGTGKSLTAKAIA-----GVWQLPL-----LRLDMGRLFGG--LVGESESRLRQMIQTAEAIAPCVLWIDEI 99
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
100-281 |
5.86e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 42.69 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 100 HNFVGTEHILLGLIRENEGVAARVFANLDLNITKARAQVVKALGNPEMSNKNAQASKSNNTPTLDSLARDLTviakDGTL 179
Cdd:COG1222 2 NDLLTIDENIKALLALIDALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESP----DVTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 180 DPVIGRDKEITRVIEVLSRRTKNN---------PV----LIGEPGVGKTAIAEGLAqaivnNEVPETLkdkrvMSLDMGT 246
Cdd:COG1222 78 DDIGGLDEQIEEIREAVELPLKNPelfrkygiePPkgvlLYGPPGTGKTLLAKAVA-----GELGAPF-----IRVRGSE 147
|
170 180 190
....*....|....*....|....*....|....*
gi 613363399 247 VVagTKYRGEFEERLKKVMEEIQQAGNVILFIDEL 281
Cdd:COG1222 148 LV--SKYIGEGARNVREVFELAREKAPSIIFIDEI 180
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
203-379 |
7.21e-04 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 43.12 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 203 NPVLIGEPGVGKTAiaegLAQAIVNNevpetlkdKRVMSLDMGTVVAGTKyrgEFEERLKKVMEEIQQAG-NVILFIDEL 281
Cdd:PRK13341 54 SLILYGPPGVGKTT----LARIIANH--------TRAHFSSLNAVLAGVK---DLRAEVDRAKERLERHGkRTILFIDEV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 282 HTLVGAggaegAIDAsniLKPALARGELQCIGATTLDEYrknIEKDAALERRFQPVQVDEPSVVDTVAIL-KGLRDRYEA 360
Cdd:PRK13341 119 HRFNKA-----QQDA---LLPWVENGTITLIGATTENPY---FEVNKALVSRSRLFRLKSLSDEDLHQLLkRALQDKERG 187
|
170 180
....*....|....*....|.
gi 613363399 361 HH--RINISDEAIEAAVKLSN 379
Cdd:PRK13341 188 YGdrKVDLEPEAEKHLVDVAN 208
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
542-647 |
7.95e-04 |
|
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: 40.96 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 542 IFLGPTGVGKTELARALAESMFGDDDamirvDMSEFMEKHA--VSRLVGAPPGYVghddgGQLTEKVRRKPYSVILFDEI 619
Cdd:cd19517 38 LFHGPPGTGKTLMARALAAECSKGGQ-----KVSFFMRKGAdcLSKWVGEAERQL-----RLLFEEAYRMQPSIIFFDEI 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 613363399 620 -----------EKAHPDVFNILLQVLDDghlTDTKGRTV 647
Cdd:cd19517 108 dglapvrsskqEQIHASIVSTLLALMDG---LDNRGQVV 143
|
|
| RecA-like_PAN_like |
cd19502 |
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ... |
527-620 |
8.11e-04 |
|
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN 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: 410910 [Multi-domain] Cd Length: 171 Bit Score: 41.17 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 527 ARAGLKDPKrpigSFIFLGPTGVGKTELARALAESMfgdDDAMIRVDMSEFMEKhavsrlvgappgYVGhdDGGQLTEKV 606
Cdd:cd19502 30 EELGIEPPK----GVLLYGPPGTGKTLLAKAVANHT---DATFIRVVGSELVQK------------YIG--EGARLVREL 88
|
90
....*....|....*...
gi 613363399 607 ----RRKPYSVILFDEIE 620
Cdd:cd19502 89 femaREKAPSIIFIDEID 106
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
501-640 |
1.00e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 42.38 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 501 SLEDtlherVIGQKDAVNSiSKAVRRA-RAGLkdpkrpIGSFIFLGPTGVGKTELARALAESMfgdDDAMIRV------- 572
Cdd:PRK13342 10 TLDE-----VVGQEHLLGP-GKPLRRMiEAGR------LSSMILWGPPGTGKTTLARIIAGAT---DAPFEALsavtsgv 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613363399 573 -DMSEFMEKHAVSRLVGappgyvghddggqltekvrrkpYSVILF-DEIekaHPdvFN-----ILLQVLDDGHLT 640
Cdd:PRK13342 75 kDLREVIEEARQRRSAG----------------------RRTILFiDEI---HR--FNkaqqdALLPHVEDGTIT 122
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
510-597 |
1.17e-03 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 42.34 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 510 VIGQKDAVNSISKAVR-RAR-----AGLKD---PKrpigSFIFLGPTGVGKTELARALAesmfgdddamirvdmsefmek 580
Cdd:COG1220 17 IIGQDEAKRAVAIALRnRWRrqqlpEELRDeitPK----NILMIGPTGVGKTEIARRLA--------------------- 71
|
90 100
....*....|....*....|....*...
gi 613363399 581 havsRLVGAP-----------PGYVGHD 597
Cdd:COG1220 72 ----KLANAPfikveatkfteVGYVGRD 95
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
506-560 |
1.19e-03 |
|
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: 41.43 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613363399 506 LHERVIGQKDAVNSISKAV----RRARAGLKDPKRPI----GSFIFLGPTGVGKTELARALAE 560
Cdd:cd19497 10 LDKYVIGQERAKKVLSVAVynhyKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAK 72
|
|
| PRK05298 |
PRK05298 |
excinuclease ABC subunit UvrB; |
390-457 |
1.20e-03 |
|
excinuclease ABC subunit UvrB;
Pssm-ID: 235395 [Multi-domain] Cd Length: 652 Bit Score: 42.34 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613363399 390 KAI-DLIDEASSKVRLKShttpnnlKEIEQEIEKVKNEKDAAVHAQEFENAANLRDKQTKLEKQYEEAK 457
Cdd:PRK05298 591 KKIrDILDSVYKKDKLSK-------KELEKLIKELEKQMKEAAKNLEFEEAARLRDEIKELKEELLGLS 652
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
510-636 |
1.62e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 41.02 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 510 VIGQKDAVNSISKAVR-------RARAGLKDPKRpigsFIFLGPTGVGKTELARALA-ESMFgdddAMIRVDMSEFmekh 581
Cdd:COG1223 4 VVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAgELKL----PLLTVRLDSL---- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613363399 582 aVSRLVGappgyvghdDGG----QLTEKVRRKPySVILFDEIE---------KAHPD---VFNILLQVLDD 636
Cdd:COG1223 72 -IGSYLG---------ETArnlrKLFDFARRAP-CVIFFDEFDaiakdrgdqNDVGEvkrVVNALLQELDG 131
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
205-335 |
1.62e-03 |
|
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: 40.23 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 205 VLIGEPGVGKTAIAEGLAqaivnnevpeTLKDKRVMSLDMGTVVagTKYRGEFEERLKKVMEEIQQAGNVILFIDELHTL 284
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVA----------TEANSTFFSVSSSDLV--SKWMGESEKLVKQLFAMARENKPSIIFIDEVDSL 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 613363399 285 VGAGGaEGAIDASNILKPALARgELQCIGATT---LDEYRKNI--EKDAALERRFQ 335
Cdd:cd19521 112 CGTRG-EGESEASRRIKTELLV-QMNGVGNDSqgvLVLGATNIpwQLDSAIRRRFE 165
|
|
| RecA-like_Lon |
cd19500 |
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ... |
530-635 |
2.90e-03 |
|
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: 39.46 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 530 GLKDPKRPIGSFI---------------FLGPTGVGKTELARALAESM--------FGD--DDAMIRvdmsefmeKHavs 584
Cdd:cd19500 14 GLEDVKERILEYLavrklkgsmkgpilcLVGPPGVGKTSLGKSIARALgrkfvrisLGGvrDEAEIR--------GH--- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 613363399 585 R--LVGAPPGYVghddgGQLTEKVRRK-PysVILFDEIEK----AHPDVFNILLQVLD 635
Cdd:cd19500 83 RrtYVGAMPGRI-----IQALKKAGTNnP--VFLLDEIDKigssFRGDPASALLEVLD 133
|
|
| PRK12402 |
PRK12402 |
replication factor C small subunit 2; Reviewed |
505-579 |
3.74e-03 |
|
replication factor C small subunit 2; Reviewed
Pssm-ID: 237090 [Multi-domain] Cd Length: 337 Bit Score: 40.36 E-value: 3.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613363399 505 TLHERVIGQKDAVNSISKAVrraraglKDPKRPigSFIFLGPTGVGKTELARALAESMFGD--DDAMIRVDMSEFME 579
Cdd:PRK12402 12 ALLEDILGQDEVVERLSRAV-------DSPNLP--HLLVQGPPGSGKTAAVRALARELYGDpwENNFTEFNVADFFD 79
|
|
| RecA-like_VPS4-like |
cd19509 |
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ... |
205-335 |
4.91e-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: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 205 VLIGEPGVGKTAIAEGLAqaivnNEVPETLkdkrvMSLDMGTVVAgtKYRGEFEERLKKVMEEIQQAGNVILFIDELHTL 284
Cdd:cd19509 36 LLYGPPGTGKTLLARAVA-----SESGSTF-----FSISASSLVS--KWVGESEKIVRALFALARELQPSIIFIDEIDSL 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 613363399 285 VGAGGaEGAIDASNILKPALArgeLQCIGATTLDEYR------KNI--EKDAALERRFQ 335
Cdd:cd19509 104 LSERG-SGEHEASRRVKTEFL---VQMDGVLNKPEDRvlvlgaTNRpwELDEAFLRRFE 158
|
|
| RecA-like_NVL_r1-like |
cd19518 |
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ... |
205-281 |
5.25e-03 |
|
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: 38.54 E-value: 5.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613363399 205 VLIGEPGVGKTAiaegLAQAIVNN-EVPetlkdkrVMSLDMGTVVAGTKyrGEFEERLKKVMEEIQQAGNVILFIDEL 281
Cdd:cd19518 38 LLHGPPGCGKTM----LANAIAGElKVP-------FLKISATEIVSGVS--GESEEKIRELFDQAISNAPCIVFIDEI 102
|
|
| RecA-like_PEX1_r2 |
cd19526 |
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ... |
199-284 |
5.51e-03 |
|
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. 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: 410934 [Multi-domain] Cd Length: 158 Bit Score: 38.18 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 199 RTKNNPVLIGEPGVGKTAIAEGLAQA----IVNNEVPETLkdkrvmsldmgtvvagTKYRGEFEERLKKVMEEIQQAGNV 274
Cdd:cd19526 25 RLRSGILLYGPPGCGKTLLASAIASEcglnFISVKGPELL----------------NKYIGASEQNVRDLFSRAQSAKPC 88
|
90
....*....|
gi 613363399 275 ILFIDELHTL 284
Cdd:cd19526 89 ILFFDEFDSI 98
|
|
| CDC48 |
TIGR01243 |
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ... |
191-291 |
5.79e-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: 40.28 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 191 RVIEVLSRRTKNNPVLIGEPGVGKTAIAEGLAQAIVNNEVpeTLKDKRVMSldmgtvvagtKYRGEFEERLKKVMEEIQQ 270
Cdd:TIGR01243 477 EIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFI--AVRGPEILS----------KWVGESEKAIREIFRKARQ 544
|
90 100
....*....|....*....|.
gi 613363399 271 AGNVILFIDELHTLVGAGGAE 291
Cdd:TIGR01243 545 AAPAIIFFDEIDAIAPARGAR 565
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
206-298 |
5.89e-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: 38.42 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 206 LIGEPGVGKTAIAEGLAQAIVNNEVpeTLKDKRVMSldmgtvvagtKYRGEFEERLKKVMEEIQQAGNVILFIDELHTLV 285
Cdd:cd19511 32 LYGPPGCGKTLLAKALASEAGLNFI--SVKGPELFS----------KYVGESERAVREIFQKARQAAPCIIFFDEIDSLA 99
|
90
....*....|...
gi 613363399 286 GAGGAEGAIDASN 298
Cdd:cd19511 100 PRRGQSDSSGVTD 112
|
|
| RecA-like_Yta7-like |
cd19517 |
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ... |
205-334 |
6.36e-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: 38.26 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 205 VLIGEPGVGKTAIAEGLAQaivnnevpETLKDKRVMSLDM--GTVVAgTKYRGEFEERLKKVMEEIQQAGNVILFIDELH 282
Cdd:cd19517 38 LFHGPPGTGKTLMARALAA--------ECSKGGQKVSFFMrkGADCL-SKWVGEAERQLRLLFEEAYRMQPSIIFFDEID 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 283 TLVGAGGAEGAIDASNILKPALA-------RGELQCIGATT-LDEYRKNIEKDAALERRF 334
Cdd:cd19517 109 GLAPVRSSKQEQIHASIVSTLLAlmdgldnRGQVVVIGATNrPDALDPALRRPGRFDREF 168
|
|
| RecA-like_CDC48_r2-like |
cd19511 |
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ... |
527-620 |
6.60e-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: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 527 ARAGLKDPKrpigSFIFLGPTGVGKTELARALAESMfgdDDAMIRVDMSEFMEKhavsrlvgappgYVGHDDGG--QLTE 604
Cdd:cd19511 20 KRLGIRPPK----GVLLYGPPGCGKTLLAKALASEA---GLNFISVKGPELFSK------------YVGESERAvrEIFQ 80
|
90
....*....|....*.
gi 613363399 605 KVRRKPYSVILFDEIE 620
Cdd:cd19511 81 KARQAAPCIIFFDEID 96
|
|
| RecA-like_VCP_r2 |
cd19529 |
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ... |
528-624 |
6.81e-03 |
|
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. 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: 410937 [Multi-domain] Cd Length: 159 Bit Score: 38.25 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 528 RAGLKDPKrpigSFIFLGPTGVGKTELARALAESMFGDddaMIRVDMSEFMekhavSRLVGAPPGYVghddgGQLTEKVR 607
Cdd:cd19529 21 RLGIRPPK----GILLYGPPGTGKTLLAKAVATESNAN---FISVKGPELL-----SKWVGESEKAI-----REIFRKAR 83
|
90
....*....|....*..
gi 613363399 608 RKPYSVILFDEIEKAHP 624
Cdd:cd19529 84 QVAPCVIFFDEIDSIAP 100
|
|
| RecA-like_FtsH |
cd19501 |
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ... |
531-620 |
7.23e-03 |
|
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and 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: 410909 [Multi-domain] Cd Length: 171 Bit Score: 38.37 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613363399 531 LKDPKR--------PIGsFIFLGPTGVGKTELARALAesmfGDDDA-MIRVDMSEFMEKhavsrLVGappgyVGHDDGGQ 601
Cdd:cd19501 23 LKNPEKftklgakiPKG-VLLVGPPGTGKTLLAKAVA----GEAGVpFFSISGSDFVEM-----FVG-----VGASRVRD 87
|
90
....*....|....*....
gi 613363399 602 LTEKVRRKPYSVILFDEIE 620
Cdd:cd19501 88 LFEQAKKNAPCIVFIDEID 106
|
|
| |
